Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P05814
|
CASB_HUMAN
|
MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV
| null | null |
calcium ion transport [GO:0006816]; lactation [GO:0007595]; negative regulation of cysteine-type endopeptidase activity [GO:2000117]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; enzyme inhibitor activity [GO:0004857]
|
PF00363;
| null |
Beta-casein family
|
PTM: Form 1-P is phosphorylated once; half of the molecules are phosphorylated on Ser-24, half on Ser-25. {ECO:0000269|PubMed:18847231, ECO:0000269|PubMed:6715339}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Important role in determination of the surface properties of the casein micelles.
|
Homo sapiens (Human)
|
P05817
|
D11_DICDI
|
MLNKLILLLILSSCLVLSVKSEVNVDCSLVRCAQPICKPHYRLNMTDSCCGRCEPCTDVACTLQVKYCQDGEVPTGCCPCTLPPTKPDCSLVKCARPVCKPYYRLNMTDSCCGRCEPCTGVACTLQIKYCKDGEVPTGCCPCTPQPTKKPDCSKVPCPKILKYCQEGELPTGCCPCTPQPTKKPDCSRVPCPKILKYCKEGELPTGCCPCTPQPTKKPDCSDVMCTMDIRYCKNGELPTGCCPCTPQETKVPDCSKAMCTMDIKYCKPGEKPFGCCPCRENLTQ
| null | null |
actin filament polymerization [GO:0030041]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-substrate adhesion [GO:0031589]; chemotaxis to folate [GO:0043326]; macropinocytosis [GO:0044351]; pattern specification process [GO:0007389]; sorocarp development [GO:0030587]; sorocarp morphogenesis [GO:0031288]
|
cell periphery [GO:0071944]; extracellular region [GO:0005576]; vesicle [GO:0031982]
| null | null | null | null | null | null | null | null | null | null | null | null |
Dictyostelium discoideum (Social amoeba)
|
P05824
|
RECN_ECOLI
|
MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALRWLEENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSLLQEMTARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDANLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPEALPQYYQSLLEEQQQLDDQADSQETLALAVTKHHQQALEIARALHQQRQQYAEELAQLITDSMHALSMPHGQFTIDVKFDEHHLGADGADRIEFRVTTNPGQPMQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQLGESTQVMCVTHLPQVAGCGHQHYFVSKETDGAMTETHMQSLNKKARLQELARLLGGSEVTRNTLANAKELLAA
| null | null |
DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; recombinational interstrand cross-link repair [GO:0036298]; recombinational repair [GO:0000725]; response to ionizing radiation [GO:0010212]; response to radiation [GO:0009314]; response to UV [GO:0009411]; response to X-ray [GO:0010165]; SOS response [GO:0009432]
|
bacterial nucleoid [GO:0043590]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]
|
PF02463;
|
3.40.50.300;
|
RecN family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21219465}. Note=In 70% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
| null | null | null | null | null |
FUNCTION: May be involved in recombinational repair of damaged DNA.
|
Escherichia coli (strain K12)
|
P05825
|
FEPA_ECOLI
|
MNKKIHSLALLVNLGIYGVAQAQEPTDTPVSHDDTIVVTAAEQNLQAPGVSTITADEIRKNPVARDVSKIIRTMPGVNLTGNSTSGQRGNNRQIDIRGMGPENTLILIDGKPVSSRNSVRQGWRGERDTRGDTSWVPPEMIERIEVLRGPAAARYGNGAAGGVVNIITKKGSGEWHGSWDAYFNAPEHKEEGATKRTNFSLTGPLGDEFSFRLYGNLDKTQADAWDINQGHQSARAGTYATTLPAGREGVINKDINGVVRWDFAPLQSLELEAGYSRQGNLYAGDTQNTNSDSYTRSKYGDETNRLYRQNYALTWNGGWDNGVTTSNWVQYEHTRNSRIPEGLAGGTEGKFNEKATQDFVDIDLDDVMLHSEVNLPIDFLVNQTLTLGTEWNQQRMKDLSSNTQALTGTNTGGAIDGVSTTDRSPYSKAEIFSLFAENNMELTDSTIVTPGLRFDHHSIVGNNWSPALNISQGLGDDFTLKMGIARAYKAPSLYQTNPNYILYSKGQGCYASAGGCYLQGNDDLKAETSINKEIGLEFKRDGWLAGVTWFRNDYRNKIEAGYVAVGQNAVGTDLYQWDNVPKAVVEGLEGSLNVPVSETVMWTNNITYMLKSENKTTGDRLSIIPEYTLNSTLSWQAREDLSMQTTFTWYGKQQPKKYNYKGQPAVGPETKEISPYSIVGLSATWDVTKNVSLTGGVDNLFDKRLWRAGNAQTTGDLAGANYIAGAGAYTYNEPGRTWYMSVNTHF
| null | null |
colicin transport [GO:0042914]; enterobactin transport [GO:0042930]; ferric-enterobactin import into cell [GO:0015685]; intracellular iron ion homeostasis [GO:0006879]; siderophore transmembrane transport [GO:0044718]; siderophore-dependent iron import into cell [GO:0033214]
|
cell envelope [GO:0030313]; cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495]
|
colicin transmembrane transporter activity [GO:0042912]; enterobactin binding [GO:1903981]; enterobactin transmembrane transporter activity [GO:0042931]; ferric-enterobactin transmembrane transporter activity [GO:0015620]; ligand-gated channel activity [GO:0022834]; protein domain specific binding [GO:0019904]; siderophore uptake transmembrane transporter activity [GO:0015344]; signaling receptor activity [GO:0038023]
|
PF07715;PF00593;
|
2.40.170.20;2.170.130.10;
|
TonB-dependent receptor family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}.
| null | null | null | null | null |
FUNCTION: This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D.
|
Escherichia coli (strain K12)
|
P05844
|
POLS_IPNVJ
|
MSTSKATATYLRSIMLPENGPASIPDDITERHILKQETSSYNLEVSESGSGLLVCFPGAPGSRVGAHYRWNLNQTALEFDQWLETSQDLKKAFNYGRLISRKYDIQSSTLPAGLYALNGTLNAATFEGSLSEVESLTYNSLMSLTTNPQDKVNNQLVTKGITVLNLPTGFDKPYVRLEDETPQGPQSMNGARMRCTAAIAPRRYEIDLPSERLPTVAATGTPTTIYEGNADIVNSTAVTGDITFQLEAEPVNETRFDFILQFLGLDNDVPVVTVTSSTLVTADNYRGASAKFTQSIPTEMITKPITRVKLAYQLNQQTAIANAATLGAKGPASVSFSSGNGNVPGVLRPITLVAYEKMTPQSILTVAGVSNYELIPNPDLLKNMVTKYGKYDPEGLNYAKMILSHREELDIRTVWRTEEYKERTRAFKEITDFTSDLPTSKAWGWRDLVRGIRKVAAPVLSTLFPMAAPLIGAADQFIGDLTKTNSAGGRYLSHAAGGRYHDVMDSWASGSEAGSYSKHLKTRLESNNYEEVELPKPTKGVIFPVVHTVESAPGEAFGSLVVVIPEAYPELLDPNQQVLSYFKNDTGCVWGIGEDIPFEGDDMCYTALPLKEIKRNGNIVVEKIFAGPAMGPSSQLALSLLVNDIDEGIPRMVFTGEIADDEETVIPICGVDIKAIAAHEHGLPLIGCQPGVDEMVANTSLASHLIQGGALPVQKAQGACRRIKYLGQLMRTTASGMDAELQGLLQATMARAKEVKDAEVFKLLKLMSWTRKNDLTDHMYEWSKEDPDAIKFGRLVSTPPKHQEKPKGPDQHTAQEAKATRISLDAVKAGADFASPEWIAENNYRGPSPGQFKYYMITGRVPNPGEEYEDYVRKPITRPTDMDKIRRLANSVYGLPHQEPAPDDFYQAVVEVFAENGGRGPDQDQMQDLRDLARQMKRRPRPAETRRQTKTPPRAATSSGSRFTPSGDDGEV
|
3.4.21.-
| null |
proteolysis [GO:0006508]
|
host cell cytoplasm [GO:0030430]; T=13 icosahedral viral capsid [GO:0039621]
|
metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198]
|
PF01766;PF01767;PF01768;
|
2.60.120.20;3.30.230.110;6.10.250.1030;1.10.8.880;1.10.150.620;2.60.120.660;
| null |
PTM: Specific enzymatic cleavages yield mature proteins. Capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, giving rise to VP2, the external capsid protein and three small peptides that all stay closely associated with the capsid.
|
SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell.; FUNCTION: The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity). {ECO:0000250}.; FUNCTION: Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation. {ECO:0000255|PROSITE-ProRule:PRU00881}.; FUNCTION: Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid composed of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C-terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity). {ECO:0000250}.; FUNCTION: Structural peptide 1 is a small peptide derived from the C-terminus of pre-VP2. It destabilizes and perforates cell membranes, suggesting a role during viral entry (By similarity). {ECO:0000250}.; FUNCTION: Structural peptide 2 is a small peptide derived from the C-terminus of pre-VP2. It is not essential for virus viability, but viral growth is affected when this protein is absent (By similarity). {ECO:0000250}.; FUNCTION: Structural peptide 3 is a small peptide derived from pre-VP2 C-terminus. It is not essential for virus viability, but viral growth is affected when this protein is absent (By similarity). {ECO:0000250}.
|
Infectious pancreatic necrosis virus (strain Jasper) (IPNV)
|
P05852
|
TSAD_ECOLI
|
MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATADLGVSVRPRWPLAELPAA
|
2.3.1.234
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
|
maintenance of translational fidelity [GO:1990145]; tRNA threonylcarbamoyladenosine modification [GO:0002949]
|
cytosol [GO:0005829]; EKC/KEOPS complex [GO:0000408]
|
glycosylation-dependent protein binding [GO:0140032]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; magnesium ion binding [GO:0000287]; N(6)-L-threonylcarbamoyladenine synthase activity [GO:0061711]
|
PF00814;
|
3.30.420.40;
|
KAE1 / TsaD family
|
PTM: Can be proteolytically processed in vitro by TsaB. {ECO:0000269|PubMed:19376873}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445, ECO:0000269|PubMed:19376873}.
|
CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_01445, ECO:0000269|PubMed:22378793};
| null | null | null | null |
FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. May also be involved in the metabolism of glycated proteins, but does not show sialoglycoprotease activity against glycophorin A. {ECO:0000269|PubMed:20824107, ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:22378793}.
|
Escherichia coli (strain K12)
|
P05854
|
NEF_HV1H3
|
MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWRYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate HXB3) (HIV-1)
|
P05855
|
NEF_HV1B8
|
MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIHHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPEKEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHMARELHPEYFKNC
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate BH8) (HIV-1)
|
P05856
|
NEF_HV1MN
|
MGGKWSKRVTGWPTVRERMRRAEPAELAADGVGAASRDLEKHGALTSSNTAATNADCAWLEAQEEEEVGFPVKPQVPLRPMTYKAALDLSHFLKEKGGLDGLIYSQKRQDILDLWVYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKIEEANKGENNCLLHPMSQHGMDDPEREVLVWKSDSHLAFQHYARELHPEYYKNC
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
|
P05857
|
NEF_HV1SC
|
MGGKWSKRSVVGWPTVRERMRKTEPAADGVGAASRDLEKHGAITSSNTPANNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAAVDLSHFLKEQGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLCFGWCFKLVPVKPEKIEEANEGENNSLLHPMSLHGMEDPEREVLEWRFDNRLAFHHMARDLHPEYYKDCLTSMCLQGTFRWGISREARLGGTGEWRALRCCI
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1)
|
P05858
|
NEF_HV1RH
|
MGGKWSKSKMGGWPAVRERMQKAEPAADGVGAASRDLEKHGTITSSNTAANNAACTWLEAQEDEDEEVGFPVRPQVPLRPMTFKAAVDLSHFLKEKGGLDGLVFSQKRQDILDLWVYHTQGYFPDWQNYTPGPGTRYPLTFGWCFKLVPVEPDKVEEATEGENNSLLHPICLHGMDDPEKEVLVWKFDSRLAFHHVAREKHPEYYKDC
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1)
|
P05859
|
NEF_HV1ZH
|
MGNKWSKGWPAVRERIRQTPPAPPAAEGVGAASQDLAKHGAISSSNTATNNPDCAWLEAQEESEEVGFPVRPQVPLRPMTFKGAFDLSFFLKEKGGLDGLIYSKKRQEILDLWVYHTQGFFPDWHNYTPGPGTRYPLCFGWCFKLVPVDPREVEEANTGENNCLLHPMSQHGMDDDEREVLMWKFDSSLARKHLAREMHPEFYKD
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype A (isolate Z321) (HIV-1)
|
P05877
|
ENV_HV1MN
|
MRVKGIRRNYQHWWGWGTMLLGLLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATQACVPTDPNPQEVELVNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNTTNTNNSTANNNSNSEGTIKGGEMKNCSFNITTSIRDKMQKEYALLYKLDIVSIDNDSTSYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAILKCNDKKFSGKGSCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVHLNESVQINCTRPNYNKRKRIHIGPGRAFYTTKNIIGTIRQAHCNISRAKWNDTLRQIVSKLKEQFKNKTIVFNQSSGGDPEIVMHSFNCGGEFFYCNTSPLFNSTWNGNNTWNNTTGSNNNITLQCKIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGKDTDTNDTEIFRPGGGDMRDNWRSELYKYKVVTIEPLGVAPTKAKRRVVQREKRAAIGALFLGFLGAAGSTMGAASVTLTVQARLLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLLGFWGCSGKLICTTTVPWNASWSNKSLDDIWNNMTWMQWEREIDNYTSLIYSLLEKSQTQQEKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSLQTRPPVPRGPDRPEGIEEEGGERDRDTSGRLVHGFLAIIWVDLRSLFLFSYHHRDLLLIAARIVELLGRRGWEVLKYWWNLLQYWSQELKSSAVSLLNATAIAVAEGTDRVIEVLQRAGRAILHIPTRIRQGLERALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
|
P05878
|
ENV_HV1SC
|
MRVKGSGRNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNIWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNLRNDTSTNATNTTSSNRGKMEGGEMTNCSFNITTSIRSKVQKEYALFYKLDVVPIDNTSYTLINCNTSVITQACPKVSFEPIPIHYCARWFAILNCNNKKFNGTGPCTNVSTVQCTHGIRPVVSTHLLLNGSLAEEEVVLRSENFTDNAKTIIVQLKEAVEINCTRPNNNTTRSIHIGPGRAFYATGDIIGDIRQAHCNISRAKWNNTLKQIVIKLRDQFENKTIIFNRSSGGDPEIVMHSFNCGGEFFYCNSTQLFSSTWNGTEGSNNTGGNDTITLPCRIKEIINMWQEVGKAMYAPPIKGQVKCSSNITGLLLTRDGGNSKNGSKNENTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGATSMTLTVQARLLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNTSWSNKSLDKIWGNMTWMEWEREIDNYTSLIYTLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRLPSQRGPDRPEGIEEEGGERDRDRSGRLVDGFLAIIWVDXRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELRNSAVSFVNATAIAVAEGTDRVIELLQRAFRAILHIPTRIRQGLERALQ
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1)
|
P05879
|
ENV_HV1C4
|
MAMRAKGIRKNCQHLWRWGTMLLGMLMICSAAANLWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTNPNPQEVVLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLNTNNTTNTTELSIIVVWEQRGKGEMRNCSFNITTSIRDKVQREYALFYKLDVEPIDDNKNTTNNTKYRLINCNTSVITQACPKVSFEPIPIHYCTPTGFALLKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTNNAKTIIVQLNVSVEINCTRPNNHTRKRVTLGPGRVWYTTGEILGNIRQAHCNISRAQWNNTLQQIATTLREQFGNKTIAFNQSSGGDPEIVMHSFNCGGEFFYCNSTQLFNSAWNVTSNGTWSVTRKQKDTGDIITLPCRIKQIINRWQVVGKAMYALPIKGLIRCSSNITGLLLTRDGGGENQTTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGMLGAMFLGFLGAAGSTMGATSMALTVQARQLLSGIVQQQNNLLRAIKAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGFWGCSGKLICTTAVPWNASWSNKTLDQIWNNMTWMEWDREIDNYTHLIYTLIEESQNQQEKNQQELLQLDKWASLWTWSDITKWLWYIKIFIMIVGGLIGLRIVFAVLSIVNRVRQGYSPLSFQTLLPNPRGPDRPEGTEEGGGERGRDGSTRLVHGFLALVWDDLRSLCLFSYHRLRDLLLIVARIVELLGRRGWEVLKYWWNLLQYWSQELKNSAVSLVNVTAIAVAEGTDRVIEVVQRIYRAFLHIPRRIRQGFERALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1)
|
P05880
|
ENV_HV1W2
|
MRVKGIMRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTTLFCASDAKAYSTEAHNVWATHACVPTDPNPQEVILGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWKNTTIIGGGEVKNCSFNITTSRRDKVHKEYALFYKLDVVPIKGDNNSSRYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPYNNVRRSLSIGPGRAFRTREIIGIIRQAHCNISRAKWNNTLKQIVEKLREQFKNKTIVFNHSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWNGTDIKGDNKNSTLITLPCRIKQIINMWQGVGKAMYAPPIQGQIRCSSNITGLLLTRDGGNSSSREEIFRPGGGNMRDNWRSELYKYKVVRIEPLGVAPTKAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGAGSLTLTVQARQLLSGIVQQQNNLLRAIDAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNASWSNKSMNQIWDNLTWMEWEREIDNYTSIIYSLIEESQNQQGKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLIGLRIVFTVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSVRLVHGFLALIWDDLRSLCLFSYHRLRDLLLIVKRIVELLGRRGWEALKYWWNLLQYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRICRAIIHIPRRIRQGLERALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22) (HIV-1)
|
P05881
|
ENV_HV1ZH
|
MKVKGIQGNWQNWWKWGTLILGLVIICSAAENLWVTVYYGVPVWKDAETTLFCASDAKAYDTEKHNVWATHACVPTDPNPQELSLGNVTEKFDMWKNNMVEQMHEDVISLWDQSLKPCVKLTPLCVTLSCHNITIKDNNTNVDTEMKEEIKNCSYNMTTELRDKQRKIYSLFYRLDIVPIGGNSSNGDSSKYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDEEFEGKGPCRNVSTVQCTHGIRPVVSTQLLLNGSLAEGEVRIRSENFTDNAKIIIVQLVKPVNITCMRPNNNTRKSISIGPGRAFFATGDIIGDIRQAHCNVSRTEWNDTLSKVAAQLRKHFVNTSTDIIFANSSGGDVEITTHSFNCGGEFFYCNTSGLFNGTWLNGTSNNTWKIDTVNDTIILPCRIKQIVNMWQRVGQAMYAPPIKGVIKCVSNITGILLTRDGVGNNTSNETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVAREKRAIGMGAFFLGFLGAAGSTMGAASITLTVQARRLLSGIVQQQNNLLRAIEAQQHLLKLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKIICPTNVPWNSSWSNKSQSDIWDKMTWLEWDKEVSNYTQVIYNLIEESQTQQEINERDLLALDKWANLWNWFDISNWLWYIKIFIMIVGGLIGLRIVFAVLSIINRVRQGYSPLSFQTLTHHQREPDRPERIEEGGGEQDRDRSIRLVSGFLPLAWDDLRSLCLFCYHRLRDCALIAARIVETLIRRGWETLKYLGNLVIYWGQELKNSAINLLDTVAIAVADWTDRVIEVVQRAGRAFLNIPRRIRQGLERALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype A (isolate Z321) (HIV-1)
|
P05882
|
ENV_HV1Z8
|
MRVMGIRMNYQHLWKWGIMLLGILMTCSVAEDLWVTVYYGVPVWKEATTTLFCASDAKSYEPEAHNIWATHACVPTDPNPREIEMENVTENFNMWKNNMVEQMHEDIISLWDQNLKPCVKLTPLCVTLNCTNAGGNKTTNGNNTTNQEEQMMEKGEMKNCSFNITTVISDKKKQVHALFYRLDVVPIDDDNSANTSNTNYTNYRLINCNTSAITQACPKVTFEPIPIHYCAPAGFAILKCKDKKFNGTGPCKKVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNVKTIIVHLNESVEINCTRPDNKITRQSTPIGLGQALYTTRIKGDIRQAYCNISAAAWNKTLQQVAKKLGDLLNQTTIIFKPPAGGDPEITTHSFNCGGEFFYCNTSRLFNSTWNSSTWNNDTLNSEGTIKLPCRIKQIINMWQGVGKAMYAPPIEGLIKCTSNITGLLLTRDGGVNNSTNETFRPGGGDMKDNWRNELYKYKVVRIEPLGIAPTRAKRRVVEREKRAIGLGAVFLGFLGAAGSTMGAVSVALTGQARQLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVESYLKDQQLLGIWGCSGKHICTTTVPWNSSWSNKSLEEIWNNMTWIEWEREIDNYTGVIYSLIENSQIQQEKNEQDLLQLDKWASLWNWFSITKWLWYIKIFIMIVGGLIGLRIVFTVLSLVNRVRQGYSPLSFQTLLPAPRGPDRPEGIEEEGGEQGRDRSIRLVNGFSALFWDDLRNLCLFSYHRLRDLILIATRIVELLGRRGWEAIKYLWSLLQYWTQELKNSFISLLNATAIAVAEGTDRIIELIRRAFRAVLHIPRRVRQGLERALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype D (isolate Z84) (HIV-1)
|
P05883
|
ENV_HV2NZ
|
MKGSKNQLLIAIVLASAYLIHCKQFVTVFYGIPAWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWNNTVTEQAVEDVWNLFETSIKPCVKLTPLCVAMNCTRNMTTWTGRTDTQNITIINDTSHARADNCTGLKEEEMIDCQFSMTGLERDKRKQYTEAWYSKDVVCDNNTSSQSKCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFAPNCSKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNNFYNLTMHCKRPGNKTVLPITFMSGFKFHSQPVINKKPRQAWCWFEGQWKEAMQEVKETLAKHPRYKGNRSRTENIKFKAPGRGSDPEVTYMWTNCRGESLYCNMTWFLNWVENRTGQKQRNYAPCRIRQIINTWHRVGKNLYLPPREGELTCNSTVTSIIANIDAGDQTNITFSAEAAELYRLELGDYKLVEITPIGFAPTSVKRYSSAHQRHTRGVFVLGFLGFLATAGSAMGAASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTSVPWVNDTLTPDWNNMTWQEWEQKVRYLEANISQSLEQAQIQQEKNMYELQKLNSWDVFTNWLDFTSWVRYIQYGVYVVVGIVALRIVIYIVQMLSRLRKGYRPVFSSPPGYIQQIHIHKDQEQPAREETEEDVGSNGGDRSWPWPIAYIHFLIRLLIRLLTGLYNICRDLLSRISPILQPIFQSLQRALTAIRDWLRLKAAYLQYGCEWIQEAFQALARTTRETLAGAGRDLWRALQRIGRGILAVPRRIRQGAELALL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.; FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. {ECO:0000250}.; FUNCTION: The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus-infected cells, on the point of undergoing apoptosis, fuse with CD4-expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion (By similarity). {ECO:0000250}.; FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). {ECO:0000250}.
|
Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2)
|
P05884
|
ENV_SIVMK
|
MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPLTDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASFRLTAQSRTLLAGIVQQQQQLLGVVKRQQELLRLTVWGTKNLQTRVTAIEKYLEDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRIREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWGDLWETLRRGGRWILAIPRRIRQGLELTLL
| null | null |
membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS (By similarity). {ECO:0000250}.; FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. SIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of SIV-specific CD4+ cells (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.; FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. {ECO:0000250}.; FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). {ECO:0000250}.
|
Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
|
P05885
|
ENV_SIVM1
|
MGCLGNQLLIAILLLSVYGIYCIQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNDDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDKWGLTKSSTTTASTTTTTTAKSVETRDIVNETSPCVVHDNCTGLEQEPMISCKFNMTGLKRDKKKEYNETWYSADLVCEQGNSTGNESRCYMNHCNTSVIQECCDKDYWDAIRCRYCAPPGYALLRCNDTNYSGFMPNCSKVVVSSCTRMMETQTSTWFRFNGTRAENRTYIYWHGRDNRTIISLNKHYNLTMKCRRPGNKTVLPVTIMSALVFHSQPVNERPKQAWCRFGGNWKEAIKEVKQTIVKHPRYTGTNNTDKINLTAPRGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRSLTTQKPKERHKRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANINWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTNVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTVTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVSAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNETWQEWERKVDFLEANITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGIYIIVGVILLRIVIYIVQMLARLRQGYRPVFSSPPSYFQXTHTQQDPALPTKEGKKGDGGGSGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPIFQRLSATLRRIREVLRLELTYLQYGWSYFQEAVQAAQRSATETLAGAWGELWEALQRGGRWILAIPRRIRQGLELTLL
| null | null |
membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS (By similarity). {ECO:0000250}.; FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. SIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of SIV-specific CD4+ cells (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.; FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. {ECO:0000250}.; FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). {ECO:0000250}.
|
Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
|
P05886
|
ENV_SIVVT
|
MRYTIITLGIIVIGIGIVLSKQWITVFYGIPVWKNSSVQAFCMTPTTSLWATTNCIPDDHDYTEVPLNITEPFEAWGDRNPLIAQAASNIHLLFEQTMKPCVKLSPLCIKMNCVELNSTRERATTPTTTPKSTGLPCVGPTSGENLQSCNASIIEREMEDEPASNCTFAMAGYVRDQKKNYYSVVWNDAEIYCKNKTNSTSKECYMIHCNDSVIKEACDKTYWDQLRLRYCAPAGYALLKCNDEDYNGYKQNCSNVSVVHCTGLMNTTVTTGLLLNGSYHENRTQIWQKHRVNNNTVLILFNKHYNLSVTCRRPGNKTVLPVTIMAGLVFHSQKYNMKLRQAWCHFEGNWRGAWREVKQKIVELPKDRYKGTNNTEHIYLQRQWGDPEASNLWFNCQGEFFYCKMDWFLNYLNNKTWDAYHNFCSSKKKGHAPGPCVQRTYVAYHIRSVINDSYTLSKKTYAPPREGHLQCRSTVTGMTVELNYNSKNRTNVTLSPQIESIWAAELGRYKLVEITPIGFAPTEVRRYTGGHERQKRVPFVLGFLGFLGAAGTAMGAAASSLTVQSRHLLAGILQQQKNLLAAVEAQQQMLKLTIWGVKNLNARVTALEKYLEDQARLNSWGCAWKQVCHTTVEWPWTNRTPDWQNMTWLEWERQIADLESNITGQLVKAREQEEKNLDAYQKLTSWSDFWSWFDFSKWLNILKMGFLVIVGIIGLRLLYTVYGCIVRVRQGYVPLSPQIHIHQVGKGRPDNADEPGEGGDNSRIKLESWXKDSKSRCMQLTAWLTRLNTWLYNSCLTLLIQLRKAFQYLQYGLAELKTGAQEILQTLAGVAQNACHQIWLACRSAYRNIVNSPRRVRQGLEEILN
| null | null |
membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS (By similarity). {ECO:0000250}.; FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. SIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of SIV-specific CD4+ cells (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.; FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. {ECO:0000250}.; FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). {ECO:0000250}.
|
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
|
P05887
|
GAG_HV1C4
|
MGARASVLSGGELDRWEKIRLRPGGKKQYRLKHIVWASRKLERFAVNPGLLETSKGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFAALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPTPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRRQGKTVKCFNCGKEGHIARNCKAPRKKGCWKCGREGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGDETTTPSQKQEPRDKELYPLASLRSLFGNDPSSQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF19317;PF08705;PF00098;
|
1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
| null | null | null | null | null |
FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1)
|
P05888
|
GAG_HV1MN
|
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHVVWASRELERFAINPGLLETSEGCRQILGQLQPSLQTGSEERKSLYNTVATLYCVHQKIKIKDTKEALEKIEEEQNKSKKKAQQAAADTGNRGNSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPAHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIIKCFNCGKEGHIAKNCRAPRKRGCWKCGKEGHQMKDCTERQANFLGKIWPSCKGRPGNFPQSRTEPTAPPEESFRFGEETTTPYQKQEKKQETIDKDLYPLASLKSLFGNDPLSQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
sequence-specific DNA binding [GO:0043565]; structural molecule activity [GO:0005198]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF08705;PF00098;
|
1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
| null | null | null | null | null |
FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
|
P05889
|
GAG_HV1W2
|
MGARASVLSGGELDKWEKIRLRPGGKKKYRLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEKKDTKEALDKIEEEQNKCKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQATQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPTTIMMQKGNFRNQRKT
| null | null |
viral process [GO:0016032]
|
host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF00540;PF00607;PF19317;
|
1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;
|
Primate lentivirus group gag polyprotein family
|
PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
| null | null | null | null | null |
FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22) (HIV-1)
|
P05890
|
GAG_HV1RH
|
MGARASVLSGGKLDKWEKIRLRPRGKKRYKLKHIVWASRELERFAVNPSLLETAEGCRQILGQLQPALQTGSEELKSLYNAVATLYCVHQNIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNGSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTETFLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPSHKARILAEAMSQVTNSATIMLQKGNFRDQRKIVKCFNCGKVGHIAKNCRAPRKKGCWKCGKEGHQMKDCTNEGRQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTPSQKQEKIDKELYPLASLKSLFGNDPSSQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF08705;PF00098;
|
1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
| null | null | null | null | null |
FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1)
|
P05891
|
GAG_HV2NZ
|
MGARNSVLRGKKADELEKIRLRPGGKKKYKLKHIVWAANELDRFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVQRHLVAETGTAEKMPNTSRPTAPPSGKNFPVQQVAGNYTHIPLSPGTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVAHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDINQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTTCQGVGGPGQKARLMAEALKEVMAPAPIPFAAAQQRKTFKCWNCGKEGHSARQWSAPRRQGCWKCGKSGHVMANCPDRQAGFLGIGHWGKKARNFPAAQVPQGLTPTAPPLDPAVDLLEKYMQQGKRQREQRERPYKEVTEDLLRFEQAETPCRETTEDLLHLNSLFGKDQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF00098;
|
1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
| null | null | null | null | null |
FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (By similarity). Most core are conical, with only 7% tubular (By similarity). The core is constituted by capsid protein hexamer subunits (By similarity). The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription (By similarity). Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). The capsid interacts with high affinity with human NONO, promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493, ECO:0000250|UniProtKB:P18095}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
|
Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2)
|
P05892
|
GAG_SIVVT
|
MGAATSALNRRQLDQFEKIRLRPNGKKKYQIKHLIWAGKEMERFGLHERLLETEEGCKRIIEVLYPLEPTGSEGLKSLFNLVCVLYCLHKEQKVKDTEEAVATVRQHCHLVEKEKSATETSSGQKKNDKGIAAPPGCSQNFPAQQQGNAWVHVPLSPRTLNAWVKAVEEKKFGAEIVPMFQALSEGCTPYDINQMLNVLGDHQGALQIVKEIINEEAAQWDVTHPLPAGPLPAGQLRDPRGSDIAGTTSSVQEQLEWIYTANPRVDVGAIYRRWIILGLQKCVKMYNPVSVLDIRQGPKEPFKDYVDRFYKAIRAEQASGEVKQWMTESLLIQNANPDCKVILKGLGMHPTLEEMLTACQGVGGPSYKAKVMAEMMQTMQNQNMVQQGGPKRQRPPLRCYNCGKFGHMQRQCPEPRKTKCLKCGKLGHLAKDCRGQVNFLGYGRWMGAKPRNFPAATLGAEPSAPPPPSGTTPYDPAKKLLQQYAEKGKQLREQKRNPPAMNPDWTEGYSLNSLFGEDQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral nucleocapsid [GO:0019013]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF00098;
|
1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). {ECO:0000250}.; FUNCTION: p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250}.
|
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
|
P05893
|
GAG_SIVMK
|
MGARNAVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTAETMPKTSRPTAPSSGRGGNYPVQQIGGNYVHLPLSPRTLNAWVKLIEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQPAPQQGQLREPSGSDIAGTTSSVDEQIQWMYRQQNPIPVGNIYRRWIQLRLQKCVRMYNPINILDVKQRPKEPFQSYVDRFYKSLRAEQTDAAVKNWMTQTLLIQNANPDCKLVLKGLGVNPTLEEMLTACQGVGGPGQKARLMAEALKEALRPVPTPFAAAQQRGPRKPIKCWNCGKEGHSARQCRAPRRQRCWKCGKMDHVMAKCPDRQAGFLGLGPWGKKPRNFPMAQVHQGLTPTAPPEDPAVDLLKNYMQLGKQQRESREKPYKEVTEDLLHLNSLFGGDQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF00098;
|
1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). {ECO:0000250}.; FUNCTION: p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250}.
|
Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
|
P05894
|
GAG_SIVM1
|
MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGTNPTLEEMLTACQGVGGPGQKARLMAEALKEALAPAPIPFAAAQQKGPRKPIKCWNCGKEGHSARQCRAPRRQGCWKCGKMDHVMAKCPNRQAGFLGLGPWGKKPRNFPMAQVHQGLTPTAPPEEPAVDLLKNYMHLGKQQRESRGKPYKEVTEDLLHLNSLFGGDQ
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF00098;
|
1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
|
Primate lentivirus group gag polyprotein family
|
PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). {ECO:0000250}.; FUNCTION: p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250}.
|
Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
|
P05895
|
POL_SIVVT
|
MGAATSALNRRQLDKFEHIRLRPTGKKKYQIKHLIWAGKEMERFGLHERLLESEEGCKKIIEVLYPLEPTGSEGLKSLFNLVCVLFCVHKDKEVKDTEEAVAIVRQCCHLVEKERNAERNTTETSSGQKKNDKGVTVPPGGSQNFPAQQQGNAWIHVPLSPRTLNAWVKAVEEKKFGAEIVPMFQALSEGCTPYDINQMLNVLGDHQGALQIVKEIINEEAAQWDIAHPPPAGPLPAGQLRDPRGSDIAGTTSTVQEQLEWIYTANPRVDVGAIYRRWIILGLQKCVKMYNPVSVLDIRQGPKEAFKDYVDRFYKAIRAEQASGEVKQWMTESLLIQNANPDCKVILKGLGMHPTLEEMLTACQGVGGPSYKAKVMAEMMQNMQSQNMMQQGGQRGRPRPPVKCYNCGKFGHMQRQCPEPRKMRCLKCGKPGHLAKDCRGQVNFFRVWTVDGGKTEKFSRRYSWSGTECASSTERHHPIRPSKEAPAAICRERETTEGAKEESTGNESGLDRGIFFELPLWRRPIKTVYIEGVPIKALLDTGADDTIIKENDLQLSGPWRPKIIGGIGGGLNVKEYNDREVKIEDKILRGTILLGATPINIIGRNLLAPAVPRLVMGQLSEKIPVTPVKLKEGARGPCVRQWPLSKEKIEALQEICSQLEQEGKISRVGGENAYNTPIFCIKKKDKSQWRMLVDFRELNKATQDFFEVQLGIPHPAGLRKMRQITVLDVGDAYYSIPLDPNFRKYTAFTIPTVNNQGPGIRYQFNCLPQGWKGSPTIFQNTAASILEEIKRNLPALTIVQYMDDLWVGSQENEHTHDKLVEQLRTKLQAWGLETPEKKMQKEPPYEWMGYKLWPHKWELSRIQLEEKDEWTVNDIQKLVGKLNWAAQLYPGLKTRICKLITGGKKNLLELVAWTPEAEAEYAENAEILKTEQEGTYYKPGIPIRAAVQKLEGGQWSYQFKQEGQVLKVGKYTKQKNTHTNELRTLAGLVQKICKEALVIWGILPVLELPIEREVWEQWWADYWQVSWIPEWDFVSTPPLLKLWYTLTKEPIPKEDVYYVGACNRNSKEGKAGYISQYGKQRVETLENTTNQQAKLTAIKMALEDSGPNVNIVTDSQYAMGILTAQPTQSDSPLVEQIIALMIQKQQIYLQWVPAHKGIGGNEEIDKLVSKGIRRVLFLEKIEEAQEKHERYHNNWKNLADTYGLPQIVAKEIVAMCPKCQIKGEPVHGQVDASPGTWQMDCTHLEKKVVIVAVHVASGFIEAEVIPRETGKETAKFLLKILSRWPITQLHTDNGPNFTSQEVAAICWWGKIEHTTGIPYNPQSQGSIESMNKQLKEIIGKIRDDCQYTEAAVLMACILHNFKRKGGIGGQTSAERLINIITTQLEIQHLQTKIQKILNFRVYYREGRDPVWKGPAQLIWKGEGAVVLKDGSDLKVVPRRKAKIIKDYEPKQRVGNEGDVEGTRGSDN
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2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16
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COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
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DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
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host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]
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aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098;
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1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: Capsid protein p24 is phosphorylated.
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SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
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CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:0000250}.; FUNCTION: Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristointegration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity). {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity). {ECO:0000250}.; FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity). {ECO:0000250}.
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Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
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P05896
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POL_SIVM1
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MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGTNPTLEEMLTACQGVGGPGQKARLMAEALKEALAPAPIPFAAAQQKGPRKPIKCWNCGKEGHSARQCRAPRRQGCWKCGKMDHVMAKCPNRQAGFFRPWPLGKEAPQFPHGSSASGADANCSPRRTSCGSAKELHALGQAAERKQREALQGGDRGFAAPQFSLWRRPVVTAHIEGQPVEVLLDTGADDSIVTGIELGPHYTPKIVGGIGGFINTKEYKNVEIEVLGKRIKGTIMTGDTPINIFGRNLLTALGMSLNLPIAKVEPVKSPLKPGKDGPKLKQWPLSKEKIVALREICEKMEKDGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNRVTQDFTEVQLGIPHPAGLAKRKRITVLDIGDAYFSIPLDEEFRQYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQYTMRHVLEPFRKANPDVTLVQYMDDILIASDRTDLEHDRVVLQLKELLNSIGFSSPEEKFQKDPPFQWMGYELWPTKWKLQKIELPQRETWTVNDIQKLVGVLNWAAQIYPGIKTKHLCRLIRGKMTLTEEVQWTEMAEAEYEENKIILSQEQEGCYYQESKPLEATVIKSQDNQWSYKIHQEDKILKVGKFAKIKNTHTNGVRLLAHVIQKIGKEAIVIWGQVPKFHLPVEKDVWEQWWTDYWQVTWIPEWDFISTPPLVRLVFNLVKDPIEGEETYYVDGSCSKQSKEGKAGYITDRGKDKVKVLEQTTNQQAELEAFLMALTDSGPKANIIVDSQYVMGIITGCPTESESRLVNQIIEEMIKKTEIYVAWVPAHKGIGGNQEIDHLVSQGIRQVLFLEKIEPAQEEHSKYHSNIKELVFKFGLPRLVAKQIVDTCDKCHQKGEAIHGQVNSDLGTWQMDCTHLEGKIVIVAVHVASGFIEAEVIPQETGRQTALFLLKLASRWPITHLHTDNGANFASQEVKMVAWWAGIEHTFGVPYNPQSQGVVEAMNHHLKNQIDRIREQANSVETIVLMAVHCMNFKRRGGIGDMTPAERLINMITTEQEIQFQQSKNSKFKNFRVYYREGRDQLWKGPGELLWKGEGAVILKVGTDIKVVPRRKAKIIKDYGGGKEMDSSSHMEDTGEAREVA
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2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16
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COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
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DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
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host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]
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aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098;
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1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: Capsid protein p24 is phosphorylated.
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SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
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CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:0000250}.; FUNCTION: Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristointegration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity). {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity). {ECO:0000250}.; FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity). {ECO:0000250}.
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Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
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P05897
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POL_SIVMK
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MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTAETMPKTSRPTAPSSGRGGNYPVQQIGGNYVHLPLSPRTLNAWVKLIEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQPAPQQGQLREPSGSDIAGTTSSVDEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDAAVKNWMTQTLLIQNANPDCKLVLKGLGVNPTLEEMLTACQGVGGPGQKARLMAEALKEALAPVPIPFAAAQKRGPRKPIKCWNCGKEGHSARQCRAPRRQGCWKCGKMDHVMAKCPDRQAGFFRPWSMGKEAPQFPHGSSASGADANCSPRGPSCGSAKELHAVGQAAERKQREALQGGDRGFAAPQFSLWRRPVVTAHIEGQPVEVLLDTGADDSIVTGIELGPHYTPKIVGGIGGFINTKEYKNVEIEVLGKRIKRTIMTGDTPINIFGRNLLTALGMSLNLPIAKVEPVKVALKPGKVGPKLKQWPLSKEKIVALREICEKMEKDGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIHFRELNRVTQELYRSPIRIPHPAGLAKRKRITVLDIGDAYFSIPLDEEFRQYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQYTMRHVLEPFRKANPDVTLVQYMDDILIASDRTDLEHDRVVLQLKELLNSIGFSTPEEKFQKDPPFQWMGYELWPTKWKLQKIELPQRETWTVNDIQKLVGVLNWAAQIYPGIKTKHLCRLIRGKMTLTEAVQWTEMAEAEYEENNIILSQEQEGCYYQEGKPLEATVIKSQDNQWTYKIHQEDKILKVRKFAKIKNTHTNGVRLLAHVIQKIGKEAIVIVGQVPKFHLPVERDVWEQWWTDYWQVTWIPEWDFISTPPLVRLVFNLVKDPIEVEETYYTDGSCNKQSKEGKAGYITDRGKDIVKVLTTTNQQAELEAIYHGIEDSGPKRNIIVELQVCYGNNNRFPTESESRLVNQIIEEMIKVRVYVAWVPALEGIGGNQEIGPLVSQGFRQVLFLEKIEPAQEEHDKYHSNVKELVFKFGLPRIVARQIVDTCDKCHQKGEAIHGQVNSDLGTWQMDCTHLEGKIVIVAVHVASGFIEAEVIPQETGRQHYFLLKLAGRWPYLHIYTHSNGANFASQEVKMVTWWAGIEAHLWVPYNPQSQGVVEAMNHHLKNQIDRIREQANSVETIVLMAVHCMNFKRRGGIGDMTPAERLINMITTEQEIQFQQSKNSKFKNFRVYYREGRDQLWKGPGELLWKGEGAVILKVGTDIKVVPRRKAKIIKDYGGGKEVDSSSHMEDTGEAREVA
|
2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16
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COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
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DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
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host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]
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aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00077;PF00078;PF06815;PF06817;PF00098;
|
1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: Capsid protein p24 is phosphorylated.
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SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
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CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:0000250}.; FUNCTION: Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristointegration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity). {ECO:0000250}.; FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity). {ECO:0000250}.; FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity). {ECO:0000250}.
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Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey)
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P05905
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TAT_HV1MN
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MEPVDPRLEPWKHPGSQPKTACTTCYCKKCCFHCQVCFTKKALGISYGRKKRRQRRRAPEDSQTHQVSLPKQPAPQFRGDPTGPKESKKKVERETETHPVD
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
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extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
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actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
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PF00539;
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4.10.20.10;
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Lentiviruses Tat family
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PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
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SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
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Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
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P05906
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TAT_HV1SC
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MDPVDPRLEPWKHPGSQPKAACTSCYCKKCCFHCQVCFTTKGLGISYGRKKRRQRRRAPQDSQTHQVSLPKQPASQARGDPTGPKESKKKVERETETDPVD
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
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extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
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actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
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PF00539;
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4.10.20.10;
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Lentiviruses Tat family
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PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
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SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
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Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1)
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P05907
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TAT_HV1C4
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MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFTKKALGISYGRKKRRQRRRAHQDSQNHQASLSKQPSSQTRGDPTGPKEPKKEVEREAETDPLD
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
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extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
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actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
|
PF00539;
|
4.10.20.10;
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Lentiviruses Tat family
|
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1)
|
P05908
|
TAT_HV1RH
|
MEPVDPRLEPWKHPGSQPKTACNNCYCKKCCYHCQVCFLTKGLGISYGRKKRRQRRGPPQGSQTHQVSLSKQPTSQPRGDPTGPKESKEKVERETETDPAVQ
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
|
actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
|
PF00539;
|
4.10.20.10;
|
Lentiviruses Tat family
|
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1)
|
P05919
|
VPU_HV1H2
|
MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL
| null | null |
receptor catabolic process [GO:0032801]; suppression by virus of host tetherin activity [GO:0039587]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral release from host cell [GO:0019076]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]
|
CD4 receptor binding [GO:0042609]; monoatomic cation channel activity [GO:0005261]
|
PF00558;
|
1.10.195.10;
|
HIV-1 VPU protein family
|
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4. {ECO:0000255|HAMAP-Rule:MF_04082}.
|
SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:8331740}.
| null | null | null | null | null |
FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack. {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:11696595, ECO:0000269|PubMed:19730691, ECO:0000269|PubMed:19837671, ECO:0000269|PubMed:24498878, ECO:0000269|PubMed:24843023, ECO:0000269|PubMed:32690953, ECO:0000269|PubMed:8794357}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
|
P05923
|
VPU_HV1BR
|
MQPIQIAIAALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDIDDL
| null | null |
receptor catabolic process [GO:0032801]; suppression by virus of host tetherin activity [GO:0039587]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral release from host cell [GO:0019076]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]
|
CD4 receptor binding [GO:0042609]; monoatomic cation channel activity [GO:0005261]
|
PF00558;
|
1.10.195.10;
|
HIV-1 VPU protein family
|
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4. {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:1541298}.
|
SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082}.
| null | null | null | null | null |
FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack. {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:11696595, ECO:0000269|PubMed:11847278, ECO:0000269|PubMed:14657387, ECO:0000269|PubMed:16571793, ECO:0000269|PubMed:16699598, ECO:0000269|PubMed:18200009, ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19286137, ECO:0000269|PubMed:19515779, ECO:0000269|PubMed:8946945}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
|
P05928
|
VPR_HV1BR
|
MEQAPEDQGPQREPHNEWTLELLEELKNEAVRHFPRIWLHGLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTQQRRARNGASRS
| null | null |
cell cycle [GO:0007049]; DNA-templated transcription [GO:0006351]; monoatomic ion transmembrane transport [GO:0034220]; protein homooligomerization [GO:0051260]; regulation of DNA-templated transcription [GO:0006355]; symbiont entry into host cell [GO:0046718]; symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell nucleus [GO:0042025]; host extracellular space [GO:0043655]; virion component [GO:0044423]
| null |
PF00522;
|
6.10.210.10;1.20.5.90;
|
HIV-1 VPR protein family
|
PTM: Phosphorylated on several residues by host. These phosphorylations regulate VPR activity for the nuclear import of the HIV-1 pre-integration complex. {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:10864665, ECO:0000269|PubMed:11860675}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. {ECO:0000255|HAMAP-Rule:MF_04080}.
| null | null | null | null | null |
FUNCTION: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions. {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:10518572, ECO:0000269|PubMed:10620603, ECO:0000269|PubMed:10708425, ECO:0000269|PubMed:12573582, ECO:0000269|PubMed:12634356, ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17630831, ECO:0000269|PubMed:2136707, ECO:0000269|PubMed:2139896, ECO:0000269|PubMed:7474100, ECO:0000269|PubMed:7666531, ECO:0000269|PubMed:7724608, ECO:0000269|PubMed:8041786, ECO:0000269|PubMed:9525900, ECO:0000269|PubMed:9539783, ECO:0000269|PubMed:9657723}.; FUNCTION: During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells. {ECO:0000255|HAMAP-Rule:MF_04080}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
|
P05933
|
CALM_SCHPO
|
MTTRNLTDEQIAEFREAFSLFDRDQDGNITSNELGVVMRSLGQSPTAAELQDMINEVDADGNGTIDFTEFLTMMARKMKDTDNEEEVREAFKVFDKDGNGYITVEELTHVLTSLGERLSQEEVADMIREADTDGDGVINYEEFSRVISSK
| null | null |
ascospore formation [GO:0030437]; ascospore-type prospore-specific spindle pole body remodeling [GO:0031322]; mitotic spindle assembly [GO:0090307]; protein localization to meiotic spindle pole body [GO:1902441]; spindle pole body organization [GO:0051300]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; central plaque of mitotic spindle pole body [GO:0061493]; central plaque of spindle pole body [GO:0005823]; cytosol [GO:0005829]; division septum [GO:0000935]; growing cell tip [GO:0035838]; mating projection tip [GO:0043332]; meiotic spindle pole body [GO:0035974]; mitotic spindle pole body [GO:0044732]; myosin I complex [GO:0045160]; new growing cell tip [GO:0035841]; old growing cell tip [GO:0035840]
|
calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234]
|
PF13499;
|
1.10.238.10;
|
Calmodulin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9635188}. Note=In the growing tips and spindle pole body during interphase and in the septum during septation. Component of a ring structure that forms prior to septation.
| null | null | null | null | null |
FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P05937
|
CALB1_HUMAN
|
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN
| null | null |
cellular response to organic substance [GO:0071310]; cochlea development [GO:0090102]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; metanephric collecting duct development [GO:0072205]; metanephric connecting tubule development [GO:0072286]; metanephric distal convoluted tubule development [GO:0072221]; metanephric part of ureteric bud development [GO:0035502]; regulation of long-term synaptic potentiation [GO:1900271]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; response to auditory stimulus [GO:0010996]; retina layer formation [GO:0010842]; short-term memory [GO:0007614]
|
axon [GO:0030424]; calyx of Held [GO:0044305]; cuticular plate [GO:0032437]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; stereocilium [GO:0032420]; synapse [GO:0045202]; terminal bouton [GO:0043195]
|
calcium ion binding [GO:0005509]; calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration [GO:0099567]; calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration [GO:0099534]; vitamin D binding [GO:0005499]; zinc ion binding [GO:0008270]
|
PF00036;PF13499;
|
1.10.238.10;
|
Calbindin family
| null | null | null | null | null | null | null |
FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
|
Homo sapiens (Human)
|
P05942
|
S10A4_RAT
|
MARPLEEALDVIVSTFHKYSGNEGDKFKLNKTELKELLTRELPSFLGRRTDEAAFQKLMNNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK
| null | null |
positive regulation of canonical NF-kappaB signal transduction [GO:0043123]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
actin binding [GO:0003779]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; chemoattractant activity [GO:0042056]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; RAGE receptor binding [GO:0050786]; transition metal ion binding [GO:0046914]
|
PF01023;
|
1.10.238.10;
|
S-100 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000250|UniProtKB:P07091}.
| null | null | null | null | null |
FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By similarity). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity). {ECO:0000250|UniProtKB:P07091, ECO:0000250|UniProtKB:P26447}.
|
Rattus norvegicus (Rat)
|
P05943
|
S10AA_RAT
|
MPSQMEHAMETMMLTFHRFAGEKNYLTKEDLRVLMEREFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFLSLVAGLIIACNDYFVVHMKQKK
| null | null |
membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; regulation of cell differentiation [GO:0045595]; regulation of cell growth [GO:0001558]; regulation of neurogenesis [GO:0050767]; response to xenobiotic stimulus [GO:0009410]; vesicle budding from membrane [GO:0006900]
|
AnxA2-p11 complex [GO:1990665]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; RNA polymerase II transcription regulator complex [GO:0090575]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein homodimerization activity [GO:0042803]; transmembrane transporter binding [GO:0044325]
|
PF01023;
|
1.10.238.10;
|
S-100 family
| null | null | null | null | null | null | null |
FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P05959
|
POL_HV1RH
|
MGARASVLSGGKLDKWEKIRLRPRGKKRYKLKHIVWASRELERFAVNPSLLETAEGCRQILGQLQPALQTGSEELKSLYNAVATLYCVHQNIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNGSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTETFLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPSHKARILAEAMSQVTNSATIMLQKGNFRDQRKIVKCFNCGKVGHIAKNCRAPRKKGCWKCGKEGHQMKDCTNEGRQANFLRENLAFPQGKARELSSEQTRANSPTRRELQVWGRDNSLSEAGEDRQGTVSFSFPQITLWQRPIVTVKIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKEFRKYTAFTIPSINNETPRIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPEIVIYQYMDDLYVGSDLEIGQHRIKIEELREHLLKWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYAGIKVKQLCKLLRGTKALTEVVQLTKEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKVATESIVIWGKTPKFKLPIQKETWEAWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIIGAETFYVDGAANRETKLGKAGYVTDRGRQKVVSLTDTTNQKTELQAIHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDRLVSTGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVVESMNKQLKQIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRDPLWKGHAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
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2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16
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COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
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DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
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host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
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aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098;
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1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.; PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
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SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12497}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
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CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. {ECO:0000250}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. {ECO:0000250|UniProtKB:P04585}.
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Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1)
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P05960
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POL_HV1C4
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MGARASVLSGGELDRWEKIRLRPGGKKQYRLKHIVWASRKLERFAVNPGLLETSKGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFAALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPTPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRRQGKTVKCFNCGKEGHIARNCKAPRKKGCWKCGREGHQMKDCTERQANFLREDLAFPQGKAREFSSEQTRANSPTRGELQVWGRDNNSLSEAGAERQGTVSFSFPQITLWQRPIVTIKIGGQLKEALLDTGADDTVLEEINLPGRWKPKMIGGIGGFIKVRQYDEV
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3.4.23.16
| null |
proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032]
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host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
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aspartic-type endopeptidase activity [GO:0004190]; lipid binding [GO:0008289]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF19317;PF00077;PF00098;
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1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10;
| null |
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry (By similarity). {ECO:0000250}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.; PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
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SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12497}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
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CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275};
| null | null | null | null |
FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. {ECO:0000250}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.
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Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1)
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P05961
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POL_HV1MN
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MGARASVLSGGELDRWENIRLRPGGKKKYKLKHVVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELKSLYNTVATLYCVHQKIEIKDTKEALEKIEEEQNKSKKKAQQAAADTGNRGNSSQVSQNYPIVQNIEGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPITPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNRTTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIIKCFNCGKEGHIAKNCRAPRKRGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAEFSSEQNRANSPTRRELQVWGRDNNSLSEAGEEAGDDRQGPVSFSFPQITLWQRPIVTIKIGGQLKEALLDTGADDTVLGEMNLPRRWKPKMIGGIGGFIKVRQYDQITIGICGHKAIGTVLVGPTPVNIIGRNLLTQLGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALIEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKKTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRAKIEELRRHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYAGIKVKQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEVQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKIATESIVIWGKTPKFRLPIQKETWETWWTEYTXATWIPEWEVVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKKGKAGYVTNRGRQKVVSLTDTTNQKTELQAIHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQEDHEKYHSNWRAMASDFNLPPIVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGPNFTSTTVKAACWWTGIKQEFGIPYNPQSQGVIESMNKELKKIIGQVRDQAEHLKRAVQMAVFIHNFKRKGGIGGYSAGERIVGIIATDIQTKELQKQITKIQNFRVYYRDSRDPLWKGPAKLLWKGEGAVVIQDNNDIKVVPRRKAKVIRDYGKQTAGDDCVASRQDED
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2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16
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COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
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DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
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host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
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aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
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PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098;
|
1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.; PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}.
|
SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12497}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. {ECO:0000250}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. {ECO:0000250|UniProtKB:P04585}.
|
Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
|
P05962
|
POL_HV2NZ
|
MGARNSVLRGKKADELEKIRLRPGGKKKYKLKHIVWAANELDRFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVQRHLVAETGTAEKMPNTSRPTAPPSGKNFPVQQVAGNYTHIPLSPGTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVAHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDINQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTTCQGVGGPGQKARLMAEALKEVMAPAPIPFAAAQQRKTFKCWNCGKEGHSARQWSAPRRQGCWKCGKSGHVMANCPDRQAGFLRDWPLGKEGPQLPRGPSPAGANTNSTPIGSSSGPTGEIYAARKKAKGAERETVQGSDRGLTAFRAGRDTMQGDDRGLAAPQFSLWKRPVVTAHIEGQPVEVLLDTRANDSIVAGIELGSNYSPKIVGGIGGFINTKEYKNVEIEVLGKRVKATIMTGDTPINIFGRNVLTALGMSLNLPVAKIEPIKIMLKPGKDGPRLKQWPLTKEKIEALKEICEKMEKEGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNKVTQDFTEIQLGIPHPAGLAKKRRITVLDVGDAYFSIPLHEDFRQYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQYTMRQILEPFRKANEDVIIIQYMDDILIASDRTDLEHDKVVLQLKELLNGLGFSTPDEKFQKDPPYRWMGYELWPTKWKLQKIQLPQKEVWTVNDIQKLVGVLNWAAQIYPGIKTKHLCRLIRGKMTLTEEVQWTELAEAELEENRIILSQKQEGHYYQEEKKLEATVQKDQDNQWTYKVHQGEKILKGGKICKDKKYPYQRVRLLAQVVQKIGKEALVIWGRIPKFHLPVERDTWEQWWDNYWQVTWIPDWDFVSTPPLVRLAFNLVGEPVPGAETFYTDGSCNRQSKEGKAGYITDRGRDRVKVLEQTTNQQAELEAFAMALTDSGPKANIIVDSQYVMGIVAGQPTESENRIVNQIIEEMIKKEAIYVAWVPAHKGIGGNQEVDHLVSQGIRQVLFLEKIEPAQEEHEKYHSNIKELSHKFGIPKLVARQIVNTCAHVQQKGEAIHGQVNAELGTWQMDCTHLEGKVIIVAVHVASGFIEAEVIPQESGRQTALFLLKLASRWPITHLHTDNGANFTSQEVKMVAWWVGIEQTFGVPYNPQSQGVVEAMNHHLKNQIDRIREQANTVETIVLMAVHCMNFKRRGGIGDMTPAERIINMITTEQEIQFLQAKNSKLKNFRVYFREGRDQLWKGPGELLWKGDGAVIVKVGTEIKVVPRRKAKIIKDYGGRQEMDSGSHLEGAREDGEMA
|
2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250};
|
DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
|
aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]
|
PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098;
|
1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10;
| null |
PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.
|
SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12497}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. {ECO:0000250}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. {ECO:0000250|UniProtKB:P04585}.
|
Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2)
|
P05976
|
MYL1_HUMAN
|
MAPKKDVKKPVAAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQDEFKEAFLLFDRTGDSKITLSQVGDVLRALGTNPTNAEVRKVLGNPSNEELNAKKIEFEQFLPMMQAISNNKDQATYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCINYEAFVKHIMSI
| null | null |
muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]
|
contractile fiber [GO:0043292]; cytosol [GO:0005829]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin II complex [GO:0016460]; sarcomere [GO:0030017]
|
calcium ion binding [GO:0005509]; structural constituent of muscle [GO:0008307]
| null |
1.10.238.10;
| null |
PTM: [Isoform MLC3]: Acetylated at position 2. {ECO:0000250}.
| null | null | null | null | null | null |
FUNCTION: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function. {ECO:0000269|PubMed:30215711}.
|
Homo sapiens (Human)
|
P05979
|
PGH1_SHEEP
|
MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMDTKGKKQLPDAEFLSRRFLLRRKFIPDPQSTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
|
cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of blood pressure [GO:0008217]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]; protein homodimerization activity [GO:0042803]
|
PF03098;
|
1.10.640.10;2.10.25.10;
|
Prostaglandin G/H synthase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000269|PubMed:7947975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000305|PubMed:7947975}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000269|PubMed:7947975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000305|PubMed:7947975}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000269|PubMed:7947975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000305|PubMed:7947975}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000269|PubMed:9448728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000305|PubMed:9448728}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000269|PubMed:9448728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000305|PubMed:9448728}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000269|PubMed:9448728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000305|PubMed:9448728}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000269|PubMed:9448728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000305|PubMed:9448728};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.1 uM for arachidonate {ECO:0000269|PubMed:7947975};
|
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:7947975}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response (PubMed:9448728). The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:7947975). Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells (PubMed:10438452). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (PubMed:9448728). {ECO:0000269|PubMed:10438452, ECO:0000269|PubMed:7947975, ECO:0000269|PubMed:9448728}.
|
Ovis aries (Sheep)
|
P05980
|
PGFS1_BOVIN
|
MDPKSQRVKLNDGHFIPVLGFGTYAPEEVPKSEALEATKFAIEVGFRHVDSAHLYQNEEQVGQAIRSKIADGTVKREDIFYTSKLWCNSLQPELVRPALEKSLQNLQLDYVDLYIIHSPVSLKPGNKFVPKDESGKLIFDSVDLCHTWEALEKCKDAGLTKSIGVSNFNHKQLEKILNKPGLKYKPVCNQVECHPYLNQSKLLEFCKSHDIVLVAYAALGAQLLSEWVNSNNPVLLEDPVLCAIAKKHKQTPALVALRYQVQRGVVVLAKSFNKKRIKENMQVFDFELTPEDMKAIDGLNRNIRYYDFQKGIGHPEYPFSEEY
|
1.1.1.188
| null |
daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; progesterone metabolic process [GO:0042448]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]
|
cytosol [GO:0005829]
|
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; androsterone dehydrogenase activity [GO:0047023]; bile acid binding [GO:0032052]; ketosteroid monooxygenase activity [GO:0047086]; prostaglandin D2 11-ketoreductase activity [GO:0036131]; prostaglandin-F synthase activity [GO:0047017]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin D2; Xref=Rhea:RHEA:10140, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404, ChEBI:CHEBI:57406, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.188;
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
| null | null |
FUNCTION: Catalyzes the reduction of PGD(2) and PGH(2) to PGF(2 alpha) and a stereoisomer, respectively. It has a broad substrate specificity and reduces also other carbonyl compounds.
|
Bos taurus (Bovine)
|
P05981
|
HEPS_HUMAN
|
MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL
|
3.4.21.106
| null |
basement membrane disassembly [GO:0034769]; cochlea morphogenesis [GO:0090103]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; pilomotor reflex [GO:0097195]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of cell growth [GO:0030307]; positive regulation of gene expression [GO:0010628]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of thyroid hormone generation [GO:2000611]; potassium ion transmembrane transport [GO:0071805]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to thyroid hormone [GO:0097066]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008]; serine-type peptidase activity [GO:0008236]
|
PF09272;PF00089;
|
3.10.250.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1885621}; Single-pass type II membrane protein {ECO:0000269|PubMed:1885621}. Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.; EC=3.4.21.106; Evidence={ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000305|PubMed:26673890};
| null | null | null | null |
FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:15839837, PubMed:21875933). Plays a role in cell growth and maintenance of cell morphology (PubMed:21875933, PubMed:8346233). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). {ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:8346233}.
|
Homo sapiens (Human)
|
P05982
|
NQO1_RAT
|
MAVRRALIVLAHAERTSFNYAMKEAAVEALKKKGWEVVESDLYAMNFNPLISRNDITGEPKDSENFQYPVESSLAYKEGRLSPDIVAEQKKLEAADLVIFQFPLYWFGVPAILKGWFERVLVAGFAYTYATMYDKGPFQNKKTLLSITTGGSGSMYSLQGVHGDMNVILWPIQSGILRFCGFQVLEPQLVYSIGHTPPDARVQVLEGWKKRLETVWEESPLYFAPSSLFDLNFQAGFLLKKEVQEEQKKNKFGLSVGHHLGKSIPADNQIKARK
|
1.6.5.2
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:1703398};
|
cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to metal ion [GO:0071248]; cellular response to oxidative stress [GO:0034599]; innate immune response [GO:0045087]; NADH oxidation [GO:0006116]; NADPH oxidation [GO:0070995]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein catabolic process [GO:0042177]; positive regulation of neuron apoptotic process [GO:0043525]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209]; removal of superoxide radicals [GO:0019430]; response to alkaloid [GO:0043279]; response to amine [GO:0014075]; response to carbohydrate [GO:0009743]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to flavonoid [GO:1905395]; response to hormone [GO:0009725]; response to hydrogen sulfide [GO:1904880]; response to ischemia [GO:0002931]; response to L-glutamine [GO:1904844]; response to lipopolysaccharide [GO:0032496]; response to nitrogen compound [GO:1901698]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to oxidative stress [GO:0006979]; response to testosterone [GO:0033574]; response to tetrachloromethane [GO:1904772]; response to xenobiotic stimulus [GO:0009410]; superoxide metabolic process [GO:0006801]; ubiquinone metabolic process [GO:0006743]; vitamin E metabolic process [GO:0042360]; vitamin K metabolic process [GO:0042373]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADPH dehydrogenase (quinone) activity [GO:0008753]; superoxide dismutase activity [GO:0004784]
|
PF02525;
|
3.40.50.360;
|
NAD(P)H dehydrogenase (quinone) family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1703398}.
|
CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630, ECO:0000269|PubMed:8999809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46161; Evidence={ECO:0000305|PubMed:1703398, ECO:0000305|PubMed:7862630, ECO:0000305|PubMed:8999809}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165; Evidence={ECO:0000305|PubMed:1703398, ECO:0000305|PubMed:7862630}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:P15559}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:0000250|UniProtKB:P15559}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADH = menadiol + NAD(+); Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378, ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:8999809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696; Evidence={ECO:0000305|PubMed:8999809};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=85 uM for NADH {ECO:0000269|PubMed:7862630}; KM=39 uM for NADPH {ECO:0000269|PubMed:7862630}; KM=110 uM for NADH {ECO:0000269|PubMed:8999809}; KM=2.5 uM for menadione {ECO:0000269|PubMed:8999809}; KM=840 uM for 5-(aziridin-1-yl)-2,4-dinitrobenzamide {ECO:0000269|PubMed:8999809}; Vmax=2400 umol/min/mg enzyme toward menadione {ECO:0000269|PubMed:8999809}; Vmax=140 nmol/min/mg enzyme toward 5-(aziridin-1-yl)-2,4-dinitrobenzamide {ECO:0000269|PubMed:8999809}; Note=kcat is 0.075 min(-1) NADH with as substrate. kcat is 0.074 min(-1) with NADPH as substrate. {ECO:0000269|PubMed:7862630};
| null | null | null |
FUNCTION: Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (PubMed:1703398, PubMed:7862630, PubMed:8999809). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (By similarity). Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (By similarity). Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (By similarity). {ECO:0000250|UniProtKB:P15559, ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630, ECO:0000269|PubMed:8999809}.
|
Rattus norvegicus (Rat)
|
P05986
|
KAPC_YEAST
|
MYVDPMNNNEIRKLSITAKTETTPDNVGQDIPVNAHSVHEECSSNTPVEINGRNSGKLKEEASAGICLVKKPMLQYRDTSGKYSLSDFQILRTLGTGSFGRVHLIRSNHNGRFYALKTLKKHTIVKLKQVEHTNDERRMLSIVSHPFIIRMWGTFQDSQQVFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVCLALEYLHSKDIIYRDLKPENILLDKNGHIKITDFGFAKYVPDVTYTLCGTPDYIAPEVVSTKPYNKSVDWWSFGVLIYEMLAGYTPFYNSNTMKTYENILNAELKFPPFFHPDAQDLLKKLITRDLSERLGNLQNGSEDVKNHPWFNEVIWEKLLARYIETPYEPPIQQGQGDTSQFDRYPEEEFNYGIQGEDPYMDLMKEF
|
2.7.11.11
| null |
mitochondrion organization [GO:0007005]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of cytoplasmic translation [GO:2000766]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265]
|
cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11;
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P05987
|
KAPR_DICDI
|
MTNNISHNQKATEKVEAQNNNNITRKRRGAISSEPLGDKPATPLPNIPKTVETQQRLEQALSNNIMFSHLEEEERNVVFLAMVEVLYKAGDIIIKQGDEGDLFYVIDSGICDIYVCQNGGSPTLVMEVFEGGSFGELALIYGSPRAATVIARTDVRLWALNGATYRRILMDQTIKKRKLYEEFLEKVSILRHIDKYERVSLADALEPVNFQDGEVIVRQGDPGDRFYIIVEGKVVVTQETVPGDHSTSHVVSELHPSDYFGEIALLTDRPRAATVTSIGYTKCVELDRQRFNRLCGPIDQMLRRNMETYNQFLNRPPSSPNLTSQKS
| null | null |
c-di-GMP signaling [GO:0061939]; culmination involved in sorocarp development [GO:0031154]; positive regulation of gene expression [GO:0010628]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of gene expression [GO:0010468]; regulation of protein kinase A signaling [GO:0010738]; regulation of protein phosphorylation [GO:0001932]; regulation of sorocarp development [GO:0031156]; regulation of sorocarp stalk cell differentiation [GO:0031285]; response to curcumin [GO:1904643]; sorocarp morphogenesis [GO:0031288]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytosol [GO:0005829]
|
cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;
|
2.60.120.10;
|
CAMP-dependent kinase regulatory chain family
|
PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain but is not phosphorylated. The physiological significance of phosphorylations by other kinases is unclear.
| null | null | null | null | null | null | null |
Dictyostelium discoideum (Social amoeba)
|
P05989
|
ILVC_SALTY
|
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPQGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGSAIPEGAVDNAQLRDVNDAIRSHAIEQVGKKLRGYMTDMKRIAVAG
|
1.1.1.86
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:4388025}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435};
|
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
|
cytosol [GO:0005829]
|
ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]
|
PF01450;PF07991;
|
3.40.50.720;
|
Ketol-acid reductoisomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:4388025}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:4388025};
| null |
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:4388025}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P05990
|
PYR1_DROME
|
MASTDCYLALEDGTVLPGYSFGYVPSENESKVGFGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEHGLPLHFEWMKGVVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPKSSFVDPNVRNLAKECSVKERQVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLEDEQFDALFLSNGPGNPESCDQIVQQVRKVIEEGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQQKDLTIPQLIEQRLRPTTPAIDSAPVMPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKSERPNGVLLTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSSQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSDVLGFDPDVVPLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLQSLLTRNGSRTDAALLLKAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGSEHDVDFPGGHTIVVGSGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVASDGRILCMAVSEHVENAGVHSGDATLVTPPQDLNAETLEAIKRITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVGLDVEPLDVLHGVGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKNAVLLSIGSFKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQWTFDKTTPDDINGELRHLAEFLANKQFDLVINLPMSGGGARRVSSFMTHGYRTRRLAVDYSIPLVTDVKCTKLLVESMRMNGGKPPMKTHTDCMTSRRIVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWAQVNELASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKRSPIVCHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHGMSEVRPLLCSPEDQEALWENIDYIDVFATDHAPHTLAEKRSERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQPGFGQNVRPKQSPLASEASQDLLPSDNDANDTFTRLLTSEGPGGGVHGISTKVHFVDGANFLRPNSPSPRIRLDSASNTTLREYLQRTTNSNPVAHSLMGKHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLTITMVGDLKNGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQRERFDNVEDYEKCCGHLVLTPEHMMRAKKRSIVLHPLPRLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGGRNTAL
|
2.1.3.2; 3.5.1.2; 3.5.2.3; 6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P27708}; Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity). {ECO:0000250|UniProtKB:P27708};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:0004359]; glutamine binding [GO:0070406]; metal ion binding [GO:0046872]
|
PF01979;PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729;
|
3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380;
|
CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000269|PubMed:10080891}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000250|UniProtKB:P07259}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:P07259}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000250|UniProtKB:P27708}; CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000250|UniProtKB:P27708};
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P27708}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000250|UniProtKB:P27708}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000250|UniProtKB:P27708}.
| null | null |
FUNCTION: Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000250|UniProtKB:P27708}.
|
Drosophila melanogaster (Fruit fly)
|
P05994
|
PAPA4_CARPA
|
MAIICSFSKLLFVAICLFGHMSLSYCDFSIVGYSQDDLTSTERLIQLFNSWMLKHNKNYKNVDEKLYRFEIFKDNLKYIDERNKMINGYWLGLNEFSDLSNDEFKEKYVGSLPEDYTNQPYDEEFVNEDIVDLPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDKQSYGCNRGYQSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEGSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKSGGKGYILIKNSWGPGWGENGYIRIRRASGNSPGVCGVYRSSYYPIKN
|
3.4.22.25
| null |
proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]
|
cysteine-type endopeptidase activity [GO:0004197]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.; EC=3.4.22.25; Evidence={ECO:0000269|PubMed:2404797};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 mM for Boc-Ala-Ala-Gly-NHPhNO(2) {ECO:0000269|PubMed:2404797}; KM=0.16 mM for Boc-Ala-Ala-Gly-NHMec {ECO:0000269|PubMed:2404797}; KM=0.08 mM for Boc-Ala-Ala-Ala-NHMec {ECO:0000269|PubMed:2404797}; Note=kcat is 22 sec(-1) with Boc-Ala-Ala-Gly-NHPhNO(2) as substrate (PubMed:2404797). kcat is 5 sec(-1) with Boc-Ala-Ala-Gly-NHMec as substrate (PubMed:2404797). kcat is 0.08 sec(-1) with Boc-Ala-Ala-Ala-NHMec as substrate (PubMed:2404797). {ECO:0000269|PubMed:2404797};
| null | null | null |
FUNCTION: Thiol protease with a substrate specificity very different from the other thiol proteases. {ECO:0000269|PubMed:2404797}.
|
Carica papaya (Papaya)
|
P05997
|
CO5A2_HUMAN
|
MMANWAEARPLLILIVLLGQFVSIKAQEEDEDEGYGEEIACTQNGQMYLNRDIWKPAPCQICVCDNGAILCDKIECQDVLDCADPVTPPGECCPVCSQTPGGGNTNFGRGRKGQKGEPGLVPVVTGIRGRPGPAGPPGSQGPRGERGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGLSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPVGPRGPQGLQGQQGGAGPTGPPGEPGDPGPMGPIGSRGPEGPPGKPGEDGEPGRNGNPGEVGFAGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEVGAPGSKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGQRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPVGSPGLPGAIGTDGTPGAKGPTGSPGTSGPPGSAGPPGSPGPQGSTGPQGIRGQPGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPVGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGSQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDPGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKPGDQGVPGDPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGSPGPSGTPGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPNGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPLGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGGPGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGDPGSRGPIGPPGRAGKRGLPGPQGPRGDKGDHGDRGDRGQKGHRGFTGLQGLPGPPGPNGEQGSAGIPGPFGPRGPPGPVGPSGKEGNPGPLGPIGPPGVRGSVGEAGPEGPPGEPGPPGPPGPPGHLTAALGDIMGHYDESMPDPLPEFTEDQAAPDDKNKTDPGVHATLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHSAKQSGEYWIDPNQGSVEDAIKVYCNMETGETCISANPSSVPRKTWWASKSPDNKPVWYGLDMNRGSQFAYGDHQSPNTAITQMTFLRLLSKEASQNITYICKNSVGYMDDQAKNLKKAVVLKGANDLDIKAEGNIRFRYIVLQDTCSKRNGNVGKTVFEYRTQNVARLPIIDLAPVDVGGTDQEFGVEIGPVCFV
| null | null |
cellular response to amino acid stimulus [GO:0071230]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; eye morphogenesis [GO:0048592]; negative regulation of endodermal cell differentiation [GO:1903225]; notochord development [GO:0030903]; ossification [GO:0001503]; skeletal system development [GO:0001501]; skin development [GO:0043588]
|
collagen type II trimer [GO:0005585]; collagen type V trimer [GO:0005588]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;6.20.200.20;
|
Fibrillar collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1. {ECO:0000269|PubMed:21757687, ECO:0000269|PubMed:8181482}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
P06002
|
OPS1_DROME
|
MESFAVAAAQLGPHFAPLSNGSVVDKVTPDMAHLISPYWNQFPAMDPIWAKILTAYMIMIGMISWCGNGVVIYIFATTKSLRTPANLLVINLAISDFGIMITNTPMMGINLYFETWVLGPMMCDIYAGLGSAFGCSSIWSMCMISLDRYQVIVKGMAGRPMTIPLALGKIAYIWFMSSIWCLAPAFGWSRYVPEGNLTSCGIDYLERDWNPRSYLIFYSIFVYYIPLFLICYSYWFIIAAVSAHEKAMREQAKKMNVKSLRSSEDAEKSAEGKLAKVALVTITLWFMAWTPYLVINCMGLFKFEGLTPLNTIWGACFAKSAACYNPIVYGISHPKYRLALKEKCPCCVFGKVDDGKSSDAQSQATASEAESKA
| null | null |
adult locomotory behavior [GO:0008344]; cellular response to light stimulus [GO:0071482]; detection of UV [GO:0009589]; detection of visible light [GO:0009584]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; optomotor response [GO:0071632]; phospholipase C-activating rhodopsin mediated signaling pathway [GO:0030265]; photoreceptor cell morphogenesis [GO:0008594]; phototaxis [GO:0042331]; phototransduction [GO:0007602]; response to light intensity [GO:0009642]; rhabdomere development [GO:0042052]; thermotaxis [GO:0043052]; visual perception [GO:0007601]
|
cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; inaD signaling complex [GO:0016027]; rhabdomere [GO:0016028]; rhabdomere membrane [GO:0033583]; subrhabdomeral cisterna [GO:0016029]
|
G protein-coupled photoreceptor activity [GO:0008020]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
|
SUBCELLULAR LOCATION: Cell projection, rhabdomere membrane {ECO:0000269|PubMed:23226104}; Multi-pass membrane protein {ECO:0000305}. Note=Upon white light stimulation, is internalized into the rhabdomere membranes. {ECO:0000269|PubMed:23226104}.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
|
Drosophila melanogaster (Fruit fly)
|
P06003
|
PSBC_SPIOL
|
MKTLYSLRRFYPVETLFNGTLTLAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNVTLSPSIIFGCLLKSPFGGEGWIVSVDDLEDIIGGHVWIGVICILGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN
| null |
COFACTOR: Note=Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01496};
|
photosynthetic electron transport in photosystem II [GO:0009772]
|
chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]
|
chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; metal ion binding [GO:0046872]
|
PF00421;
|
1.10.10.670;
|
PsbB/PsbC family, PsbC subfamily
|
PTM: Over time a tryptophan in the fifth lumenal loop is converted to 2-hydroxy-2,3-dihydrotryptophan, 2-oxo-2,3-dihydrotryptophan, and kynurenine by oxidizing species from the active site. This oxidation targets the protein for turnover. {ECO:0000269|PubMed:12417747}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:3121625}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496}.
| null | null | null | null | null |
FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01496}.
|
Spinacia oleracea (Spinach)
|
P06006
|
PSBD_PEA
|
MTIALGKFTKDQNDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFAVGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDLTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMATQDQPHENLIFPEEVLPRGNAL
|
1.10.3.9
|
COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01383};
|
photosynthetic electron transport in photosystem II [GO:0009772]
|
chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]
|
chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxygen evolving activity [GO:0010242]
|
PF00124;
|
1.20.85.10;
|
Reaction center PufL/M/PsbA/D family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:9407103}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383}.
|
CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01383};
| null | null | null | null |
FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. {ECO:0000255|HAMAP-Rule:MF_01383}.
|
Pisum sativum (Garden pea) (Lathyrus oleraceus)
|
P06008
|
RCEH_BLAVI
|
MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVYELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAERAEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYFRYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSAYYAGGLLYATPERAESLL
| null |
COFACTOR: Name=a bacteriochlorophyll; Xref=ChEBI:CHEBI:38201; Note=Binds 4 bacteriochlorophylls per trimer.; COFACTOR: Name=a bacteriopheophytin; Xref=ChEBI:CHEBI:60411; Note=Binds 2 bacteriopheophytins per trimer.; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe cation per trimer.; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 4 Mg(2+) ions per trimer.; COFACTOR: Name=a menaquinone; Xref=ChEBI:CHEBI:16374; Note=Binds 1 menaquinone per trimer.; COFACTOR: Name=a ubiquinone; Xref=ChEBI:CHEBI:16389; Note=Binds 1 ubiquinone per trimer.;
|
photosynthesis, light reaction [GO:0019684]
|
plasma membrane light-harvesting complex [GO:0030077]; plasma membrane-derived chromatophore membrane [GO:0042717]
|
bacteriochlorophyll binding [GO:0042314]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]
|
PF05239;PF03967;
|
3.90.50.10;4.10.540.10;
|
Reaction center PuhA family
| null |
SUBCELLULAR LOCATION: Cellular chromatophore membrane; Single-pass membrane protein.
| null | null | null | null | null |
FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
|
Blastochloris viridis (Rhodopseudomonas viridis)
|
P06019
|
REPC_BPMU
|
MKSNFIEKNNTEKSIWCSPQEIMAADGMPGSVAGVHYRANVQGWTKQKKEGVKGGKAVEYDVMSMPTKEREQVIAHLGLSTPDTGAQANEKQDSSELINKLTTTLINMIEELEPDEARKALKLLSKGGLLALMPLVFNEQKLYSFIGFSQQSIQTLMMLDALPEEKRKEILSKYGIHEQESVVVPSQEPQEVKKAV
| null | null |
latency-replication decision [GO:0098689]; viral latency [GO:0019042]
|
host cell cytoplasm [GO:0030430]; transcription repressor complex [GO:0017053]
|
DNA binding [GO:0003677]
|
PF02316;
|
1.10.10.10;
|
Mulikevirus repressor c protein family
|
PTM: C-terminally truncated forms act as exceptionally stable repressors that prevent prophage induction.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Promotes latency by binding operators O1 and O2 in the enhancer/operator region, thereby repressing the transcription from the Pe (early) promoter and blocking the expression of the genes required for replication (lytic growth). Competes with DDE-recombinase A for binding to the internal activation sequence (IAS), which overlaps O1 and O2. The outcome of this competition determines if the virus enters latency or starts replication. Makes the cell immune to superinfection by repressing genes expression of any subsequent incoming viral genome. {ECO:0000269|PubMed:11517307, ECO:0000269|PubMed:12217693, ECO:0000269|PubMed:16154589, ECO:0000269|PubMed:18230617, ECO:0000269|PubMed:8626285}.
|
Escherichia phage Mu (Bacteriophage Mu)
|
P06022
|
ACTC_BPMU
|
MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:19170593}; Note=Binding magnesium induces a conformational change that allows DNA-binding. {ECO:0000305|PubMed:19170593};
| null |
host cell cytoplasm [GO:0030430]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]
|
PF08765;
|
1.10.10.60;
|
C/mor transcriptional regulatory family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP. {ECO:0000269|PubMed:9367769}.
|
Escherichia phage Mu (Bacteriophage Mu)
|
P06028
|
GLPB_HUMAN
|
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAPVVIILIILCVMAGIIGTILLISYSIRRLIKA
| null | null | null |
ankyrin-1 complex [GO:0170014]; plasma membrane [GO:0005886]
| null |
PF01102;
|
1.20.5.70;
|
Glycophorin-A family
|
PTM: The N-terminal extracellular domain is heavily glycosylated on serine and threonine residues. {ECO:0000269|PubMed:7681597}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane. {ECO:0000269|PubMed:35835865}.
|
Homo sapiens (Human)
|
P06100
|
NOT2_YEAST
|
MEKFGLKALVPLLKLEDKELSSTYDHSMTLGADLSSMLYSLGIPRDSQDHRVLDTFQSPWAETSRSEVEPRFFTPESFTNIPGVLQSTVTPPCFNSIQNDQQRVALFQDETLFFLFYKHPGTVIQELTYLELRKRNWRYHKTLKAWLTKDPMMEPIVSADGLSERGSYVFFDPQRWEKCQRDFLLFYNAIM
| null | null |
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; deadenylation-independent decapping of nuclear-transcribed mRNA [GO:0031087]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; protein ubiquitination [GO:0016567]; regulation of cell cycle [GO:0051726]; regulation of stem cell population maintenance [GO:2000036]; response to pheromone triggering conjugation with cellular fusion [GO:0000749]; transcription elongation by RNA polymerase II [GO:0006368]
|
CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]
| null |
PF04153;
|
2.30.30.1020;
|
CNOT2/3/5 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889048}. Nucleus {ECO:0000269|PubMed:11889048}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. NOT2 is required for the integrity of the complex. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery. {ECO:0000269|PubMed:9463387}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06101
|
CDC37_YEAST
|
MAIDYSKWDKIELSDDSDVEVHPNVDKKSFIKWKQQSIHEQRFKRNQDIKNLETQVDMYSHLNKRVDRILSNLPESSLTDLPAVTKFLNANFDKMEKSKGENVDPEIATYNEMVEDLFEQLAKDLDKEGKDSKSPSLIRDAILKHRAKIDSVTVEAKKKLDELYKEKNAHISSEDIHTGFDSSFMNKQKGGAKPLEATPSEALSSAAESNILNKLAKSSVPQTFIDFKDDPMKLAKETEEFGKISINEYSKSQKFLLEHLPIISEQQKDALMMKAFEYQLHGDDKMTLQVIHQSELMAYIKEIYDMKKIPYLNPMELSNVINMFFEKVIFNKDKPMGKESFLRSVQEKFLHIQKRSKILQQEEMDESNAEGVETIQLKSLDDSTELEVNLPDFNSKDPEEMKKVKVFKTLIPEKMQEAIMTKNLDNINKVFEDIPIEEAEKLLEVFNDIDIIGIKAILENEKDFQSLKDQYEQDHEDATMENLSLNDRDGGGDNHEEVKHTADTVD
| null | null |
cell division [GO:0051301]; p38MAPK cascade [GO:0038066]; positive regulation of MAPK cascade [GO:0043410]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of cell cycle [GO:0051726]; spindle pole body duplication [GO:0030474]
|
cytoplasm [GO:0005737]
|
heat shock protein binding [GO:0031072]; protein kinase binding [GO:0019901]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF08564;PF08565;PF03234;
|
1.20.58.610;
|
CDC37 family
|
PTM: Phosphorylation at Ser-14 is required for the interactions with HOG1 and SLT2 MAP kinases and is crucial for adaptation to stress conditions due to high osmolarity or cell wall perturbation. {ECO:0000269|PubMed:17220467}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
| null | null | null | null | null |
FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall perturbation. {ECO:0000269|PubMed:17220467}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06102
|
NOT3_YEAST
|
MAHRKLQQEVDRVFKKINEGLEIFNSYYERHESCTNNPSQKDKLESDLKREVKKLQRLREQIKSWQSSPDIKDKDSLLDYRRSVEIAMEKYKAVEKASKEKAYSNISLKKSETLDPQERERRDISEYLSQMIDELERQYDSLQVEIDKLLLLNKKKKTSSTTNDEKKEQYKRFQARYRWHQQQMELALRLLANEELDPQDVKNVQDDINYFVESNQDPDFVEDETIYDGLNLQSNEAIAHEVAQYFASQNAEDNNTSDANESLQDISKLSKKEQRKLEREAKKAAKLAAKNATGAAIPVAGPSSTPSPVIPVADASKETERSPSSSPIHNATKPEEAVKTSIKSPRSSADNLLPSLQKSPSSATPETPTNVHTHIHQTPNGITGATTLKPATLPAKPAGELKWAVAASQAVEKDRKVTSASSTISNTSTKTPTTAAATTTSSNANSRIGSALNTPKLSTSSLSLQPDNTGASSSAATAAAVLAAGAAAVHQNNQAFYRNMSSSHHPLVSLATNPKSEHEVATTVNQNGPENTTKKVMEQKEEESPEERNKLQVPTFGVFDDDFESDRDSETEPEEEEQPSTPKYLSLEQREAKTNEIKKEFVSDFETLLLPSGVQEFIMSSELYNSQIESKITYKRSRDMCEISRLVEVPQGVNPPSPLDAFRSTQQWDVMRCSLRDIIIGSERLKEDSSSIYAKILENFRTLEMFSLFYNYYFAITPLEREIAYKILNERDWKVSKDGTMWFLRQGEVKFFNEICEVGDYKIFKLDDWTVIDKINFRLDYSFLQPPVDTASEVRDVSVDNNNVNDQSNVTLEQQKQEISHGKQLLKQLKQGKISV
| null | null |
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; protein ubiquitination [GO:0016567]
|
CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]
| null |
PF04153;PF04065;
|
2.30.30.1020;
|
CNOT2/3/5 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus.
| null | null | null | null | null |
FUNCTION: Acts as a component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery. {ECO:0000269|PubMed:9463387}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06103
|
EIF3B_YEAST
|
MKNFLPRTLKNIYELYFNNISVHSIVSRNTQLKRSKIIQMTTETFEDIKLEDIPVDDIDFSDLEEQYKVTEEFNFDQYIVVNGAPVIPSAKVPVLKKALTSLFSKAGKVVNMEFPIDEATGKTKGFLFVECGSMNDAKKIIKSFHGKRLDLKHRLFLYTMKDVERYNSDDFDTEFREPDMPTFVPSSSLKSWLMDDKVRDQFVLQDDVKTSVFWNSMFNEEDSLVESRENWSTNYVRFSPKGTYLFSYHQQGVTAWGGPNFDRLRRFYHPDVRNSSVSPNEKYLVTFSTEPIIVEEDNEFSPFTKKNEGHQLCIWDIASGLLMATFPVIKSPYLKWPLVRWSYNDKYCARMVGDSLIVHDATKNFMPLEAKALKPSGIRDFSFAPEGVKLQPFRNGDEPSVLLAYWTPETNNSACTATIAEVPRGRVLKTVNLVQVSNVTLHWQNQAEFLCFNVERHTKSGKTQFSNLQICRLTERDIPVEKVELKDSVFEFGWEPHGNRFVTISVHEVADMNYAIPANTIRFYAPETKEKTDVIKRWSLVKEIPKTFANTVSWSPAGRFVVVGALVGPNMRRSDLQFYDMDYPGEKNINDNNDVSASLKDVAHPTYSAATNITWDPSGRYVTAWSSSLKHKVEHGYKIFNIAGNLVKEDIIAGFKNFAWRPRPASILSNAERKKVRKNLREWSAQFEEQDAMEADTAMRDLILHQRELLKQWTEYREKIGQEMEKSMNFKIFDVQPEDASDDFTTIEEIVEEVLEETKEKVE
| null | null |
cytoplasmic translational initiation [GO:0002183]; formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
cytoplasmic stress granule [GO:0010494]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; multi-eIF complex [GO:0043614]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369]
|
PF08662;PF00076;
|
3.30.70.330;2.130.10.10;
|
EIF-3 subunit B family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:14562095}.
| null | null | null | null | null |
FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:11387228}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06104
|
UBC2_YEAST
|
MSTPARRRLMRDFKRMKEDAPPGVSASPLPDNVMVWNAMIIGPADTPYEDGTFRLLLEFDEEYPNKPPHVKFLSEMFHPNVYANGEICLDILQNRWTPTYDVASILTSIQSLFNDPNPASPANVEAATLFKDHKSQYVKRVKETVEKSWEDDMDDMDDDDDDDDDDDDDEAD
|
2.3.2.23
| null |
cytoplasm protein quality control by the ubiquitin-proteasome system [GO:0071629]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; DNA-templated transcription termination [GO:0006353]; double-strand break repair via homologous recombination [GO:0000724]; ERAD pathway [GO:0036503]; error-free postreplication DNA repair [GO:0042275]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; meiotic DNA double-strand break formation [GO:0042138]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of dipeptide transport [GO:0090089]; sporulation resulting in formation of a cellular spore [GO:0030435]; stress-induced homeostatically regulated protein degradation pathway [GO:0120174]; subtelomeric heterochromatin formation [GO:0031509]; telomere maintenance via recombination [GO:0000722]; transcription by RNA polymerase II [GO:0006366]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; HULC complex [GO:0033503]; MUB1-RAD6-UBR2 ubiquitin ligase complex [GO:1990304]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505]; RAD6-UBR2 ubiquitin ligase complex [GO:1990305]; UBR1-RAD6 ubiquitin ligase complex [GO:1990303]
|
ATP binding [GO:0005524]; proteasome binding [GO:0070628]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00179;
|
3.10.110.10;
|
Ubiquitin-conjugating enzyme family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}. Nucleus {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}.
| null | null |
FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:12077605, ECO:0000269|PubMed:12226657, ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15388802, ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:16247017, ECO:0000269|PubMed:16307922, ECO:0000269|PubMed:1651502, ECO:0000269|PubMed:2065660, ECO:0000269|PubMed:2157209, ECO:0000269|PubMed:3306404, ECO:0000269|PubMed:7038392, ECO:0000269|PubMed:7926769, ECO:0000269|PubMed:8436296, ECO:0000269|PubMed:9287349, ECO:0000269|PubMed:9343433}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06105
|
SC160_YEAST
|
MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKPAVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVAANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYLKKLASNLDEEKVKIPSKFQFLIDAEELKEKYNVIVTFPSTPDDELVSFVGLRDKVGEAITYARSSSKSYVVESLDISKAHSKNLTHAKNLIMYFTKYSVLKGLEESHPNVKISLPSIQSLPTAETVTIHISAKSDEANDIKAVRKELISFVNNIPPSETLVITDLDYELFGGSIKHCLLASESSVAFVQFGDYYPNDNSILLVALTEDEDFKPSIEEIQASLNKANESLNSLRTKQNNMETKTYEFSEEVQDSLFKPSSATWKLIMEDISEQEGHLQIKLHTPEENQLTVRGDEKAAKAANKIFESILNSPSSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVTLTGLEYNLTHAKKYLAAEAKKWADIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLDFEMENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAAKRVESIVAEASDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGGEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKDAENSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRENFDREVDVPASIYEYVSERGAFIQKLRMDLSVNVRFGNTSKKANKLARAPIEIPLEKVCGSTEGENAEKTKFTIEEVGAPTSSEEGDITMRLTYEPIDLSSILSDGEEKEVTKDTSNDSAKKEEALDTAVKLIKERIAKAPSATYAGYVWGADTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMVLKSLRR
| null | null |
chemotropism [GO:0043577]; chromosome segregation [GO:0007059]; meiotic telomere clustering [GO:0045141]; nuclear division [GO:0000280]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; silent mating-type cassette heterochromatin formation [GO:0030466]; subtelomeric heterochromatin formation [GO:0031509]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole membrane [GO:0000329]; nuclear membrane [GO:0031965]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175]; nucleus [GO:0005634]
|
G-protein alpha-subunit binding [GO:0001965]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF00013;
|
3.30.1370.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic surface of the ER-nuclear envelope membranes.
| null | null | null | null | null |
FUNCTION: Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER-nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06106
|
CYSD_YEAST
|
MPSHFDTVQLHAGQENPGDNAHRSRAVPIYATTSYVFENSKHGSQLFGLEVPGYVYSRFQNPTSNVLEERIAALEGGAAALAVSSGQAAQTLAIQGLAHTGDNIVSTSYLYGGTYNQFKISFKRFGIEARFVEGDNPEEFEKVFDERTKAVYLETIGNPKYNVPDFEKIVAIAHKHGIPVVVDNTFGAGGYFCQPIKYGADIVTHSATKWIGGHGTTIGGIIVDSGKFPWKDYPEKFPQFSQPAEGYHGTIYNEAYGNLAYIVHVRTELLRDLGPLMNPFASFLLLQGVETLSLRAERHGENALKLAKWLEQSPYVSWVSYPGLASHSHHENAKKYLSNGFGGVLSFGVKDLPNADKETDPFKLSGAQVVDNLKLASNLANVGDAKTLVIAPYFTTHKQLNDKEKLASGVTKDLIRVSVGIEFIDDIIADFQQSFETVFAGQKP
|
2.5.1.47; 2.5.1.49
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806};
|
cysteine biosynthetic process [GO:0019344]; cysteine biosynthetic process from serine [GO:0006535]; L-homocysteine biosynthetic process [GO:0071269]; methionine metabolic process [GO:0006555]; sulfate assimilation [GO:0000103]; transsulfuration [GO:0019346]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
cysteine synthase activity [GO:0004124]; O-acetylhomoserine aminocarboxypropyltransferase activity [GO:0003961]; O-acetylhomoserine sulfhydrylase activity [GO:0051009]; pyridoxal phosphate binding [GO:0030170]
|
PF01053;
|
3.90.1150.10;3.40.640.10;
|
Trans-sulfuration enzymes family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
|
CATALYTIC ACTIVITY: Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:36379252, ECO:0000269|PubMed:36455053}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.7 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:7765825}; KM=6.67 mM for O-acetyl-L-homoserine (at pH 7.8 in Tris-HCl buffer) {ECO:0000269|PubMed:4609980}; KM=5.12 mM for O-acetyl-L-serine (at pH 7.8 in potassium phosphate buffer) {ECO:0000269|PubMed:4609980}; KM=8.03 uM for O-acetyl-L-homoserine (OAH) (at 30 degrees Celsius in potassium phosphate buffer) {ECO:0000269|PubMed:36379252};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine. {ECO:0000305|PubMed:12586406, ECO:0000305|PubMed:1732168}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 (for O-acetylhomoserine sulfhydrylase activity in Tris-HCl buffer) and 8.4 (for both O-acetylhomoserine sulfhydrylase and O-acetylserine sulfhydrylase activities in barbital-HCl buffer). {ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307};
| null |
FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:36379252, PubMed:36455053, PubMed:4609980, PubMed:7765825, PubMed:795806). Required to efficiently reduce toxic levels of hydrogen sulfide generated when the sulfate assimilation pathway (SAP) is active (PubMed:36379252, PubMed:36455053). Also catalyzes the conversion of O-acetylserine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway (PubMed:36455053, PubMed:4609980, PubMed:7765825, PubMed:795806). However, it seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through the cystathionine pathway and not via direct incorporation of sulfur into OAS (PubMed:1732168). It therefore has no metabolic role in cysteine biosynthesis and may only have a regulatory role controlling OAS levels (PubMed:12586406). {ECO:0000269|PubMed:36379252, ECO:0000269|PubMed:36455053, ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806, ECO:0000305|PubMed:12586406, ECO:0000305|PubMed:1732168}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06115
|
CATT_YEAST
|
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
|
1.11.1.6
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413;
|
hydrogen peroxide catabolic process [GO:0042744]; response to hydrogen peroxide [GO:0042542]; response to reactive oxygen species [GO:0000302]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]
|
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00199;PF06628;
|
2.40.180.10;
|
Catalase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
| null | null | null | null |
FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06126
|
CD1A_HUMAN
|
MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSNSSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCELHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLSDTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSVGFIILAVIVPLLLLIGLALWFRKRCFC
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723]
|
PF07654;PF16497;
|
2.60.40.10;3.30.500.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:11600221, ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:11231314}; Single-pass type I membrane protein {ECO:0000255}. Note=Subject to intracellular trafficking between the cell membrane and endosomes (PubMed:11231314). Localizes to cell surface lipid rafts (PubMed:18178838). {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:18178838}.
| null | null | null | null | null |
FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:16272286, ECO:0000269|PubMed:18178838}.
|
Homo sapiens (Human)
|
P06127
|
CD5_HUMAN
|
MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL
| null | null |
apoptotic signaling pathway [GO:0097190]; cell recognition [GO:0008037]; T cell costimulation [GO:0031295]
|
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
signaling receptor activity [GO:0038023]
|
PF00530;
|
3.10.250.10;
| null |
PTM: Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: May act as a receptor in regulating T-cell proliferation.
|
Homo sapiens (Human)
|
P06129
|
BTUB_ECOLI
|
MIKKASLLTACSVTAFSAWAQDTSPDTLVVTANRFEQPRSTVLAPTTVVTRQDIDRWQSTSVNDVLRRLPGVDITQNGGSGQLSSIFIRGTNASHVLVLIDGVRLNLAGVSGSADLSQFPIALVQRVEYIRGPRSAVYGSDAIGGVVNIITTRDEPGTEISAGWGSNSYQNYDVSTQQQLGDKTRVTLLGDYAHTHGYDVVAYGNTGTQAQTDNDGFLSKTLYGALEHNFTDAWSGFVRGYGYDNRTNYDAYYSPGSPLLDTRKLYSQSWDAGLRYNGELIKSQLITSYSHSKDYNYDPHYGRYDSSATLDEMKQYTVQWANNVIVGHGSIGAGVDWQKQTTTPGTGYVEDGYDQRNTGIYLTGLQQVGDFTFEGAARSDDNSQFGRHGTWQTSAGWEFIEGYRFIASYGTSYKAPNLGQLYGFYGNPNLDPEKSKQWEGAFEGLTAGVNWRISGYRNDVSDLIDYDDHTLKYYNEGKARIKGVEATANFDTGPLTHTVSYDYVDARNAITDTPLLRRAKQQVKYQLDWQLYDFDWGITYQYLGTRYDKDYSSYPYQTVKMGGVSLWDLAVAYPVTSHLTVRGKIANLFDKDYETVYGYQTAGREYTLSGSYTF
| null | null |
cobalamin transport [GO:0015889]; monoatomic ion transmembrane transport [GO:0034220]
|
cell outer membrane [GO:0009279]; membrane [GO:0016020]; pore complex [GO:0046930]; transmembrane transporter complex [GO:1902495]
|
ABC-type vitamin B12 transporter activity [GO:0015420]; calcium ion binding [GO:0005509]; porin activity [GO:0015288]; protein domain specific binding [GO:0019904]; siderophore uptake transmembrane transporter activity [GO:0015344]
|
PF07715;PF00593;
|
2.40.170.20;2.170.130.10;
|
TonB-dependent receptor family, BtuB (TC 1.B.14.3.1) subfamily
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:12595710, ECO:0000269|PubMed:12652322, ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:12595710, ECO:0000269|PubMed:12652322, ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793}.
| null | null | null | null | null |
FUNCTION: Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space (PubMed:4579869). It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:10485884, ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793, ECO:0000269|PubMed:4579869}.; FUNCTION: (Microbial infection) Acts as a receptor for bacteriophages BF23 and C1, and for A and E colicins (PubMed:14528295, PubMed:4579869). Cyanocobalamin (CN-B12) in solid medium protects against colicins E1 and E3 (PubMed:4579869). Does not act as the translocon for colicin E3 (ColE3). The translocon is OmpF; trimeric complexes with ColE3, BtuB and OmpF can be cross-linked and immunoprecipitated (PubMed:18636093). {ECO:0000269|PubMed:14528295, ECO:0000269|PubMed:18636093, ECO:0000269|PubMed:4579869}.
|
Escherichia coli (strain K12)
|
P06132
|
DCUP_HUMAN
|
MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN
|
4.1.1.37
| null |
heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; porphyrin-containing compound catabolic process [GO:0006787]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
uroporphyrinogen decarboxylase activity [GO:0004853]
|
PF01208;
|
3.20.20.210;
|
Uroporphyrinogen decarboxylase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37; Evidence={ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:18004775, ECO:0000269|PubMed:21668429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19866; Evidence={ECO:0000305|PubMed:11069625, ECO:0000305|PubMed:14633982, ECO:0000305|PubMed:21668429}; CATALYTIC ACTIVITY: Reaction=4 H(+) + uroporphyrinogen I = 4 CO2 + coproporphyrinogen I; Xref=Rhea:RHEA:31239, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:62626, ChEBI:CHEBI:62631; Evidence={ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31240; Evidence={ECO:0000305|PubMed:11719352, ECO:0000305|PubMed:14633982, ECO:0000305|PubMed:21668429};
| null |
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. {ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:18004775};
| null |
FUNCTION: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway (PubMed:11069625, PubMed:11719352, PubMed:14633982, PubMed:18004775, PubMed:21668429). Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (PubMed:11069625, PubMed:11719352, PubMed:14633982, PubMed:21668429). In vitro also decarboxylates pentacarboxylate porphyrinogen I (PubMed:12071824). {ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:12071824, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:18004775, ECO:0000269|PubMed:21668429}.
|
Homo sapiens (Human)
|
P06133
|
UD2B4_HUMAN
|
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSASISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFNDILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAIEKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVLGRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTMSSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
|
2.4.1.17
| null |
cellular glucuronidation [GO:0052695]; estrogen metabolic process [GO:0008210]
|
endoplasmic reticulum membrane [GO:0005789]
|
glucuronosyltransferase activity [GO:0015020]
|
PF00201;
|
3.40.50.2000;
|
UDP-glycosyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8333863}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033; Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:23288867}; CATALYTIC ACTIVITY: Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642; Evidence={ECO:0000269|PubMed:18719240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873; Evidence={ECO:0000305|PubMed:18719240}; CATALYTIC ACTIVITY: Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate = 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52916, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136883; Evidence={ECO:0000269|PubMed:23288867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52917; Evidence={ECO:0000305|PubMed:23288867};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.77 uM for 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; KM=57.8 uM for calcitriol (when assaying glucuronidation at position 25) {ECO:0000269|PubMed:18177842}; Vmax=135 pmol/min/mg enzyme for the formation of 17alpha-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; Vmax=17 pmol/min/mg enzyme for the formation of 17alpha-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=3.8 pmol/min/mg enzyme for the formation of 16alpha,17beta-estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=9.2 pmol/min/mg enzyme for the formation of 16beta,17beta-estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=174 pmol/min/mg enzyme for the formation of 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=4.3 pmol/min/mg enzyme for the formation of calcitriol 25-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18177842}; Note=Some kinetic parameters were assessed using commercial enzymes, which may represent a mix of both active and inactive protein forms, and therefore modify the kinetic values. {ECO:0000305|PubMed:18177842, ECO:0000305|PubMed:18719240};
| null | null | null |
FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:18719240, PubMed:23288867). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:18719240, PubMed:23288867). Catalyzes the glucuronidation of the endogenous estrogen hormones such as estradiol and estriol (PubMed:18719240, PubMed:23288867). {ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867}.
|
Homo sapiens (Human)
|
P06134
|
ADA_ECOLI
|
MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQQHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADLMFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIPCHRVVRGDGTLSGYRWGVSRKAQLLRREAENEER
|
2.1.1.63; 2.1.1.n11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
DNA damage response [GO:0006974]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA demethylation [GO:0080111]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]
| null |
DNA-binding transcription factor activity [GO:0003700]; methylated-DNA-[protein]-cysteine S-methyltransferase activity [GO:0003908]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
|
PF02805;PF01035;PF12833;PF02870;
|
3.40.10.10;1.10.10.60;3.30.160.70;1.10.10.10;
|
MGMT family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2'-deoxyribonucleoside 5'-methylphosphotriester)-DNA + L-cysteinyl-[protein] = 2'-deoxyribonucleotide-DNA + H(+) + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56324, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:14462, Rhea:RHEA-COMP:14463, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:140284, ChEBI:CHEBI:140286; EC=2.1.1.n11; Evidence={ECO:0000269|PubMed:2987862}; CATALYTIC ACTIVITY: Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63; Evidence={ECO:0000255|PROSITE-ProRule:PRU10017, ECO:0000269|PubMed:2987862}; CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387; EC=2.1.1.63; Evidence={ECO:0000255|PROSITE-ProRule:PRU10017, ECO:0000269|PubMed:2987862};
| null | null | null | null |
FUNCTION: Involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme (Cys-321). Also specifically repairs the Sp diastereomer of DNA methylphosphotriester lesions by the same mechanism, although the methyl transfer occurs onto a different cysteine residue (Cys-38). Cannot demethylate the other diastereomer, Rp-methylphosphotriester. This is a suicide reaction: the enzyme is irreversibly inactivated. {ECO:0000269|PubMed:2987862}.; FUNCTION: The methylation of Ada by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of its own gene, ada, and other alkylation resistance genes, alkA, alkB and aidB. {ECO:0000269|PubMed:2987862}.
|
Escherichia coli (strain K12)
|
P06136
|
FTSQ_ECOLI
|
MSQAALNTRNSEEEVSSRRNNGTRLAGILFLLTVLTTVLVSGWVVLGWMEDAQRLPLSKLVLTGERHYTRNDDIRQSILALGEPGTFMTQDVNIIQTQIEQRLPWIKQVSVRKQWPDELKIHLVEYVPIARWNDQHMVDAEGNTFSVPPERTSKQVLPMLYGPEGSANEVLQGYREMGQMLAKDRFTLKEAAMTARRSWQLTLNNDIKLNLGRGDTMKRLARFVELYPVLQQQAQTDGKRISYVDLRYDSGAAVGWAPLPPEESTQQQNQAQAEQQ
| null | null |
cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]
|
cell division site [GO:0032153]; divisome complex [GO:1990586]; FtsQBL complex [GO:1990587]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]
|
PF03799;PF08478;
|
3.40.50.11690;3.10.20.310;
|
FtsQ/DivIB family, FtsQ subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520, ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918, ECO:0000269|PubMed:9882666}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520, ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918, ECO:0000269|PubMed:9882666}. Note=Localizes to the division septum. Localization requires FtsZ, FtsA, ZipA and FtsK, but not FtsL, FtsI and FtsN. Insertion into the membrane requires YidC and the Sec translocase.
| null | null | null | null | null |
FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly. {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:17185541, ECO:0000269|PubMed:19233928}.
|
Escherichia coli (strain K12)
|
P06140
|
HA1B_RABIT
|
MGSIPPRTLLLLLAGALTLKDTQAGSHSMRYFYTSVSRPGLGEPRFIIVGYVDDTQFVRFDSDAASPRMEQRAPWMGQVEPEYWDQQTQIAKDTAQTFRVNLNTALRYYNQSAAGSHTFQTMFGCEVWADGRFFHGYRQYAYDGADYIALNEDLRSWTAADTAAQNTQRKWEAAGEAERHRAYLERECVEWLRRYLEMGKETLQRADPPKAHVTHHPASDREATLRCWALGFYPAEISLTWQRDGEDQTQDTELVETRPGGDGTFQKWAAVVVPSGEEQRYTCRVQHEGLPEPLTLTWEPPAQPTALIVGIVAGVLGVLLILGAVVAVVRRKKHSSDGKGGRYTPAAGGHRDQGSDDSLMP
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Oryctolagus cuniculus (Rabbit)
|
P06149
|
DLD_ECOLI
|
MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE
|
1.1.5.12
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233};
|
aerobic respiration [GO:0009060]; anaerobic respiration [GO:0009061]; lactate oxidation [GO:0019516]; respiratory electron transport chain [GO:0022904]; transmembrane transport [GO:0055085]
|
cytoplasmic side of plasma membrane [GO:0009898]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; plasma membrane [GO:0005886]
|
D-lactate dehydrogenase (quinone) activity [GO:0102029]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor [GO:0016901]; quinone binding [GO:0048038]
|
PF01565;PF09330;
|
3.30.465.10;3.30.70.610;3.30.1370.20;3.30.43.10;
|
Quinone-dependent D-lactate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688}. Note=May bind the membrane through electrostatic rather than hydrophobic forces. {ECO:0000305|PubMed:10944213}.
|
CATALYTIC ACTIVITY: Reaction=(R)-lactate + a quinone = a quinol + pyruvate; Xref=Rhea:RHEA:51468, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.12; Evidence={ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:7578233};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for D-lactate {ECO:0000269|PubMed:2185834};
| null | null | null |
FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. {ECO:0000269|PubMed:2185834, ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233}.
|
Escherichia coli (strain K12)
|
P06150
|
LDH_THECA
|
MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATPFAHPVWVRAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVVPRVLEAAPEAVLLVATNPVDVMTQVAYRLSALPPGRVVGSGTILDTARFRALLAEHLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRALSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVYTVSAFTPEVEGVLEVSLSLPRILGAGGVEGTVYPSLSPEEREALRRSAEILKEAAFALGF
|
1.1.1.27
| null |
glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089]
|
cytoplasm [GO:0005737]
|
L-lactate dehydrogenase activity [GO:0004459]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, LDH family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:25258319, ECO:0000269|PubMed:3377774, ECO:0000269|Ref.4, ECO:0000305|PubMed:6499843};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.02 mM for pyruvate (in the presence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:3377774}; KM=0.03 mM for NADH (in the presence and in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:3377774}; KM=0.04 mM for pyruvate (in the presence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:25258319}; KM=7.8 mM for pyruvate (in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:3377774}; KM=36 mM for pyruvate (in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:25258319}; Vmax=40.1 umol/min/mg enzyme with pyruvate as substrate (in the presence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:25258319}; Vmax=11 umol/min/mg enzyme with pyruvate as substrate (in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:25258319}; Note=kcat is 745 sec(-1) for pyruvate (in the presence of fructose 1,6-bisphosphate (FBP)). kcat is 131 sec(-1) for pyruvate (in the absence of fructose 1,6-bisphosphate (FBP)). {ECO:0000269|PubMed:3377774};
|
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
| null | null |
FUNCTION: Catalyzes the conversion of lactate to pyruvate. {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:25258319, ECO:0000269|PubMed:3377774, ECO:0000269|PubMed:6499843, ECO:0000269|Ref.4, ECO:0000305|PubMed:3533539}.
|
Thermus caldophilus
|
P06151
|
LDHA_MOUSE
|
MATLKDQLIVNLLKEEQAPQNKITVVGVGAVGMACAISILMKDLADELALVDVMEDKLKGEMMDLQHGSLFLKTPKIVSSKDYCVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPHCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWVLGEHGDSSVPVWSGVNVAGVSLKSLNPELGTDADKEQWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGINEDVFLSVPCILGQNGISDVVKVTLTPEEEARLKKSADTLWGIQKELQF
|
1.1.1.27
| null |
cellular response to extracellular stimulus [GO:0031668]; glucose catabolic process to lactate via pyruvate [GO:0019661]; lactate biosynthetic process from pyruvate [GO:0019244]; lactate metabolic process [GO:0006089]; liver development [GO:0001889]; NAD metabolic process [GO:0019674]; positive regulation of apoptotic process [GO:0043065]; pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090]; skeletal muscle tissue development [GO:0007519]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; sperm fibrous sheath [GO:0035686]
|
identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; lactate dehydrogenase activity [GO:0004457]; NAD binding [GO:0051287]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, LDH family
|
PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
|
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000250|UniProtKB:P00338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; Evidence={ECO:0000250|UniProtKB:P00338}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446; Evidence={ECO:0000250|UniProtKB:P00338};
| null |
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}.
| null | null |
FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000250|UniProtKB:P00338}.
|
Mus musculus (Mouse)
|
P06159
|
NCAP_PI3H4
|
MLSLFDTFNARRQENITKSAGGAIIPGQKNTVSIFALGPTITDDNEKMTLALLFLSHSLDNEKQHAQRAGFLVSLLSMAYANPELYLTTNGSNADVKYVIYMIEKDLKRQKYGGFVVKTREMIYEKTTEWIFGSDLDYDQETMLQNGRNNSTIEDLVHTFGYPSCLGALIIQIWIVLVKAITSISGLRKGFFTRLEAFRQDGTVQAGLVLSGDTVDQIGSIMRSQQSLVTLMVETLITMNTSRNDLTTIEKNIQIVGNYIRDAGLASFFNTIRYGIETRMAALTLSTLRPDINRLKALMELYLSKGPRAPFICILRDPIHGEFAPGNYPAIWSYAMGVAVVQNRAMQQYVTGRSYLDIDMFQLGQAVARDAEAQMSSTLEDELGVTHEAKESLKRHIRNINSSETSFHKPTGGSAIEMAIDEEPEQFEHRADQEQDGEPQSSIIQYAWAEGNRSDDRTEQATESDNIKTEQQNIRDRLNKRLNDKKKQGSQPSTNPTNRTNQDEIDDLFNAFGSN
| null | null | null |
helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF00973;
| null |
Paramyxoviruses nucleocapsid family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
| null | null | null | null | null |
FUNCTION: Forms the helical nucleocapsid (NC) in a ratio of 1 N per 6 ribonucleotides, protecting the genome from nucleases (Probable). The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (PubMed:10846069). Forms the encapsidation complex with the phosphoprotein protein P (PubMed:10846069). Before encapsidation, the newly synthesized free N protein, so-called N0, is chaperoned by P (PubMed:34730394). Together with P, inhibits the integrated stress response (ISR) in the infected cell via the formation of inclusion bodies (IBs) shielding its own newly synthesized viral RNAs (PubMed:29518158). Stress granule formation is thus blocked, which allows protein synthesis and viral replication (PubMed:29518158). {ECO:0000269|PubMed:10846069, ECO:0000269|PubMed:29518158, ECO:0000269|PubMed:34730394, ECO:0000305}.
|
Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human parainfluenza 3 virus (strain NIH 47885))
|
P06168
|
ILV5_YEAST
|
MLRTQAARLICNSRVITAKRTFALATRAAAYSRPAARFVKPMITTRGLKQINFGGTVETVYERADWPREKLLDYFKNDTFALIGYGSQGYGQGLNLRDNGLNVIIGVRKDGASWKAAIEDGWVPGKNLFTVEDAIKRGSYVMNLLSDAAQSETWPAIKPLLTKGKTLYFSHGFSPVFKDLTHVEPPKDLDVILVAPKGSGRTVRSLFKEGRGINSSYAVWNDVTGKAHEKAQALAVAIGSGYVYQTTFEREVNSDLYGERGCLMGGIHGMFLAQYDVLRENGHSPSEAFNETVEEATQSLYPLIGKYGMDYMYDACSTTARRGALDWYPIFKNALKPVFQDLYESTKNGTETKRSLEFNSQPDYREKLEKELDTIRNMEIWKVGKEVRKLRPENQ
|
1.1.1.86
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
|
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; mitochondrial genome maintenance [GO:0000002]; valine biosynthetic process [GO:0009099]
|
cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]
|
double-stranded DNA binding [GO:0003690]; ketol-acid reductoisomerase activity [GO:0004455]; metal ion binding [GO:0046872]
|
PF01450;PF07991;
|
3.40.50.720;
|
Ketol-acid reductoisomerase family
| null |
SUBCELLULAR LOCATION: Mitochondrion.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000305|PubMed:3027658}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22070; Evidence={ECO:0000305|PubMed:3027658}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13495; Evidence={ECO:0000305};
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000305|PubMed:3027658}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000305|PubMed:3027658}.
| null | null |
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes the second common step in the parallel biosynthesis of isoleucine and valine. Converts alpha-aceto-alpha-hydroxybutyrate (AHB) to alpha,beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-acetolactate (AL) to alpha,beta-dihydroxy-isovalerate (DHV) in isoleucine and valine biosynthesis, respectively. {ECO:0000305|PubMed:3027658}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06169
|
PDC1_YEAST
|
MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVEQAKLTAATNAKQ
|
4.1.1.-; 4.1.1.43; 4.1.1.72; 4.1.1.74
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10651824}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:10651824}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:10651824}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000269|PubMed:10651824};
|
aromatic amino acid family catabolic process to alcohol via Ehrlich pathway [GO:0000949]; branched-chain amino acid catabolic process [GO:0009083]; glycolytic fermentation to ethanol [GO:0019655]; L-phenylalanine catabolic process [GO:0006559]; pyruvate metabolic process [GO:0006090]; tryptophan catabolic process [GO:0006569]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
branched-chain-2-oxoacid decarboxylase activity [GO:0047433]; indolepyruvate decarboxylase activity [GO:0047434]; magnesium ion binding [GO:0000287]; phenylpyruvate decarboxylase activity [GO:0050177]; pyruvate decarboxylase activity [GO:0004737]; thiamine pyrophosphate binding [GO:0030976]
|
PF02775;PF00205;PF02776;
|
3.40.50.970;3.40.50.1220;
|
TPP enzyme family
|
PTM: Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1. {ECO:0000269|PubMed:10545125, ECO:0000269|PubMed:9298649}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; Evidence={ECO:0000269|PubMed:4687392}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2; Xref=Rhea:RHEA:54356, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:48943; EC=4.1.1.72; Evidence={ECO:0000269|PubMed:9748245}; CATALYTIC ACTIVITY: Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2; Xref=Rhea:RHEA:21108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16182, ChEBI:CHEBI:16526, ChEBI:CHEBI:35146; EC=4.1.1.72; Evidence={ECO:0000269|PubMed:10753893}; CATALYTIC ACTIVITY: Reaction=H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde; Xref=Rhea:RHEA:18017, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640, ChEBI:CHEBI:18086; EC=4.1.1.74; Evidence={ECO:0000269|PubMed:12499363}; CATALYTIC ACTIVITY: Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2; Xref=Rhea:RHEA:14185, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424, ChEBI:CHEBI:16526, ChEBI:CHEBI:18005; EC=4.1.1.43; Evidence={ECO:0000269|PubMed:12499363}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + H(+) = CO2 + propanal; Xref=Rhea:RHEA:55072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16763, ChEBI:CHEBI:17153; Evidence={ECO:0000269|PubMed:22904058}; CATALYTIC ACTIVITY: Reaction=2-oxopentanoate + H(+) = butanal + CO2; Xref=Rhea:RHEA:50312, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743, ChEBI:CHEBI:16526, ChEBI:CHEBI:28644; Evidence={ECO:0000269|PubMed:22904058, ECO:0000269|PubMed:23642236}; CATALYTIC ACTIVITY: Reaction=2 acetaldehyde = acetoin; Xref=Rhea:RHEA:54364, ChEBI:CHEBI:15343, ChEBI:CHEBI:15688; Evidence={ECO:0000269|PubMed:11141278, ECO:0000305|PubMed:6383467}; CATALYTIC ACTIVITY: Reaction=acetaldehyde + H(+) + pyruvate = acetoin + CO2; Xref=Rhea:RHEA:54368, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:15688, ChEBI:CHEBI:16526; Evidence={ECO:0000269|PubMed:11141278, ECO:0000305|PubMed:6383467};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 mM for pyruvate {ECO:0000269|PubMed:22904058}; KM=1 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058}; KM=1.5 mM for 2-oxopentanoate {ECO:0000269|PubMed:22904058}; Vmax=1.5 umol/min/mg enzyme for pyruvate {ECO:0000269|PubMed:22904058}; Vmax=0.5 umol/min/mg enzyme for 2-oxobutanoate {ECO:0000269|PubMed:22904058}; Vmax=0.4 umol/min/mg enzyme for 2-oxopentanoate {ECO:0000269|PubMed:22904058}; Vmax=38 umol/min/mg enzyme for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:22904058}; Vmax=15 umol/min/mg enzyme for 4-methyl-2-oxopentanoate {ECO:0000269|PubMed:22904058}; Vmax=9 umol/min/mg enzyme for 3-methyl-2-oxopentanoate {ECO:0000269|PubMed:22904058}; Vmax=41 umol/min/mg enzyme for 4-methylthio-2-oxobutanoate {ECO:0000269|PubMed:22904058};
|
PATHWAY: Fermentation; ethanol fermentation.; PATHWAY: Amino-acid degradation; Ehrlich pathway.
| null | null |
FUNCTION: Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. {ECO:0000269|PubMed:10231381, ECO:0000269|PubMed:10234824, ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:11141278, ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:12902239, ECO:0000269|PubMed:22904058, ECO:0000269|PubMed:4687392, ECO:0000269|PubMed:8866484, ECO:0000269|PubMed:9341119, ECO:0000269|PubMed:9748245}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06181
|
LIG8_PHACH
|
MAFKQLFAAISLALLLSAANAAAVIEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFVQKHGVTPGDFIAFAGRVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHTVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSRTACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIPGNLPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA
|
1.11.1.14
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:16593451}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:16593451};
|
cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lignin catabolic process [GO:0046274]; response to reactive oxygen species [GO:0000302]
| null |
diarylpropane peroxidase activity [GO:0016690]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00141;PF11895;
|
1.10.520.10;1.10.420.10;
|
Peroxidase family, Ligninase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O; Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591, ChEBI:CHEBI:86963; EC=1.11.1.14; Evidence={ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054}; CATALYTIC ACTIVITY: Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150, ChEBI:CHEBI:88143; EC=1.11.1.14; Evidence={ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for H(2)O(2) {ECO:0000269|PubMed:2303054}; KM=116 uM for (3,4-dimethoxyphenyl)methanol {ECO:0000269|PubMed:3240864}; KM=30 uM for H(2)O(2) {ECO:0000269|PubMed:16593451};
|
PATHWAY: Secondary metabolite metabolism; lignin degradation.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3. {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054};
| null |
FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054}.
|
Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
|
P06186
|
PRGR_RABIT
|
MTELKAKEPRAPHVAGGAPSPTEVGSQLLGRPDPGPFQGSQTSEASSVVSAIPISLDGLLFPRPCQGQNPPDGKTQDPPSLSDVEGAFPGVEAPEGAGDSSSRPPEKDSGLLDSVLDTLLAPSGPGQSHASPATCEAISPWCLFGPDLPEDPRAAPATKGVLAPLMSRPEDKAGDSSGTAAAHKVLPRGLSPSRQLLLPSSGSPHWPAVKPSPQPAAVQVDEEDSSESEGTVGPLLKGQPRALGGTAAGGGAAPVASGAAAGGVALVPKEDSRFSAPRVSLAEQDAPVAPGRSPLATSVVDFIHVPILPLNHAFLATRTRQLLEGESYDGGAAAASPFVPQRGSPSASSTPVAGGDFPDCTYPPDAEPKDDAFPLYGDFQPPALKIKEEEEAAEAAARSPRTYLVAGANPAAFPDFQLAAPPPPSLPPRVPSSRPGEAAVAASPGSASVSSSSSSGSTLECILYKAEGAPPQQGPFAPLPCKPPGAGACLLPRDGLPSTSASGAAAGAAPALYPTLGLNGLPQLGYQAAVLKEGLPQVYTPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVMRALDAVALPQPVGIPNESQRITFSPSQEIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQSQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
| null | null |
glandular epithelial cell maturation [GO:0002071]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:0042326]; ovulation from ovarian follicle [GO:0001542]; paracrine signaling [GO:0038001]; progesterone receptor signaling pathway [GO:0050847]; regulation of epithelial cell proliferation [GO:0050678]; tertiary branching involved in mammary gland duct morphogenesis [GO:0060748]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATPase binding [GO:0051117]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; estrogen response element binding [GO:0034056]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]; transcription coactivator binding [GO:0001223]; zinc ion binding [GO:0008270]
|
PF00104;PF02161;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-293 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-387. Phosphorylation on Ser-102 and Ser-344 also requires induction by hormone. Basal phosphorylation on Ser-82, Ser-191 and Ser-399 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-399 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-293, but not at Ser-191, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-344 by ERK1/2 MAPK is required for interaction with SP1 (By similarity). {ECO:0000250}.; PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-387, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-293 (By similarity). {ECO:0000250}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-293 (By similarity). {ECO:0000250}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000250|UniProtKB:P06401}.
|
Oryctolagus cuniculus (Rabbit)
|
P06191
|
ALR2_SALTY
|
MTRPIQASLDLQVMKQNLAIVRRAAPEARVWSVVKANAYGHGIERVWSALGATDGFAMLNLEEAITLRERGWKGPILMLEGFFHAQDLEAYDTYRLTTCIHSNWQLKALQNARLNAPLDIYVKVNSGMNRLGFQPERAQTVWQQLRAMRNVGEMTLMSHFAQADHPEGIGEAMRRIALATEGLQCAYSLSNSAATLWHPQAHYDWVRPGIILYGASPSGQWRDIADTGLKPVMTLSSEIIGVQTLSAGERVGYGGGYSVTQEQRIGIVAAGYADGYPRHAPTGTPVLVDGIRTRTVGTVSMDMLAVDLTPCPQAGIGTPVELWGKEIKVDDVASAAGTLGYELLCAVAPRVPFVTT
|
5.1.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6391537, ECO:0000269|PubMed:6439236};
|
D-alanine biosynthetic process [GO:0030632]; peptidoglycan biosynthetic process [GO:0009252]
|
cytosol [GO:0005829]
|
alanine racemase activity [GO:0008784]; pyridoxal phosphate binding [GO:0030170]
|
PF00842;PF01168;
|
3.20.20.10;
|
Alanine racemase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000269|PubMed:6391537};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for D-alanine {ECO:0000269|PubMed:6391537}; KM=8.2 mM for L-alanine {ECO:0000269|PubMed:6391537};
| null | null | null |
FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. {ECO:0000269|PubMed:6391537}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P06197
|
PIS_YEAST
|
MSSNSTPEKVTAEHVLWYIPNKIGYVRVITAALSFFVMKNHPTAFTWLYSTSCLLDALDGTMARKYNQVSSLGAVLDMVTDRSSTAGLMCFLCVQYPQWCVFFQLMLGLDITSHYMHMYASLSAGKTSHKSVGEGESRLLHLYYTRRDVLFTICAFNELFYAGLYLQLFSNSATFGKWTTIISFPGYVFKQTANVVQLKRAALILADNDAKNANEKNKTY
|
2.7.8.11
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Note=Divalent metal cations; Mn(2+) or Mg(2+). {ECO:0000250|UniProtKB:Q59RA2};
|
phosphatidylinositol biosynthetic process [GO:0006661]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity [GO:0003881]; metal ion binding [GO:0046872]
|
PF01066;
|
1.20.120.1760;
|
CDP-alcohol phosphatidyltransferase class-I family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25687304}; Multi-pass membrane protein {ECO:0000305|PubMed:25687304}. Mitochondrion outer membrane {ECO:0000269|PubMed:16823961}; Multi-pass membrane protein {ECO:0000269|PubMed:16823961}.
|
CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; Evidence={ECO:0000305|PubMed:25687304};
| null | null | null | null |
FUNCTION: Catalyzes the synthesis of phosphatidylinositol (PtdIns). {ECO:0000269|PubMed:25687304}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06199
|
ACM2_PIG
|
MNNSTNSSNSGLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQEPVSPSLVQGRIVKPNNNNMPGSDEALEHNKIQNGKAPRDAVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENSKQTCIKIVTKTQKSDSCTPANTTVELVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR
| null | null |
adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; regulation of heart contraction [GO:0008016]; regulation of smooth muscle contraction [GO:0006940]
|
dendrite [GO:0030425]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM2 sub-subfamily
|
PTM: Phosphorylated in response to agonist treatment. {ECO:0000269|PubMed:9228066}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20976005, ECO:0000305|PubMed:3107123, ECO:0000305|PubMed:9228066}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000269|PubMed:9228066}.
| null | null | null | null | null |
FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. {ECO:0000269|PubMed:9228066}.
|
Sus scrofa (Pig)
|
P06202
|
OPPA_SALTY
|
MSNITKKSLIAAGILTALIAASAATAADVPAGVQLADKQTLVRNNGSEVQSLDPHKIEGVPESNVSRDLFEGLLISDVEGHPSPGVAEKWENKDFKVWTFHLRENAKWSDGTPVTAHDFVYSWQRLADPNTASPYASYLQYGHIANIDDIIAGKKPATDLGVKALDDHTFEVTLSEPVPYFYKLLVHPSVSPVPKSAVEKFGDKWTQPANIVTNGAYKLKNWVVNERIVLERNPQYWDNAKTVINQVTYLPISSEVTDVNRYRSGEIDMTYNNMPIELFQKLKKEIPNEVRVDPYLCTYYYEINNQKAPFNDVRVRTALKLALDRDIIVNKVKNQGDLPAYSYTPPYTDGAKLVEPEWFKWSQQKRNEEAKKLLAEAGFTADKPLTFDLLYNTSDLHKKLAIAVASIWKKNLGVNVNLENQEWKTFLDTRHQGTFDVARAGWCADYNEPTSFLNTMLSDSSNNTAHYKSPAFDKLIADTLKVADDTQRSELYAKAEQQLDKDSAIVPVYYYVNARLVKPWVGGYTGKDPLDNIYVKNLYIIKH
| null | null |
peptide transport [GO:0015833]; protein transport [GO:0015031]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; outer membrane-bounded periplasmic space [GO:0030288]
|
peptide transmembrane transporter activity [GO:1904680]
|
PF00496;
|
3.40.190.10;
|
Bacterial solute-binding protein 5 family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2821267, ECO:0000269|PubMed:3525163}.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex OppABCDF involved in the uptake of oligopeptides, including the cell wall murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate (PubMed:2821267, PubMed:3301822). Plays an important nutritional role and is involved in the recycling of cell wall peptides (PubMed:2821267, PubMed:3301822). Binds peptides containing from two to five amino acid residues regardless of their sequence (PubMed:10438628, PubMed:8202710, PubMed:8747465, PubMed:8946852, PubMed:9245406). Also binds cell wall peptides, such as L-alanyl-gamma-D-glutamyl-meso-diaminopimelate (PubMed:3301822). {ECO:0000269|PubMed:10438628, ECO:0000269|PubMed:2821267, ECO:0000269|PubMed:3301822, ECO:0000269|PubMed:8202710, ECO:0000269|PubMed:8747465, ECO:0000269|PubMed:8946852, ECO:0000269|PubMed:9245406}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P06208
|
LEU1_YEAST
|
MVKESIIALAEHAASRASRVIPPVKLAYKNMLKDPSSKYKPFNAPKLSNRKWPDNRITRAPRWLSTDLRDGNQSLPDPMSVEQKKEYFHKLVNIGFKEIEVSFPSASQTDFDFTRYAVENAPDDVSIQCLVQSREHLIKRTVEALTGAKKATIHTYLATSDMFREIVFNMSREEAISKAVEATKLVRKLTKDDPSQQATRWSYEFSPECFSDTPGEFAVEICEAVKKAWEPTEENPIIFNLPATVEVASPNVYADQIEYFATHITEREKVCISTHCHNDRGCGVAATELGMLAGADRVEGCLFGNGERTGNVDLVTVAMNMYTQGVSPNLDFSDLTSVLDVVERCNKIPVSQRAPYGGDLVVCAFSGSHQDAIKKGFNLQNKKRAQGETQWRIPYLPLDPKDIGRDYEAVIRVNSQSGKGGAAWVILRSLGLDLPRNMQIEFSSAVQDHADSLGRELKSDEISKLFKEAYNYNDEQYQAISLVNYNVEKFGTERRVFTGQVKVGDQIVDIEGTGNGPISSLVDALSNLLNVRFAVANYTEHSLGSGSSTQAASYIHLSYRRNADNEKAYKWGVGVSEDVGDSSVRAIFATINNIIHSGDVSIPSLAEVEGKNAAASGSA
|
2.3.3.13
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P9WQB3, ECO:0000250|UniProtKB:Q9JZG1};
|
amino acid biosynthetic process [GO:0008652]; leucine biosynthetic process [GO:0009098]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
2-isopropylmalate synthase activity [GO:0003852]; metal ion binding [GO:0046872]
|
PF00682;PF08502;
|
3.30.160.270;3.20.20.70;
|
Alpha-IPM synthase/homocitrate synthase family, LeuA type 2 subfamily
| null |
SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:3275644}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:3275644}.
|
CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; Evidence={ECO:0000269|PubMed:3275644}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21525; Evidence={ECO:0000269|PubMed:3275644};
| null |
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000305|PubMed:3275644}.
| null | null |
FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000269|PubMed:10790691, ECO:0000269|PubMed:3275644}.
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Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06209
|
POLG_POL32
|
MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYKDSASNAASKQDYSQDPSKFTEPLKDVLIKTAPALNSPNVEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATSRFYTLDTVMWGKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGSLGVFAIPEFCLAGDSDTQRYTSYANANPGEKGGKFYAQFNKDTAVTSPKREFCPVDYLLGCGVLIGNAFVFPHQIINLRTNNSATLVLPYVNALSIDSMVKHNNWGIAILPLSPLDFAQDSSVEIPITVTIAPMCSEFNGLRNVTAPKLQGLPVLNTPGSNQYLTSDNHQSPCAIPEFDVTPPIDIPGEVKNVMELAEIDTMIPLNLENTKRNTMDMYRVRLSDSANLSGPILCLSLSPAADPRLSHTMLGEVLNYYTHWAGSLKFTFLFCGSMMATGKLLVAYAPPGAQPPTSRKEAMLGTHVIWDLGLQSSCTMVVPWISNVTYRQTTQDSFTEGGYISMFYQTRIVVPLSTPKAMDMLGFVSACNDFSVRLLRDTTHISQAAMPQGVDDLITEVAQNALALSLPKPQSNLPDTKASGPAHSKEVPTLTAVETGATNPLVPSDTVQTRHVIQQRSRSESTIESFFARGACVAIIEVDNEQPATNVQKLFATWRITYKDTVQLRRKLEFFTYSRFDMEFTFVVTANFTNSNNGHALNQVYQIMYIPPGAPTPKSWDDYTWQTSSNPSIFYTYGAAPARISVPYVGLANAYSHFYDGFAKVPLKSDANDQVGDSLYSAMAVDDFGVLAIRVVNDHNPTKVTSKVRVYMKPKHVRVWCPRPPRAVPYYGPGVDYKDGLAPLSEKGLTTYGFGHQNKAVYTAGYKICNYHLATQEDLQNAVSVMWNRDLLVTESKAQGIDSIARCNCSTGVYYCESRSRYYPVSFVGPTFQYMEANDYYPARYQSHMLIGHGFASPGDCGGILRCQHGVIGIITAGGEGLVAFSDIRDLYAYEEEAMEQGISSYVESLGAAFGSGFTQQIGDKIIELTGMVTSTITEKLLKNLIKIVSSLVIITRNYDDTTTVLATLALLGCDVSPWQWLKKKACDILEIPYVMRQGDSWLKKFTEACNAAKGLEWVSNKISKFIDWLREKIIPQARDKLEFVTKLKQLEMLENQIATIHQSCPSQEHQEILFNNVRWLSIQSKRFAPLYALEAKRIQKLEHTINNYIQFKSKHRIEPVCLLVHGSPGTGKSVATNLIARAIAEKENTSTYSLPPDPSHFDGYKQQGVVIMDDLNQNPDGADMKLFCQMVSTVEFIPPMASLEEKGILFTSNYVLASTNSSRITPPTVAHSDALARRFAFDMDIQVMSEYSRDGKLNMTMATEMCKNCHQPANFKRCCPLVCGKAIQLMDKSSRVRYSIDQITTMIVNEKNRRSNIGNCMEALFQGPLQYKDLKIDIKTTPPPECINDLLQAVDSQEVRDYCEKKGWIVNITSQVQTERNINRAMTILQAVTTFAAVAGVVYVMYKLFAGHQGAYTGLPNKRPNVPTIRTAKVQGPGFDYAVAMAKRNILTATTSKGEFTMLGVHDNVAILPTHASPGETIVIDGKEIEVLDAKALEDQAGTNLEITIVTLKRNEKFRDIRPHIPAQITETNDGVLIVNTSKYPNMYVPVGAVTEQGYLNLGGRQTARTLMYNFPTRAGQCGGVITCTGKVIGMHVGGNGSHGFAAALKRSYFTQSQGEIQWMRPSKEVGYPIINAPSKTKLEPSAFHYVFEGVKEPAVLTKNDPRFKTGFEEAIFSKYVGNKITEVDEYMKEAVDHYAGQLMSLDINTEQMCLEDAMYGTDGLEALDLSTSAGYPYVTMGKKKRDILNKQTRDTKEMQRLLDTYGINLPLVTYVKDELRSKTKVEQGKSRLIEASSLNDSVAMRMAFGNLYAAFHKNPGVVTGSAVGCDPDLFWSKIPVLMEEKLFAFDYTGYDASLSPAWFEALKMVLEKIGFGDRVDYIDYLNHSHHLYKNKTYCVKGGMPSGCSGTSIFNSMINNLIIRTLLLKTYKGIDLDHLKMIAYGDDVIASYPHEVDASLLAQSGKDYGLTMTPADKSATFETVTWENVTFLKRFFRADERYPFLIHPVMPMKEIHESIRWTKDPRNTQDHVRSLCLLAWHNGEDEYNKFLAMIRSVPIGRALLLPEYSTLYRRWLDSF
|
2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15
|
COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313};
|
DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont genome entry into host cell via pore formation in plasma membrane [GO:0044694]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity [GO:0039554]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
|
PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910;
|
1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10;
|
Picornaviruses polyprotein family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
|
SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.; SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
|
CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
| null | null | null | null |
FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153 (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Cleaves host RIGI and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by cleaving host G3BP1 (By similarity). Stress granule formation is thus inhibited, which allows protein synthesis and viral replication (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
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Poliovirus type 3 (strain 23127)
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P06210
|
POLG_POL2L
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MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFAQDPSKFTEPIKDVLIKTAPTLNSPNIEACGYSDRVMQLTLGNSTITTQEAANSVVAYGRWPEYIKDSEANPVDQPTEPDVAACRFYTLDTVTWRKESRGWWWKLPDALKDMGLFGQNMFYHYLGRAGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSTTHMFTKYENANPGEKGGEFKGSFTLDTNATNPARNFCPVDYLFGSGVLAGNAFVYPHQIINLRTNNCATLVLPYVNSLSIDSMTKHNNWGIAILPLAPLDFATESSTEIPITLTIAPMCCEFNGLRNITVPRTQGLPVLNTPGSNQYLTADNYQSPCAIPEFDVTPPIDIPGEVRNMMELAEIDTMIPLNLTNQRKNTMDMYRVELNDAAHSDTPILCLSLSPASDPRLAHTMLGEILNYYTHWAGSLKFTFLFCGSMMATGKLLVSYAPPGAEAPKSRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTINDSFTEGGYISMFYQTRVVVPLSTPRKMDILGFVSACNDFSVRLLRDTTHISQEAMPQGLGDLIEGVVEGVTRNALTPLTPANNLPDTQSSGPAHSKETPALTAVETGATNPLVPSDTVQTRHVIQKRTRSESTVESFFARGACVAIIEVDNDAPTKRASKLFSVWKITYKDTVQLRRKLEFFTYSRFDMEFTFVVTSNYTDANNGHALNQVYQIMYIPPGAPIPGKWNDYTWQTSSNPSVFYTYGAPPARISVPYVGIANAYSHFYDGFAKVPLAGQASTEGDSLYGAASLNDFGSLAVRVVNDHNPTKLTSKIRVYMKPKHVRVWCPRPPRAVPYYGPGVDYKDGLAPLPGKGLTTYGFGHQNKAVYTAGYKICNYHLATQEDLQNAVNIMWIRDLLVVESKAQGIDSIARCNCHTGVYYCESRRKYYPVSFTGPTFQYMEANEYYPARYQSHMLIGHGFASPGDCGGILRCQHGVIGIITAGGEGLVAFSDIRDLYAYEEEAMEQGVSNYIESLGAAFGSGFTQQIGNKISELTSMVTSTITEKLLKNLIKIISSLVIITRNYEDTTTVLATLALLGCDASPWQWLKKKACDILEIPYIMRQGDSWLKKFTEACNAAKGLEWVSNKISKFIDWLKEKIIPQARDKLEFVTKLKQLEMLENQIATIHQSCPSQEHQEILFNNVRWLSIQSKRFAPLYAVEAKRIQKLEHTINNYVQFKSKHRIEPVCLLVHGSPGTGKSVATNLIARAIAEKENTSTYSLPPDPSHFDGYKQQGVVIMDDLNQNPDGADMKLFCQMVSTVEFIPPMASLEEKGILFTSNYVLASTNSSRITPPTVAHSDALARRFAFDMDIQIMSEYSRDGKLNMAMATEMCKNCHHPANFKRCCPLVCGKAIQLMDKSSRVRYSIDQITTMIINERNRRSSIGNCMEALFQGPLQYKDLKIDIKTTPPPECINDLLQAVDSQEVRDYCEKKGWIVDITSQVQTERNINRAMTILQAVTTFAAVAGVVYVMYKLFAGHQGAYTGLPNKRPNVPTIRTAKVQGPGFDYAVAMAKRNILTATTIKGEFTMLGVHDNVAILPTHASPGETIVIDGKEVEVLDAKALEDQAGTNLEITIVTLKRNEKFRDIRPHIPTQITETNDGVLIVNTSKYPNMYVPVGAVTEQGYLNLSGRQTARTLMYNFPTRAGQCGGVITCTGKVIGMHVGGNGSHGFAAALKRSYFTQSQGEIQWMRPSKEVGYPVINAPSKTKLEPSAFHYVFEGVKEPAVLTKSDPRLKTDFEEAIFSKYVGNKITEVDEYMKEAVDHYAGQLMSLDINTEQMCLEDAMYGTDGLEALDLSTSAGYPYVAMGKKKRDILNKQTRDTKEMQRLLDTYGINLPLVTYVKDELRSKTKVEQGKSRLIEASSLNDSVAMRMAFGNLYAAFHKNPGVVTGSAVGCDPDLFWSKIPVLMEEKLFAFDYTGYDASLSPAWFEALKMVLEKIGFGDRVDYIDYLNHSHHLYKNKTYCVKGGMPSGCSGTSIFNSMINNLIIRTLLLKTYKGIDLDHLKMIAYGDDVIASYPHEVDASLLAQSGKDYGLTMTPADKSATFETVTWENVTFLKRFFRADEKYPFLVHPVMPMKEIHESIRWTKDPRNTQDHVRSLCLLAWHNGEEEYNKFLAKIRSVPIGRALLLPEYSTLYRRWLDSF
|
2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15
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COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313};
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DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont genome entry into host cell via pore formation in plasma membrane [GO:0044694]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity [GO:0039554]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
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ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
|
PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910;
|
1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10;
|
Picornaviruses polyprotein family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
|
SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.; SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
|
CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
| null | null | null | null |
FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153 (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3CD]: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Cleaves host RIGI and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by cleaving host G3BP1 (By similarity). Stress granule formation is thus inhibited, which allows protein synthesis and viral replication (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
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Poliovirus type 2 (strain Lansing)
|
P06211
|
ESR1_RAT
|
MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPAVFNYPEGAAYEFNAAAAAAAAGASAPVYGQSSITYGPGSEAAAFGANSLGAFPQLNSVSPSPLMLLHPPPHVSPFLHPHGHQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSSEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGTSGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPLIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKINDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQSQLTTTSSTSAHSLQTYYIPPEAEGFPNTI
| null | null |
androgen metabolic process [GO:0008209]; antral ovarian follicle growth [GO:0001547]; baculum development [GO:1990375]; cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; cellular response to wortmannin [GO:1904568]; decidualization [GO:0046697]; epithelial cell development [GO:0002064]; epithelial cell proliferation involved in mammary gland duct elongation [GO:0060750]; fibroblast proliferation [GO:0048144]; intracellular estrogen receptor signaling pathway [GO:0030520]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; male gonad development [GO:0008584]; mammary gland alveolus development [GO:0060749]; mammary gland branching involved in pregnancy [GO:0060745]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of gene expression [GO:0010629]; negative regulation of glucose import [GO:0046325]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of triglyceride metabolic process [GO:0090209]; osteoblast development [GO:0002076]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of phospholipase C activity [GO:0010863]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis [GO:0060527]; prostate epithelial cord elongation [GO:0060523]; protein localization to chromatin [GO:0071168]; regulation of branching involved in prostate gland morphogenesis [GO:0060687]; regulation of DNA-templated transcription [GO:0006355]; regulation of epithelial cell apoptotic process [GO:1904035]; regulation of inflammatory response [GO:0050727]; regulation of toll-like receptor signaling pathway [GO:0034121]; regulation of transcription by RNA polymerase II [GO:0006357]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]; RNA polymerase II preinitiation complex assembly [GO:0051123]; Sertoli cell development [GO:0060009]; Sertoli cell proliferation [GO:0060011]; stem cell differentiation [GO:0048863]; transcription by RNA polymerase II [GO:0006366]; uterus development [GO:0060065]; vagina development [GO:0060068]
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chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; T-tubule [GO:0030315]; terminal bouton [GO:0043195]; transcription regulator complex [GO:0005667]
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14-3-3 protein binding [GO:0071889]; ATPase binding [GO:0051117]; beta-catenin binding [GO:0008013]; calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; estrogen response element binding [GO:0034056]; hormone binding [GO:0042562]; identical protein binding [GO:0042802]; nuclear estrogen receptor activity [GO:0030284]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; promoter-specific chromatin binding [GO:1990841]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; steroid binding [GO:0005496]; TBP-class protein binding [GO:0017025]; TFIIB-class transcription factor binding [GO:0001093]; transcription coactivator binding [GO:0001223]; transcription coregulator binding [GO:0001221]; transcription corepressor binding [GO:0001222]; type 1 metabotropic glutamate receptor binding [GO:0031798]; zinc ion binding [GO:0008270]
|
PF12743;PF00104;PF02159;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-123 by PPP5C inhibits its transactivation activity (By similarity). Phosphorylated by LMTK3 (in vitro) (By similarity). {ECO:0000250|UniProtKB:P03372}.; PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation (By similarity). Deubiquitinated by OTUB1 (By similarity). Ubiquitinated by STUB1/CHIP; in the CA1 hippocampal region following loss of endogenous circulating estradiol (17-beta-estradiol/E2) (PubMed:21808025). {ECO:0000250|UniProtKB:P03372, ECO:0000269|PubMed:21808025}.; PTM: Palmitoylated at Cys-452 by ZDHHC7 and ZDHHC21. This modification is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor (By similarity). {ECO:0000250}.; PTM: Dimethylated by PRMT1 at Arg-265. The methylation may favor cytoplasmic localization. Demethylated by JMJD6 at Arg-265. {ECO:0000250|UniProtKB:P03372}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity). Maintains neuronal survival in response to ischemic reperfusion injury when in the presence of circulating estradiol (17-beta-estradiol/E2) (PubMed:21808025). {ECO:0000250, ECO:0000269|PubMed:21808025}.
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Rattus norvegicus (Rat)
|
P06212
|
ESR1_CHICK
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MTMTLHTKASGVTLLHQIQGTELETLSRPQLKIPLERSLSDMYVESNKTGVFNYPEGATYDFGTTAPVYGSTTLSYAPTSESFGSSSLAGFHSLNNVPPSPVVFLQTAPQLSPFIHHHSQQVPYYLENEQGSFGMREAAPPAFYRPSSDNRRHSIRERMSSTNEKGSLSMESTKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGEMMKQKRQREEQDSRNGEASSTELRAPTLWTSPLVVKHNKKNSPALSLTAEQMVSALLEAEPPIVYSEYDPNRPFNEASMMTLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATAARFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEERDYIHRVLDKITDTLIHLMAKSGLSLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPAARSAAPMEEENRNQLTTAPASSHSLQSFYINSKEEESMQNTI
| null | null |
cellular response to estrogen stimulus [GO:0071391]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of gene expression [GO:0010628]; regulation of transcription by RNA polymerase II [GO:0006357]
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cytoplasm [GO:0005737]; nucleus [GO:0005634]
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estrogen response element binding [GO:0034056]; Hsp90 protein binding [GO:0051879]; nuclear estrogen receptor activity [GO:0030284]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270]
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PF12743;PF00104;PF02159;PF00105;
|
3.30.50.10;1.10.565.10;
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Nuclear hormone receptor family, NR3 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
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Gallus gallus (Chicken)
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P06213
|
INSR_HUMAN
|
MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENKAPESEELEMEFEDMENVPLDRSSHCQREEAGGRDGGSSLGFKRSYEEHIPYTHMNGGKKNGRILTLPRSNPS
|
2.7.10.1
| null |
activation of protein kinase activity [GO:0032147]; activation of protein kinase B activity [GO:0032148]; adrenal gland development [GO:0030325]; amyloid-beta clearance [GO:0097242]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; dendritic spine maintenance [GO:0097062]; epidermis development [GO:0008544]; exocrine pancreas development [GO:0031017]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; heart morphogenesis [GO:0003007]; insulin receptor signaling pathway [GO:0008286]; learning [GO:0007612]; male gonad development [GO:0008584]; male sex determination [GO:0030238]; memory [GO:0007613]; neuron projection maintenance [GO:1990535]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of developmental growth [GO:0048639]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of receptor internalization [GO:0002092]; positive regulation of respiratory burst [GO:0060267]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of female gonad development [GO:2000194]; symbiont entry into host cell [GO:0046718]; transport across blood-brain barrier [GO:0150104]
|
axon [GO:0030424]; caveola [GO:0005901]; dendrite membrane [GO:0032590]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; insulin receptor complex [GO:0005899]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
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amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; cargo receptor activity [GO:0038024]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein domain specific binding [GO:0019904]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; PTB domain binding [GO:0051425]
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PF00041;PF00757;PF17870;PF07714;PF01030;
|
2.60.40.10;3.80.20.20;1.10.510.10;
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Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
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PTM: After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. {ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222}.; PTM: Autophosphorylated on tyrosine residues in response to insulin. Phosphorylation of Tyr-999 is required for binding to IRS1, SHC1 and STAT5B. Dephosphorylated by PTPRE at Tyr-999, Tyr-1185, Tyr-1189 and Tyr-1190. Dephosphorylated by PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates insulin-induced signaling. Dephosphorylation at Tyr-1189 and Tyr-1190 requires the SH2/SH3 adapter protein NCK1, probably to recruit its interaction partner PTPN1 (PubMed:21707536). {ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:21707536, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016}.; PTM: S-nitrosylation at Cys-1083 by BLVRB inhibits the receptor tyrosine kinase, thereby inhibiting insulin signaling. {ECO:0000269|PubMed:38056462}.
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SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15208}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000250|UniProtKB:P15208}. Lysosome {ECO:0000250|UniProtKB:P15208}. Note=Binding of insulin to INSR induces internalization and lysosomal degradation of the receptor, a means for down-regulating this signaling pathway after stimulation. In the presence of SORL1, internalized INSR molecules are redirected back to the cell surface, thereby preventing their lysosomal catabolism and strengthening insulin signal reception. {ECO:0000250|UniProtKB:P15208}.
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CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:11124964, ECO:0000269|PubMed:11598120, ECO:0000269|PubMed:12707268, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:19056263, ECO:0000269|PubMed:19071018, ECO:0000269|PubMed:19394223, ECO:0000269|PubMed:9312016};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. In adipocytes, inhibits lipolysis (By similarity). {ECO:0000250|UniProtKB:P15208, ECO:0000269|PubMed:12138094, ECO:0000269|PubMed:16314505, ECO:0000269|PubMed:16831875, ECO:0000269|PubMed:8257688, ECO:0000269|PubMed:8276809, ECO:0000269|PubMed:8452530, ECO:0000269|PubMed:9428692}.
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Homo sapiens (Human)
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