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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P04739
|
PILA_PSEAE
|
MKAQKGFTLIELMIVVAIIGILAAIAIPQYQNYVARSEGASALATINPLKTTVEESLSRGIAGSKIKIGTTASTATETYVGVEPDANKLGVIAVAIEDSGAGDITFTFQTGTSSPKNATKVITLNRTADGVWACKSTQDPMFTPKGCDN
| null | null |
cell adhesion involved in single-species biofilm formation [GO:0043709]; regulation of calcium-mediated signaling [GO:0050848]; single-species biofilm formation on inanimate substrate [GO:0044011]; type IV pilus-dependent motility [GO:0043107]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; host cell endoplasmic reticulum membrane [GO:0044167]; pilus [GO:0009289]; plasma membrane [GO:0005886]; type IV pilus [GO:0044096]
| null |
PF07963;PF00114;
|
3.30.700.10;
|
N-Me-Phe pilin family
|
PTM: Methylated by prepilin peptidase PilD at the amino group of the N-terminal phenylalanine once the leader sequence is cleaved. {ECO:0000269|PubMed:1429457}.
|
SUBCELLULAR LOCATION: Fimbrium. Cell inner membrane {ECO:0000269|PubMed:27162347}; Single-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23266901}.
| null | null | null | null | null |
FUNCTION: Major component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:26041805, PubMed:31431558, PubMed:9282737). In addition, plays a critical role in type II secretion of exoenzymes by interacting with specific components such as XcpT or XcpU (PubMed:9282737). Modulates host calcium signaling through interaction with host calcium-modulating cyclophilin ligand (PubMed:23266901). {ECO:0000269|PubMed:23266901, ECO:0000269|PubMed:26041805, ECO:0000269|PubMed:31431558, ECO:0000269|PubMed:9282737}.
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
P04746
|
AMYP_HUMAN
|
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097, ECO:0000269|PubMed:8528071}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097, ECO:0000269|PubMed:8528071}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097, ECO:0000269|PubMed:8528071}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097, ECO:0000269|PubMed:8528071};
|
carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975]; polysaccharide digestion [GO:0044245]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404]
|
PF00128;PF02806;
|
3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097};
| null | null | null | null | null |
Homo sapiens (Human)
|
P04751
|
ACTC_XENLA
|
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIQRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
|
3.6.4.-
| null |
actin filament organization [GO:0007015]; actin-myosin filament sliding [GO:0033275]; heart contraction [GO:0060047]; mesenchyme migration [GO:0090131]; positive regulation of gene expression [GO:0010628]
|
actin filament [GO:0005884]; cell body [GO:0044297]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; sarcomere [GO:0030017]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; myosin binding [GO:0017022]
|
PF00022;
|
3.30.420.40;
|
Actin family
|
PTM: [Actin, alpha cardiac muscle 1, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. {ECO:0000250|UniProtKB:P68033}.; PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000250|UniProtKB:P68033}.; PTM: Monomethylation at Lys-86 (K86me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P68032}.; PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68032}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137};
| null | null | null | null |
FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility.
|
Xenopus laevis (African clawed frog)
|
P04756
|
ACHA_MOUSE
|
MELSTVLLLLGLCSAGLVLGSEHETRLVAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPTTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHIMPEWVRKVFIDTIPNIMFFSTMKRPSRDKQEKRIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGVKYIAETMKSDQESNNAAEEWKYVAMVMDHILLGVFMLVCLIGTLAVFAGRLIELHQQG
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell cellular homeostasis [GO:0046716]; neuromuscular junction development [GO:0007528]; neuromuscular synaptic transmission [GO:0007274]; neuron cellular homeostasis [GO:0070050]; neuronal action potential [GO:0019228]; regulation of membrane potential [GO:0042391]; response to nicotine [GO:0035094]; skeletal muscle contraction [GO:0003009]; skeletal muscle tissue growth [GO:0048630]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; cell surface [GO:0009986]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P02709}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02709};
| null | null | null | null |
FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250|UniProtKB:P02708}.
|
Mus musculus (Mouse)
|
P04757
|
ACHA3_RAT
|
MGVVLLPPPLSMLMLVLMLLPAASASEAEHRLFQYLFEDYNEIIRPVANVSHPVIIQFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWKPSDYQGVEFMRVPAEKIWKPDIVLYNNADGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHEIKYNCCEEIYQDITYSLYIRRLPLFYTINLIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHYRTPTTHTMPTWVKAVFLNLLPRVMFMTRPTSGEGDTPKTRTFYGAELSNLNCFSRADSKSCKEGYPCQDGTCGYCHHRRVKISNFSANLTRSSSSESVNAVLSLSALSPEIKEAIQSVKYIAENMKAQNVAKEIQDDWKYVAMVIDRIFLWVFILVCILGTAGLFLQPLMARDDT
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; excitatory postsynaptic potential [GO:0060079]; heart development [GO:0007507]; locomotory behavior [GO:0007626]; membrane depolarization [GO:0051899]; nervous system development [GO:0007399]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of acetylcholine secretion, neurotransmission [GO:0014056]; regulation of dendrite morphogenesis [GO:0048814]; regulation of membrane potential [GO:0042391]; regulation of muscle contraction [GO:0006937]; regulation of smooth muscle contraction [GO:0006940]; response to acetylcholine [GO:1905144]; response to carbon monoxide [GO:0034465]; response to inorganic substance [GO:0010035]; response to nicotine [GO:0035094]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]; synaptic transmission involved in micturition [GO:0060084]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; dopaminergic synapse [GO:0098691]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; postsynaptic specialization membrane [GO:0099634]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; protein-containing complex binding [GO:0044877]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-3/CHRNA3 sub-subfamily
|
PTM: Ubiquitinated; by STUB1/CHIP and thereafter degraded by the 26S proteosome complex. {ECO:0000269|PubMed:19474315, ECO:0000269|PubMed:26265139}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:19474315}; Multi-pass membrane protein. Endoplasmic reticulum {ECO:0000269|PubMed:19474315}. Golgi apparatus {ECO:0000269|PubMed:19474315}. Note=Interaction with UBXN2A/UBXD4 promotes translocation to the plasma membrane. {ECO:0000269|PubMed:19474315}.
| null | null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Rattus norvegicus (Rat)
|
P04758
|
ACHB_BOVIN
|
MTPGALLLLLLGVLGAHLAPGARGSEAEGRLREKLFSGYDSTVRPAREVGDRVWVSIGLTLAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPEEHEGIDSLRISAESVWLPDVVLLNNNDGNFDVALDINVVVSSDGSMRWQPPGIYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLQTGLSPEGQERQEVYIHEGTFIENGQWEIIHKPSRLIQPSVDPRGGGEGRREEVTFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLSVPIIIKYLMFTMVLVTFSVILSVVVLNLHHRSPHTHQMPLWVRQIFIHKLPLYLGLKRPKPERDQMQEPPSIAPRDSPGSGWGRGTDEYFIRKPPNDFLFPKPNRFQPELSAPDLRRFIDGPNRAVGLPPELREVVSSISYIARQLQEQEDHDVLKEDWQFVAMVVDRLFLWTFIIFTSVGTLVIFLDATYHLPPADPFP
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell development [GO:0055001]; muscle contraction [GO:0006936]; nervous system process [GO:0050877]; neuromuscular synaptic transmission [GO:0007274]; postsynaptic membrane organization [GO:0001941]; signal transduction [GO:0007165]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; channel activity [GO:0015267]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-1/CHRNB1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}.
|
Bos taurus (Bovine)
|
P04759
|
ACHD_BOVIN
|
MEGSVLTLVLLAALVVCGSWGLNEEERLIRHLFEEKAYNKELRPAAHKESVEISLALTLSNLISLKEVEETLTTNVWIEQGWTDSRLQWDAEDFGNISVLRLPADMVWLPEIVLENNNDGSFQISYSCNVLIYPSGSVYWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTTKEITLSLKQAEEDGRSYPVEWIIIDPEGFTENGEWEIVHRPARVNVDPSVPLDSPNRQDVTFYLIIRRKPLFYVINILVPCVLISFMINLVFYLPADCGEKTSMAISVLLAQSVFLLLISKRLPATSMAIPLIGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEPVKKLFLETLPEILHMSRPAEDGPSPGTLIRRSSSLGYISKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARRPPAGSEQAQQELFSELKPAVDGANFIVNHMKDQNNYNEEKDCWNRVARTVDRLCLFVVTPIMVVGTAWIFLQGAYNQPPPQPFPGDPFSYLEKDKRFI
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; musculoskeletal movement [GO:0050881]; skeletal muscle tissue growth [GO:0048630]
|
acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202]
|
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Delta/CHRND sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}.
|
Bos taurus (Bovine)
|
P04760
|
ACHG_MOUSE
|
MQGGQRPHLLLLLLAVCLGAQSRNQEERLLADLMRNYDPHLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPKDYEGLWILRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSSCSISVTYFPFDWQNCSLIFQSQTYSTSEINLQLSQEDGQAIEWIFIDPEAFTENGEWAIRHRPAKMLLDSVAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVATNVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLMVVTILIVVNSVVVLNVSLRSPHTHSMARGVRKLFLRLLPQLLRMHVRPLAPAAVQDARFRLQNGSSSGWPIMAREEGDLCLPRSELLFRQRQRNGLVQAVLEKLENGPEVRQSQEFCGSLKQASPAIQACVDACNLMARARRQQSHFDSGNEEWLLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNQVPDLPFPGDPRPYLPLPD
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; regulation of membrane potential [GO:0042391]; skeletal muscle contraction [GO:0003009]
|
acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; ligand-gated monoatomic ion channel activity [GO:0015276]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Mus musculus (Mouse)
|
P04761
|
ACM1_PIG
|
MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPAKQPPRSSPNTVKRPTRKGRERAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFIVTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC
| null | null |
adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; cognition [GO:0050890]; entrainment of circadian clock [GO:0009649]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; phototransduction, visible light [GO:0007603]; regulation of locomotion [GO:0040012]; saliva secretion [GO:0046541]
|
dendrite [GO:0030425]; 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, CHRM1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
| 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 Pi turnover.
|
Sus scrofa (Pig)
|
P04762
|
CATA_RAT
|
MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPANYFAEVEQMAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMHDNQGGAPNYYPNSFSAPEQQGSALEHHSQCSADVKRFNSANEDNVTQVRTFYTKVLNEEERKRLCENIANHLKDAQLFIQRKAVKNFTDVHPDYGARVQALLDQYNSQKPKNAIHTYVQAGSHIAAKGKANL
|
1.11.1.6
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04040}; COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P04040};
|
aerobic respiration [GO:0009060]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular oxidant detoxification [GO:0098869]; cellular response to growth factor stimulus [GO:0071363]; cholesterol metabolic process [GO:0008203]; hemoglobin metabolic process [GO:0020027]; hydrogen peroxide catabolic process [GO:0042744]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell division [GO:0051781]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; response to activity [GO:0014823]; response to cadmium ion [GO:0046686]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to inactivity [GO:0014854]; response to insulin [GO:0032868]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to light intensity [GO:0009642]; response to oxidative stress [GO:0006979]; response to ozone [GO:0010193]; response to phenylpropanoid [GO:0080184]; response to reactive oxygen species [GO:0000302]; response to toxic substance [GO:0009636]; response to UV [GO:0009411]; response to vitamin A [GO:0033189]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; triglyceride metabolic process [GO:0006641]; ureteric bud development [GO:0001657]; UV protection [GO:0009650]
|
catalase complex [GO:0062151]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
|
aminoacylase activity [GO:0004046]; antioxidant activity [GO:0016209]; catalase activity [GO:0004096]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; protein homodimerization activity [GO:0042803]
|
PF00199;PF06628;
|
2.40.180.10;
|
Catalase family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:26961980}.
|
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: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. {ECO:0000250|UniProtKB:P04040}.
|
Rattus norvegicus (Rat)
|
P04764
|
ENOA_RAT
|
MSILKIHAREIFDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDNDKTRFMGKGVSKAVEHINKTIAPALVSKKLNVVEQEKIDQLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKSAIAKAGYTDQVVIGMDVAASEFYRAGKYDLDFKSPDDASRYITPDQLADLYKSFIKDYPVVSIEDPFDQDDWDAWQKFTATAGIQVVGDDLTVTNPKRIAKAAGEKSCNCLLLKVNQIGSVTESLQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQILRIEEELGSKAKFAGRSFRNPLAK
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06733}; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. {ECO:0000250|UniProtKB:P06733};
|
canonical glycolysis [GO:0061621]; cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; ERK1 and ERK2 cascade [GO:0070371]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; in utero embryonic development [GO:0001701]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of muscle contraction [GO:0045933]; positive regulation of plasminogen activation [GO:0010756]; response to virus [GO:0009615]
|
cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear outer membrane [GO:0005640]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]
|
DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; enzyme binding [GO:0019899]; GTPase binding [GO:0051020]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
|
PTM: ISGylated. {ECO:0000250|UniProtKB:P06733}.; PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000269|PubMed:8594891}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000305|PubMed:8594891};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:8594891}.
| null | null |
FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production. {ECO:0000250|UniProtKB:P06733}.
|
Rattus norvegicus (Rat)
|
P04768
|
PR2C3_MOUSE
|
MLPSSIQPCSWILLLLLVNSSLLWKNVASFPMCAMRNGRCFMSFEDTFELAGSLSHNISIEVSELFNEFEKHYSNVSGLRDKSPMRCNTSFLPTPENKEQARLTHYAALLKSGAMILDAWESPLDDLVSELSTIKNVPDIIISKATDIKKKINAVRNGVNALMSTMLQNGDEEKKNPAWFLQSDNEDARIHSLYGMISCLDNDFKKVDIYLNVLKCYMLKIDNC
| null | null |
female pregnancy [GO:0007565]; hematopoietic stem cell proliferation [GO:0071425]; mammary gland development [GO:0030879]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; positive regulation of lactation [GO:1903489]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; response to nutrient levels [GO:0031667]
|
endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
|
PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}.
| null | null | null | null | null |
FUNCTION: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May play a role in microvilli formation and cell proliferation of neuroblastoma cells. {ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}.
|
Mus musculus (Mouse)
|
P04769
|
PR7D1_MOUSE
|
MLPSLIQPCSSGTLLMLLMSNLFLWEKVSSAPINASEAVLSDLKDLFDNATVLSGEMSKLGVIMRKEFFMNSFSSETFNKIILDLHKSTENITKAFNSCHTVPINVPETVEDVRKTSFEEFLKMVLHMLLAWKEPLKHLVTELSALPECPYRILSKAEAIEAKNKDLLEYIIRIISKVNPAIKENEDYPTWSDLDSLKSADKETQFFALYMFSFCLRIDLETVDFLVNFLKCLLLYDDVCYSEF
| null | null |
blood vessel endothelial cell migration [GO:0043534]; female pregnancy [GO:0007565]; mammary gland development [GO:0030879]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; placenta blood vessel development [GO:0060674]; placenta development [GO:0001890]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of lactation [GO:1903489]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; response to nutrient levels [GO:0031667]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P04773
|
GLNA_CRIGR
|
MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSESSNSDMYLSPVAMFRDPFRKEPNKLVFCEVFKYNQKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSDGFPGPQGLYYCGVGADKAYRRDIMEAHYRACLYAGVKITGTYAEVKHAQWEFQIGPCEGIRMGDHLWVARFILHRVCKDFGVIATFDSKPIPGNWNGAGCHTNFSTKTMREENGLKHIKEAIEKLSKRHRYHIRAYDPKGGLDNARRLTGFHKTSNINDFSAGVADRSASIRIPRTVGQEKKGYFEARCPSANCDPFAVTEAIVRTCLLNETGDQPFQYKN
|
2.3.1.225; 6.3.1.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P09606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15104};
|
angiogenesis [GO:0001525]; glutamine biosynthetic process [GO:0006542]; protein palmitoylation [GO:0018345]; regulation of endothelial cell migration [GO:0010594]; regulation of sprouting angiogenesis [GO:1903670]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]
|
PF00120;PF03951;
|
3.10.20.70;3.30.590.10;
|
Glutamine synthetase family
|
PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000250|UniProtKB:P15104}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P15104}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000250|UniProtKB:P15104}; Lipid-anchor {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol, with a fraction associated with the cell membrane. {ECO:0000250|UniProtKB:P15104}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P15104}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:P15104};
| null | null | null | null |
FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity). Plays a role in ribosomal 40S subunit biogenesis (By similarity). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (By similarity). {ECO:0000250|UniProtKB:P15104, ECO:0000250|UniProtKB:P15105}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
P04774
|
SCN1A_RAT
|
MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVQWPPTNASLEEHSIEKNVTTDYNGTLVNETVFEFDWKSYIQDSRYHYFLEGVLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEAAQQAAAATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDDDEFHKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAGLPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHIVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEHFNHVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIATDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIRNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVAYVKRKIYEFIQQSFVRKQKILDEIKPLDDLNNRKDNCTSNHTTEIGKDLDCLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPAEEQPVMEPEETLEPEACFTEGCVQRFKCCQISVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGDTFEITEVNNHSDCLKLIERNETARWKNVKVNFDNVGFGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSDYVTSILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKLKGGANLLVKEDMIIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK
| null | null |
adult walking behavior [GO:0007628]; cardiac muscle cell action potential involved in contraction [GO:0086002]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; determination of adult lifespan [GO:0008340]; establishment of localization in cell [GO:0051649]; membrane depolarization during action potential [GO:0086010]; nerve development [GO:0021675]; neuromuscular process controlling posture [GO:0050884]; neuronal action potential [GO:0019228]; neuronal action potential propagation [GO:0019227]; regulation of membrane potential [GO:0042391]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
axon [GO:0030424]; axon initial segment [GO:0043194]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; sodium channel complex [GO:0034706]; T-tubule [GO:0030315]; voltage-gated sodium channel complex [GO:0001518]; Z disc [GO:0030018]
|
sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;PF06512;PF11933;
|
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
|
Sodium channel (TC 1.A.1.10) family, Nav1.1/SCN1A subfamily
|
PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35498}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P35498};
| null | null | null | null |
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons. Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli. {ECO:0000250|UniProtKB:A2APX8}.
|
Rattus norvegicus (Rat)
|
P04775
|
SCN2A_RAT
|
MARSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRNPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTVNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFQFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFNFKGRVKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGPSALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPSRQRAMSMASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHHFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIALGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYLLKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK
| null | null |
axon development [GO:0061564]; cellular response to hypoxia [GO:0071456]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; intrinsic apoptotic signaling pathway in response to osmotic stress [GO:0008627]; membrane depolarization during action potential [GO:0086010]; memory [GO:0007613]; myelination [GO:0042552]; nerve development [GO:0021675]; nervous system development [GO:0007399]; neuron apoptotic process [GO:0051402]; neuronal action potential [GO:0019228]; optic nerve development [GO:0021554]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
axon [GO:0030424]; axon initial segment [GO:0043194]; glutamatergic synapse [GO:0098978]; intercalated disc [GO:0014704]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; T-tubule [GO:0030315]; voltage-gated sodium channel complex [GO:0001518]
|
calmodulin binding [GO:0005516]; leucine zipper domain binding [GO:0043522]; sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;PF06512;PF11933;
|
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
|
Sodium channel (TC 1.A.1.10) family, Nav1.2/SCN2A subfamily
|
PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis.; PTM: Phosphorylation at Ser-1506 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000269|PubMed:1322892, ECO:0000269|PubMed:1658937, ECO:0000269|PubMed:20131913}.; PTM: Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases voltage-gated sodium current and mediates the early response to acute hypoxia in neurons (PubMed:28029095). Sumoylated SCN2A is located at the cell membrane (PubMed:28029095). {ECO:0000269|PubMed:28029095}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827969, ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:28029095, ECO:0000269|PubMed:9893979}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:28029095};
| null | null | null | null |
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory (By similarity). {ECO:0000250|UniProtKB:B1AWN6, ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:28029095, ECO:0000269|PubMed:9893979}.
|
Rattus norvegicus (Rat)
|
P04776
|
GLYG1_SOYBN
|
MAKLVFSLCFLLFSGCCFAFSSREQPQQNECQIQKLNALKPDNRIESEGGLIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSKSRRNGIDETICTMRLRHNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAEFGSLRKNAMFVPHYNLNANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNALPEEVIQHTFNLKSQQARQIKNNNPFKFLVPPQESQKRAVA
| null | null | null |
endoplasmic reticulum [GO:0005783]; protein storage vacuole [GO:0000326]
|
nutrient reservoir activity [GO:0045735]
|
PF00190;
|
2.60.120.10;
|
11S seed storage protein (globulins) family
|
PTM: During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269|PubMed:29037738}.; PTM: The precursor is post-translationally processed to form a covalently linked A1a-Bx subunit complex.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:29348620}. Protein storage vacuole {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles. {ECO:0000269|PubMed:29348620}.
| null | null | null | null | null |
FUNCTION: Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, PubMed:28590128, Ref.15). {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233, ECO:0000269|PubMed:28590128, ECO:0000269|Ref.15}.
|
Glycine max (Soybean) (Glycine hispida)
|
P04778
|
CB1C_ARATH
|
MAASTMALSSPAFAGKAVKLSPAASEVLGSGRVTMRKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK
| null |
COFACTOR: Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin. {ECO:0000250};
|
photosynthesis, light harvesting in photosystem I [GO:0009768]; response to light stimulus [GO:0009416]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; nucleus [GO:0005634]; photosystem I [GO:0009522]; photosystem II [GO:0009523]; plastoglobule [GO:0010287]; thylakoid [GO:0009579]
|
chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]
|
PF00504;
|
1.10.3460.10;
|
Light-harvesting chlorophyll a/b-binding (LHC) protein family
|
PTM: Photoregulated by reversible phosphorylation of its threonine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
|
Arabidopsis thaliana (Mouse-ear cress)
|
P04785
|
PDIA1_RAT
|
MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDAGSDSAKQFLLAAEAVDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITQFCHHFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDNDDLDLEEALEPDMEEDDDQKAVKDEL
|
5.3.4.1
| null |
cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; insulin processing [GO:0030070]; positive regulation of cell adhesion [GO:0045785]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of viral entry into host cell [GO:0046598]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902175]; response to endoplasmic reticulum stress [GO:0034976]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; procollagen-proline 4-dioxygenase complex [GO:0016222]; protein-containing complex [GO:0032991]
|
actin binding [GO:0003779]; enzyme binding [GO:0019899]; integrin binding [GO:0005178]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; protein-disulfide reductase activity [GO:0015035]; thiol oxidase activity [GO:0016972]
|
PF00085;PF13848;
|
3.40.30.10;
|
Protein disulfide isomerase family
|
PTM: Phosphorylation of Ser-359 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone. It also promotes interaction with ERN1. {ECO:0000250|UniProtKB:P07237}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000250|UniProtKB:P09103}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}.
|
CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P07237};
| null | null | null | null |
FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. {ECO:0000250|UniProtKB:P07237}.
|
Rattus norvegicus (Rat)
|
P04786
|
TOP1_YEAST
|
MTIADASKVNHELSSDDDDDVPLSQTLKKRKVASMNSASLQDEAEPYDSDEAISKISKKKTKKIKTEPVQSSSLPSPPAKKSATSKPKKIKKEDGDVKVKTTKKEEQENEKKKREEEEEEDKKAKEEEEEYKWWEKENEDDTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLTSQEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSKDAPVPPAPEGHKWGEIRHDNTVQWLAMWRENIFNSFKYVRLAANSSLKGQSDYKKFEKARQLKSYIDAIRRDYTRNLKSKVMLERQKAVAIYLIDVFALRAGGEKSEDEADTVGCCSLRYEHVTLKPPNTVIFDFLGKDSIRFYQEVEVDKQVFKNLTIFKRPPKQPGHQLFDRLDPSILNKYLQNYMPGLTAKVFRTYNASKTMQDQLDLIPNKGSVAEKILKYNAANRTVAILCNHQRTVTKGHAQTVEKANNRIQELEWQKIRCKRAILQLDKDLLKKEPKYFEEIDDLTKEDEATIHKRIIDREIEKYQRKFVRENDKRKFEKEELLPESQLKEWLEKVDEKKQEFEKELKTGEVELKSSWNSVEKIKAQVEKLEQRIQTSSIQLKDKEENSQVSLGTSKINYIDPRLSVVFCKKYDVPIEKIFTKTLREKFKWAIESVDENWRF
|
5.6.2.1
| null |
chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA topological change [GO:0006265]; mitotic chromosome condensation [GO:0007076]; nuclear migration [GO:0007097]; rDNA heterochromatin formation [GO:0000183]; regulation of mitotic recombination [GO:0000019]; regulation of transcription by RNA polymerase II [GO:0006357]; rRNA transcription [GO:0009303]; transcription elongation by RNA polymerase II [GO:0006368]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]
|
PF14370;PF01028;PF02919;
|
1.10.132.10;2.170.11.10;1.10.10.41;
|
Type IB topoisomerase family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000250}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04789
|
TPIS_TRYBB
|
MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
|
5.3.1.1
| null |
gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; glycosome [GO:0020015]
|
triose-phosphate isomerase activity [GO:0004807]
|
PF00121;
|
3.20.20.70;
|
Triosephosphate isomerase family
| null |
SUBCELLULAR LOCATION: Glycosome.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1;
| null |
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
| null | null | null |
Trypanosoma brucei brucei
|
P04792
|
HSPB1_HUMAN
|
MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK
| null | null |
anterograde axonal protein transport [GO:0099641]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; chaperone-mediated protein folding [GO:0061077]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of protein kinase activity [GO:0006469]; platelet aggregation [GO:0070527]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of tumor necrosis factor production [GO:0032760]; protein refolding [GO:0042026]; regulation of autophagy [GO:0010506]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of protein phosphorylation [GO:0001932]; regulation of translational initiation [GO:0006446]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]; response to virus [GO:0009615]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]
|
axon cytoplasm [GO:1904115]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; spindle [GO:0005819]; Z disc [GO:0030018]
|
identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein kinase C inhibitor activity [GO:0008426]; RNA binding [GO:0003723]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; ubiquitin binding [GO:0043130]; unfolded protein binding [GO:0051082]
|
PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
|
PTM: Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:19166925, PubMed:8093612). {ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8325890}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777697, ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000269|PubMed:19464326}.
| null | null | null | null | null |
FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742). {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742}.
|
Homo sapiens (Human)
|
P04797
|
G3P_RAT
|
MVKVGVNGFGRIGRLVTRAAFSCDKVDIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQAAEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE
|
1.2.1.12; 2.6.99.-
| null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cAMP-mediated signaling [GO:0019933]; canonical glycolysis [GO:0061621]; cellular response to type II interferon [GO:0071346]; female pregnancy [GO:0007565]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of translation [GO:0017148]; negative regulation of vascular associated smooth muscle cell apoptotic process [GO:1905460]; neuron apoptotic process [GO:0051402]; nitric oxide mediated signal transduction [GO:0007263]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cytokine production [GO:0001819]; positive regulation of type I interferon production [GO:0032481]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; glutamatergic synapse [GO:0098978]; lipid droplet [GO:0005811]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density, intracellular component [GO:0099092]; ribonucleoprotein complex [GO:1990904]
|
aspartic-type endopeptidase inhibitor activity [GO:0019828]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
|
PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus (PubMed:1281150, PubMed:15951807, PubMed:20972425, PubMed:8626764). The effect of S-nitrosylation on enzymatic activity is unclear: according to some authors, it inhibits enzymatic activity and increases endogenous ADP-ribosylation, inhibiting the enzyme in a non-reversible manner (PubMed:8626764). According to others, it does not affect glycolysis (PubMed:15951807). ADP-ribosylation is likely to be a pathophysiological event associated with inhibition of gluconeogenesis (PubMed:8626764). S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000269|PubMed:1281150, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:20972425, ECO:0000269|PubMed:8626764}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: Sulfhydration at Cys-150 increases catalytic activity. {ECO:0000250|UniProtKB:P16858}.; PTM: Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.; PTM: Succination of Cys-150 and Cys-245 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits glyceraldehyde-3-phosphate dehydrogenase activity. Fumarate concentration as well as succination of cysteine residues in GAPDH is significantly increased in muscle of diabetic rats. It was proposed that the S-(2-succinyl)cysteine chemical modification may be a useful biomarker of mitochondrial and oxidative stress in diabetes and that succination of GAPDH and other thiol proteins by fumarate may contribute to the metabolic changes underlying the development of diabetes complications. {ECO:0000269|PubMed:17934141}.
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SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15312048}. Nucleus {ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794, ECO:0000269|PubMed:20972425}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (PubMed:15951807). Colocalizes with CHP1 to small punctate structures along the microtubules tracks (PubMed:15312048). {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807}.
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CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009, ECO:0000305|PubMed:17934141}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000269|PubMed:20972425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000269|PubMed:20972425};
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PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
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FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:15951807, PubMed:17934141, PubMed:20972425). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:17934141). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (PubMed:15312048). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (PubMed:10424669, PubMed:15951807, PubMed:20972425). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (PubMed:15951807, PubMed:20972425). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P10096, ECO:0000269|PubMed:10424669, ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:17934141, ECO:0000269|PubMed:20972425}.
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Rattus norvegicus (Rat)
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P04798
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CP1A1_HUMAN
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MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPHLALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQSMSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAGPGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPILRYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANVQLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEFSVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
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1.14.14.1; 4.2.1.152
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COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23508959};
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9-cis-retinoic acid biosynthetic process [GO:0042904]; amine metabolic process [GO:0009308]; camera-type eye development [GO:0043010]; cellular response to copper ion [GO:0071280]; cellular response to organic cyclic compound [GO:0071407]; coumarin metabolic process [GO:0009804]; dibenzo-p-dioxin catabolic process [GO:0019341]; digestive tract development [GO:0048565]; epoxygenase P450 pathway [GO:0019373]; estrogen metabolic process [GO:0008210]; ethylene metabolic process [GO:0009692]; fatty acid metabolic process [GO:0006631]; flavonoid metabolic process [GO:0009812]; hepatocyte differentiation [GO:0070365]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide biosynthetic process [GO:0050665]; insecticide metabolic process [GO:0017143]; lipid hydroxylation [GO:0002933]; long-chain fatty acid biosynthetic process [GO:0042759]; long-chain fatty acid metabolic process [GO:0001676]; maternal process involved in parturition [GO:0060137]; nitric oxide metabolic process [GO:0046209]; omega-hydroxylase P450 pathway [GO:0097267]; porphyrin-containing compound metabolic process [GO:0006778]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; progesterone metabolic process [GO:0042448]; response to 3-methylcholanthrene [GO:1904681]; response to arsenic-containing substance [GO:0046685]; response to food [GO:0032094]; response to herbicide [GO:0009635]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to immobilization stress [GO:0035902]; response to iron(III) ion [GO:0010041]; response to lipopolysaccharide [GO:0032496]; response to nematode [GO:0009624]; response to vitamin A [GO:0033189]; retinol metabolic process [GO:0042572]; steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202]; tissue remodeling [GO:0048771]; vitamin D metabolic process [GO:0042359]; xenobiotic metabolic process [GO:0006805]
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endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]
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17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; flavonoid 3'-monooxygenase activity [GO:0016711]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; long-chain fatty acid omega-1 hydroxylase activity [GO:0120319]; long-chain fatty acid omega-hydroxylase activity [GO:0102033]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on diphenols and related substances as donors [GO:0016679]; oxygen binding [GO:0019825]; steroid 17-alpha-monooxygenase activity [GO:0004508]; vitamin D 24-hydroxylase activity [GO:0070576]
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PF00067;
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1.10.630.10;
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Cytochrome P450 family
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SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Microsome membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Cytoplasm {ECO:0000250|UniProtKB:P00185}.
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CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:15805301, ECO:0000269|PubMed:18577768}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15041462, ECO:0000305|PubMed:15805301, ECO:0000305|PubMed:18577768}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87602; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47308, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87605; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47309; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 15alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47312, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87618; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47313; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47204, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47205; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:14559847}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; Evidence={ECO:0000305|PubMed:11555828, ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; Evidence={ECO:0000269|PubMed:12865317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; Evidence={ECO:0000305|PubMed:12865317}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47284, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62847; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47285; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47288, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87598; Evidence={ECO:0000269|PubMed:12865317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47289; Evidence={ECO:0000305|PubMed:12865317}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47276, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87593; Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47277; Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132024; Evidence={ECO:0000269|PubMed:18577768}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077; Evidence={ECO:0000305|PubMed:18577768}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49972, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132019; Evidence={ECO:0000269|PubMed:15041462}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49973; Evidence={ECO:0000305|PubMed:15041462}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49968, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132016; Evidence={ECO:0000269|PubMed:15041462}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49969; Evidence={ECO:0000305|PubMed:15041462}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39811, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63590; Evidence={ECO:0000269|PubMed:15041462}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812; Evidence={ECO:0000305|PubMed:15041462}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76627; Evidence={ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:18577768}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; Evidence={ECO:0000305|PubMed:15041462, ECO:0000305|PubMed:18577768}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence={ECO:0000269|PubMed:15041462}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence={ECO:0000305|PubMed:15041462}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131975; Evidence={ECO:0000269|PubMed:20972997}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885; Evidence={ECO:0000305|PubMed:20972997}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49880, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131970; Evidence={ECO:0000269|PubMed:20972997}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881; Evidence={ECO:0000305|PubMed:20972997}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:19965576}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; Evidence={ECO:0000305|PubMed:19965576}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972997}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; Evidence={ECO:0000305|PubMed:19965576, ECO:0000305|PubMed:20972997}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:19965576}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000305|PubMed:15041462, ECO:0000305|PubMed:19965576}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52124, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136411; Evidence={ECO:0000269|PubMed:19965576}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52125; Evidence={ECO:0000305|PubMed:19965576}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136410; Evidence={ECO:0000269|PubMed:19965576}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121; Evidence={ECO:0000305|PubMed:19965576}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10681376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; Evidence={ECO:0000305|PubMed:10681376}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10681376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089; Evidence={ECO:0000305|PubMed:10681376}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; Evidence={ECO:0000269|PubMed:21068195}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; Evidence={ECO:0000305|PubMed:21068195}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000269|PubMed:21068195}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; Evidence={ECO:0000305|PubMed:21068195}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000269|PubMed:21068195}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; Evidence={ECO:0000305|PubMed:21068195}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342; Evidence={ECO:0000269|PubMed:21068195}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633; Evidence={ECO:0000305|PubMed:21068195};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for all-trans retinol {ECO:0000269|PubMed:10681376}; KM=9.5 uM for 17beta-estradiol (2-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=11.8 uM for 17beta-estradiol (4-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=79 uM for 17beta-estradiol (6alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=19.6 uM for 17beta-estradiol (15alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=12.2 uM for estrone (2-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=22.6 uM for estrone (4-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=86 uM for estrone (6alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=85 uM for estrone (15alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=507 pmol/min/nmol enzyme toward all-trans retinol {ECO:0000269|PubMed:10681376}; Vmax=0.6 pmol/min/pmol enzyme toward 17beta-estradiol (2-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=0.02 pmol/min/pmol enzyme toward 17beta-estradiol (4-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=3.6 pmol/min/pmol enzyme toward 17beta-estradiol (6alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=0.9 pmol/min/pmol enzyme toward 17beta-estradiol (15alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=0.4 pmol/min/pmol enzyme toward estrone (2-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=0.1 pmol/min/pmol enzyme toward estrone (4-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=0.2 pmol/min/pmol enzyme toward estrone (6alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; Vmax=1.2 pmol/min/pmol enzyme toward estrone (15alpha-hydroxylation) {ECO:0000269|PubMed:15805301};
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PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847, ECO:0000269|PubMed:15805301}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:18577768, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972997, ECO:0000269|PubMed:21068195}.; PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:10681376}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15805301). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997). Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195). {ECO:0000269|PubMed:10681376, ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847, ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:15805301, ECO:0000269|PubMed:18577768, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972997, ECO:0000269|PubMed:21068195}.
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Homo sapiens (Human)
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P04799
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CP1A2_RAT
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MAFSQYISLAPELLLATAIFCLVFWVLRGTRTQVPKGLKSPPGPWGLPFIGHMLTLGKNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLITNGKSMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSVSSCYLEEHVSKEANHLISKFQKLMAEVGHFEPVNQVVESVANVIGAMCFGKNFPRKSEEMLNLVKSSKDFVENVTSGNAVDFFPVLRYLPNPALKRFKNFNDNFVLFLQKTVQEHYQDFNKNSIQDITGALFKHSENYKDNGGLIPQEKIVNIVNDIFGAGFETVTTAIFWSILLLVTEPKVQRKIHEELDTVIGRDRQPRLSDRPQLPYLEAFILEIYRYTSFVPFTIPHSTTRDTSLNGFHIPKECCIFINQWQVNHDEKQWKDPFVFRPERFLTNDNTAIDKTLSEKVMLFGLGKRRCIGEIPAKWEVFLFLAILLHQLEFTVPPGVKVDLTPSYGLTMKPRTCEHVQAWPRFSK
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1.14.14.1; 4.2.1.152
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COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
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alkaloid metabolic process [GO:0009820]; arachidonic acid metabolic process [GO:0019369]; cellular aromatic compound metabolic process [GO:0006725]; cellular respiration [GO:0045333]; cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cholesterol metabolic process [GO:0008203]; dibenzo-p-dioxin metabolic process [GO:0018894]; estrogen metabolic process [GO:0008210]; heterocycle metabolic process [GO:0046483]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide biosynthetic process [GO:0050665]; lung development [GO:0030324]; monocarboxylic acid metabolic process [GO:0032787]; monoterpenoid metabolic process [GO:0016098]; nitroglycerin metabolic process [GO:0018937]; oxidative demethylation [GO:0070989]; porphyrin-containing compound metabolic process [GO:0006778]; post-embryonic development [GO:0009791]; progesterone metabolic process [GO:0042448]; regulation of gene expression [GO:0010468]; response to estradiol [GO:0032355]; response to immobilization stress [GO:0035902]; response to lipopolysaccharide [GO:0032496]; response to nitroglycerin [GO:1904842]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; retinol metabolic process [GO:0042572]; steroid catabolic process [GO:0006706]; toxin biosynthetic process [GO:0009403]; toxin metabolic process [GO:0009404]; vitamin E metabolic process [GO:0042360]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]
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endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
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17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:0020037]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; nitrite reductase (NO-forming) activity [GO:0050421]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; steroid 17-alpha-monooxygenase activity [GO:0004508]
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PF00067;
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1.10.630.10;
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Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}.
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CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131965; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131964; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136524; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285; Evidence={ECO:0000250|UniProtKB:P05177};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P05177}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. {ECO:0000250|UniProtKB:P05177}.
|
Rattus norvegicus (Rat)
|
P04800
|
CP3A1_RAT
|
MDLLSALTLETWVLLAVVLVLLYGFGTRTHGLFKKQGIPGPKPLPFFGTVLNYYMGLWKFDVECHKKYGKIWGLFDGQMPLFAITDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIEFFKKFVYRMKETRLDSVQKHRVDFLQLMMNAHNDSKDKESHTALSDMEITAQSIIFIFAGYEPTSSTLSFVLHSLATHPDTQKKLQEEIDRALPNKAPPTYDTVMEMEYLDMVLNETLRLYPIGNRLERVCKKDVEINGVFMPKGSVVMIPSYALHRDPQHWPEPEEFRPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALMNMKLALTKVLQNFSFQPCKETQIPLKLSRQGLLQPTKPIILKVVPRDEIITGS
|
1.14.14.1
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
oxidative demethylation [GO:0070989]; response to cadmium ion [GO:0046686]; response to dexamethasone [GO:0071548]; response to glucocorticoid [GO:0051384]; response to metal ion [GO:0010038]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; steroid metabolic process [GO:0008202]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]
|
aromatase activity [GO:0070330]; demethylase activity [GO:0032451]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; testosterone 6-beta-hydroxylase activity [GO:0050649]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1;
| null | null | null | null |
FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
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Rattus norvegicus (Rat)
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P04802
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SYDC_YEAST
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MSQDENIVKAVEESAEPAQVILGEDGKPLSKKALKKLQKEQEKQRKKEERALQLEAEREAREKKAAAEDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP
|
6.1.1.12
| null |
aspartyl-tRNA aminoacylation [GO:0006422]
|
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
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aspartate-tRNA ligase activity [GO:0004815]; ATP binding [GO:0005524]; RNA binding [GO:0003723]
|
PF00152;PF01336;
|
2.40.50.140;
|
Class-II aminoacyl-tRNA synthetase family, Type 2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12;
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04805
|
SYE_ECOLI
|
MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ
|
6.1.1.17
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204};
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glutamyl-tRNA aminoacylation [GO:0006424]
|
cytosol [GO:0005829]
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ATP binding [GO:0005524]; glutamate-tRNA ligase activity [GO:0004818]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
|
PF19269;PF00749;
|
1.10.10.350;3.40.50.620;
|
Class-I aminoacyl-tRNA synthetase family, Glutamate--tRNA ligase type 1 subfamily
|
PTM: Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu). {ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24343429}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:8218204};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.32 uM for tRNA(Glu) {ECO:0000269|PubMed:14764088}; KM=0.105 mM for Glu {ECO:0000269|PubMed:14764088};
| null | null | null |
FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000269|PubMed:14764088, ECO:0000269|PubMed:6280993, ECO:0000269|PubMed:6986385, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204}.; FUNCTION: Phosphorylation of GltX by HipA prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to multidrug resistance and persistence (PubMed:24095282, PubMed:24343429). Overexpression of GltX prevents HipA-induced growth arrest, persister formation and increases in (p)ppGpp levels (PubMed:24343429, PubMed:28430938). {ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24343429, ECO:0000269|PubMed:28430938}.
|
Escherichia coli (strain K12)
|
P04806
|
HXKA_YEAST
|
MVHLGPKKPQARKGSMADVPKELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHDMRTTKHQEELWSFIADSLKDFMVEQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLIASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLADDIPSNSPMAINCEYGSFDNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGHIAADGSVYNKYPGFKEAAAKGLRDIYGWTGDASKDPITIVPAEDGSGAGAAVIAALSEKRIAEGKSLGIIGA
|
2.7.1.1
| null |
carbohydrate phosphorylation [GO:0046835]; fructose import across plasma membrane [GO:1990539]; fructose metabolic process [GO:0006000]; glucose 6-phosphate metabolic process [GO:0051156]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]; mannose metabolic process [GO:0006013]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; mannokinase activity [GO:0019158]
|
PF00349;PF03727;
|
1.10.287.1250;3.30.420.40;3.40.367.20;
|
Hexokinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000305|PubMed:332086}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000305|PubMed:332086}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000305|PubMed:332086};
| null |
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:332086}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:332086}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:332086). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:332086). {ECO:0000269|PubMed:332086}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04807
|
HXKB_YEAST
|
MVHLGPKKPQARKGSMADVPKELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDAMRTTQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSAPMAINCEYGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKAANALKDIYGWTQTSLDDYPIKIVPAEDGSGAGAAVIAALAQKRIAEGKSVGIIGA
|
2.7.1.1
| null |
carbohydrate phosphorylation [GO:0046835]; fructose import across plasma membrane [GO:1990539]; fructose metabolic process [GO:0006000]; glucose 6-phosphate metabolic process [GO:0051156]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]; mannose metabolic process [GO:0006013]; negative regulation of apoptotic signaling pathway [GO:2001234]; regulation of cell size [GO:0008361]; regulation of transcription by glucose [GO:0046015]
|
cytosol [GO:0005829]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; mannokinase activity [GO:0019158]
|
PF00349;PF03727;
|
1.10.287.1250;3.30.420.40;3.40.367.20;
|
Hexokinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000305|PubMed:332086}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000305|PubMed:332086}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000305|PubMed:332086};
| null |
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:332086}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:332086}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:332086). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:332086). {ECO:0000269|PubMed:332086}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04810
|
HSP83_DROSI
|
MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFMKGVVD
| null | null |
cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; pole plasm mRNA localization [GO:0019094]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of neuroblast proliferation [GO:0002052]; proteasome assembly [GO:0043248]; protein stabilization [GO:0050821]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; RISC complex assembly [GO:0070922]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082]
|
PF13589;PF00183;
|
3.30.230.80;3.30.565.10;
|
Heat shock protein 90 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
|
Drosophila simulans (Fruit fly)
|
P04811
|
HSP83_DROVI
|
MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLFIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEDDEKKEGDEKKEMDTDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFIKGVVD
| null | null |
cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; pole plasm mRNA localization [GO:0019094]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of neuroblast proliferation [GO:0002052]; proteasome assembly [GO:0043248]; protein stabilization [GO:0050821]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; RISC complex assembly [GO:0070922]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082]
|
PF13589;PF00183;
|
3.30.230.80;3.30.565.10;
|
Heat shock protein 90 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
|
Drosophila virilis (Fruit fly)
|
P04817
|
CAN1_YEAST
|
MTNSKEDADIEEKHMYNEPVTTLFHDVEASQTHHRRGSIPLKDEKSKELYPLRSFPTRVNGEDTFSMEDGIGDEDEGEVQNAEVKRELKQRHIGMIALGGTIGTGLFIGLSTPLTNAGPVGALISYLFMGSLAYSVTQSLGEMATFIPVTSSFTVFSQRFLSPAFGAANGYMYWFSWAITFALELSVVGQVIQFWTYKVPLAAWISIFWVIITIMNLFPVKYYGEFEFWVASIKVLAIIGFLIYCFCMVCGAGVTGPVGFRYWRNPGAWGPGIISKDKNEGRFLGWVSSLINAAFTFQGTELVGITAGEAANPRKSVPRAIKKVVFRILTFYIGSLLFIGLLVPYNDPKLTQSTSYVSTSPFIIAIENSGTKVLPHIFNAVILTTIISAANSNIYVGSRILFGLSKNKLAPKFLSRTTKGGVPYIAVFVTAAFGALAYMETSTGGDKVFEWLLNITGVAGFFAWLFISISHIRFMQALKYRGISRDELPFKAKLMPGLAYYAATFMTIIIIIQGFTAFAPKFNGVSFAAAYISIFLFLAVWILFQCIFRCRFIWKIGDVDIDSDRRDIEAIVWEDHEPKTFWDKFWNVVA
| null | null |
amino acid transmembrane transport [GO:0003333]; basic amino acid transport [GO:0015802]; L-arginine transmembrane transport [GO:1903826]; transmembrane transport [GO:0055085]
|
eisosome [GO:0032126]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
amino acid transmembrane transporter activity [GO:0015171]; basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459]
|
PF00324;
|
1.20.1740.10;
|
Amino acid-polyamine-organocation (APC) superfamily, YAT (TC 2.A.3.10) family
|
PTM: Phosphorylated probably at multiple sites (PubMed:9544242). {ECO:0000269|PubMed:9544242}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12100990, ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946, ECO:0000269|PubMed:21880895, ECO:0000269|PubMed:37005249}; Multi-pass membrane protein {ECO:0000269|PubMed:21880895}. Endosome membrane {ECO:0000269|PubMed:21880895}; Multi-pass membrane protein {ECO:0000269|PubMed:21880895}. Note=Recycled via the retromer-mediated pathway (PubMed:21880895). Requires phosphatidyl ethanolamine (PE) for localization and exclusively associated with lipid rafts called MCCs (membrane compartment occupied by CAN1) (PubMed:12100990, PubMed:14551254, PubMed:21223946). {ECO:0000269|PubMed:12100990, ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946, ECO:0000269|PubMed:21880895}.
| null | null | null | null | null |
FUNCTION: High-affinity permease for arginine. {ECO:0000269|PubMed:10654085, ECO:0000269|PubMed:11746604, ECO:0000269|PubMed:8436127, ECO:0000269|PubMed:9231419}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04818
|
TYSY_HUMAN
|
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV
|
2.1.1.45
| null |
cartilage development [GO:0051216]; circadian rhythm [GO:0007623]; developmental growth [GO:0048589]; DNA biosynthetic process [GO:0071897]; dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; intestinal epithelial cell maturation [GO:0060574]; liver regeneration [GO:0097421]; methylation [GO:0032259]; negative regulation of translation [GO:0017148]; response to cytokine [GO:0034097]; response to ethanol [GO:0045471]; response to folic acid [GO:0051593]; response to glucocorticoid [GO:0051384]; response to organophosphorus [GO:0046683]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; tetrahydrofolate interconversion [GO:0035999]; uracil metabolic process [GO:0019860]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
dihydrofolate reductase activity [GO:0004146]; folic acid binding [GO:0005542]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; sequence-specific mRNA binding [GO:1990825]; thymidylate synthase activity [GO:0004799]
|
PF00303;
|
3.30.572.10;
|
Thymidylate synthase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21876188}. Cytoplasm {ECO:0000269|PubMed:21876188}. Mitochondrion {ECO:0000269|PubMed:21876188}. Mitochondrion matrix {ECO:0000269|PubMed:21876188}. Mitochondrion inner membrane {ECO:0000269|PubMed:21876188}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000269|PubMed:11278511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12105; Evidence={ECO:0000305|PubMed:11278511};
| null |
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000305|PubMed:11278511}.
| null | null |
FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:0000269|PubMed:11278511, ECO:0000269|PubMed:21876188}.
|
Homo sapiens (Human)
|
P04819
|
DNLI1_YEAST
|
MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVLISLSKALLLHDENREDSPDKDVPMDVLESAQQKIRDAFCQVPNYEIVINSCLEHGIMNLDKYCTLRPGIPLKPMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFIQDLDTTKNLILDCEAVAWDKDQGKILPFQVLSTRKRKDVELNDVKVKVCLFAFDILCYNDERLINKSLKERREYLTKVTKVVPGEFQYATQITTNNLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKDYLEGVGDSLDLCVLGAYYGRGKRTGTYGGFLLGCYNQDTGEFETCCKIGTGFSDEMLQLLHDRLTPTIIDGPKATFVFDSSAEPDVWFEPTTLFEVLTADLSLSPIYKAGSATFDKGVSLRFPRFLRIREDKGVEDATSSDQIVELYENQSHMQN
|
6.5.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
base-excision repair [GO:0006284]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA ligation [GO:0006266]; DNA recombination [GO:0006310]; lagging strand elongation [GO:0006273]; maintenance of DNA trinucleotide repeats [GO:0035753]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; Okazaki fragment processing involved in mitotic DNA replication [GO:1903461]
|
mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872]
|
PF04679;PF01068;PF04675;
|
3.30.1490.70;1.10.3260.10;3.30.470.30;2.40.50.140;
|
ATP-dependent DNA ligase family
| null |
SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135};
| null | null | null | null |
FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. The mitochondrial form is required for mitochondrial DNA maintenance but is non-essential while the nuclear form is essential for cell viability.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04821
|
CDC25_YEAST
|
MSDTNTSIPNTSSAREAGNASQTPSISSSSNTSTTTNTESSSASLSSSPSTSELTSIRPIGIVVAAYDFNYPIKKDSSSQLLSVQQGETIYILNKNSSGWWDGLVIDDSNGKVNRGWFPQNFGRPLRDSHLRKHSHPMKKYSSSKSSRRSSLNSLGNSAYLHVPRNPSKSRRGSSTLSASLSNAHNAETSSGHNNTVSMNNSPFSAPNDASHITPQSSNFNSNASLSQDMTKSADGSSEMNTNAIMNNNETNLQTSGEKAGPPLVAEETIKILPLEEIEMIINGIRSNIASTWSPIPLITKTSDYKLVYYNKDLDIYCSELPLISNSIMESDDICDSEPKFPPNDHLVNLYTRDLRKNANIEDSSTRSKQSESEQNRSSLLMEKQDSKETDGNNNSINDDDNNNENNKNEFNEAGPSSLNSLSAPDLTQNIQSRVVAPSRSSILAKSDIFYHYSRDIKLWTELQDLTVYYTKTAHKMFLKENRLNFTKYFDLISDSIVFTQLGCRLMQHEIKAKSCSKEIKKIFKGLISSLSRISINSHLYFDSAFHRKKMDTMNDKDNDNQENNCSRTEGDDGKIEVDSVHDLVSVPLSGKRNVSTSTTDTLTPMRSSFSTVNENDMENFSVLGPRNSVNSVVTPRTSIQNSTLEDFSPSNKNFKSAKSIYEMVDVEFSKFLRHVQLLYFVLQSSVFSDDNTLPQLLPRFFKGSFSGGSWTNPFSTFITDEFGNATKNKAVTSNEVTASSSKNSSISRIPPKMADAIASASGYSANSETNSQIDLKASSAASGSVFTPFNRPSHNRTFSRARVSKRKKKYPLTVDTLNTMKKKSSQIFEKLNNATGEHLKIISKPKSRIRNLEINSSTYEQINQNVLLLEILENLDLSIFINLKNLIKTPSILLDLESEEFLVHAMSSVSSVLTEFFDIKQAFHDIVIRLIMTTQQTTLDDPYLFSSMRSNFPVGHHEPFKNISNTPLVKGPFHKKNEQLALSLFHVLVSQDVEFNNLEFLNNSDDFKDACEKYVEISNLACIIVDQLIEERENLLNYAARMMKNNLTAELLKGEQEKWFDIYSEDYSDDDSENDEAIIDDELGSEDYIERKAANIEKNLPWFLTSDYETSLVYDSRGKIRGGTKEALIEHLTSHELVDAAFNVTMLITFRSILTTREFFYALIYRYNLYPPEGLSYDDYNIWIEKKSNPIKCRVVNIMRTFLTQYWTRNYYEPGIPLILNFAKMVVSEKIPGAEDLLQKINEKLINENEKEPVDPKQQDSVSAVVQTTKRDNKSPIHMSSSSLPSSASSAFFRLKKLKLLDIDPYTYATQLTVLEHDLYLRITMFECLDRAWGTKYCNMGGSPNITKFIANANTLTNFVSHTIVKQADVKTRSKLTQYFVTVAQHCKELNNFSSMTAIVSALYSSPIYRLKKTWDLVSTESKDLLKNLNNLMDSKRNFVKYRELLRSVTDVACVPFFGVYLSDLTFTFVGNPDFLHNSTNIINFSKRTKIANIVEEIISFKRFHYKLKRLDDIQTVIEASLENVPHIEKQYQLSLQVEPRSGNTKGSTHASSASGTKTAKFLSEFTDDKNGNFLKLGKKKPPSRLFR
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; Ras protein signal transduction [GO:0007265]; regulation of cell cycle [GO:0051726]; traversing start control point of mitotic cell cycle [GO:0007089]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00617;PF00618;PF00018;
|
1.10.840.10;2.30.30.40;1.20.870.10;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered. {ECO:0000269|PubMed:2017169}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04822
|
IL1A_RABIT
|
MAKVPDLFEDLKNCFSENEEYSSAIDHLSLNQKSFYDASYEPLHEDCMNKVVSLSTSETSVSPNLTFQENVVAVTASGKILKKRRLSLNQPITDVDLETNVSDPEEGIIKPRSVPYTFQRNMRYKYLRIIKQEFTLNDALNQSLVRDTSDQYLRAAPLQNLGDAVKFDMGVYMTSEDSILPVTLRISQTPLFVSAQNEDEPVLLKEMPETPRIITDSESDILFFWETQGNKNYFKSAANPQLFIATKPEHLVHMARGLPSMTDFQIS
| null | null |
cellular response to heat [GO:0034605]; cellular response to lipopolysaccharide [GO:0071222]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; cytokine-mediated signaling pathway [GO:0019221]; ectopic germ cell programmed cell death [GO:0035234]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fever generation [GO:0001660]; immune response [GO:0006955]; intracellular sodium ion homeostasis [GO:0006883]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of protein secretion [GO:0050714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial growth factor production [GO:0010575]; response to copper ion [GO:0046688]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
copper ion binding [GO:0005507]; cytokine activity [GO:0005125]; interleukin-1 receptor binding [GO:0005149]
|
PF00340;PF02394;
|
2.80.10.50;
|
IL-1 family
|
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000250|UniProtKB:P01583}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000250|UniProtKB:P01583}.; PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A. {ECO:0000250|UniProtKB:P01583}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000250|UniProtKB:P01583}.
| null | null | null | null | null |
FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity. {ECO:0000250|UniProtKB:P01583}.
|
Oryctolagus cuniculus (Rabbit)
|
P04823
|
IL3_RAT
|
MVLASSTTSILCMLLPLLMLFHQGLQISDRGSDAHHLLRTLDCRTIALEILVKLPVSGLNNSDDKANLRNSTLRRVNLDEFLKSQEEFDSQDTTDIKSKLQKLKCCIPAAASDSVLPGVYNKDLDDFKKKLRFYVIHLKDLQPVSVSRPPQPTSSSDNFRPMTVEC
| null | null |
B cell apoptotic process [GO:0001783]; B cell proliferation [GO:0042100]; cell population proliferation [GO:0008283]; cytokine-mediated signaling pathway [GO:0019221]; embryonic hemopoiesis [GO:0035162]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; hematopoietic progenitor cell differentiation [GO:0002244]; hemopoiesis [GO:0030097]; immune response [GO:0006955]; interleukin-3-mediated signaling pathway [GO:0038156]; JNK cascade [GO:0007254]; mast cell apoptotic process [GO:0033024]; mast cell proliferation [GO:0070662]; monocyte differentiation [GO:0030224]; myeloid cell apoptotic process [GO:0033028]; myeloid leukocyte differentiation [GO:0002573]; negative regulation of autophagy [GO:0010507]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of mast cell apoptotic process [GO:0033026]; negative regulation of myeloid cell apoptotic process [GO:0033033]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of hematopoietic progenitor cell differentiation [GO:1901534]; positive regulation of JNK cascade [GO:0046330]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of myeloid leukocyte differentiation [GO:0002763]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of cell growth [GO:0001558]; regulation of gene expression [GO:0010468]; regulation of glycolytic process [GO:0006110]; regulation of protein dephosphorylation [GO:0035304]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; T cell proliferation [GO:0042098]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-3 receptor binding [GO:0005135]
|
PF02059;
|
1.20.1250.10;
|
IL-3 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Stimulates also mature basophils, eosinophils, and monocytes to become functionally activated. In addition, plays an important role in neural cell proliferation and survival. Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation (PubMed:34183475). Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB (By similarity). Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program. Alternatively, contributes to cell survival under oxidative stress in non-hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK (By similarity). {ECO:0000250|UniProtKB:P08700}.
|
Rattus norvegicus (Rat)
|
P04824
|
MEL1_YEASX
|
MFAFYFLTACISLKGVFGVSPSYNGLGLTPQMGWDNWNTFACDVSEQLLLDTADRISDLGLKDMGYKYIILDDCWSSGRDSDGFLVADEQKFPNGMGHVADHLHNNSFLFGMYSSAGEYTCAGYPGSLGREEEDAQFFANNRVDYLKYDNCYNKGQFGTPEISYHRYKAMSDALNKTGRPIFYSLCNWGQDLTFYWGSGIANSWRMSGDVTAEFTRPDSRCPCDGDEYDCKYAGFHCSIMNILNKAAPMGQNAGVGGWNDLDNLEVGVGNLTDDEEKAHFSMWAMVKSPLIIGANVNNLKASSYSIYSQASVIAINQDSNGIPATRVWRYYVSDTDEYGQGEIQMWSGPLDNGDQVVALLNGGSVSRPMNTTLEEIFFDSNLGSKKLTSTWDIYDLWANRVDNSTASAILGRNKTATGILYNATEQSYKDGLSKNDTRLFGQKIGSLSPNAILNTTVPAHGIAFYRLRPSS
|
3.2.1.22
| null |
glycoside catabolic process [GO:0016139]; oligosaccharide metabolic process [GO:0009311]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
alpha-galactosidase activity [GO:0004557]
|
PF16499;PF17801;
|
3.20.20.70;2.60.40.1180;
|
Glycosyl hydrolase 27 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20592022}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
| null | null | null | null | null |
Saccharomyces cerevisiae (Baker's yeast)
|
P04825
|
AMPN_ECOLI
|
MTQQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIVAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQFAEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGMQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDDYNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGGHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTFLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELADELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQFHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKGLENLSGDLYEKITKALA
|
3.4.11.2
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865};
|
proteolysis [GO:0006508]
|
plasma membrane [GO:0005886]
|
aminopeptidase activity [GO:0004177]; identical protein binding [GO:0042802]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]
|
PF11940;PF17432;PF01433;PF17900;
|
2.60.40.1840;3.30.2010.30;1.10.390.10;1.25.50.10;2.60.40.1730;
|
Peptidase M1 family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
|
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865};
| null | null | null | null |
FUNCTION: Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}.
|
Escherichia coli (strain K12)
|
P04839
|
CY24B_HUMAN
|
MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF
|
1.-.-.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
|
cellular response to cadmium ion [GO:0071276]; cellular response to ethanol [GO:0071361]; cellular response to L-glutamine [GO:1904845]; defense response [GO:0006952]; hydrogen peroxide biosynthetic process [GO:0050665]; hypoxia-inducible factor-1alpha signaling pathway [GO:0097411]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; monoatomic ion transmembrane transport [GO:0034220]; positive regulation of angiogenesis [GO:0045766]; positive regulation of tumor necrosis factor production [GO:0032760]; respiratory burst [GO:0045730]; response to aldosterone [GO:1904044]; response to angiotensin [GO:1990776]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]
|
dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; monoatomic ion channel complex [GO:0034702]; NADPH oxidase complex [GO:0043020]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; perinuclear endoplasmic reticulum [GO:0097038]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821]
|
flavin adenine dinucleotide binding [GO:0050660]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]
|
PF08022;PF01794;PF08030;
|
3.40.50.80;2.40.30.10;
| null |
PTM: Glycosylated. {ECO:0000269|PubMed:19159218}.; PTM: Phosphorylated on Ser and Thr residues. {ECO:0000269|PubMed:19028840}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000250|UniProtKB:Q61093}.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:28351984}.
| null | null | null | null | null |
FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
|
Homo sapiens (Human)
|
P04840
|
VDAC1_YEAST
|
MSPPVYSDISRNINDLLNKDFYHATPAAFDVQTTTANGIKFSLKAKQPVKDGPLSTNVEAKLNDKQTGLGLTQGWSNTNNLQTKLEFANLTPGLKNELITSLTPGVAKSAVLNTTFTQPFFTARGAFDLCLKSPTFVGDLTMAHEGIVGGAEFGYDISAGSISRYAMALSYFAKDYSLGATLNNEQITTVDFFQNVNAFLQVGAKATMNCKLPNSNVNIEFATRYLPDASSQVKAKVSDSGIVTLAYKQLLRPGVTLGVGSSFDALKLSEPVHKLGWSLSFDA
| null | null |
apoptotic process [GO:0006915]; cell redox homeostasis [GO:0045454]; DNA transport [GO:0051027]; mitochondrion organization [GO:0007005]; monoatomic ion transport [GO:0006811]; positive regulation of protein import into nucleus [GO:0042307]
|
cytoplasm [GO:0005737]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; pore complex [GO:0046930]
|
porin activity [GO:0015288]; ubiquinone binding [GO:0048039]; voltage-gated monoatomic anion channel activity [GO:0008308]
|
PF01459;
|
2.40.160.10;
|
Eukaryotic mitochondrial porin family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane.
| null | null | null | null | null |
FUNCTION: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Is the major permeability factor of the mitochondrial outer membrane. {ECO:0000269|PubMed:9435273}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04842
|
ALOX1_KOMPG
|
MAIPEEFDILVLGGGSSGSCIAGRLANLDHSLKVGLIEAGENNLNNPWVYLPGIYPRNMKLDSKTASFYTSNPSPHLNGRRAIVPCANVLGGGSSINFMMYTRGSASDYDDFQAEGWKTKDLLPLMKKTETYQRACNNPDIHGFEGPIKVSFGNYTYPVCQDFLRASESQGIPYVDDLEDLVTAHGAEHWLKWINRDTGRRSDSAHAFVHSTMRNHDNLYLICNTKVDKIIVEDGRAAAVRTVPSKPLNPKKPSHKIYRARKQIVLSCGTISSPLVLQRSGFGDPIKLRAAGVKPLVNLPGVGRNFQDHYCFFSPYRIKPQYESFDDFVRGDAEIQKRVFDQWYANGTGPLATNGIEAGVKIRPTPEELSQMDESFQEGYREYFEDKPDKPVMHYSIIAGFFGDHTKIPPGKYMTMFHFLEYPFSRGSIHITSPDPYAAPDFDPGFMNDERDMAPMVWAYKKSRETARRMDHFAGEVTSHHPLFPYSSEARALEMDLETSNAYGGPLNLSAGLAHGSWTQPLKKPTAKNEGHVTSNQVELHPDIEYDEEDDKAIENYIREHTETTWHCLGTCSIGPREGSKIVKWGGVLDHRSNVYGVKGLKVGDLSVCPDNVGCNTYTTALLIGEKTATLVGEDLGYSGEALDMTVPQFKLGTYEKTGLARF
|
1.1.3.13
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692;
|
methane catabolic process [GO:0046188]; methanol metabolic process [GO:0015945]
|
peroxisomal matrix [GO:0005782]
|
alcohol oxidase activity [GO:0047639]; flavin adenine dinucleotide binding [GO:0050660]
|
PF05199;PF00732;
|
3.50.50.60;3.30.560.10;
|
GMC oxidoreductase family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:9396748}.
|
CATALYTIC ACTIVITY: Reaction=a primary alcohol + O2 = an aldehyde + H2O2; Xref=Rhea:RHEA:19829, ChEBI:CHEBI:15379, ChEBI:CHEBI:15734, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478; EC=1.1.3.13;
| null |
PATHWAY: Energy metabolism; methane degradation.
| null | null |
FUNCTION: Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. {ECO:0000269|PubMed:9396748}.
|
Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
|
P04843
|
RPN1_HUMAN
|
MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTEGSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL
| null | null |
protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; melanosome [GO:0042470]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791]
|
RNA binding [GO:0003723]
|
PF04597;
| null |
OST1 family
|
PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, promoting reticulophagy of endoplasmic reticulum sheets. {ECO:0000269|PubMed:32160526}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000305}. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
| null | null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:31831667}.
| null | null |
FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2RQ08, ECO:0000269|PubMed:31831667}.
|
Homo sapiens (Human)
|
P04844
|
RPN2_HUMAN
|
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMFQTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
| null | null |
protein modification process [GO:0036211]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear body [GO:0016604]; oligosaccharyltransferase complex [GO:0008250]
| null |
PF05817;
| null |
SWP1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}.
| null | null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:31831667}.
| null | null |
FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000250|UniProtKB:F1PCT7, ECO:0000269|PubMed:31831667}.
|
Homo sapiens (Human)
|
P04850
|
HN_PIV5
|
MVAEDAPVRATCRVLFRTTTLIFLCTLLALSISILYESLITQKQIMSQAGSTGSNSGLGSITDLLNNILSVANQIIYNSAVALPLQLDTLESTLLTAIKSLQTSDKLEQNCSWSAALINDNRYINGINQFYFSIAEGRNLTLGPLLNMPSFIPTATTPEGCTRIPSFSLTKTHWCYTHNVILNGCQDHVSSNQFVSMGIIEPTSAGFPFFRTLKTLYLSDGVNRKSCSISTVPGGCMMYCFVSTQPERDDYFSAAPPEQRIIIMYYNDTIVERIINPPGVLDVWATLNPGTGSGVYYLGWVLFPIYGGVIKGTSLWNNQANKYFIPQMVAALCSQNQATQVQNAKSSYYSSWFGNRMIQSGILACPLRQDLTNECLVLPFSNDQVLMGAEGRLYMYGDSVYYYQRSNSWWPMTMLYKVTITFTNGQPSAISAQNVPTQQVPRPGTGDCSATNRCPGFCLTGVYADAWLLTNPSSTSTFGSEATFTGSYLNTATQRINPTMYIANNTQIISSQQFGSSGQEAAYGHTTCFRDTGSVMVYCIYIIELSSSLLGQFQIVPFIRQVTLS
|
3.2.1.18
| null |
symbiont entry into host cell [GO:0046718]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; host cell surface receptor binding [GO:0046789]; identical protein binding [GO:0042802]
|
PF00423;
|
1.20.5.110;2.120.10.10;
|
Paramyxoviruses hemagglutinin-neuraminidase family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18;
| null | null | null | null |
FUNCTION: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). {ECO:0000250}.; FUNCTION: Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins. {ECO:0000250}.
|
Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5)
|
P04853
|
HN_SENDZ
|
MDGDRGKRDSYWSTSPSGSTTKPASGWERSSKADTWLLILSFTQWALSIATVIICIIISARQGYSMKEYSMTVEALNMSSREVKESLTSLIRQEVIARAVNIQSSVQTGIPVLLNKNSRDVIQMIDKSCSRQELTQHCESTIAVHHADGIAPLEPHSFWRCPVGEPYLSSDPEISLLPGPSLLSGSTTISGCVRLPSLSIGEAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMFPDLNPVVSHTYDINDNRKSCSVVATGTRGYQLCSMPTVDERTDYSSDGIEDLVLDVLDLKGRTKSHRYRNSEVDLDHPFSALYPSVGNGIATEGSLIFLGYGGLTTPLQGDTKCRTQGCQQVSQDTCNEALKITWLGGKQVVSVIIQVNDYLSERPKIRVTTIPITQNYLGAEGRLLKLGDRVYIYTRSSGWHSQLQIGVLDVSHPLTINWTPHEALSRPGNKECNWYNKCPKECISGVYTDAYPLSPDAANVATVTLYANTSRVNPTIMYSNTTNIINMLRIKDVQLEAAYTTTSCITHFGKGYCFHIIEINQKSLNTLQPMLFKTSIPKLCKAES
|
3.2.1.18
| null |
symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; host cell surface receptor binding [GO:0046789]
|
PF00423;
|
2.120.10.10;
|
Paramyxoviruses hemagglutinin-neuraminidase family
|
PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. {ECO:0000269|PubMed:10876159, ECO:0000269|PubMed:6263875}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Folded in the endoplasmic reticulum. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18;
| null | null | null | null |
FUNCTION: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.; FUNCTION: Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins.
|
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
|
P04855
|
FUS_SENDZ
|
MTAYIQRSQCISTSLLVVLTTLVSCQIPRDRLSNIGVIVDEGKSLKIAGSHESRYIVLSLVPGVDFENGCGTAQVIQYKSLLNRLLIPLRDALDLQEALITVTNDTTQNAGAPQSRFFGAVIGTIALGVATSAQITAGIALAEAREAKRDIALIKESMTKTHKSIELLQNAVGEQILALKTLQDFVNDEIKPAISELGCETAALRLGIKLTQHYSELLTAFGSNFGTIGEKSLTLQALSSLYSANITEIMTTIKTGQSNIYDVIYTEQIKGTVIDVDLERYMVTLSVKIPILSEVPGVLIHKASSISYNIDGEEWYVTVPSHILSRASFLGGADITDCVESRLTYICPRDPAQLIPDSQQKCILGDTTRCPVTKVVDSLIPKFAFVNGGVVANCIASTCTCGTGRRPISQDRSKGVVFLTHDNCGLIGVNGVELYANRRGHDATWGVQNLTVGPAIAIRPIDISLNLADATNFLQDSKAELEKARKILSEVGRWYNSRETVITIIVVMVVILVVIIVIIIVLYRLRRSMLMGNPDDRIPRDTYTLEPKIRHMYTNGGFDAMAEKR
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00523;
|
1.10.287.2480;2.60.40.1690;2.40.490.10;
|
Paramyxoviruses fusion glycoprotein family
|
PTM: In natural infection, inactive F0 is matured into F1 and F2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing occurs on the cell surface and induces a conformational change in the protein that unmasks the fusion peptide. F0 maturation is a primary determinant for organ tropism and pathogenicity. F1 and F2 display interchain and intrachain disulfide bonds, that are necessary for correct folding and intracellular transport.; PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. Glycosylation at Asn-245 is essential for membrane localization and F0 cleavage. {ECO:0000269|PubMed:10876159, ECO:0000269|PubMed:6263875}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Folded in the endoplasmic reticulum by the human CANX and HSPA5 chaperones.
| null | null | null | null | null |
FUNCTION: 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 viral and plasma cell membrane fusion, the heptad repeat (HR) regions 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) interacts with HN tetramer at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
|
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
|
P04859
|
PHOSP_SENDH
|
MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLESDSTKKGIGENTSSMKEMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQESVESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPDLIREDEFRDEIRNPVYQERDTEPRASNASRLLPSKEKPTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEEDIESLTN
| null | null |
DNA-templated transcription [GO:0006351]; negative stranded viral RNA replication [GO:0039689]
|
host cell cytoplasm [GO:0030430]; protein-containing complex [GO:0032991]
|
disordered domain specific binding [GO:0097718]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF01806;
|
1.10.287.340;1.10.8.10;1.10.287.320;
|
Respirovirus P protein family
|
PTM: Phosphorylated by PKC/PRKCZ, and other unknown kinases. Phosphorylation is necessary for viral transcription and replication. The N-terminus contains the majority of phosphorylated sites. Ser-249 is the major site of phosphorylation, but is not necessary for most functions. {ECO:0000269|PubMed:10544094, ECO:0000269|PubMed:10704359, ECO:0000269|PubMed:8614993, ECO:0000269|PubMed:9195969}.
|
SUBCELLULAR LOCATION: Host cytoplasm.
| null | null | null | null | null |
FUNCTION: Essential cofactor of the RNA polymerase L that plays a central role in the transcription and replication by forming the polymerase complex with RNA polymerase L and recruiting L to the genomic N-RNA template for RNA synthesis. Plays also a central role in the encapsidation of nascent RNA chains by forming the encapsidation complex with the nucleocapsid protein N (N-P complex). Acts as a chaperone for newly synthesized free N protein, so-called N0, allowing encapsidation of nascent RNA chains during replication (By similarity). The nucleoprotein protein N prevents excessive phosphorylation of P, which leads to down-regulation of viral transcription/ replication. Participates, together with N, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (By similarity). Recruits host PI4KB and remodel the host endoplasmic reticulum membrane to form viral replication factories (By similarity). {ECO:0000250|UniProtKB:P06162, ECO:0000250|UniProtKB:Q77M42}.
|
Sendai virus (strain Harris) (SeV)
|
P04862
|
C_SENDZ
|
MASATLTAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSMLSCRVNQLTSEGTEAGSTTPSTLPKDQALLIEPKVRAKEKSQHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWAMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQVIMEEAWSLAAHIVQE
| null | null |
symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
| null |
PF01692;
| null |
Respirovirus protein C family
|
PTM: Y1 and Y2 proteins are produced not only by alternative initiation, but also by proteolytic cleavage of C'. Only alternative initiation is detected in vitro, whereas in vivo cleavage seems to be predominant. {ECO:0000250|UniProtKB:P04861}.
|
SUBCELLULAR LOCATION: [Isoform C' protein]: Host cytoplasm {ECO:0000269|PubMed:2171459, ECO:0000269|PubMed:3026113}. Note=Protein C' seems to localize around the Golgi. {ECO:0000269|PubMed:3026113}.; SUBCELLULAR LOCATION: [Isoform C protein]: Host cytoplasm {ECO:0000269|PubMed:2171459, ECO:0000269|PubMed:3026113}. Virion. Note=The C protein is found in virion at a ratio of approximately 40 molecules per virion, presumably associated with the nucleocapsid. {ECO:0000269|PubMed:2171459}.
| null | null | null | null | null |
FUNCTION: The different isoforms prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN-alpha/beta pathway requires binding to STAT1 in the cytoplasm. They inhibit IFN-gamma induced serine phosphorylation of STAT1. Block the IFN-gamma pathway by binding to and stabilizing the parallel form of the STAT1 dimer, further inducing high-molecular-weight complex (HMWC) formation and inhibition of transcription by IFN-gamma. May also have a role in preventing the cell to enter apoptosis. Modulate regulation of viral transcription and replication. Overexpression inhibits the viral RNA polymerase. The absence of all C', C, Y1 and Y2 proteins leads to viral delayed growth. Plays an important role in virion particles release. Modulates virion shape. {ECO:0000269|PubMed:10823869, ECO:0000269|PubMed:11264369, ECO:0000269|PubMed:11821064, ECO:0000269|PubMed:12737992, ECO:0000269|PubMed:15178339, ECO:0000269|PubMed:15220418, ECO:0000269|PubMed:15231380, ECO:0000269|PubMed:26339056}.
|
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
|
P04867
|
TGB1_BSMV
|
MDMTKTVEEKKTNGTDSVKGVFENSTIPKVPTGQEMGGDGSSTSKLKETLKVADQTPLSVDNGAKSKLDSSDRQVPGVADQTPLSVDNGAKSKLDSSDRQVPGPELKPNVKKSKKKRIQKPAQPSGPNDLKGGTKGSSQVGENVSENYTGISKEAAKQKQKTPKSVKMQSNLADKFKANDTRRSELINKFQQFVHETCLKSDFEYTGRQYFRARSNFFEMIKLASLYDKHLKECMARACTLERERLKRKLLLVRALKPAVDFLTGIISGVPGSGKSTIVRTLLKGEFPAVCALANPALMNDYSGIEGVYGLDDLLLSAVPITSDLLIIDEYTLAESAEILLLQRRLRASMVLLVGDVAQGKATTASSIEYLTLPVIYRSETTYRLGQETASLCSKQGNRMVSKGGRDTVIITDYDGETDETEKNIAFTVDTVRDVKDCGYDCALAIDVQGKEFDSVTLFLRNEDRKALADKHLRLVALSRHKSKLIIRADAEIRQAFLTGDIDLSSKASNSHRYSAKPDEDHSWFKAK
|
3.6.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12069530};
|
transport of virus in host, cell to cell [GO:0046740]
|
host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; host cell plasmodesma [GO:0044219]; host cytoskeleton [GO:0044163]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; RNA binding [GO:0003723]
|
PF01443;
|
3.40.50.300;
|
Virgaviridae/benyvirus TGB1 movement protein family
| null |
SUBCELLULAR LOCATION: Host cell junction, host plasmodesma {ECO:0000269|PubMed:19570874}. Host nucleus {ECO:0000269|PubMed:28872759}. Host cytoplasm {ECO:0000269|PubMed:28872759}. Host nucleus, host nucleolus {ECO:0000269|PubMed:28872759}. Host cytoplasm, host cytoskeleton {ECO:0000250|UniProtKB:Q9IV54}. Note=TGB1 nuclear-cytoplasmic trafficking is required for cell-to-cell movement and systemic infection (PubMed:28872759). Associates with host microtubules (By similarity). {ECO:0000250|UniProtKB:Q9IV54, ECO:0000269|PubMed:28872759}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:8995680};
| null | null | null | null |
FUNCTION: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding (PubMed:18353960). Multifunctional movement protein with RNA-binding, ATPase and helicase activities (PubMed:12069530, PubMed:8995680). Engages in homologous interactions leading to the formation of a ribonucleoprotein complex containing plus-sense viral RNAs (vRNPs) (PubMed:18353960). ATPase activity is probably required for vRNPs movement complex assembly (PubMed:32730331). Intracellular delivery of TGBp1-containing vRNPs to plasmodesmata is facilitated by TGBp2 and TGBp3 (By similarity). {ECO:0000250|UniProtKB:Q9IV54, ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:18353960, ECO:0000269|PubMed:32730331, ECO:0000269|PubMed:8995680}.
|
Barley stripe mosaic virus (BSMV)
|
P04884
|
GLYCO_VSIVO
|
MKCLLYLAFLFIGVNCKFTIVFPHNQKGNWKNVPSNYHYCPSSSDLNWHNDLIGTALQVKMPKSHKAIQADGWMCHASKWVTTCDFRWYGPKYITHSIRSFTPSVEQCKESIEQTKQGTWLNPGFPPQSCGYATVTDAEAAIVQVTPHHVLVDEYTGEWVDSQFINGKCSNDICPTVHNSTTWHSDYKVKGLCDSNLISTDITFFSEDGELSSLGKEGTGFRSNYFAYETGDKACKMQYCKHWGVRLPSGVWFEMADKDLFAAARFPECPEGSSISAPSQTSVDVSLIQDVERILDYSLCQETWSKIRAGLPISPVDLSYLAPKNPGTGPVFTIINGTLKYFETRYIRVDIAAPILSRMVGMISGTTTERELWDDWAPYEDVEIGPNGVLRTSLGYKFPLYMIGHGMLDSDLHLSSKAQVFEHPHIQDAASQLPDDETLFFGDTGLSKNPIEFVEGWFSSWKSSIASFFFIIGLIIGLFLVLRVGIYLCIKLKHTKKRQIYTDIEMNRLGK
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00974;
|
2.30.29.130;2.30.30.640;
|
Vesiculovirus glycoprotein family
|
PTM: Glycosylated by host. Palmitoylated by host on Cys-489 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. Host membrane; Single-pass type I membrane protein. Note=The cytoplasmic domain sorts the protein to neurons dentrites instead of axons. When expressed in ex vivo polarized cells like epithelial cells, it sorts the protein to the basolateral side (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Attaches the virus to host cellular receptor, inducing clathrin-dependent endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane. In neurons, neo-synthesized glycoproteins are sorted to the dendrites, where the virus buds. {ECO:0000269|PubMed:20921141}.
|
Vesicular stomatitis Indiana virus (strain Orsay) (VSIV)
|
P04896
|
GNAS2_BOVIN
|
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
| null | null |
adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; sensory perception of chemical stimulus [GO:0007606]
|
cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]
|
adenylate cyclase activator activity [GO:0010856]; beta-2 adrenergic receptor binding [GO:0031698]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; D1 dopamine receptor binding [GO:0031748]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; insulin-like growth factor receptor binding [GO:0005159]; ionotropic glutamate receptor binding [GO:0035255]; metal ion binding [GO:0046872]; mu-type opioid receptor binding [GO:0031852]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, G(s) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63094}; Lipid-anchor {ECO:0000250|UniProtKB:P63094}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146, PubMed:2022671, PubMed:9395396). GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2 (By similarity). {ECO:0000250|UniProtKB:P63092, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:9395396, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146}.
|
Bos taurus (Bovine)
|
P04897
|
GNAI2_RAT
|
MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled adenosine receptor signaling pathway [GO:0001973]; G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process [GO:0140199]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of synaptic transmission [GO:0050805]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of urine volume [GO:0035810]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of calcium ion transport [GO:0051924]
|
cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; neuronal dense core vesicle [GO:0098992]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, G(i/o/t/z) subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division.
|
Rattus norvegicus (Rat)
|
P04899
|
GNAI2_HUMAN
|
MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPSRADDARQLFALSCTAEEQGVLPDDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITHSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled adenosine receptor signaling pathway [GO:0001973]; G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; negative regulation of adenylate cyclase activity [GO:0007194]; negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process [GO:0140199]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of synaptic transmission [GO:0050805]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of urine volume [GO:0035810]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of calcium ion transport [GO:0051924]; response to nutrient [GO:0007584]; signal transduction [GO:0007165]
|
cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; midbody [GO:0030496]; neuronal dense core vesicle [GO:0098992]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, G(i/o/t/z) subfamily
|
PTM: (Microbial infection) Deamidated at Gln-205 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. {ECO:0000269|PubMed:17635935}.; FUNCTION: [Isoform sGi2]: Regulates the cell surface density of dopamine receptors DRD2 by sequestrating them as an intracellular pool. {ECO:0000269|PubMed:17550964}.
|
Homo sapiens (Human)
|
P04903
|
GSTA2_RAT
|
MSGKPVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILDLTEMIIQLVICPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLLYVEEFDASLLTSFPLLKAFKSRISSLPNVKKFLQPGSQRKPAMDAKQIEEARKVFKF
|
2.5.1.18
| null |
epithelial cell differentiation [GO:0030855]; glutathione metabolic process [GO:0006749]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
dinitrosyl-iron complex binding [GO:0035731]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]
|
PF00043;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P10648}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P10648};
| null | null | null | null |
FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. {ECO:0000250|UniProtKB:P10648}.
|
Rattus norvegicus (Rat)
|
P04904
|
GSTA3_RAT
|
MPGKPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNLYGKDMKERALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYHVEELDPSALANFPLLKALRTRVSNLPTVKKFLQPGSQRKPLEDEKCVESAVKIFS
|
2.5.1.18
| null |
glutathione metabolic process [GO:0006749]; lipid metabolic process [GO:0006629]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]
|
PF00043;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:Q16772}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:Q16772}; CATALYTIC ACTIVITY: Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione; Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865; Evidence={ECO:0000250|UniProtKB:Q16772}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937; Evidence={ECO:0000250|UniProtKB:Q16772}; CATALYTIC ACTIVITY: Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928, ChEBI:CHEBI:17026, ChEBI:CHEBI:63837; Evidence={ECO:0000250|UniProtKB:Q16772}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929; Evidence={ECO:0000250|UniProtKB:Q16772};
| null | null | null | null |
FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively (By similarity). Has substantial activity toward aflatoxin B1-8,9-epoxide (By similarity). {ECO:0000250|UniProtKB:P30115, ECO:0000250|UniProtKB:Q16772}.
|
Rattus norvegicus (Rat)
|
P04905
|
GSTM1_RAT
|
MPMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK
|
2.5.1.18
| null |
cellular detoxification of nitrogen compound [GO:0070458]; cellular response to xenobiotic stimulus [GO:0071466]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; nitrobenzene metabolic process [GO:0018916]; prostaglandin metabolic process [GO:0006693]; response to amino acid [GO:0043200]; response to axon injury [GO:0048678]; response to ethanol [GO:0045471]; response to lead ion [GO:0010288]; response to metal ion [GO:0010038]; response to xenobiotic stimulus [GO:0009410]; sensory perception of smell [GO:0007608]; xenobiotic catabolic process [GO:0042178]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
|
enzyme binding [GO:0019899]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; nickel cation binding [GO:0016151]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; steroid binding [GO:0005496]
|
PF00043;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Mu family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:8110735, ECO:0000269|PubMed:8664265}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000305|PubMed:8110735, ECO:0000305|PubMed:8664265}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133768; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797; Evidence={ECO:0000250|UniProtKB:P09488}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P09488}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133772; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000250|UniProtKB:P09488}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133769; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000250|UniProtKB:P09488}; CATALYTIC ACTIVITY: Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000250|UniProtKB:P09488};
| null | null | null | null |
FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process (PubMed:8110735, PubMed:8664265). Participates in the formation of novel hepoxilin regioisomers (By similarity). {ECO:0000250|UniProtKB:P09488, ECO:0000269|PubMed:8110735, ECO:0000269|PubMed:8664265}.
|
Rattus norvegicus (Rat)
|
P04906
|
GSTP1_RAT
|
MPPYTIVYFPVRGRCEATRMLLADQGQSWKEEVVTIDVWLQGSLKSTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKDQKEAALVDMVNDGVEDLRCKYGTLIYTNYENGKDDYVKALPGHLKPFETLLSQNQGGKAFIVGNQISFADYNLLDLLLVHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPDHLNRPINGNGKQ
|
2.5.1.18
| null |
animal organ regeneration [GO:0031100]; cellular response to cell-matrix adhesion [GO:0071460]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0071222]; common myeloid progenitor cell proliferation [GO:0035726]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; negative regulation of biosynthetic process [GO:0009890]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of leukocyte proliferation [GO:0070664]; negative regulation of monocyte chemotactic protein-1 production [GO:0071638]; negative regulation of nitric-oxide synthase biosynthetic process [GO:0051771]; negative regulation of smooth muscle cell chemotaxis [GO:0071672]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; oligodendrocyte development [GO:0014003]; positive regulation of superoxide anion generation [GO:0032930]; prostaglandin metabolic process [GO:0006693]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of stress-activated MAPK cascade [GO:0032872]; response to amino acid [GO:0043200]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to L-ascorbic acid [GO:0033591]; response to nutrient levels [GO:0031667]; response to reactive oxygen species [GO:0000302]; response to toxic substance [GO:0009636]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; TRAF2-GSTP1 complex [GO:0097057]
|
dinitrosyl-iron complex binding [GO:0035731]; fatty acid binding [GO:0005504]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; JUN kinase binding [GO:0008432]; kinase regulator activity [GO:0019207]; organic cyclic compound binding [GO:0097159]; protein kinase binding [GO:0019901]; S-nitrosoglutathione binding [GO:0035730]; toxic substance binding [GO:0015643]
|
PF14497;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Pi family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133772; Evidence={ECO:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133769; Evidence={ECO:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000250|UniProtKB:P09211};
| null | null | null | null |
FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000250|UniProtKB:P09211}.
|
Rattus norvegicus (Rat)
|
P04908
|
H2A1B_HUMAN
|
MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
| null | null |
chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; negative regulation of cell population proliferation [GO:0008285]; protein localization to CENP-A containing chromatin [GO:0061644]
|
CENP-A containing nucleosome [GO:0043505]; extracellular exosome [GO:0070062]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000269|PubMed:15823041}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM37 may promote transformation of cells in a number of breast cancers (PubMed:25470042). Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (PubMed:27083998). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16702407, ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22980979, ECO:0000269|PubMed:24352239, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:27083998}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000269|PubMed:11709551, ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:15078818, ECO:0000269|PubMed:15823041, ECO:0000269|PubMed:16457589, ECO:0000269|PubMed:24140421}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239). {ECO:0000269|PubMed:24352239}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000250|UniProtKB:P22752}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Homo sapiens (Human)
|
P04909
|
H2A1_SCHPO
|
MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKTSGRTGKPSQEL
| null | null |
double-strand break repair [GO:0006302]; heterochromatin organization [GO:0070828]; homologous chromosome segregation [GO:0045143]; mitotic chromosome condensation [GO:0007076]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]
|
chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]
|
chromatin-protein adaptor activity [GO:0140463]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:15226425}.; PTM: Acetylated by esa1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:15226425}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P04910
|
H2A2_SCHPO
|
MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL
| null | null |
double-strand break repair [GO:0006302]; heterochromatin organization [GO:0070828]; homologous chromosome segregation [GO:0045143]; mitotic chromosome condensation [GO:0007076]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]
|
chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]
|
chromatin-protein adaptor activity [GO:0140463]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:15226425}.; PTM: Acetylated by esa1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:15226425}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P04911
|
H2A1_YEAST
|
MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKATKASQEL
| null | null |
chromatin organization [GO:0006325]; DNA repair [GO:0006281]; heterochromatin organization [GO:0070828]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741}.; PTM: N-acetylated by NAT4.; PTM: Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.; PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239). {ECO:0000269|PubMed:24352239}.; PTM: Sumoylated to from H2AK126su. May lead to transcriptional repression. {ECO:0000269|PubMed:16598039}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741, ECO:0000269|PubMed:16299494}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04912
|
H2A2_YEAST
|
MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL
| null | null |
chromatin organization [GO:0006325]; DNA repair [GO:0006281]; heterochromatin organization [GO:0070828]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741}.; PTM: N-acetylated by NAT4.; PTM: Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.; PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239). {ECO:0000269|PubMed:24352239}.; PTM: Sumoylated to from H2AK126su. May lead to transcriptional repression. {ECO:0000269|PubMed:16598039}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741, ECO:0000269|PubMed:16299494}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04913
|
H2B1_SCHPO
|
MSAAEKKPASKAPAGKAPRDTMKSADKKRGKNRKETYSSYIYKVLKQVHPDTGISNQAMRILNSFVNDIFERIATEASKLAAYNKKSTISSREIQTAVRLILPGELAKHAVTEGTKSVTKYSSSAQ
| null | null |
chromatin remodeling [GO:0006338]; double-strand break repair via homologous recombination [GO:0000724]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
chromatin-protein adaptor activity [GO:0140463]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitinated by the rhp6/ubc2-bre1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity). {ECO:0000250}.; PTM: Phosphorylated by shk1 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation (By similarity). {ECO:0000250}.; PTM: Acetylation of N-terminal lysines and particularly formation of H2BK11ac has a positive effect on transcription. {ECO:0000250}.; PTM: Sumoylation to form H2BK6su or H2BK7su occurs preferentially near the telomeres and represses gene transcription. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P04916
|
RET4_RAT
|
MEWVWALVLLAALGGGSAERDCRVSSFRVKENFDKARFSGLWYAIAKKDPEGLFLQDNIIAEFSVDEKGHMSATAKGRVRLLSNWEVCADMVGTFTDTEDPAKFKMKYWGVASFLQRGNDDHWIIDTDYDTFALQYSCRLQNLDGTCADSYSFVFSRDPNGLTPETRRLVRQRQEELCLERQYRWIEHNGYCQSRPSRNSL
| null | null |
cardiac muscle tissue development [GO:0048738]; detection of light stimulus involved in visual perception [GO:0050908]; embryonic organ morphogenesis [GO:0048562]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; embryonic skeletal system development [GO:0048706]; eye development [GO:0001654]; female genitalia morphogenesis [GO:0048807]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; heart trabecula formation [GO:0060347]; lung development [GO:0030324]; maintenance of gastrointestinal epithelium [GO:0030277]; male gonad development [GO:0008584]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of insulin secretion [GO:0032024]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to muscle activity [GO:0014850]; response to retinoic acid [GO:0032526]; response to xenobiotic stimulus [GO:0009410]; retina development in camera-type eye [GO:0060041]; retinal metabolic process [GO:0042574]; retinol metabolic process [GO:0042572]; retinol transport [GO:0034633]; spermatogenesis [GO:0007283]; urinary bladder development [GO:0060157]; uterus development [GO:0060065]; vagina development [GO:0060068]; vitamin A import into cell [GO:0071939]
|
extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
protein-containing complex binding [GO:0044877]; retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4708098}.
| null | null | null | null | null |
FUNCTION: Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues (PubMed:4708098). Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane (By similarity). {ECO:0000250|UniProtKB:P02753, ECO:0000269|PubMed:4708098}.
|
Rattus norvegicus (Rat)
|
P04917
|
SRGN_RAT
|
MRQVPVGTRLVLALAFVLVWGSSVQGYPARRARYQWVRCKPDGIFANCIEEKGPRFDLIAEESNVGPPMTDPVLMRGFPNDFFPISDDYSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSLADMEWEYQPTDENNIVYFNYGPFDRMLTEQNQEQPGDFII
| null | null |
apoptotic process [GO:0006915]; biomineral tissue development [GO:0031214]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; maintenance of granzyme B location in T cell secretory granule [GO:0033382]; maintenance of protease location in mast cell secretory granule [GO:0033373]; mast cell secretory granule organization [GO:0033364]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of bone mineralization [GO:0030502]; negative regulation of cytokine production [GO:0001818]; protein processing [GO:0016485]; regulation of postsynapse organization [GO:0099175]; secretory granule organization [GO:0033363]; T cell secretory granule organization [GO:0033371]
|
cytolytic granule [GO:0044194]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; mast cell granule [GO:0042629]; postsynaptic specialization, intracellular component [GO:0099091]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granule [GO:0030141]; zymogen granule [GO:0042588]
|
collagen binding [GO:0005518]
|
PF04360;
| null |
Serglycin family
|
PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250|UniProtKB:P10124}. Cytolytic granule {ECO:0000250|UniProtKB:P10124}. Secreted, extracellular space {ECO:0000250|UniProtKB:P10124}. Golgi apparatus {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T-lymphocytes from where it is secreted upon cell activation. Secreted constitutively by endothelial cells and macrophages. Located to Golgi apparatus during neutrophil differentiation (By similarity). {ECO:0000250|UniProtKB:P10124, ECO:0000250|UniProtKB:P13609}.
| null | null | null | null | null |
FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P04919
|
B3AT_MOUSE
|
MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREELLRSLESFLDCSLVLPPTDAPSEKALLNLVPVQKELLRRRYLPSPAKPDPNLYNTLDLNGGKGGPGDEDDPLRRTGRIFGGLIRDIRRRYPYYLSDITDALSPQVLAAVIFIYFAALSPAVTFGGLLGEKTRNLMGVSELLISTAVQGILFALLGAQPLLVLGFSGPLLVFEEAFFSFCESNNLEYIVGRAWIGFWLILLVMLVVAFEGSFLVQYISRYTQEIFSFLISLIFIYETFSKLIKIFQDYPLQQTYAPVVMKPKPQGPVPNTALFSLVLMAGTFLLAMTLRKFKNSTYFPGKLRRVIGDFGVPISILIMVLVDSFIKGTYTQKLSVPDGLKVSNSSARGWVIHPLGLYRLFPTWMMFASVLPALLVFILIFLESQITTLIVSKPERKMIKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPFVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRLILPLIFRELELQCLDGDDAKVTFDEENGLDEYDEVPMPV
| null | null |
bicarbonate transport [GO:0015701]; blood coagulation [GO:0007596]; chloride transport [GO:0006821]; erythrocyte development [GO:0048821]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; negative regulation of urine volume [GO:0035811]; pH elevation [GO:0045852]; plasma membrane phospholipid scrambling [GO:0017121]; positive regulation of T cell proliferation [GO:0042102]; protein localization to plasma membrane [GO:0072659]; regulation of intracellular pH [GO:0051453]; response to activity [GO:0014823]; response to arsenic-containing substance [GO:0046685]; response to carbon dioxide [GO:0010037]; response to hydrogen peroxide [GO:0042542]; transmembrane transport [GO:0055085]
|
ankyrin-1 complex [GO:0170014]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cortical cytoskeleton [GO:0030863]; cytoplasmic side of plasma membrane [GO:0009898]; intercalated disc [GO:0014704]; membrane [GO:0016020]; plasma membrane [GO:0005886]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; ankyrin binding [GO:0030506]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; hemoglobin binding [GO:0030492]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; solute:inorganic anion antiporter activity [GO:0005452]
|
PF07565;PF00955;
|
1.10.287.570;
|
Anion exchanger (TC 2.A.31) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2713407}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000250|UniProtKB:P02730}.
|
CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P02730};
| null | null | null | null |
FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine. {ECO:0000250|UniProtKB:P02730}.
|
Mus musculus (Mouse)
|
P04920
|
B3A2_HUMAN
|
MSSAPRRPAKGADSFCTPEPESLGPGTPGFPEQEEDELHRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEDEASEAEGARALTQPSPVSTPSSVQFFLQEDDSADRKAERTSPSSPAPLPHQEATPRASKGAQAGTQVEEAEAEAVAVASGTAGGDDGGASGRPLPKAQPGHRSYNLQERRRIGSMTGAEQALLPRVPTDEIEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQSGREGREPGPTPRARPRAPHKPHEVFVELNELLLDKNQEPQWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTLAHGAVLLDLDQQTLPGVAHQVVEQMVISDQIKAEDRANVLRALLLKHSHPSDEKDFSFPRNISAGSLGSLLGHHHGQGAESDPHVTEPLMGGVPETRLEVERERELPPPAPPAGITRSKSKHELKLLEKIPENAEATVVLVGCVEFLSRPTMAFVRLREAVELDAVLEVPVPVRFLFLLLGPSSANMDYHEIGRSISTLMSDKQFHEAAYLADEREDLLTAINAFLDCSVVLPPSEVQGEELLRSVAHFQRQMLKKREEQGRLLPTGAGLEPKSAQDKALLQMVEAAGAAEDDPLRRTGRPFGGLIRDVRRRYPHYLSDFRDALDPQCLAAVIFIYFAALSPAITFGGLLGEKTQDLIGVSELIMSTALQGVVFCLLGAQPLLVIGFSGPLLVFEEAFFSFCSSNHLEYLVGRVWIGFWLVFLALLMVALEGSFLVRFVSRFTQEIFAFLISLIFIYETFYKLVKIFQEHPLHGCSASNSSEVDGGENMTWAGARPTLGPGNRSLAGQSGQGKPRGQPNTALLSLVLMAGTFFIAFFLRKFKNSRFFPGRIRRVIGDFGVPIAILIMVLVDYSIEDTYTQKLSVPSGFSVTAPEKRGWVINPLGEKSPFPVWMMVASLLPAILVFILIFMETQITTLIISKKERMLQKGSGFHLDLLLIVAMGGICALFGLPWLAAATVRSVTHANALTVMSKAVAPGDKPKIQEVKEQRVTGLLVALLVGLSIVIGDLLRQIPLAVLFGIFLYMGVTSLNGIQFYERLHLLLMPPKHHPDVTYVKKVRTLRMHLFTALQLLCLALLWAVMSTAASLAFPFILILTVPLRMVVLTRIFTDREMKCLDANEAEPVFDEREGVDEYNEMPMPV
| null | null |
amelogenesis [GO:0097186]; bicarbonate transport [GO:0015701]; digestive tract development [GO:0048565]; monoatomic anion transport [GO:0006820]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000565]; osteoclast differentiation [GO:0030316]; positive regulation of enamel mineralization [GO:0070175]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of bone resorption [GO:0045124]; regulation of intracellular pH [GO:0051453]; spermatogenesis [GO:0007283]; transmembrane transport [GO:0055085]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; monoatomic anion transmembrane transporter activity [GO:0008509]; solute:inorganic anion antiporter activity [GO:0005452]; transmembrane transporter activity [GO:0022857]
|
PF07565;PF00955;
|
1.10.287.570;
|
Anion exchanger (TC 2.A.31) family
| null |
SUBCELLULAR LOCATION: [Isoform A]: Apical cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform B1]: Apical cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform B2]: Apical cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:34668226}; CATALYTIC ACTIVITY: [Isoform A]: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15184086}; CATALYTIC ACTIVITY: [Isoform B1]: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15184086}; CATALYTIC ACTIVITY: [Isoform B2]: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15184086};
| null | null | null | null |
FUNCTION: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity). {ECO:0000250|UniProtKB:P13808, ECO:0000269|PubMed:15184086, ECO:0000269|PubMed:34668226}.
|
Homo sapiens (Human)
|
P04921
|
GLPC_HUMAN
|
MWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDGRMETSTPTIMDIVVIAGVIAAVAIVLVSLLFVMLRYMYRHKGTYHTNEAKGTEFAESADAALQGDPALQDAGDSSRKEYFI
| null | null | null |
cortical cytoskeleton [GO:0030863]; membrane [GO:0016020]; plasma membrane [GO:0005886]
| null | null | null |
Glycophorin-C family
|
PTM: O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7106126}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Note=Linked to the membrane via band 4.1.
| null | null | null | null | null |
FUNCTION: This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.
|
Homo sapiens (Human)
|
P04924
|
TNFA_RABIT
|
MSTESMIRDVELAEGPLPKKAGGPQGSKRCLCLSLFSFLLVAGATTLFCLLHFRVIGPQEEEQSPNNLHLVNPVAQMVTLRSASRALSDKPLAHVVANPQVEGQLQWLSQRANALLANGMKLTDNQLVVPADGLYLIYSQVLFSGQGCRSYVLLTHTVSRFAVSYPNKVNLLSAIKSPCHRETPEEAEPMAWYEPIYLGGVFQLEKGDRLSTEVNQPEYLDLAESGQVYFGIIAL
| null | null |
antiviral innate immune response [GO:0140374]; cellular response to amino acid stimulus [GO:0071230]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nicotine [GO:0071316]; cellular response to type II interferon [GO:0071346]; chronic inflammatory response to antigenic stimulus [GO:0002439]; cortical actin cytoskeleton organization [GO:0030866]; defense response to Gram-positive bacterium [GO:0050830]; embryonic digestive tract development [GO:0048566]; endothelial cell apoptotic process [GO:0072577]; epithelial cell proliferation involved in salivary gland morphogenesis [GO:0060664]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glucose metabolic process [GO:0006006]; humoral immune response [GO:0006959]; inflammatory response to wounding [GO:0090594]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; JNK cascade [GO:0007254]; leukocyte tethering or rolling [GO:0050901]; macrophage activation involved in immune response [GO:0002281]; microglial cell activation [GO:0001774]; necroptotic signaling pathway [GO:0097527]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of branching involved in lung morphogenesis [GO:0061048]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of glucose import [GO:0046325]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein-containing complex disassembly [GO:0043242]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular wound healing [GO:0061044]; negative regulation of viral genome replication [GO:0045071]; osteoclast differentiation [GO:0030316]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of blood microparticle formation [GO:2000334]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chronic inflammatory response to antigenic stimulus [GO:0002876]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of fever generation [GO:0031622]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of hair follicle development [GO:0051798]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-33 production [GO:0150129]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of leukocyte adhesion to arterial endothelial cell [GO:1904999]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein transport [GO:0051222]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of synoviocyte proliferation [GO:1901647]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translational initiation by iron [GO:0045994]; positive regulation of type II interferon production [GO:0032729]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; positive regulation of vitamin D biosynthetic process [GO:0060557]; protein localization to plasma membrane [GO:0072659]; regulation of branching involved in salivary gland morphogenesis [GO:0060693]; regulation of endothelial cell apoptotic process [GO:2000351]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of immunoglobulin production [GO:0002637]; regulation of insulin secretion [GO:0050796]; regulation of membrane lipid metabolic process [GO:1905038]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of synapse organization [GO:0050807]; response to glucocorticoid [GO:0051384]; sequestering of triglyceride [GO:0030730]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor production [GO:0010573]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; phagocytic cup [GO:0001891]; recycling endosome [GO:0055037]
|
cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). {ECO:0000250}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By similarity). {ECO:0000250}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated by SIRT6, promoting its secretion. {ECO:0000250|UniProtKB:P01375}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). {ECO:0000250|UniProtKB:P01375, ECO:0000250|UniProtKB:P06804}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
|
Oryctolagus cuniculus (Rabbit)
|
P04925
|
PRIO_MOUSE
|
MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG
| null | null |
activation of protein kinase activity [GO:0032147]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; cellular response to xenobiotic stimulus [GO:0071466]; intracellular copper ion homeostasis [GO:0006878]; learning or memory [GO:0007611]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of amyloid precursor protein catabolic process [GO:1902992]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of dendritic spine maintenance [GO:1902951]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of type II interferon production [GO:0032689]; neuron projection maintenance [GO:1990535]; nucleobase-containing compound metabolic process [GO:0006139]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein targeting to membrane [GO:0090314]; protein destabilization [GO:0031648]; protein homooligomerization [GO:0051260]; regulation of calcium ion import across plasma membrane [GO:1905664]; regulation of glutamate receptor signaling pathway [GO:1900449]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of potassium ion transmembrane transport [GO:1901379]; regulation of protein localization [GO:0032880]; response to amyloid-beta [GO:1904645]; response to cadmium ion [GO:0046686]; response to copper ion [GO:0046688]; response to oxidative stress [GO:0006979]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; side of membrane [GO:0098552]; terminal bouton [GO:0043195]
|
amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; ATP-dependent protein binding [GO:0043008]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; lamin binding [GO:0005521]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; molecular condensate scaffold activity [GO:0140693]; molecular function activator activity [GO:0140677]; protease binding [GO:0002020]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor activity [GO:0038023]; transmembrane transporter binding [GO:0044325]; type 5 metabotropic glutamate receptor binding [GO:0031802]
|
PF00377;PF11587;
|
1.10.790.10;
|
Prion family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19568430}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:9837873}; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000269|PubMed:11756421}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to. vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16923158, ECO:0000269|PubMed:9837873}.
| null | null | null | null | null |
FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (PubMed:12732622, PubMed:16492732, PubMed:19242475, PubMed:19568430). {ECO:0000250|UniProtKB:P04156, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19242475, ECO:0000269|PubMed:19568430}.
|
Mus musculus (Mouse)
|
P04932
|
MSP1_PLAFK
|
MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFHKEKMILNEEEITTKGASAQSGTSGTSGTSGPSGPSGTSPSSRSNTLPRSNTSSGASPPADASDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLDKINEIKNPPPANSGNTPNTLLDKNKKIEEHEKEIKEIAKTIKFNIDSLFTDPLELEYYLREKNKNIDISAKVETKESTEPNEYPNGVTYPLSYNDINNALNELNSFGDLINPFDYTKEPSKNIYTDNERKKFINEIKEKIKIEKKKIESDKKSYEDRSKSLNDITKEYEKLLNEIYDSKFNNNIDLTNFEKMMGKRYSYKVEKLTHHNTFASYENSKHNLEKLTKALKYMEDYSLRNIVVEKELKYYKNLISKIENEIETLVENIKKDEEQLFEKKITKDENKPDEKILEVSDIVKVQVQKVLLMNKIDELKKTQLILKNVELKHNIHVPNSYKQENKQEPYYLIVLKKEIDKLKVFMPKVESLINEEKKNIKTEGQSDNSEPSTEGEITGQATTKPGQQAGSALEGDSVQAQAQEQKQAQPPVPVPVPEAKAQVPTPPAPVNNKTENVSKLDYLEKLYEFLNTSYICHKYILVSHSTMNEKILKQYKITKEEESKLSSCDPLDLLFNIQNNIPVMYSMFDSLNNSLSQLFMEIYEKEMVCNLYKLKDNDKIKNLLEEAKKVSTSVKTLSSSSMQPLSLTPQDKPEVSANDDTSHSTNLNNSLKLFENILSLGKNKNIYQELIGQKSSENFYEKILKDSDTFYNESFTNFVKSKADDINSLNDESKRKKLEEDINKLKKTLQLSFDLYNKYKLKLERLFDKKKTVGKYKMQIKKLTLLKEQLESKLNSLNNPKHVLQNFSVFFNKKKEAEIAETENTLENTKILLKHYKGLVKYYNGESSPLKTLSEESIQTEDNYASLENFKVLSKLEGKLKDNLNLEKKKLSYLSSGLHHLIAELKEVIKNKNYTGNSPSENNTDVNNALESYKKFLPEGTDVATVVSESGSDTLEQSQPKKPASTHVGAESNTITTSQNVDDEVDDVIIVPIFGESEEDYDDLGQVVTGEAVTPSVIDNILSKIENEYEVLYLKPLAGVYRSLKKQLENNVMTFNVNVKDILNSRFNKRENFKNVLESDLIPYKDLTSSNYVVKDPYKFLNKEKRDKFLSSYNYIKDSIDTDINFANDVLGYYKILSEKYKSDLDSIKKYINDKQGENEKYLPFLNNIETLYKTVNDKIDLFVIHLEAKVLNYTYEKSNVEVKIKELNYLKTIQDKLADFKKNNNFVGIADLSTDYNHNNLLTKFLSTGMVFENLAKTVLSNLLDGNLQGMLNISQHQCVKKQCPQNSGCFRHLDEREECKCLLNYKQEGDKCVENPNPTCNENNGGCDADAKCTEEDSGSNGKKITCECTKPDSYPLFDGIFCSSSNFLGISFLLILMLILYSFI
| null | null | null |
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; vacuolar membrane [GO:0005774]
| null |
PF12946;PF07462;
|
2.10.25.10;
| null |
PTM: The p190 precursor is cleaved by SUB1 prior to merozoite egress into 4 subunits p83, p30, p38, and p42 which remain non-covalently associated. SUB1-mediated proteolytic cleavage occurs in an orderly manner; the first cleavage occurs at the p83/p30 site, followed by cleavage at the p30/p38 site, the last cleavage occurs at the p38/p42 site. The order of cleavage is essential for parasite viability (By similarity). SUB1-mediated processing is essential for merozoite egress (By similarity). In a second processing step during erythrocyte invasion, p42 is cleaved by SUB2 into p33 and p19; the latter remains attached to the merozoite surface via its GPI-anchor and stays on the surface during the subsequent ring stage (By similarity). {ECO:0000250|UniProtKB:P04933, ECO:0000250|UniProtKB:Q8I0U8}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04933}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P04933}.; SUBCELLULAR LOCATION: [p19 subunit]: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=In free merozoites, localizes to the cell membrane (By similarity). Following merozoite invasion of host erythrocytes, p19 subunit is endocytosed into small food vacuoles in the ring stage and persists throughout the subsequent intra-erythrocytic stages at the surface of the food vacuole where it forms clusters (By similarity). {ECO:0000250|UniProtKB:Q8I0U8}.
| null | null | null | null | null |
FUNCTION: During the asexual blood stage, involved in merozoite egress from host erythrocytes possibly via its interaction with the host cytoskeleton protein spectrin resulting in the destabilization of the host cytoskeleton and thus leading to erythrocyte cell membrane rupture (By similarity). Involved in the binding to host erythrocytes and is required for host erythrocyte invasion (By similarity). {ECO:0000250|UniProtKB:P04933, ECO:0000250|UniProtKB:Q8I0U8}.; FUNCTION: [p33 subunit]: By binding to host proinflammatory cytokine S100P may interfere with host immune responses. {ECO:0000250|UniProtKB:Q8I0U8}.; FUNCTION: [p19 subunit]: Involved in merozoite invasion of host erythrocytes. May play a role in the biogenesis and/or function of the food vacuole during the intraerythrocytic development. {ECO:0000250|UniProtKB:Q8I0U8}.
|
Plasmodium falciparum (isolate K1 / Thailand)
|
P04933
|
MSP1_PLAFW
|
MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSKGSVASGGSGGSVASGGSVASGGSVASGGSVASGGSGNSRRTNPSDNSSDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLDKINEIKNPPPANSGNTPNTLLDKNKKIEEHEKEIKEIAKTIKFNIDSLFTDPLELEYYLREKNKNIDISAKVETKESTEPNEYPNGVTYPLSYNDINNALNELNSFGDLINPFDYTKEPSKNIYTDNERKKFINEIKEKIKIEKKKIESDKKSYEDRSKSLNDITKEYEKLLNEIYDSKFNNNIDLTNFEKMMGKRYSYKVEKLTHHNTFASYENSKHNLEKLTKALKYMEDYSLRNIVVEKELKYYKNLISKIENEIETLVENIKKDEEQLFEKKITKDENKPDEKILEVSDIVKVQVQKVLLMNKIDELKKTQLILKNVELKHNIHVPNSYKQENKQEPYYLIVLKKEIDKLKVFMPKVESLINEEKKNIKTEGQSDNSEPSTEGEITGQATTKPGQQAGSALEGDSVQAQAQEQKQAQPPVPVPVPEAKAQVPTPPAPVNNKTENVSKLDYLEKLYEFLNTSYICHKYILVSHSTMNEKILKQYKITKEEESKLSSCDPLDLLFNIQNNIPVMYSMFDSLNNSLSQLFMEIYEKEMVCNLYKLKDNDKIKNLLEEAKKVSTSVKTLSSSSMQPLSLTPQDKPEVSANDDTSHSTNLNNSLKLFENILSLGKNKNIYQELIGQKSSENFYEKILKDSDTFYNESFTNFVKSKADDINSLNDESKRKKLEEDINKLKKTLQLSFDLYNKYKLKLERLFDKKKTVGKYKMQIKKLTLLKEQLESKLNSLNNPKHVLQNFSVFFNKKKEAEIAETENTLENTKILLKHYKGLVKYYNGESSPLKTLSEESIQTEDNYASLENFKVLSKLEGKLKDNLNLEKKKLSYLSSGLHHLIAELKEVIKNKNYTGNSPSENNTDVNNALESYKKFLPEGTDVATVVSESGSDTLEQSQPKKPASTHVGAESNTITTSQNVDDEVDDVIIVPIFGESEEDYDDLGQVVTGEAVTPSVIDNILSKIENEYEVLYLKPLAGVYRSLKKQLENNVMTFNVNVKDILNSRFNKRENFKNVLESDLIPYKDLTSSNYVVKDPYKFLNKEKRDKFLSSYNYIKDSIDTDINFANDVLGYYKILSEKYKSDLDSIKKYINDKQGENEKYLPFLNNIETLYKTVNDKIDLFVIHLEAKVLNYTYEKSNVEVKIKELNYLKTIQDKLADFKKNNNFVGIADLSTDYNHNNLLTKFLSTGMVFENLAKTVLSNLLDGNLQGMLNISQHQCVKKQCPQNSGCFRHLDEREECKCLLNYKQEGDKCVENPNPTCNENNGGCDADAKCTEEDSGSNGKKITCECTKPDSYPLFDGIFCSSSNFLGISFLLILMLILYSFI
| null | null | null |
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; vacuolar membrane [GO:0005774]
| null |
PF12946;PF07462;
|
2.10.25.10;
| null |
PTM: The p190 precursor is cleaved by SUB1 prior to merozoite egress into 4 subunits p83, p30, p38, and p42 which remain non-covalently associated (PubMed:12404375, PubMed:14766224, PubMed:20735778, PubMed:2995820). SUB1-mediated proteolytic cleavage occurs in an orderly manner; the first cleavage occurs at the p83/p30 site, followed by cleavage at the p30/p38 site, the last cleavage occurs at the p38/p42 site (PubMed:20735778). The order of cleavage is essential for parasite viability (PubMed:20735778). SUB1-mediated processing is essential for merozoite egress (By similarity). In a second processing step during erythrocyte invasion, p42 is cleaved by SUB2 into p33 and p19; the latter remains attached to the merozoite surface via its GPI-anchor and stays on the surface during the subsequent ring stage (PubMed:20735778). {ECO:0000250|UniProtKB:Q8I0U8, ECO:0000269|PubMed:12404375, ECO:0000269|PubMed:14766224, ECO:0000269|PubMed:20735778, ECO:0000269|PubMed:2995820}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20735778}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:2995820}.; SUBCELLULAR LOCATION: [p19 subunit]: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=In free merozoites, localizes to the cell membrane (By similarity). Following merozoite invasion of host erythrocytes, p19 subunit is endocytosed into small food vacuoles in the ring stage and persists throughout the subsequent intra-erythrocytic stages at the surface of the food vacuole where it forms clusters (By similarity). {ECO:0000250|UniProtKB:Q8I0U8}.
| null | null | null | null | null |
FUNCTION: During the asexual blood stage, involved in merozoite egress from host erythrocytes possibly via its interaction with the host cytoskeleton protein spectrin resulting in the destabilization of the host cytoskeleton and thus leading to erythrocyte cell membrane rupture (By similarity). Involved in the binding to host erythrocytes and is required for host erythrocyte invasion (PubMed:10802320). {ECO:0000250|UniProtKB:Q8I0U8, ECO:0000269|PubMed:10802320}.; FUNCTION: [p33 subunit]: By binding to host proinflammatory cytokine S100P may interfere with host immune responses. {ECO:0000250|UniProtKB:Q8I0U8}.; FUNCTION: [p19 subunit]: Involved in merozoite invasion of host erythrocytes (By similarity). May play a role in the biogenesis and/or function of the food vacuole during the intraerythrocytic development (By similarity). {ECO:0000250|UniProtKB:Q8I0U8}.
|
Plasmodium falciparum (isolate Wellcome)
|
P04936
|
POLG_HRV2
|
MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDVLEKGIPTLQSPTVEACGYSDRIIQITRGDSTITSQDVANAIVAYGVWPHYLSSKDASAIDKPSQPDTSSNRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQGTLIVALIPEHQIASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTLLGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPLETSSAINTIPITISISPMCAEFSGARAKRQGLPVFITPGSGQFLTTDDFQSPCALPWYHPTKEISIPGEVKNLVEICQVDSLVPINNTDTYINSENMYSVVLQSSINAPDKIFSIRTDVASQPLATTLIGEISSYFTHWTGSLRFSFMFCGTANTTVKLLLAYTPPGIAEPTTRKDAMLGTHVIWDVGLQSTISMVVPWISASHYRNTSPGRSTSGYITCWYQTRLVIPPQTPPTARLLCFVSGCKDFCLRMARDTNLHLQSGAIAQNPVENYIDEVLNEVLVVPNINSSNPTTSNSAPALDAAETGHTSSVQPEDVIETRYVQTSQTRDEMSLESFLGRSGCIHESKLEVTLANYNKENFTVWAINLQEMAQIRRKFELFTYTRFDSEITLVPCISALSQDIGHITMQYMYVPPGAPVPNSRDDYAWQSGTNASVFWQHGQAYPRFSLPFLSVASAYYMFYDGYDEQDQNYGTANTNNMGSLCSRIVTEKHIHKVHIMTRIYHKAKHVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTAIVTRPIITTAGPSDMYVHVGNLIYRNLHLFNSEMHESILVSYSSDLIIYRTNTVGDDYIPSCDCTQATYYCKHKNRYFPITVTSHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKLLCKHGVIGIVTAGGDNHVAFIDLRHFHCAEEQGVTDYIHMLGEAFGNGFVDSVKEHIHAINPVGNISKKIIKWMLRIISAMVIIIRNSSDPQTILATLTLIGCSGSPWRFLKEKFCKWTQLNYIHKESDSWLKKFTEACNAARGLEWIGNKISKFIEWMKSMLPQAQLKVKYLNELKKLNLYEKQVESLRVADMKTQEKIKMEIDTLHDLSRKFLPLYASEAKRIKTLYIKCDNIIKQKKRCEPVAIVIHGPPGAGKSITTNFLAKMITNDSDIYSLPPDPKYFDGYDQQSVVIMDDIMQNPAGDDMTLFCQMVSSVTFIPPMADLPDKGKAFDSRFVLCSTNHSLLTPPTITSLPAMNRRFFLDLDIIVHDNFKDPQGKLNVAAAFRPCDVDNRIGNARCCPFVCGKAVSFKDRNSCNKYSLAQVYNIMIEEDRRRRQVVDVMTAIFQGPIDMKNPPPPAITDLLQSVRTPEVIKYCEGNRWIIPAECKIEKELNLANTIITIIANVIGMARIIYVIYKLFCTLQGPYSGEPKPKTKIPERRVVTQGPEEEFGMSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGITTKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNNEDDYPNCNLALLANQPEPTIINVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAMLLRSYFTDVQGQITLSKKTSECNLPSIHTPCKTKLQPSVFYDVFPGSKEPAVLSEKDARLQVDFNEALFSKYKGNTDCSINDHIRIASSHYAAQLITLDIDPKPITLEDSVFGTDGLEALDLNTSAGFPYIAMGVKKRDLINNKTKDISKLKEAIDKYGVDLPMVTFLKDELRKHEKVIKGKTRVIEASSVNDTLLFRTTFGNLFSKFHLNPGIVTGSAVGCDPEVFWSKIPAMLDDKCIMAFDYTNYDGSIHPIWFEALKQVLVDLSFNPTLIDRLCKSKHIFKNTYYEVEGGVPSGCSGTSIFNTMINNIIIRTLVLDAYKNIDLDKLKIIAYGDDVIFSYIHELDMEAIAIEGVKYGLTITPADKSNTFVKLDYSNVTFLKRGFKQDEKYNFLIHPTFPEDEIFESIRWTKKPSQMHEHVLSLCHLMWHNGRDAYKKFVEKIRSVSAGRALYIPPYDLLLHEWYEKF
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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]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; 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 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]
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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]
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PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910;
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1.20.960.20;2.40.10.120;2.60.120.20;3.30.70.270;3.40.50.300;6.10.20.20;4.10.880.10;2.40.10.10;
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Picornaviruses polyprotein family
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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}.
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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.
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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 to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process (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 (PubMed:11034318). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (PubMed:20622012). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301, ECO:0000269|PubMed:11034318, ECO:0000269|PubMed:20622012}.; 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. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (PubMed:17005635). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (PubMed:17005635). 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 (Probable). {ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512}.; 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: [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}.; 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 NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.
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Human rhinovirus 2 (HRV-2)
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P04937
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FINC_RAT
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MLRGPGPGRLLLLAVLCLGTSVRCTETGKSKRQAQQIVQPPSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHVLQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGDKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFHYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYSNRNYSDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGQWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDRCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHQEVTRFDFTTSASTPVTSNTVTGETAPFSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGVPRSDDVPAPKDLQFVEVTDVKVTIMWTPPNSAVTGYRVDVLPVNLPGEHGQRLPVNRNTFAEVTGLSPGVTYLFKVFAVHQGRESKPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTVGLTRGGQPKQYNVGPMASKYPLRNLQPGSEYTVTLMAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTALEEVVHADQSSCTFENRNPGLEYNVSVYTVKDDKESAPISDTVIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDVTANSFTVHWVAPRAPITGYIIRHHAEHSAGRPRQDRVPPSRNSITLTNLNPGTEYIVTIIAVNGREESPPLIGQQSTVSDVPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYQTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTAPKNGLGPTKSQTVSPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGDEDTAELHGLRPGSEYTVSVVALHGGMESQPLIGVQSTAIPAPTNLKFTQVSPTTLTAQWTAPSVKLTGYRVRVTPKEKTGPMKEINLSPDSTSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRTISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVVIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTNPGYDTENGIQLPGTSHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALHNQRRHKVREEVVTVGNTVNEGLNQPTDDSCFDPYTVSHYAVGEEWERLSDSGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYHQRTNTNVNCPIECFMPLDVQADRDDSRE
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acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; cellular response to amyloid-beta [GO:1904646]; cellular response to angiotensin [GO:1904385]; cellular response to BMP stimulus [GO:0071773]; cellular response to glucose stimulus [GO:0071333]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mercury ion [GO:0071288]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; heart development [GO:0007507]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of apoptotic process [GO:0043066]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of monocyte activation [GO:0150102]; negative regulation of transforming growth factor beta production [GO:0071635]; nervous system development [GO:0007399]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; ossification [GO:0001503]; positive regulation of axon extension [GO:0045773]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of substrate-dependent cell migration, cell attachment to substrate [GO:1904237]; regulation of cell shape [GO:0008360]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of protein phosphorylation [GO:0001932]; response to activity [GO:0014823]; response to glucocorticoid [GO:0051384]; response to iron ion [GO:0010039]; response to ischemia [GO:0002931]; response to ozone [GO:0010193]; response to xenobiotic stimulus [GO:0009410]; substrate adhesion-dependent cell spreading [GO:0034446]; wound healing [GO:0042060]
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apical plasma membrane [GO:0016324]; basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]
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extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; mercury ion binding [GO:0045340]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]; proteoglycan binding [GO:0043394]; signaling receptor binding [GO:0005102]
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PF00039;PF00040;PF00041;
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2.10.70.10;2.10.10.10;2.60.40.10;
| null |
PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11276}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02751}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250|UniProtKB:P02751}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000250|UniProtKB:P11276}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}.
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SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11276}. Secreted {ECO:0000250|UniProtKB:P11276}.
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FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). {ECO:0000250|UniProtKB:P02751, ECO:0000250|UniProtKB:P11276}.; FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.; FUNCTION: Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. {ECO:0000250|UniProtKB:P11276}.
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Rattus norvegicus (Rat)
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P04938
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MUP11_MOUSE
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MKMLLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE
| null | null |
aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; cellular response to testosterone stimulus [GO:0071394]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of lipid storage [GO:0010888]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q5FW60}.
| null | null | null | null | null |
FUNCTION: Major urinary proteins (Mups) bind pheromones, and thus stabilize them to allow slow release into the air from urine marks. May protect pheromones from oxidation. May also act as pheromones themselves. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suckling, territory establishment and dominance (Probable). Binds the pheromone analog 2-sec-butyl-4,5-dihydrothiazole (SBT) in vitro (PubMed:25279835). {ECO:0000269|PubMed:25279835, ECO:0000305}.
|
Mus musculus (Mouse)
|
P04939
|
MUP3_MOUSE
|
MKLLLPLLLLLCLELTLVCIHAEESSSMERNFNVEQISGYWFSIAEASYEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE
| null | null |
aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of lipid storage [GO:0010888]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; response to stilbenoid [GO:0035634]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
|
PTM: Glycosylated. {ECO:0000269|PubMed:16944957}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.
|
Mus musculus (Mouse)
|
P04950
|
OPS3_DROME
|
MESGNVSSSLFGNVSTALRPEARLSAETRLLGWNVPPEELRHIPEHWLTYPEPPESMNYLLGTLYIFFTLMSMLGNGLVIWVFSAAKSLRTPSNILVINLAFCDFMMMVKTPIFIYNSFHQGYALGHLGCQIFGIIGSYTGIAAGATNAFIAYDRFNVITRPMEGKMTHGKAIAMIIFIYMYATPWVVACYTETWGRFVPEGYLTSCTFDYLTDNFDTRLFVACIFFFSFVCPTTMITYYYSQIVGHVFSHEKALRDQAKKMNVESLRSNVDKNKETAEIRIAKAAITICFLFFCSWTPYGVMSLIGAFGDKTLLTPGATMIPACACKMVACIDPFVYAISHPRYRMELQKRCPWLALNEKAPESSAVASTSTTQEPQQTTAA
| null | null |
absorption of UV light [GO:0016039]; cellular response to light stimulus [GO:0071482]; detection of UV [GO:0009589]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; phototransduction, UV [GO:0007604]; visual perception [GO:0007601]
|
membrane [GO:0016020]
|
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: Membrane; Multi-pass membrane protein.
| 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)
|
P04958
|
TETX_CLOTE
|
MPITINNFRYSDPVNNDTIIMMEPPYCKGLDIYYKAFKITDRIWIVPERYEFGTKPEDFNPPSSLIEGASEYYDPNYLRTDSDKDRFLQTMVKLFNRIKNNVAGEALLDKIINAIPYLGNSYSLLDKFDTNSNSVSFNLLEQDPSGATTKSAMLTNLIIFGPGPVLNKNEVRGIVLRVDNKNYFPCRDGFGSIMQMAFCPEYVPTFDNVIENITSLTIGKSKYFQDPALLLMHELIHVLHGLYGMQVSSHEIIPSKQEIYMQHTYPISAEELFTFGGQDANLISIDIKNDLYEKTLNDYKAIANKLSQVTSCNDPNIDIDSYKQIYQQKYQFDKDSNGQYIVNEDKFQILYNSIMYGFTEIELGKKFNIKTRLSYFSMNHDPVKIPNLLDDTIYNDTEGFNIESKDLKSEYKGQNMRVNTNAFRNVDGSGLVSKLIGLCKKIIPPTNIRENLYNRTASLTDLGGELCIKIKNEDLTFIAEKNSFSEEPFQDEIVSYNTKNKPLNFNYSLDKIIVDYNLQSKITLPNDRTTPVTKGIPYAPEYKSNAASTIEIHNIDDNTIYQYLYAQKSPTTLQRITMTNSVDDALINSTKIYSYFPSVISKVNQGAQGILFLQWVRDIIDDFTNESSQKTTIDKISDVSTIVPYIGPALNIVKQGYEGNFIGALETTGVVLLLEYIPEITLPVIAALSIAESSTQKEKIIKTIDNFLEKRYEKWIEVYKLVKAKWLGTVNTQFQKRSYQMYRSLEYQVDAIKKIIDYEYKIYSGPDKEQIADEINNLKNKLEEKANKAMININIFMRESSRSFLVNQMINEAKKQLLEFDTQSKNILMQYIKANSKFIGITELKKLESKINKVFSTPIPFSYSKNLDCWVDNEEDIDVILKKSTILNLDINNDIISDISGFNSSVITYPDAQLVPGINGKAIHLVNNESSEVIVHKAMDIEYNDMFNNFTVSFWLRVPKVSASHLEQYGTNEYSIISSMKKHSLSIGSGWSVSLKGNNLIWTLKDSAGEVRQITFRDLPDKFNAYLANKWVFITITNDRLSSANLYINGVLMGSAEITGLGAIREDNNITLKLDRCNNNNQYVSIDKFRIFCKALNPKEIEKLYTSYLSITFLRDFWGNPLRYDTEYYLIPVASSSKDVQLKNITDYMYLTNAPSYTNGKLNIYYRRLYNGLKFIIKRYTPNNEIDSFVKSGDFIKLYVSYNNNEHIVGYPKDGNAFNNLDRILRVGYNAPGIPLYKKMEAVKLRDLKTYSVQLKLYDDKNASLGLVGTHNGQIGNDPNRDILIASNWYFNHLKDKILGCDWYFVPTDEGWTND
|
3.4.24.68
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
modulation by symbiont of host neurotransmitter secretion [GO:0044079]; proteolysis [GO:0006508]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270]
|
PF01742;PF07951;PF07953;PF07952;
|
2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10;
|
Peptidase M27 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.; EC=3.4.24.68;
| null | null | null | null |
FUNCTION: Tetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2.
|
Clostridium tetani (strain Massachusetts / E88)
|
P04961
|
PCNA_RAT
|
MFEARLIQGSILKKVLEALKDLINEACWDISSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVSIEMNEPVQLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS
| null | null |
base-excision repair, gap-filling [GO:0006287]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; epithelial cell differentiation [GO:0030855]; estrous cycle [GO:0044849]; heart development [GO:0007507]; leading strand elongation [GO:0006272]; liver regeneration [GO:0097421]; mismatch repair [GO:0006298]; mitotic telomere maintenance via semi-conservative replication [GO:1902990]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of deoxyribonuclease activity [GO:0032077]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; replication fork processing [GO:0031297]; response to cadmium ion [GO:0046686]; response to dexamethasone [GO:0071548]; response to estradiol [GO:0032355]; response to L-glutamate [GO:1902065]; response to lipid [GO:0033993]; response to oxidative stress [GO:0006979]; translesion synthesis [GO:0019985]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nuclear lamina [GO:0005652]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]; PCNA complex [GO:0043626]; PCNA-p21 complex [GO:0070557]; replication fork [GO:0005657]
|
chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; dinucleotide insertion or deletion binding [GO:0032139]; DNA polymerase binding [GO:0070182]; DNA polymerase processivity factor activity [GO:0030337]; enzyme binding [GO:0019899]; histone acetyltransferase binding [GO:0035035]; identical protein binding [GO:0042802]; MutLalpha complex binding [GO:0032405]; nuclear estrogen receptor binding [GO:0030331]; protein-containing complex binding [GO:0044877]; purine-specific mismatch base pair DNA N-glycosylase activity [GO:0000701]; receptor tyrosine kinase binding [GO:0030971]
|
PF02747;PF00705;
|
3.70.10.10;
|
PCNA family
|
PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation. Lysine acetylation disrupts association with chromatin, hence promoting PCNA ubiquitination and proteasomal degradation in response to UV damage in a CREBBP- and EP300-dependent manner. Acetylation disrupts interaction with NUDT15 and promotes degradation (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Ubiquitinated. Following DNA damage, can be either monoubiquitinated to stimulate direct bypass of DNA lesions by specialized DNA polymerases or polyubiquitinated to promote recombination-dependent DNA synthesis across DNA lesions by template switching mechanisms. Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner. An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free pathway, also known as template switching, employs recombination mechanisms to synthesize across the lesion, using as a template the undamaged, newly synthesized strand of the sister chromatid. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during S phase (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Methylated on glutamate residues by ARMT1. {ECO:0000250|UniProtKB:P12004}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12004}. Note=Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:P12004}.
| null | null | null | null | null |
FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (By similarity). {ECO:0000250|UniProtKB:P12004}.
|
Rattus norvegicus (Rat)
|
P04963
|
PRXC_LEPFU
|
MFSKVLPFVGAVAALPHSVRQEPGSGIGYPYDNNTLPYVAPGPTDSRAPCPALNALANHGYIPHDGRAISRETLQNAFLNHMGIANSVIELALTNAFVVCEYVTGSDCGDSLVNLTLLAEPHAFEHDHSFSRKDYKQGVANSNDFIDNRNFDAETFQTSLDVVAGKTHFDYADMNEIRLQRESLSNELDFPGWFTESKPIQNVESGFIFALVSDFNLPDNDENPLVRIDWWKYWFTNESFPYHLGWHPPSPAREIEFVTSASSAVLAASVTSTPSSLPSGAIGPGAEAVPLSFASTMTPFLLATNAPYYAQDPTLGPNDKREAAPAATTSMAVFKNPYLEAIGTQDIKNQQAYVSSKAAAMASAMAANKARNL
|
1.11.1.10
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mn(2+) ion per subunit.;
| null | null |
chloride peroxidase activity [GO:0016691]; metal ion binding [GO:0046872]
|
PF01328;
|
1.10.489.10;
|
Chloroperoxidase family
|
PTM: N- and O-glycosylated.
| null |
CATALYTIC ACTIVITY: Reaction=RH + Cl(-) + H2O2 = RCl + 2 H2O.; EC=1.11.1.10;
| null | null | null | null |
FUNCTION: Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases.
|
Leptoxyphium fumago (Caldariomyces fumago)
|
P04964
|
DAPDH_CORGL
|
MTNIRVAIVGYGNLGRSVEKLIAKQPDMDLVGIFSRRATLDTKTPVFDVADVDKHADDVDVLFLCMGSATDIPEQAPKFAQFACTVDTYDNHRDIPRHRQVMNEAATAAGNVALVSTGWDPGMFSINRVYAAAVLAEHQQHTFWGPGLSQGHSDALRRIPGVQKAVQYTLPSEDALEKARRGEAGDLTGKQTHKRQCFVVADAADHERIENDIRTMPDYFVGYEVEVNFIDEATFDSEHTGMPHGGHVITTGDTGGFNHTVEYILKLDRNPDFTASSQIAFGRAAHRMKQQGQSGAFTVLEVAPYLLSPENLDDLIARDV
|
1.4.1.16
| null |
diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process via diaminopimelate [GO:0009089]
| null |
diaminopimelate dehydrogenase activity [GO:0047850]
|
PF16654;
|
3.40.50.720;
|
Diaminopimelate dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:13561, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:57791, ChEBI:CHEBI:58349, ChEBI:CHEBI:58556; EC=1.4.1.16; Evidence={ECO:0000269|PubMed:8865347, ECO:0000269|Ref.4};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for meso-2,6-diaminoheptanedioate {ECO:0000269|Ref.4}; KM=0.12 mM for NADP(+) {ECO:0000269|Ref.4}; KM=0.13 mM for NADPH {ECO:0000269|Ref.4}; KM=0.28 mM for L-2-amino-6-oxoheptanedioate {ECO:0000269|Ref.4}; KM=36 mM for ammonia {ECO:0000269|Ref.4};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 9.8 for the oxidative deamination of meso-diaminopimelate and 7.9 for the reductive amination of L-2-amino-6-oxopimelate. {ECO:0000269|Ref.4};
| null |
FUNCTION: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L-methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L-tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D-alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+). {ECO:0000269|PubMed:8865347, ECO:0000269|Ref.4}.
|
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
|
P04968
|
ILVA_ECOLI
|
MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHEPDFETRLNELGYDCHDETNNPAFRFFLAG
|
4.3.1.19
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:5321308};
|
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; threonine catabolic process [GO:0006567]; threonine metabolic process [GO:0006566]
| null |
amino acid binding [GO:0016597]; L-serine ammonia-lyase activity [GO:0003941]; pyridoxal phosphate binding [GO:0030170]; threonine deaminase activity [GO:0004794]
|
PF00291;PF00585;
|
3.40.50.1100;
|
Serine/threonine dehydratase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
| null | null |
FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. {ECO:0000269|PubMed:13405870}.
|
Escherichia coli (strain K12)
|
P04971
|
VSPF_BOTAT
|
MVLIRVIANLLILQVSYAQKSSELVIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIHLGKHAGSVANYDEVVRYPKEKFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP
|
3.4.21.74
| null |
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Snake venom subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74;
| null | null | null | null |
FUNCTION: Thrombin-like snake venom serine protease. Cleaves Arg-Gly bonds in fibrinogen alpha chains (FGA). {ECO:0000269|PubMed:1011993}.
|
Bothrops atrox (Barba amarilla) (Fer-de-lance)
|
P04972
|
CNRG_BOVIN
|
MNLEPPKAEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII
|
3.1.4.35
| null |
positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment membrane [GO:0042622]
|
3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; ion binding [GO:0043167]; molecular adaptor activity [GO:0060090]; zinc ion binding [GO:0008270]
|
PF04868;
|
4.10.1120.10;
|
Rod/cone cGMP-PDE gamma subunit family
| null | null |
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35;
| null | null | null | null |
FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
|
Bos taurus (Bovine)
|
P04975
|
CLCB_BOVIN
|
MADDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDEGFGAPAGSQGGLAQPGPASGASEDMGATVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQRKRLQELDAASKVMEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADIIGYVASEEAFVKESKEETPGTEWEKVAQLCDFNPKSSKQCKDVSRLRSVLMSLKQTPLSR
| null | null |
clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]
|
clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin vesicle coat [GO:0030125]; plasma membrane [GO:0005886]; postsynaptic endocytic zone cytoplasmic component [GO:0099631]; synaptic vesicle membrane [GO:0030672]
|
clathrin heavy chain binding [GO:0032050]; structural molecule activity [GO:0005198]
|
PF01086;
| null |
Clathrin light chain family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
| null | null | null | null | null |
FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
|
Bos taurus (Bovine)
|
P04977
|
TOX1_BORPE
|
MRCTRAIRQTARTGWLTWLAILAVTAPVTSPAWADDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF
|
2.4.2.-
| null | null |
extracellular region [GO:0005576]
|
NAD+ ADP-ribosyltransferase activity [GO:0003950]; nucleotidyltransferase activity [GO:0016779]; toxin activity [GO:0090729]
|
PF02917;
|
3.90.210.10;
|
Bacterial exotoxin subunit A family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11854200}. Note=The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.
| null | null | null | null | null |
FUNCTION: S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD(+) into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.
|
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
|
P04982
|
RBSD_ECOLI
|
MKKGTVLNSDISSVISRLGHTDTLVVCDAGLPIPKSTTRIDMALTQGVPSFMQVLGVVTNEMQVEAAIIAEEIKHHNPQLHETLLTHLEQLQKHQGNTIEIRYTTHEQFKQQTAESQAVIRSGECSPYANIILCAGVTF
|
5.4.99.62
| null |
D-ribose catabolic process [GO:0019303]
|
cytosol [GO:0005829]
|
D-ribose pyranase activity [GO:0062193]; identical protein binding [GO:0042802]; intramolecular lyase activity [GO:0016872]; intramolecular transferase activity [GO:0016866]; monosaccharide binding [GO:0048029]
|
PF05025;
|
3.40.1650.10;
|
RbsD / FucU family, RbsD subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-ribopyranose = beta-D-ribofuranose; Xref=Rhea:RHEA:25432, ChEBI:CHEBI:27476, ChEBI:CHEBI:47002; EC=5.4.99.62; Evidence={ECO:0000269|PubMed:15060078}; CATALYTIC ACTIVITY: Reaction=beta-D-allofuranose = beta-D-allopyranose; Xref=Rhea:RHEA:25609, ChEBI:CHEBI:40656, ChEBI:CHEBI:50256; EC=5.4.99.62; Evidence={ECO:0000269|PubMed:15060078};
| null |
PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
| null | null |
FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. {ECO:0000269|PubMed:15060078}.
|
Escherichia coli (strain K12)
|
P04983
|
RBSA_ECOLI
|
MEALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGTLLWLGKETTFTGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKTMYAEADKLLAKLNLRFKSDKLVGDLSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVASLTEDSLIEMMVGRKLEDQYPHLDKAPGDIRLKVDNLCGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRVNQE
|
7.5.2.7
| null |
D-ribose transmembrane transport [GO:0015752]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]
|
ABC-type D-ribose transporter activity [GO:0015611]; ABC-type monosaccharide transporter activity [GO:0015407]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; D-ribose transmembrane transporter activity [GO:0015591]
|
PF00005;
|
3.40.50.300;
|
ABC transporter superfamily, Ribose importer (TC 3.A.1.2.1) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}.
|
CATALYTIC ACTIVITY: Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:8762140};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for ATP {ECO:0000269|PubMed:8762140};
| null | null | null |
FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:8762140}.
|
Escherichia coli (strain K12)
|
P04985
|
ELN_BOVIN
|
MRSLTAAARRPEVLLLLLCILQPSQPGGVPGAVPGGVPGGVFFPGAGLGGLGVGGLGPGVKPAKPGVGGLVGPGLGAEGSALPGAFPGGFFGAGGGAAGAAAAYKAAAKAGAAGLGVGGIGGVGGLGVSTGAVVPQLGAGVGAGVKPGKVPGVGLPGVYPGGVLPGAGARFPGIGVLPGVPTGAGVKPKAQVGAGAFAGIPGVGPFGGQQPGLPLGYPIKAPKLPAGYGLPYKTGKLPYGFGPGGVAGSAGKAGYPTGTGVGPQAAAAAAKAAAKLGAGGAGVLPGVGVGGPGIPGAPGAIPGIGGIAGVGAPDAAAAAAAAAKAAKFGAAGGLPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGALSPAATAKAAAKAAKFGARGAVGIGGIPTFGLGPGGFPGIGDAAAAPAAAAAKAAKIGAGGVGALGGVVPGAPGAIPGLPGVGGVPGVGIPAAAAAKAAAKAAQFGLGPGVGVAPGVGVVPGVGVVPGVGVAPGIGLGPGGVIGAGVPAAAKSAAKAAAKAQFRAAAGLPAGVPGLGVGAGVPGLGVGAGVPGLGVGAGVPGPGAVPGTLAAAKAAKFGPGGVGALGGVGDLGGAGIPGGVAGVVPAAAAAAKAAAKAAQFGLGGVGGLGVGGLGAVPGAVGLGGVSPAAAAKAAKFGAAGLGGVLGAGQPFPIGGGAGGLGVGGKPPKPFGGALGALGFPGGACLGKSCGRKRK
| null | null | null |
collagen-containing extracellular matrix [GO:0062023]; elastic fiber [GO:0071953]; extracellular region [GO:0005576]
|
extracellular matrix structural constituent [GO:0005201]
| null | null |
Elastin family
|
PTM: Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.; PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of elastic fibers. {ECO:0000250|UniProtKB:P15502}.
| null | null | null | null | null |
FUNCTION: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity). {ECO:0000250|UniProtKB:P54320}.
|
Bos taurus (Bovine)
|
P04992
|
RBL_PETHY
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYQAKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGHRYRIERVIGERDQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLKATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIRFNFAAVDVLDK
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast [GO:0009507]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
Petunia hybrida (Petunia)
|
P04993
|
RECD_ECOLI
|
MKLQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENNEASHPLLATCVSEIGELQNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLFPVSDEINWQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYANAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYRFGSDSGIGQLAAAINRGDKTAVKTVFQQDFTDIEKRLLQSGEDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRHPHSRWYEGRPVMIARNDSALGLFNGDIGIALDRGQGTRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGLAALFSSRE
|
5.6.2.3
| null |
DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; double-strand break repair via homologous recombination [GO:0000724]; recombinational repair [GO:0000725]
|
exodeoxyribonuclease V complex [GO:0009338]
|
5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exodeoxyribonuclease V activity [GO:0008854]; helicase activity [GO:0004386]; isomerase activity [GO:0016853]; single-stranded DNA helicase activity [GO:0017116]
|
PF13245;PF21185;PF13538;
|
3.40.50.300;1.10.10.1020;
|
RecD family
| null | null |
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.; EC=5.6.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01487, ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01487, ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438};
| null | null | null | null |
FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. In the holoenzyme this subunit contributes ssDNA-dependent ATPase and fast 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD. {ECO:0000269|PubMed:10197988, ECO:0000269|PubMed:10840065, ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438, ECO:0000269|PubMed:1535156, ECO:0000269|PubMed:16041061, ECO:0000269|PubMed:1618858, ECO:0000269|PubMed:18079176, ECO:0000269|PubMed:23851395, ECO:0000269|PubMed:7608206, ECO:0000269|PubMed:9192629, ECO:0000269|PubMed:9230304, ECO:0000269|PubMed:9448271, ECO:0000269|PubMed:9790841}.
|
Escherichia coli (strain K12)
|
P04994
|
EX7L_ECOLI
|
MLPSQSPAIFTVSRLNQTVRLLLEHEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKKPLPSPAHCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGDDAPGQIVRAIELANQRNECDVLIVGRGGGSLEDLWSFNDERVARAIFTSRIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQVQSTRQRLEMAMDYYLANRTRRFTQIHHRLQQQHPQLRLARQQTMLERLQKRMSFALENQLKRTGQQQQRLTQRLNQQNPQPKIHRAQTRIQQLEYRLAETLRAQLSATRERFGNAVTHLEAVSPLSTLARGYSVTTATDGNVLKKVKQVKAGEMLTTRLEDGWIESEVKNIQPVKKSRKKVH
|
3.1.11.6
|
COFACTOR: Note=Does not require a metal cofactor. {ECO:0000269|PubMed:4602029};
|
DNA catabolic process [GO:0006308]; mismatch repair [GO:0006298]
|
cytoplasm [GO:0005737]; exodeoxyribonuclease VII complex [GO:0009318]
|
DNA binding [GO:0003677]; exodeoxyribonuclease VII activity [GO:0008855]
|
PF02601;PF13742;
| null |
XseA family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:6284744}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00378, ECO:0000269|PubMed:22718974, ECO:0000269|PubMed:4602029, ECO:0000269|PubMed:4602030};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 to 7.9. {ECO:0000269|PubMed:4602029};
| null |
FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. It can also excise thymine dimers in vitro (Probable) (PubMed:22718974, PubMed:4602029, PubMed:4602030). ssDNA-binding requires both subunits (PubMed:22718974). Required for production of the mature 5'-end of retron Ec78 or Ec83 msDNA. Overproduction of this subunit in the absence of an equivalent quantity of the small subunit is toxic, causing cell elongation and chromosome fragmentation or loss; its toxicity is mostly suppressed by RecA (PubMed:26626352). {ECO:0000269|PubMed:22718974, ECO:0000269|PubMed:26626352, ECO:0000269|PubMed:4602029, ECO:0000269|PubMed:4602030, ECO:0000305|PubMed:6284744}.
|
Escherichia coli (strain K12)
|
P04995
|
EX1_ECOLI
|
MMNDGKQQSTFLFHDYETFGTHPALDRPAQFAAIRTDSEFNVIGEPEVFYCKPADDYLPQPGAVLITGITPQEARAKGENEAAFAARIHSLFTVPKTCILGYNNVRFDDEVTRNIFYRNFYDPYAWSWQHDNSRWDLLDVMRACYALRPEGINWPENDDGLPSFRLEHLTKANGIEHSNAHDAMADVYATIAMAKLVKTRQPRLFDYLFTHRNKHKLMALIDVPQMKPLVHVSGMFGAWRGNTSWVAPLAWHPENRNAVIMVDLAGDISPLLELDSDTLRERLYTAKTDLGDNAAVPVKLVHINKCPVLAQANTLRPEDADRLGINRQHCLDNLKILRENPQVREKVVAIFAEAEPFTPSDNVDAQLYNGFFSDADRAAMKIVLETEPRNLPALDITFVDKRIEKLLFNYRARNFPGTLDYAEQQRWLEHRRQVFTPEFLQGYADELQMLVQQYADDKEKVALLKALWQYAEEIV
|
3.1.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:18591666};
|
DNA catabolic process [GO:0006308]; DNA repair [GO:0006281]
| null |
3'-5'-RNA exonuclease activity [GO:0000175]; 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; magnesium ion binding [GO:0000287]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310]; single-stranded DNA binding [GO:0003697]
|
PF08411;PF00929;
|
1.10.287.1240;3.30.1520.20;1.20.1280.70;3.30.420.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
| null | null | null | null |
FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027). {ECO:0000269|PubMed:1329027, ECO:0000269|PubMed:23609540}.
|
Escherichia coli (strain K12)
|
P05000
|
IFNW1_HUMAN
|
MALLFPLLAALVMTSYSPVGSLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMSVLHEMLQQIFSLFHTERSSAAWNMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISSPALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; regulation of cell cycle [GO:0051726]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
P05013
|
IFNA6_HUMAN
|
MALPFALLMALVVLSCKSSCSLDCDLPQTHSLGHRRTMMLLAQMRRISLFSCLKDRHDFRFPQEEFDGNQFQKAEAISVLHEVIQQTFNLFSTKDSSVAWDERLLDKLYTELYQQLNDLEACVMQEVWVGGTPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSSSRNLQERLRRKE
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
|
Homo sapiens (Human)
|
P05014
|
IFNA4_HUMAN
|
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRHDFGFPEEEFDGHQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD
| null | null |
adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune response [GO:0002323]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; T cell activation involved in immune response [GO:0002286]; type I interferon-mediated signaling pathway [GO:0060337]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132]
|
PF00143;
|
1.20.1250.10;
|
Alpha/beta interferon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
|
Homo sapiens (Human)
|
P05017
|
IGF1_MOUSE
|
MGKISSLPTQLFKICLCDFLKIKIHIMSSSHLFYLALCLLTFTSSTTAGPETLCGAELVDALQFVCGPRGFYFNKPTGYGSSIRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPTKAARSIRAQRHTDMPKTQKEVHLKNTSRGSAGNKTYRM
| null | null |
androgen receptor signaling pathway [GO:0030521]; blood vessel remodeling [GO:0001974]; branching morphogenesis of an epithelial tube [GO:0048754]; cell activation [GO:0001775]; cell development [GO:0048468]; cell population proliferation [GO:0008283]; cellular response to glucose stimulus [GO:0071333]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cerebellar granule cell precursor proliferation [GO:0021930]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; circadian rhythm [GO:0007623]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; exocrine pancreas development [GO:0031017]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; glial cell differentiation [GO:0010001]; inner ear development [GO:0048839]; insulin-like growth factor receptor signaling pathway [GO:0048009]; lung alveolus development [GO:0048286]; lung development [GO:0030324]; lung lobe morphogenesis [GO:0060463]; lung vasculature development [GO:0060426]; mammary gland development [GO:0030879]; memory [GO:0007613]; multicellular organism growth [GO:0035264]; myotube differentiation [GO:0014902]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cholangiocyte apoptotic process [GO:1904193]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of gene expression [GO:0010629]; negative regulation of immune system process [GO:0002683]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of oligodendrocyte apoptotic process [GO:1900142]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; nervous system development [GO:0007399]; osteoblast differentiation [GO:0001649]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cerebellar granule cell precursor proliferation [GO:0021940]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of myelination [GO:0031643]; positive regulation of myoblast proliferation [GO:2000288]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type B pancreatic cell proliferation [GO:1904692]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis [GO:0060527]; prostate gland epithelium morphogenesis [GO:0060740]; prostate gland growth [GO:0060736]; prostate gland stromal morphogenesis [GO:0060741]; regulation of calcium ion transport [GO:0051924]; regulation of cell population proliferation [GO:0042127]; regulation of establishment or maintenance of cell polarity [GO:0032878]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of protein metabolic process [GO:0051246]; regulation of protein phosphorylation [GO:0001932]; regulation of translation [GO:0006417]; response to ethanol [GO:0045471]; retinal cell apoptotic process [GO:1990009]; sensory perception of smell [GO:0007608]; type B pancreatic cell proliferation [GO:0044342]; type I pneumocyte differentiation [GO:0060509]; type II pneumocyte differentiation [GO:0060510]
|
alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; insulin-like growth factor ternary complex [GO:0042567]; interstitial matrix [GO:0005614]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0099013]; platelet alpha granule [GO:0031091]; postsynapse [GO:0098794]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protein serine/threonine kinase activator activity [GO:0043539]; receptor ligand activity [GO:0048018]; steroid binding [GO:0005496]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496647}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (By similarity). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb (PubMed:21496647). Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (By similarity). As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250|UniProtKB:P05019, ECO:0000250|UniProtKB:P08025, ECO:0000269|PubMed:21496647}.
|
Mus musculus (Mouse)
|
P05019
|
IGF1_HUMAN
|
MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK
| null | null |
activation of protein kinase B activity [GO:0032148]; bone mineralization involved in bone maturation [GO:0035630]; cell activation [GO:0001775]; cell population proliferation [GO:0008283]; cellular response to amyloid-beta [GO:1904646]; epithelial to mesenchymal transition [GO:0001837]; glycolate metabolic process [GO:0009441]; insulin-like growth factor receptor signaling pathway [GO:0048009]; muscle hypertrophy [GO:0014896]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast proliferation [GO:0051450]; myotube cell development [GO:0014904]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of gene expression [GO:0010629]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of neuroinflammatory response [GO:0150079]; negative regulation of oocyte development [GO:0060283]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of vascular associated smooth muscle cell apoptotic process [GO:1905460]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA binding [GO:0043388]; positive regulation of DNA-templated transcription [GO:0045893]; 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 gene expression [GO:0010628]; 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 glycoprotein biosynthetic process [GO:0010560]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein secretion [GO:0050714]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; positive regulation of trophectodermal cell proliferation [GO:1904075]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein stabilization [GO:0050821]; proteoglycan biosynthetic process [GO:0030166]; Ras protein signal transduction [GO:0007265]; regulation of gene expression [GO:0010468]; regulation of protein phosphorylation [GO:0001932]; response to heat [GO:0009408]; signal transduction [GO:0007165]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; skeletal system development [GO:0001501]; wound healing [GO:0042060]
|
alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; insulin-like growth factor binding protein complex [GO:0016942]; insulin-like growth factor ternary complex [GO:0042567]; platelet alpha granule lumen [GO:0031093]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (PubMed:21076856, PubMed:24132240). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb (By similarity). Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:19578119, PubMed:22351760, PubMed:23243309, PubMed:23696648). As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250|UniProtKB:P05017, ECO:0000250|UniProtKB:P08025, ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:21076856, ECO:0000269|PubMed:22351760, ECO:0000269|PubMed:23243309, ECO:0000269|PubMed:23696648, ECO:0000269|PubMed:24132240}.
|
Homo sapiens (Human)
|
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