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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P07014
|
SDHB_ECOLI
|
MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA
|
1.3.5.1
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Note=Binds 1 [3Fe-4S] cluster.; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster.;
|
aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; respiratory electron transport chain [GO:0022904]; tricarboxylic acid cycle [GO:0006099]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; succinate dehydrogenase complex [GO:0045281]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177]
|
PF13085;PF13534;
|
3.10.20.30;1.10.1060.10;
|
Succinate dehydrogenase/fumarate reductase iron-sulfur protein family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}.
|
CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
| null |
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.
| null | null |
FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
|
Escherichia coli (strain K12)
|
P07017
|
MCP2_ECOLI
|
MINRIRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQNAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRIAEQDPNWETF
| null | null |
cellular response to amino acid stimulus [GO:0071230]; chemotaxis [GO:0006935]; detection of chemical stimulus [GO:0009593]; positive regulation of post-translational protein modification [GO:1901875]; protein homooligomerization [GO:0051260]; regulation of chemotaxis [GO:0050920]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]
|
cell tip [GO:0051286]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; protein histidine kinase binding [GO:0043424]; protein homodimerization activity [GO:0042803]; transmembrane signaling receptor activity [GO:0004888]
|
PF00672;PF00015;PF02203;
|
1.20.120.30;1.10.287.950;
|
Methyl-accepting chemotaxis (MCP) protein family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
| null | null | null | null | null |
FUNCTION: Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel.; FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
|
Escherichia coli (strain K12)
|
P07024
|
USHA_ECOLI
|
MKLLQRGVALALLTTFTLASETALAYEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQKTLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDTAKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARALPAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPVNLKKKVTWEDGKSERVLYTPEIAENQQMISLLSPFQNKGKAQLEVKIGETNGRLEGDRDKVRFVQTNMGRLILAAQMDRTGADFAVMSGGGIRDSIEAGDISYKNVLKVQPFGNVVVYADMTGKEVIDYLTAVAQMKPDSGAYPQFANVSFVAKDGKLNDLKIKGEPVDPAKTYRMATLNFNATGGDGYPRLDNKPGYVNTGFIDAEVLKAYIQKSSPLDVSVYEPKGEVSWQ
|
3.1.3.5; 3.6.1.45
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
|
nucleotide catabolic process [GO:0009166]
|
outer membrane-bounded periplasmic space [GO:0030288]
|
5'-nucleotidase activity [GO:0008253]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; UDP-sugar diphosphatase activity [GO:0008768]; XMP 5'-nucleosidase activity [GO:0106411]
|
PF02872;PF00149;
|
3.60.21.10;3.90.780.10;
|
5'-nucleotidase family
| null |
SUBCELLULAR LOCATION: Periplasm. Note=Exported from the cell, except a small proportion that is internally localized.
|
CATALYTIC ACTIVITY: Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.; EC=3.6.1.45; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
| null | null | null | null |
FUNCTION: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.
|
Escherichia coli (strain K12)
|
P07056
|
UCRI_NEUCR
|
MAPVSIVSRAAMRAAAAPARAVRALTTSTALQGSSSSTFESPFKGESKAAKVPDFGKYMSKAPPSTNMLFSYFMVGTMGAITAAGAKSTIQEFLKNMSASADVLAMAKVEVDLNAIPEGKNVIIKWRGKPVFIRHRTPAEIEEANKVNVATLRDPETDADRVKKPEWLVMLGVCTHLGCVPIGEAGDYGGWFCPCHGSHYDISGRIRKGPAPLNLEIPLYEFPEEGKLVIG
|
7.1.1.8
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628};
|
mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF00355;PF02921;
|
2.102.10.10;1.20.5.270;
|
Rieske iron-sulfur protein family
|
PTM: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 25 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized Rieske protein. {ECO:0000269|PubMed:3022944}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:226365}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.
|
CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1847681, ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:3015618};
| null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable) (PubMed:3015618). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). {ECO:0000250|UniProtKB:P08067, ECO:0000269|PubMed:3015618, ECO:0000305|PubMed:1847681, ECO:0000305|PubMed:19239619}.
|
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
|
P07064
|
SOMA_ONCKE
|
MGQVFLLMPVLLVSCFLSQGAAIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVDKHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLITGSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL
| null | null |
animal organ development [GO:0048513]; calcium ion homeostasis [GO:0055074]; chloride ion homeostasis [GO:0055064]; growth hormone receptor signaling pathway [GO:0060396]; hyperosmotic salinity response [GO:0042538]; magnesium ion homeostasis [GO:0010960]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of oxygen metabolic process [GO:2000376]; positive regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903408]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of phagocytosis [GO:0050766]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of superoxide dismutase activity [GO:1901671]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein secretion [GO:0009306]; regulation of immunoglobulin production [GO:0002637]; response to dopamine [GO:1903350]; response to growth hormone [GO:0060416]; response to starvation [GO:0042594]; response to temperature stimulus [GO:0009266]; sodium ion homeostasis [GO:0055078]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; metal ion binding [GO:0046872]
|
PF00103;
|
1.20.1250.10;
|
Somatotropin/prolactin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation.
|
Oncorhynchus keta (Chum salmon) (Salmo keta)
|
P07071
|
NRDD_BPT4
|
MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHESGIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVASHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEYEVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEEGVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDSTGNEILDGRNNLGVVTLNLPRIALDSYIGTQFNEQKFVELFNERMDLCFEALMCRISSLKGVKATVAPILYQEGAFGVRLKPDDDIIELFKNGRSSVSLGYIGIHELNILVGRDIGREILTKMNAHLKQWTERTGFAFSLYSTPAENLCYRFCKLDTEKYGSVKDVTDKGWYTNSFHVSVEENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPVDKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMHRVKHQ
|
1.1.98.6
| null |
2'-deoxyribonucleotide biosynthetic process [GO:0009265]; DNA replication [GO:0006260]
|
anaerobic ribonucleoside-triphosphate reductase complex [GO:0031250]
|
metal ion binding [GO:0046872]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]; ribonucleoside-triphosphate reductase activity [GO:0008998]
|
PF13597;
|
3.20.70.20;
|
Anaerobic ribonucleoside-triphosphate reductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O; Xref=Rhea:RHEA:51476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.1.98.6; Evidence={ECO:0000269|PubMed:8702830};
| null | null | null | null |
FUNCTION: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair. {ECO:0000269|PubMed:8051113, ECO:0000269|PubMed:8702830}.
|
Enterobacteria phage T4 (Bacteriophage T4)
|
P07091
|
S10A4_MOUSE
|
MARPLEEALDVIVSTFHKYSGKEGDKFKLNKTELKELLTRELPSFLGKRTDEAAFQKVMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK
| null | null |
positive regulation of canonical NF-kappaB signal transduction [GO:0043123]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
actin binding [GO:0003779]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; chemoattractant activity [GO:0042056]; identical protein binding [GO:0042802]; RAGE receptor binding [GO:0050786]; transition metal ion binding [GO:0046914]
|
PF01023;
|
1.10.238.10;
|
S-100 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000269|PubMed:8051043}.
| null | null | null | null | null |
FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:20519440). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:8051043). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (PubMed:8051043). Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (PubMed:20103644). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity). {ECO:0000250|UniProtKB:P26447, ECO:0000269|PubMed:20103644, ECO:0000269|PubMed:20519440, ECO:0000269|PubMed:8051043}.
|
Mus musculus (Mouse)
|
P07092
|
GDN_RAT
|
MNWHFPFFILTTVTLSSVYSQLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTALAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP
| null | null |
blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cerebellar granular layer morphogenesis [GO:0021683]; dense core granule biogenesis [GO:0061110]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; embryo implantation [GO:0007566]; innervation [GO:0060384]; long-term synaptic potentiation [GO:0060291]; mating plug formation [GO:0042628]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of platelet activation [GO:0010544]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of proteolysis [GO:0045861]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of sodium ion transport [GO:0010766]; platelet activation [GO:0030168]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of neuron projection development [GO:0010976]; protein catabolic process [GO:0030163]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of timing of cell differentiation [GO:0048505]; response to wounding [GO:0009611]; secretion by cell [GO:0032940]; secretory granule organization [GO:0033363]; seminal vesicle epithelium development [GO:0061108]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; platelet alpha granule [GO:0031091]
|
glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102]
|
PF00079;
|
2.30.39.10;3.30.497.10;2.10.310.10;
|
Serpin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. {ECO:0000269|PubMed:2337608}.
|
Rattus norvegicus (Rat)
|
P07093
|
GDN_HUMAN
|
MNWHLPLFLLASVTLPSICSHFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITTGSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP
| null | null |
cell differentiation [GO:0030154]; cerebellar granular layer morphogenesis [GO:0021683]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; innervation [GO:0060384]; long-term synaptic potentiation [GO:0060291]; mating plug formation [GO:0042628]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein processing [GO:0010955]; negative regulation of proteolysis [GO:0045861]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of sodium ion transport [GO:0010766]; platelet activation [GO:0030168]; positive regulation of astrocyte differentiation [GO:0048711]; protein catabolic process [GO:0030163]; regulation of cell migration [GO:0030334]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of timing of cell differentiation [GO:0048505]; secretion by cell [GO:0032940]; secretory granule organization [GO:0033363]; seminal vesicle epithelium development [GO:0061108]
|
collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; neuromuscular junction [GO:0031594]; platelet alpha granule [GO:0031091]
|
glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102]
|
PF00079;
|
2.30.39.10;3.30.497.10;2.10.310.10;
|
Serpin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.
|
Homo sapiens (Human)
|
P07097
|
THIL_SHIZO
|
MSTPSIVIASARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLAGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
|
2.3.1.9
| null |
fatty acid beta-oxidation [GO:0006635]; poly-hydroxybutyrate biosynthetic process [GO:0042619]
|
cytosol [GO:0005829]
|
acetyl-CoA C-acetyltransferase activity [GO:0003985]
|
PF02803;PF00108;
|
3.40.47.10;
|
Thiolase-like superfamily, Thiolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
| null |
PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis. {ECO:0000305}.; PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
| null | null | null |
Shinella zoogloeoides (Crabtreella saccharophila)
|
P07098
|
LIPF_HUMAN
|
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
|
3.1.1.3
| null |
lipid catabolic process [GO:0016042]; malate metabolic process [GO:0006108]; triglyceride metabolic process [GO:0006641]
|
extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]
|
lipid binding [GO:0008289]; malate dehydrogenase activity [GO:0016615]; triglyceride lipase activity [GO:0004806]
|
PF00561;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753; Evidence={ECO:0000269|PubMed:2243091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence={ECO:0000305|PubMed:2243091}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol + H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:76979; Evidence={ECO:0000269|PubMed:2243091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence={ECO:0000305|PubMed:2243091};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:10358049, PubMed:2243091). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (PubMed:2243091). {ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}.
|
Homo sapiens (Human)
|
P07099
|
HYEP_HUMAN
|
MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGWPGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYMHIQCTKPDTVGSALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFSLDDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERMKVYVPTGFSAFPFELLHTPEKWVRFKYPKLISYSYMVRGGHFAAFEEPELLAQDIRKFLSVLERQ
|
3.3.2.9
| null |
arachidonic acid metabolic process [GO:0019369]; aromatic compound catabolic process [GO:0019439]; epoxide metabolic process [GO:0097176]; response to organic cyclic compound [GO:0014070]; response to toxic substance [GO:0009636]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]
|
cis-stilbene-oxide hydrolase activity [GO:0033961]; epoxide hydrolase activity [GO:0004301]; oxysterol binding [GO:0008142]
|
PF00561;
|
3.40.50.1820;
|
Peptidase S33 family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:24958911}; Single-pass type III membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P07687}.
|
CATALYTIC ACTIVITY: Reaction=cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin; Xref=Rhea:RHEA:23900, ChEBI:CHEBI:15377, ChEBI:CHEBI:50004, ChEBI:CHEBI:50014; EC=3.3.2.9; Evidence={ECO:0000269|PubMed:24958911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23901; Evidence={ECO:0000269|PubMed:24958911}; CATALYTIC ACTIVITY: Reaction=1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol; Xref=Rhea:RHEA:55764, ChEBI:CHEBI:15377, ChEBI:CHEBI:139161, ChEBI:CHEBI:139164; EC=3.3.2.9; Evidence={ECO:0000250|UniProtKB:P07687}; CATALYTIC ACTIVITY: Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-(5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44048, ChEBI:CHEBI:15377, ChEBI:CHEBI:84025, ChEBI:CHEBI:84032; Evidence={ECO:0000269|PubMed:22798687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049; Evidence={ECO:0000269|PubMed:22798687}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44044, ChEBI:CHEBI:15377, ChEBI:CHEBI:76625, ChEBI:CHEBI:84031; Evidence={ECO:0000269|PubMed:22798687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045; Evidence={ECO:0000269|PubMed:22798687}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:24958911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:24958911};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for 8,9-EET {ECO:0000269|PubMed:22798687}; KM=0.4 uM for 11,12-EET {ECO:0000269|PubMed:22798687}; KM=0.9 uM for 14,15-EET {ECO:0000269|PubMed:22798687}; KM=5.8 uM for leukotoxin {ECO:0000269|PubMed:22798687}; Vmax=0.12 umol/min/mg enzyme with 8,9-EET as substrate {ECO:0000269|PubMed:22798687}; Vmax=0.6 umol/min/mg enzyme with 11,12-EET as substrate {ECO:0000269|PubMed:22798687}; Vmax=0.04 umol/min/mg enzyme with 14,15-EET as substrate {ECO:0000269|PubMed:22798687}; Vmax=0.008 umol/min/mg enzyme with leukotoxin as substrate {ECO:0000269|PubMed:22798687};
| null | null | null |
FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water (By similarity). Plays a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids (PubMed:22798687). Metabolizes the abundant endocannabinoid 2-arachidonoylglycerol (2-AG) to free arachidonic acid (AA) and glycerol (PubMed:24958911). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity). {ECO:0000250|UniProtKB:P07687, ECO:0000250|UniProtKB:Q9D379, ECO:0000269|PubMed:22798687, ECO:0000269|PubMed:24958911}.
|
Homo sapiens (Human)
|
P07101
|
TY3H_HUMAN
|
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
|
1.14.16.2
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P04177};
|
aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; anatomical structure morphogenesis [GO:0009653]; animal organ morphogenesis [GO:0009887]; cellular response to alkaloid [GO:0071312]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; cellular response to manganese ion [GO:0071287]; cellular response to nicotine [GO:0071316]; cellular response to xenobiotic stimulus [GO:0071466]; cerebral cortex development [GO:0021987]; circadian sleep/wake cycle [GO:0042745]; dopamine biosynthetic process [GO:0042416]; dopamine biosynthetic process from tyrosine [GO:0006585]; eating behavior [GO:0042755]; embryonic camera-type eye morphogenesis [GO:0048596]; epinephrine biosynthetic process [GO:0042418]; eye photoreceptor cell development [GO:0042462]; fatty acid metabolic process [GO:0006631]; glycoside metabolic process [GO:0016137]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; hyaloid vascular plexus regression [GO:1990384]; isoquinoline alkaloid metabolic process [GO:0033076]; learning [GO:0007612]; locomotory behavior [GO:0007626]; mating behavior [GO:0007617]; memory [GO:0007613]; norepinephrine biosynthetic process [GO:0042421]; phthalate metabolic process [GO:0018963]; phytoalexin metabolic process [GO:0052314]; pigmentation [GO:0043473]; regulation of heart contraction [GO:0008016]; response to activity [GO:0014823]; response to amphetamine [GO:0001975]; response to corticosterone [GO:0051412]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to ether [GO:0045472]; response to herbicide [GO:0009635]; response to hypoxia [GO:0001666]; response to immobilization stress [GO:0035902]; response to isolation stress [GO:0035900]; response to light stimulus [GO:0009416]; response to lipopolysaccharide [GO:0032496]; response to nutrient levels [GO:0031667]; response to peptide hormone [GO:0043434]; response to pyrethroid [GO:0046684]; response to salt stress [GO:0009651]; response to zinc ion [GO:0010043]; social behavior [GO:0035176]; sphingolipid metabolic process [GO:0006665]; synaptic transmission, dopaminergic [GO:0001963]; terpene metabolic process [GO:0042214]; visual perception [GO:0007601]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; melanosome membrane [GO:0033162]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; smooth endoplasmic reticulum [GO:0005790]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
amino acid binding [GO:0016597]; dopamine binding [GO:0035240]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802]; oxygen binding [GO:0019825]; protein domain specific binding [GO:0019904]; tetrahydrobiopterin binding [GO:0034617]; tyrosine 3-monooxygenase activity [GO:0004511]
|
PF00351;PF21417;PF12549;
|
3.30.70.260;1.10.800.10;
|
Biopterin-dependent aromatic amino acid hydroxylase family
|
PTM: Phosphorylated on Ser-19, Ser-62 and Ser-71 by several protein kinases with different site specificities. Phosphorylation at Ser-62 and Ser-71 leads to an increase of TH activity (PubMed:7901013). Phosphorylation at Ser-71 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (PubMed:15287903). Phosphorylation of Ser-19 and Ser-62 triggers the proteasomal degradation of TH through the ubiquitin-proteasome pathway (By similarity). Phosphorylation at Ser-62 facilitates transport of TH from the soma to the nerve terminals via the microtubule network (PubMed:28637871). Phosphorylation at Ser-19 induces the high-affinity binding to the 14-3-3 protein YWHAG; this interaction may influence the phosphorylation and dephosphorylation of other sites (PubMed:24947669). Ser-19 increases the phosphorylation at Ser-71 in a hierarchical manner, leading to increased activity (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000269|PubMed:15287903, ECO:0000269|PubMed:24947669, ECO:0000269|PubMed:28637871, ECO:0000269|PubMed:7901013}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P04177}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000269|PubMed:15287903, ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:17391063, ECO:0000269|PubMed:24753243, ECO:0000269|PubMed:34922205, ECO:0000269|PubMed:8528210, ECO:0000269|Ref.18}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18202; Evidence={ECO:0000305|PubMed:17391063};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for 6R-tetrahydrobiopterin {ECO:0000269|PubMed:24753243}; KM=5.1 uM for L-tyrosine {ECO:0000269|PubMed:24753243}; KM=35 uM for L-tyrosine (in presence of N-ethylmaleimide) {ECO:0000269|PubMed:34922205}; KM=15 uM for L-tyrosine {ECO:0000269|PubMed:34922205}; KM=57 uM for 6R-tetrahydrobiopterin {ECO:0000269|PubMed:34922205}; KM=32 uM for 6R-tetrahydrobiopterin (in presence of N-ethylmaleimide) {ECO:0000269|PubMed:34922205}; Vmax=591 nmol/min/mg enzyme with 6R-tetrahydrobiopterin as substrate {ECO:0000269|PubMed:24753243}; Vmax=2460 nmol/min/mg enzyme with L-tyrosine as substrate {ECO:0000269|PubMed:24753243}; Vmax=35 nmol/min/mg enzyme with L-tyrosine as substrate (in presence of N-ethylmaleimide) {ECO:0000269|PubMed:34922205}; Vmax=141 nmol/min/mg enzyme with L-tyrosine as substrate {ECO:0000269|PubMed:34922205}; Vmax=26 nmol/min/mg enzyme with 6R-tetrahydrobiopterin as substrate (in presence of N-ethylmaleimide) {ECO:0000269|PubMed:34922205}; Vmax=138 nmol/min/mg enzyme with 6R-tetrahydrobiopterin as substrate {ECO:0000269|PubMed:34922205};
|
PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000269|PubMed:17391063}.
| null | null |
FUNCTION: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:15287903, PubMed:1680128, PubMed:17391063, PubMed:24753243, PubMed:34922205, PubMed:8528210, Ref.18). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P24529, ECO:0000269|PubMed:15287903, ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:17391063, ECO:0000269|PubMed:24753243, ECO:0000269|PubMed:34922205, ECO:0000269|PubMed:8528210, ECO:0000269|Ref.18}.; FUNCTION: [Isoform 5]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}.; FUNCTION: [Isoform 6]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}.
|
Homo sapiens (Human)
|
P07102
|
PPA_ECOLI
|
MKAILIPFLSLLIPLTPQSAFAQSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTWPVKLGWLTPRGGELIAYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADVDERTRKTGEAFAAGLAPDCAITVHTQADTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTGHRQTAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKVSADNVSLTGAVSLASMLTEIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFYLLQRTPEVARSRATPLLDLIKTALTPHPPQKQAYGVTLPTSVLFIAGHDTNLANLGGALELNWTLPGQPDNTPPGGELVFERWRRLSDNSQWIQVSLVFQTLQQMRDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQIVNEARIPACSL
|
3.1.3.-; 3.6.1.-
| null |
cellular response to anoxia [GO:0071454]; cellular response to phosphate starvation [GO:0016036]; dephosphorylation [GO:0016311]; lysosome organization [GO:0007040]
|
lysosome [GO:0005764]; outer membrane-bounded periplasmic space [GO:0030288]
|
4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]; GTPase activity [GO:0003924]; inositol phosphate phosphatase activity [GO:0052745]; nucleotidase activity [GO:0008252]; sugar-phosphatase activity [GO:0050308]
|
PF00328;
|
3.40.50.1240;
|
Histidine acid phosphatase family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904}.
|
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate; Xref=Rhea:RHEA:68308, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:177294; Evidence={ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:8387749, ECO:0000269|Ref.8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68309; Evidence={ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:8387749, ECO:0000269|Ref.8}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O = 1D-myo-inositol 2,3,4,5-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:68312, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177294, ChEBI:CHEBI:177295; Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68313; Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 2,4,5-triphosphate + phosphate; Xref=Rhea:RHEA:68316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177295, ChEBI:CHEBI:177296; Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68317; Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2,4,5-triphosphate + H2O = 1D-myo-inositol 2,5-bisphosphate + phosphate; Xref=Rhea:RHEA:68320, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177296, ChEBI:CHEBI:177297; Evidence={ECO:0000269|PubMed:11035187}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68321; Evidence={ECO:0000269|PubMed:11035187}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2,5-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:68324, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:177297; Evidence={ECO:0000269|PubMed:11035187}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68325; Evidence={ECO:0000269|PubMed:11035187}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:6282821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:6282821};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for phytate {ECO:0000269|Ref.8}; KM=0.63 mM for phytate {ECO:0000269|PubMed:10696472}; KM=15 uM for D-Ins(1,2,3,4,5)P5 {ECO:0000269|PubMed:11035187}; KM=0.35 mM for GTP {ECO:0000269|PubMed:6282821}; KM=1.8 mM for ppGpp {ECO:0000269|PubMed:6282821}; KM=0.15 mM for tripolyphosphate {ECO:0000269|PubMed:1429631}; KM=6.5 mM for GDP {ECO:0000269|PubMed:6282821}; KM=20 mM for ATP {ECO:0000269|PubMed:6282821}; KM=2.77 mM for pNPP {ECO:0000269|PubMed:6282821}; KM=2.6 mM for pNPP {ECO:0000269|Ref.8}; KM=2.8 mM for pNPP {ECO:0000269|PubMed:1429631}; KM=5 mM for 2,3-bisphosphoglycerate {ECO:0000269|PubMed:6282821}; KM=5 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:6282821}; KM=3 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:1429631}; Vmax=2326 umol/min/mg enzyme with phytate as substrate {ECO:0000269|PubMed:10696472}; Vmax=9235 umol/min/mg enzyme with D-Ins(1,2,3,4,5)P5 as substrate {ECO:0000269|PubMed:11035187}; Vmax=22 nmol/min/mg enzyme with GTP as substrate {ECO:0000269|PubMed:6282821}; Vmax=40 nmol/min/mg enzyme with ppGpp as substrate {ECO:0000269|PubMed:6282821}; Vmax=440 umol/min/mg enzyme with tripolyphosphate as substrate {ECO:0000269|PubMed:1429631}; Vmax=5 nmol/min/mg enzyme with GDP as substrate {ECO:0000269|PubMed:6282821}; Vmax=62 nmol/min/mg enzyme with ATP as substrate {ECO:0000269|PubMed:6282821}; Vmax=208 nmol/min/mg enzyme with pNPP as substrate {ECO:0000269|PubMed:6282821}; Vmax=530 umol/min/mg enzyme with pNPP as substrate {ECO:0000269|PubMed:1429631}; Vmax=625 nmol/min/mg enzyme with 2,3-bisphosphoglycerate as substrate {ECO:0000269|PubMed:6282821}; Vmax=384 nmol/min/mg enzyme with fructose 1,6-bisphosphate as substrate {ECO:0000269|PubMed:6282821}; Vmax=764 umol/min/mg enzyme with fructose 1,6-bisphosphate as substrate {ECO:0000269|PubMed:1429631};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for phytase activity (PubMed:10696472, PubMed:8387749). Optimum pH is 2.5 for acid phosphatase activity (PubMed:6282821). Optimum pH is 2.5-3.0 for acid phosphatase activity (PubMed:10696472). {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8387749};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius for phytase activity (PubMed:8387749). Optimum temperature is 60 degrees Celsius for phytase activity (PubMed:10696472). {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:8387749};
|
FUNCTION: Catalyzes the hydrolysis of phytate (or myo-inositol hexakisphosphate, an indigestible organic form of phosphorus that is found in many plant tissues) to myo-inositol and inorganic phosphate (PubMed:10696472, PubMed:11035187, PubMed:30712472, PubMed:8387749, Ref.8). Dephosphorylates phytate in a stereospecific way by sequential removal of phosphate groups to produce myo-inositol 2-monophosphate (PubMed:11035187). Also shows phosphoanhydride phosphatase activity and hydrolyzes the distal phosphoryl residues of GTP, the 5'-beta-phosphoryl residue of the regulatory nucleotide ppGpp and tripolyphosphates (PubMed:1429631, PubMed:6282821, PubMed:8407904). Does not split most phosphomonoesters with the exception of the synthetic substrate p-nitrophenyl phosphate (pNPP), 2,3-bisphosphoglycerate and fructose 1,6-bisphosphate (PubMed:10696472, PubMed:1429631, PubMed:6282821, PubMed:8387749, PubMed:8407904, Ref.8). {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904, ECO:0000269|Ref.8}.
|
Escherichia coli (strain K12)
|
P07103
|
GUNZ_DICD3
|
MPLSYLDKNPVIDSKKHALRKKLFLSCAYFGLSLACLSSNAWASVEPLSVNGNKIYAGEKAKSFAGNSLFWSNNGWGGEKFYTADTVASLKKDWKSSIVRAAMGVQESGGYLQDPAGNKAKVERVVDAAIANDMYAIIGWHSHSAENNRSEAIRFFQEMARKYGNKPNVIYEIYNEPLQVSWSNTIKPYAEAVISAIRAIDPDNLIIVGTPSWSQNVDEASRDPINAKNIAYTLHFYAGTHGESLRNKARQALNNGIALFVTEWGTVNADGNGGVNQTETDAWVTFMRDNNISNANWALNDKNEGASTYYPDSKNLTESGKKVKSIIQSWPYKAGSAASATTDPSTDTTTDTTVDEPTTTDTPATADCANANVYPNWVSKDWAGGQPTHNEAGQSIVYKGNLYTANWYTASVPGSDSSWTQVGSCN
|
3.2.1.4
| null |
cellulose catabolic process [GO:0030245]
|
extracellular region [GO:0005576]
|
carbohydrate binding [GO:0030246]; cellulase activity [GO:0008810]
|
PF14600;PF00150;
|
2.10.10.20;3.20.20.80;
|
Glycosyl hydrolase 5 (cellulase A) family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
| null | null | null | null |
FUNCTION: Represents 97% of the global cellulase activity.
|
Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
|
P07107
|
ACBP_BOVIN
|
MSQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
| null | null |
fatty acid metabolic process [GO:0006631]
|
endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]
|
fatty-acyl-CoA binding [GO:0000062]
|
PF00887;
|
1.20.80.10;
|
ACBP family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17953517}. Golgi apparatus {ECO:0000269|PubMed:17953517}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}.
| null | null | null | null | null |
FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. {ECO:0000269|PubMed:11491287}.
|
Bos taurus (Bovine)
|
P07108
|
ACBP_HUMAN
|
MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKKKYGI
| null | null |
fatty acid metabolic process [GO:0006631]; negative regulation of protein lipidation [GO:1903060]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of phospholipid transport [GO:2001140]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; perinuclear endoplasmic reticulum [GO:0097038]; protein-lipid complex [GO:0032994]
|
benzodiazepine receptor binding [GO:0030156]; fatty-acyl-CoA binding [GO:0000062]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA binding [GO:0036042]
|
PF00887;
|
1.20.80.10;
|
ACBP family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Golgi apparatus {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Note=Golgi localization is dependent on ligand binding (PubMed:17953517). {ECO:0000269|PubMed:17953517}.
| null | null | null | null | null |
FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.
|
Homo sapiens (Human)
|
P07112
|
MOBA2_ECOLX
|
MAIYHLTAKTGSRSGGQSARAKADYIQREGKYARDMDEVLHAESGHMPEFVERPADYWDAADLYERANGRLFKEVEFALPVELTLDQQKALASEFAQHLTGAERLPYTLAIHAGGGENPHCHLMISERINDGIERPAAQWFKRYNGKTPEKGGAQKTEALKPKAWLEQTREAWADHANRALERAGHDARIDHRTLEAQGIERLPGVHLGPNVVEMEGRGIRTDRADVALNIDTANAQIIDLQEYREAIDHERNRQSEEIQRHQRVSGADRTAGPEHGDTGRRSPAGHEPDPAGQRGAGGGVAESPAPDRGGMGGAGQRVAGGSRRGEQRRAERPERVAGVALEAMANRDAGFHDAYGGAADRIVALARPDATDNRGRLDLAALGGPMKNDRTLQAIGRQLKAMGCERFDIGVRDATTGQMMNREWSAAEVLQNTPWLKRMNAQGNDVYIRPAEQERHGLVLVDDLSEFDLDDMKAEGREPALVVETSPKNYQAWVKVADAAGGELRGQIARTLASEYDADPASADSRHYGRLAGFTNRKDKHTTRAGYQPWVLLRESKGKTATAGPALVQQAGQQIEQAQRQQEKARRLASLELPERQLSRHRRTALDEYRSEMAGLVKRFGDDLSKCDFIAAQKLASRGRSAEEIGKAMAEASPALAERKPGHEADYIERTVSKVMGLPSVQLARAELARAPAPRQRGMDRGGPDFSM
|
2.7.7.101; 5.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Name=Ba(2+); Xref=ChEBI:CHEBI:37136; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Note=Divalent metal cation. Can use Mg(2+), or to a lesser extent, Mn(2+), Ca(2+) or Ba(2+). {ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650};
| null |
cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428]
|
DNA binding [GO:0003677]; DNA primase activity [GO:0003896]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872]
|
PF03389;PF16793;
|
1.10.1240.50;3.30.930.30;3.30.1490.240;3.30.70.1790;1.20.5.460;
|
MobA/MobL family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.101; Evidence={ECO:0000269|PubMed:10217797};
| null | null | null | null |
FUNCTION: Part of the relaxosome complex that is responsible for plasmid transfer during conjugation. Locally unwinds DNA and catalyzes the cleavage of one of the DNA strands at oriT. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MobA remains covalently linked at the 5' end of the strand, and once in the recipient cell, it probably catalyzes the rejoining of the two ends of the strand, re-forming the circular plasmid DNA. The primase activity of MobA is essential for the synthesis of primers that will initiate the DNA replication events necessary to form the double-stranded plasmid in the recipient cell. {ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8955311}.
|
Escherichia coli
|
P07117
|
PUTP_ECOLI
|
MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAVFLSGISESWIAIGLTLGAWINWKLVAGRLRVHTEYNNNALTLPDYFTGRFEDKSRILRIISALVILLFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALILTPVIVIISVGGFGDSLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMILCLAGAVAVGFFGIAYFNDHPALAGAVNQNAERVFIELAQILFNPWIAGILLSAILAAVMSTLSCQLLVCSSAITEDLYKAFLRKHASQKELVWVGRVMVLVVALVAIALAANPENRVLGLVSYAWAGFGAAFGPVVLFSVMWSRMTRNGALAGMIIGALTVIVWKQFGWLGLYEIIPGFIFGSIGIVVFSLLGKAPSAAMQKRFAEADAHYHSAPPSRLQES
| null | null |
proline transport [GO:0015824]; short-chain fatty acid transport [GO:0015912]; transmembrane transport [GO:0055085]
|
plasma membrane [GO:0005886]
|
L-proline transmembrane transporter activity [GO:0015193]; proline:sodium symporter activity [GO:0005298]; sodium ion binding [GO:0031402]
|
PF00474;
|
1.20.1730.10;
|
Sodium:solute symporter (SSF) (TC 2.A.21) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:3007935, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:3902503, ECO:0000269|PubMed:9756872}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:9756872}.
|
CATALYTIC ACTIVITY: Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence={ECO:0000269|PubMed:1567896, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:9693004};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for L-proline {ECO:0000269|PubMed:3512540}; KM=2 uM for L-proline (for Na(+)-driven transport) {ECO:0000269|PubMed:9693004}; KM=31 uM for Na(+) (in intact cells) {ECO:0000269|PubMed:9693004}; KM=730 uM for Na(+) (for reconstituted PutP in proteoliposomes) {ECO:0000269|PubMed:9693004}; Vmax=16 nmol/min/mg enzyme {ECO:0000269|PubMed:3512540}; Vmax=1130 nmol/min/mg enzyme (for Na(+)-driven transport) {ECO:0000269|PubMed:9693004};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:3512540};
| null |
FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-proline (PubMed:1567896, PubMed:3512540, PubMed:9693004). This protein is also capable of using lithium as the transport cation (PubMed:1567896, PubMed:9693004). Also catalyzes the uptake of propionate (PubMed:17088549). {ECO:0000269|PubMed:1567896, ECO:0000269|PubMed:17088549, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:9693004}.
|
Escherichia coli (strain K12)
|
P07118
|
SYV_ECOLI
|
MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAQVFDTKGNESDVYSSEIPAEFQKLERFAARKAVVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDEAGNVYVGRNEDEVRKENNLGADVVLRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQLADKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEGQDCGFNGGEMTLSLADRWILAEFNQTIKAYREALDSFRFDIAAGILYEFTWNQFCDWYLELTKPVMNGGTEAELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVLCGITADTIMLQPFPQYDASQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSADAERRVNENRGFLQTLARLESITVLPADDKGPVSVTKIIDGAELLIPMAGLINKEDELARLAKEVAKIEGEISRIENKLANEGFVARAPEAVIAKEREKLEGYAEAKAKLIEQQAVIAAL
|
6.1.1.9
| null |
cytosolic valyl-tRNA aminoacylation [GO:0061475]; positive regulation of translational fidelity [GO:0045903]; valyl-tRNA aminoacylation [GO:0006438]
|
cytosol [GO:0005829]
|
aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; valine-tRNA ligase activity [GO:0004832]
|
PF08264;PF00133;PF10458;
|
3.40.50.620;1.10.287.380;3.90.740.10;
|
Class-I aminoacyl-tRNA synthetase family, ValS type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 uM for tRNA {ECO:0000269|PubMed:12475234}; KM=47 uM for valine {ECO:0000269|PubMed:12475234};
| null | null | null |
FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
|
Escherichia coli (strain K12)
|
P07140
|
ACES_DROME
|
MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKALINDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTIDGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDATALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVGDHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEYFFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKEDPVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSWAGTCDGDSGSASISPRLQLLGIAALIYICAALRTKRVF
|
3.1.1.7
| null |
acetylcholine catabolic process [GO:0006581]; acetylcholine catabolic process in synaptic cleft [GO:0001507]; chemical synaptic transmission [GO:0007268]; choline catabolic process [GO:0042426]; choline metabolic process [GO:0019695]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202]; synaptic cleft [GO:0043083]
|
acetylcholinesterase activity [GO:0003990]; cholinesterase activity [GO:0004104]; protein homodimerization activity [GO:0042803]; serine hydrolase activity [GO:0017171]; sulfate binding [GO:0043199]
|
PF00135;
|
3.40.50.1820;
|
Type-B carboxylesterase/lipase family
|
PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell. {ECO:0000269|PubMed:2975507}.; PTM: Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion. {ECO:0000269|PubMed:1730712}.
|
SUBCELLULAR LOCATION: Synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.
|
CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
| null | null | null | null |
FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
|
Drosophila melanogaster (Fruit fly)
|
P07141
|
CSF1_MOUSE
|
MTARGAAGRCPSSTWLGSRLLLVCLLMSRSIAKEVSEHCSHMIGNGHLKVLQQLIDSQMETSCQIAFEFVDQEQLDDPVCYLKKAFFLVQDIIDETMRFKDNTPNANATERLQELSNNLNSCFTKDYEEQNKACVRTFHETPLQLLEKIKNFFNETKNLLEKDWNIFTKNCNNSFAKCSSRDVVTKPDCNCLYPKATPSSDPASASPHQPPAPSMAPLAGLAWDDSQRTEGSSLLPSELPLRIEDPGSAKQRPPRSTCQTLESTEQPNHGDRLTEDSQPHPSAGGPVPGVEDILESSLGTNWVLEEASGEASEGFLTQEAKFSPSTPVGGSIQAETDRPRALSASPFPKSTEDQKPVDITDRPLTEVNPMRPIGQTQNNTPEKTDGTSTLREDHQEPGSPHIATPNPQRVSNSATPVAQLLLPKSHSWGIVLPLGELEGKRSTRDRRSPAELEGGSASEGAARPVARFNSIPLTDTGHVEQHEGSSDPQIPESVFHLLVPGIILVLLTVGGLLFYKWKWRSHRDPQTLDSSVGRPEDSSLTQDEDRQVELPV
| null | null |
branching involved in mammary gland duct morphogenesis [GO:0060444]; developmental process involved in reproduction [GO:0003006]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; macrophage colony-stimulating factor signaling pathway [GO:0038145]; macrophage differentiation [GO:0030225]; macrophage homeostasis [GO:0061519]; mammary duct terminal end bud growth [GO:0060763]; mammary gland fat development [GO:0060611]; microglial cell proliferation [GO:0061518]; monocyte differentiation [GO:0030224]; monocyte homeostasis [GO:0035702]; myeloid leukocyte migration [GO:0097529]; neutrophil homeostasis [GO:0001780]; ossification [GO:0001503]; osteoclast differentiation [GO:0030316]; osteoclast proliferation [GO:0002158]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of gene expression [GO:0010628]; positive regulation of leukocyte migration [GO:0002687]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage colony-stimulating factor signaling pathway [GO:1902228]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of macrophage proliferation [GO:0120041]; positive regulation of microglial cell migration [GO:1904141]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of mononuclear cell migration [GO:0071677]; positive regulation of mononuclear cell proliferation [GO:0032946]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of odontogenesis of dentin-containing tooth [GO:0042488]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of Ras protein signal transduction [GO:0046579]; Ras protein signal transduction [GO:0007265]; regulation of ossification [GO:0030278]; response to ischemia [GO:0002931]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
CSF1-CSF1R complex [GO:1990682]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; macrophage colony-stimulating factor receptor binding [GO:0005157]; protein homodimerization activity [GO:0042803]
|
PF05337;
|
1.20.1250.10;
| null |
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09603}.; PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000269|PubMed:1733926}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor 1]: Secreted, extracellular space {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance.
|
Mus musculus (Mouse)
|
P07142
|
CY1_NEUCR
|
MLARTCLRSTRTFASAKNGAFKFAKRSASTQSSGAAAESPLRLNIAAAAATAVAAGSIAWYYHLYGFASAMTPAEEGLHATKYPWVHEQWLKTFDHQALRRGFQVYREVCASCHSLSRVPYRALVGTILTVDEAKALAEENEYDTEPNDQGEIEKRPGKLSDYLPDPYKNDEAARFANNGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGASVGAGLNFNPYFPGTGIAMARVLYDGLVDYEDGTPASTSQMAKDVVEFLNWAAEPEMDDRKRMGMKVLVVTSVLFALSVYVKRYKWAWLKSRKIVYDPPKSPPPATNLALPQQRAKS
|
7.1.1.8
|
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143};
|
mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
mitochondrial respiratory chain complex III [GO:0005750]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF02167;
|
1.10.760.10;1.20.5.100;
|
Cytochrome c family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:226365}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}.
|
CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1847681, ECO:0000269|PubMed:3015618};
| null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable) (PubMed:3015618). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c (By similarity). {ECO:0000250|UniProtKB:P07143, ECO:0000269|PubMed:3015618, ECO:0000305|PubMed:1847681, ECO:0000305|PubMed:19239619}.
|
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
|
P07143
|
CY1_YEAST
|
MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAEAMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFVFNPPKPRK
|
7.1.1.8
|
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
|
cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF02167;
|
1.10.760.10;1.20.5.100;
|
Cytochrome c family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
|
CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:11279090};
| null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c (PubMed:18390544). {ECO:0000269|PubMed:18390544, ECO:0000305|PubMed:11880631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07146
|
TRY2_MOUSE
|
MSALLILALVGAAVAFPVDDDDKIVGGYTCRESSVPYQVSLNAGYHFCGGSLINDQWVVSAAHCYKYRIQVRLGEHNINVLEGNEQFVDSAKIIRHPNYNSWTLDNDIMLIKLASPVTLNARVASVPLPSSCAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLPQADCEASYPGDITNNMICVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCAQPDAPGVYTKVCNYVDWIQNTIADN
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
|
collagen catabolic process [GO:0030574]; digestion [GO:0007586]; proteolysis [GO:0006508]; response to caffeine [GO:0031000]; response to nicotine [GO:0035094]; response to nutrient [GO:0007584]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null | null |
Mus musculus (Mouse)
|
P07147
|
TYRP1_MOUSE
|
MKSYNVLPLAYISLFLMLFYQVWAQFPRECANIEALRRGVCCPDLLPSSGPGTDPCGSSSGRGRCVAVIADSRPHSRHYPHDGKDDREAWPLRFFNRTCQCNDNFSGHNCGTCRPGWRGAACNQKILTVRRNLLDLSPEEKSHFVRALDMAKRTTHPQFVIATRRLEDILGPDGNTPQFENISVYNYFVWTHYYSVKKTFLGTGQESFGDVDFSHEGPAFLTWHRYHLLQLERDMQEMLQEPSFSLPYWNFATGKNVCDVCTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEEYDTLGTLCNSTEGGPIRRNPAGNVGRPAVQRLPEPQDVTQCLEVRVFDTPPFYSNSTDSFRNTVEGYSAPTGKYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTFPLENAPIGHNRQYNMVPFWPPVTNTEMFVTAPDNLGYAYEVQWPGQEFTVSEIITIAVVAALLLVAAIFGVASCLIRSRSTKNEANQPLLTDHYQRYAEDYEELPNPNHSMV
|
1.14.18.-
|
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:P17643}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P17643}; Note=Contains bound zinc ions after heterologous expression in insect cells. {ECO:0000250|UniProtKB:P17643};
|
acetoacetic acid metabolic process [GO:0043438]; melanin biosynthetic process from tyrosine [GO:0006583]; melanin metabolic process [GO:0006582]; melanocyte differentiation [GO:0030318]; melanosome organization [GO:0032438]; pigmentation [GO:0043473]; positive regulation of melanin biosynthetic process [GO:0048023]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; endosome membrane [GO:0010008]; melanosome [GO:0042470]; melanosome membrane [GO:0033162]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; tyrosinase activity [GO:0004503]
|
PF00264;
|
1.10.1280.10;
|
Tyrosinase family
|
PTM: Glycosylated. {ECO:0000269|PubMed:1537333}.
|
SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18650808, ECO:0000269|PubMed:26620560}; Single-pass type I membrane protein {ECO:0000269|PubMed:17182842}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:26620560}.
|
CATALYTIC ACTIVITY: Reaction=2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2 indole-5,6-quinone-2-carboxylate; Xref=Rhea:RHEA:68388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16875, ChEBI:CHEBI:177869; Evidence={ECO:0000269|PubMed:7813420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389; Evidence={ECO:0000305|PubMed:7813420};
| null |
PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:2245916}.
| null | null |
FUNCTION: Plays a role in melanin biosynthesis (PubMed:2245916). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid (PubMed:7813420). May regulate or influence the type of melanin synthesized (PubMed:2245916, PubMed:7813420). Also to a lower extent, capable of hydroxylating tyrosine and producing melanin (PubMed:1537333). {ECO:0000269|PubMed:1537333, ECO:0000269|PubMed:2245916, ECO:0000269|PubMed:7813420}.
|
Mus musculus (Mouse)
|
P07148
|
FABPL_HUMAN
|
MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI
| null | null |
cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; fatty acid transport [GO:0015908]; intestinal absorption [GO:0050892]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of fatty acid beta-oxidation [GO:0032000]; response to vitamin B3 [GO:0033552]
|
apical cortex [GO:0045179]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; protein-containing complex [GO:0032991]
|
antioxidant activity [GO:0016209]; bile acid binding [GO:0032052]; chromatin binding [GO:0003682]; fatty acid binding [GO:0005504]; heterocyclic compound binding [GO:1901363]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]; phospholipid binding [GO:0005543]
|
PF14651;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). {ECO:0000250|UniProtKB:P82289, ECO:0000269|PubMed:25732850}.
|
Homo sapiens (Human)
|
P07149
|
FAS1_YEAST
|
MDAYSTRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVLNLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIKNYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQGNTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLDAEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVIQLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLPPSILEDSLENNEGVPSPMLSISNLTQEQVQDYVNKTNSHLPAGKQVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLDQSRIPFSERKLKFSNRFLPVASPFHSHLLVPASDLINKDLVKNNVSFNAKDIQIPVYDTFDGSDLRVLSGSISERIVDCIIRLPVKWETTTQFKATHILDFGPGGASGLGVLTHRNKDGTGVRVIVAGTLDINPDDDYGFKQEIFDVTSNGLKKNPNWLEEYHPKLIKNKSGKIFVETKFSKLIGRPPLLVPGMTPCTVSPDFVAATTNAGYTIELAGGGYFSAAGMTAAIDSVVSQIEKGSTFGINLIYVNPFMLQWGIPLIKELRSKGYPIQFLTIGAGVPSLEVASEYIETLGLKYLGLKPGSIDAISQVINIAKAHPNFPIALQWTGGRGGGHHSFEDAHTPMLQMYSKIRRHPNIMLIFGSGFGSADDTYPYLTGEWSTKFDYPPMPFDGFLFGSRVMIAKEVKTSPDAKKCIAACTGVPDDKWEQTYKKPTGGIVTVRSEMGEPIHKIATRGVMLWKEFDETIFNLPKNKLVPTLEAKRDYIISRLNADFQKPWFATVNGQARDLATMTYEEVAKRLVELMFIRSTNSWFDVTWRTFTGDFLRRVEERFTKSKTLSLIQSYSLLDKPDEAIEKVFNAYPAAREQFLNAQDIDHFLSMCQNPMQKPVPFVPVLDRRFEIFFKKDSLWQSEHLEAVVDQDVQRTCILHGPVAAQFTKVIDEPIKSIMDGIHDGHIKKLLHQYYGDDESKIPAVEYFGGESPVDVQSQVDSSSVSEDSAVFKATSSTDEESWFKALAGSEINWRHASFLCSFITQDKMFVSNPIRKVFKPSQGMVVEISNGNTSSKTVVTLSEPVQGELKPTVILKLLKENIIQMEMIENRTMDGKPVSLPLLYNFNPDNGFAPISEVMEDRNQRIKEMYWKLWIDEPFNLDFDPRDVIKGKDFEITAKEVYDFTHAVGNNCEDFVSRPDRTMLAPMDFAIVVGWRAIIKAIFPNTVDGDLLKLVHLSNGYKMIPGAKPLQVGDVVSTTAVIESVVNQPTGKIVDVVGTLSRNGKPVMEVTSSFFYRGNYTDFENTFQKTVEPVYQMHIKTSKDIAVLRSKEWFQLDDEDFDLLNKTLTFETETEVTFKNANIFSSVKCFGPIKVELPTKETVEIGIVDYEAGASHGNPVVDFLKRNGSTLEQKVNLENPIPIAVLDSYTPSTNEPYARVSGDLNPIHVSRHFASYANLPGTITHGMFSSASVRALIENWAADSVSSRVRGYTCQFVDMVLPNTALKTSIQHVGMINGRKLIKFETRNEDDVVVLTGEAEIEQPVTTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVINNPVNLTIHFGGEKGKRIRENYSAMIFETIVDGKLKTEKIFKEINEHSTSYTFRSEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPADATFAGHSLGEYAALASLADVMSIESLVEVVFYRGMTMQVAVPRDELGRSNYGMIAINPGRVAASFSQEALQYVVERVGKRTGWLVEIVNYNVENQQYVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLSLEEVEGHLFEIIDEASKKSAVKPRPLKLERGFACIPLVGISVPFHSTYLMNGVKPFKSFLKKNIIKENVKVARLAGKYIPNLTAKPFQVTKEYFQDVYDLTGSEPIKEIIDNWEKYEQS
|
1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59
| null |
long-chain fatty acid biosynthetic process [GO:0042759]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fatty acid synthase complex [GO:0005835]; lipid droplet [GO:0005811]; mitochondrion [GO:0005739]
|
(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity [GO:0004319]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty-acyl-CoA synthase activity [GO:0004321]; palmitoyltransferase activity [GO:0016409]
|
PF00698;PF08354;PF17951;PF17828;PF13452;PF01575;PF16073;
|
1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3330;6.10.140.1400;6.10.60.10;6.20.240.10;3.20.20.70;3.10.129.10;3.40.366.10;
|
Fungal fatty acid synthetase subunit beta family
| null | null |
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
| null | null | null | null |
FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07150
|
ANXA1_RAT
|
MAMVSEFLKQACYIEKQEQEYVQAVKSYKGGPGSAVSPYPSFNPSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLAMLKTPAQFDADELRAAMKGLGTDEDTLIEILTTRSNQQIREITRVYREELKRDLAKDITSDTSGDFRNALLALAKGDRCEDMSVNQDLADTDARALYEAGERRKGTDVNVFNTILTTRSYPHLRKVFQNYRKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKTLIRIMVSRSEIDMNEIKVFYQKKYGIPLCQAILDETKGDYEKILVALCGGN
| null | null |
actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; DNA duplex unwinding [GO:0032508]; endocrine pancreas development [GO:0031018]; estrous cycle [GO:0044849]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; gliogenesis [GO:0042063]; granulocyte chemotaxis [GO:0071621]; hepatocyte differentiation [GO:0070365]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; insulin secretion [GO:0030073]; keratinocyte differentiation [GO:0030216]; localization [GO:0051179]; monocyte chemotaxis [GO:0002548]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of exocytosis [GO:0045920]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of protein secretion [GO:0050709]; negative regulation of T-helper 2 cell differentiation [GO:0045629]; neutrophil activation [GO:0042119]; neutrophil clearance [GO:0097350]; neutrophil homeostasis [GO:0001780]; phagocytosis [GO:0006909]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of neutrophil apoptotic process [GO:0033031]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; positive regulation of vesicle fusion [GO:0031340]; positive regulation of wound healing [GO:0090303]; prolactin secretion [GO:0070459]; prostate gland development [GO:0030850]; regulation of cell population proliferation [GO:0042127]; regulation of cell shape [GO:0008360]; regulation of hormone secretion [GO:0046883]; regulation of inflammatory response [GO:0050727]; regulation of interleukin-1 production [GO:0032652]; regulation of leukocyte migration [GO:0002685]; response to estradiol [GO:0032355]; response to glucocorticoid [GO:0051384]; response to hormone [GO:0009725]; response to interleukin-1 [GO:0070555]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to X-ray [GO:0010165]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; mast cell granule [GO:0042629]; mitochondrial membrane [GO:0031966]; motile cilium [GO:0031514]; nucleus [GO:0005634]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; synaptic membrane [GO:0097060]
|
cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; DNA/DNA annealing activity [GO:1990814]; double-stranded DNA helicase activity [GO:0036121]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; phospholipid binding [GO:0005543]; single-stranded DNA binding [GO:0003697]
|
PF00191;
|
1.10.220.10;
|
Annexin family
|
PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12467520}. Cytoplasm {ECO:0000269|PubMed:12467520}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000269|PubMed:3020049}; Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Endosome membrane {ECO:0000269|PubMed:3020049}; Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Secreted {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04083}; Extracellular side {ECO:0000250|UniProtKB:P04083}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (By similarity). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (PubMed:3020049). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107, ECO:0000269|PubMed:3020049}.
| null | null | null | null | null |
FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:3020049). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:3020049}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P04083}.
|
Rattus norvegicus (Rat)
|
P07151
|
B2MG_RAT
|
MARSVTVIFLVLVSLAVVLAIQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDWSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
| null | null |
amyloid fibril formation [GO:1990000]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent [GO:0002481]; cellular response to iron ion [GO:0071281]; cellular response to iron(III) ion [GO:0071283]; cellular response to nicotine [GO:0071316]; intracellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; learning or memory [GO:0007611]; multicellular organismal-level iron ion homeostasis [GO:0060586]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of forebrain neuron differentiation [GO:2000978]; negative regulation of neurogenesis [GO:0050768]; negative regulation of neuron projection development [GO:0010977]; peptide antigen assembly with MHC class I protein complex [GO:0002502]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of cellular senescence [GO:2000774]; positive regulation of immune response [GO:0050778]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; protein homotetramerization [GO:0051289]; protein refolding [GO:0042026]; regulation of erythrocyte differentiation [GO:0045646]; regulation of iron ion transport [GO:0034756]; response to cadmium ion [GO:0046686]; response to molecule of bacterial origin [GO:0002237]; response to xenobiotic stimulus [GO:0009410]; sensory perception of smell [GO:0007608]; T cell differentiation in thymus [GO:0033077]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; HFE-transferrin receptor complex [GO:1990712]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class I peptide loading complex [GO:0042824]; MHC class I protein complex [GO:0042612]; MHC class II protein complex [GO:0042613]
|
identical protein binding [GO:0042802]; MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:0005198]
|
PF07654;
|
2.60.40.10;
|
Beta-2-microglobulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
|
Rattus norvegicus (Rat)
|
P07154
|
CATL1_RAT
|
MTPLLLLAVLCLGTALATPKFDQTFNAQWHQWKSTHRRLYGTNEEEWRRAVWEKNMRMIQLHNGEYSNGKHGFTMEMNAFGDMTNEEFRQIVNGYRHQKHKKGRLFQEPLMLQIPKTVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHDQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEYAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKDLDHGVLVVGYGYEGTDSNKDKYWLVKNSWGKEWGMDGYIKIAKDRNNHCGLATAASYPIVN
|
3.4.22.15
| null |
adaptive immune response [GO:0002250]; antigen processing and presentation of peptide antigen [GO:0048002]; autophagic cell death [GO:0048102]; CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; cellular response to starvation [GO:0009267]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; elastin catabolic process [GO:0060309]; enkephalin processing [GO:0034230]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; hair follicle morphogenesis [GO:0031069]; immune response [GO:0006955]; keratinocyte proliferation [GO:0043616]; male gonad development [GO:0008584]; negative regulation of keratinocyte proliferation [GO:0010839]; nerve development [GO:0021675]; positive regulation of apoptotic signaling pathway [GO:2001235]; protein autoprocessing [GO:0016540]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to gonadotropin [GO:0034698]; response to odorant [GO:1990834]; response to organic cyclic compound [GO:0014070]; Sertoli cell differentiation [GO:0060008]; spermatogenesis [GO:0007283]; symbiont entry into host cell [GO:0046718]; thyroid hormone generation [GO:0006590]; zymogen activation [GO:0031638]
|
apical plasma membrane [GO:0016324]; chromaffin granule [GO:0042583]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; microvillus [GO:0005902]; multivesicular body [GO:0005771]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]
|
aminopeptidase activity [GO:0004177]; collagen binding [GO:0005518]; cysteine-type carboxypeptidase activity [GO:0016807]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; fibronectin binding [GO:0001968]; histone binding [GO:0042393]; kininogen binding [GO:0030984]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; proteoglycan binding [GO:0043394]; serpin family protein binding [GO:0097655]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
|
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (By similarity). {ECO:0000250|UniProtKB:P06797, ECO:0000250|UniProtKB:P07711}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:7777858}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted {ECO:0000269|PubMed:7777858}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797}.
|
CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000250|UniProtKB:P07711};
| null | null | null | null |
FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (PubMed:7777858). {ECO:0000250|UniProtKB:P06797, ECO:0000250|UniProtKB:P07711, ECO:0000250|UniProtKB:P25975, ECO:0000269|PubMed:7777858}.
|
Rattus norvegicus (Rat)
|
P07156
|
HMGB1_CRIGR
|
VNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE
| null | null |
adaptive immune response [GO:0002250]; apoptotic cell clearance [GO:0043277]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0017055]; neutrophil clearance [GO:0097350]; positive regulation of DNA ligation [GO:0051106]; positive regulation of toll-like receptor 9 signaling pathway [GO:0034165]; regulation of T cell mediated immune response to tumor cell [GO:0002840]
|
condensed chromosome [GO:0000793]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
DNA binding, bending [GO:0008301]
|
PF00505;PF09011;
|
1.10.30.10;
|
HMGB family
|
PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) leads to cytoplasmic localization and subsequent secretion (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; PTM: Reduction/oxidation of cysteine residues and a possible intramolecular disulfide bond give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB1 (HMGB1C23hC45hC106h), 2-disulfide HMGB1 (HMGB1C23-C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so). {ECO:0000250|UniProtKB:P09429}.; PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation with LPS (By similarity). {ECO:0000250|UniProtKB:P63158}.; PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing peptide which may mediate immunogenic activity; the peptide antagonizes apoptosis-induced immune tolerance. Can be proteolytically cleaved by a thrombin:thrombomodulin complex; reduces binding to heparin and pro-inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103}.; PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. {ECO:0000250|UniProtKB:P09429}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Extracellular side {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus. Translocates from the nucleus to the cytoplasm upon autophagy stimulation. Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced HGMB1 which subsequently gets oxidized. Also released from apoptotic cells. Active secretion from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells, natural killer cells and plasma cells in response to various stimuli such as LPS and cytokines involves a nonconventional secretory process via secretory lysosomes. Found on the surface of activated platelets. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.
| null | null | null | null | null |
FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10.Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
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Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
P07170
|
KAD2_YEAST
|
MSSSESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGEALVQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDASQPPATVWADILNKLGKD
|
2.7.4.3
| null |
ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; DNA replication initiation [GO:0006270]; nucleotide metabolic process [GO:0009117]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]
|
PF00406;PF05191;
|
3.40.50.300;
|
Adenylate kinase family, AK2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:2850178}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:2850178}. Note=90% cytoplasmic, 10% mitochondrial. {ECO:0000269|PubMed:2850178}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:2850178};
| null | null | null | null |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:18433446, ECO:0000269|PubMed:2848829, ECO:0000269|PubMed:2850178}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07171
|
CALB1_RAT
|
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALILSAGDN
| null | null |
cellular response to organic substance [GO:0071310]; cochlea development [GO:0090102]; learning or memory [GO:0007611]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; metanephric collecting duct development [GO:0072205]; metanephric connecting tubule development [GO:0072286]; metanephric distal convoluted tubule development [GO:0072221]; metanephric part of ureteric bud development [GO:0035502]; regulation of long-term synaptic potentiation [GO:1900271]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; regulation of synaptic plasticity [GO:0048167]; response to auditory stimulus [GO:0010996]; retina development in camera-type eye [GO:0060041]; retina layer formation [GO:0010842]; short-term memory [GO:0007614]; vitamin D metabolic process [GO:0042359]
|
axon [GO:0030424]; calyx of Held [GO:0044305]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; postsynapse [GO:0098794]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; stereocilium [GO:0032420]; synapse [GO:0045202]; terminal bouton [GO:0043195]
|
calcium ion binding [GO:0005509]; calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration [GO:0099567]; calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration [GO:0099534]; vitamin D binding [GO:0005499]; zinc ion binding [GO:0008270]
|
PF00036;PF13499;
|
1.10.238.10;
|
Calbindin family
| null | null | null | null | null | null | null |
FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
|
Rattus norvegicus (Rat)
|
P07173
|
CYCR_BLAVI
|
MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
| null | null |
photosynthesis [GO:0015979]; photosynthesis, light reaction [GO:0019684]
|
plasma membrane light-harvesting complex [GO:0030077]; plasma membrane-derived chromatophore membrane [GO:0042717]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
|
PF02276;
|
1.10.468.10;
| null |
PTM: Binds 4 heme groups per subunit. {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:10736158, ECO:0000269|PubMed:22054235, ECO:0000269|PubMed:6392571, ECO:0000269|PubMed:9351808, ECO:0000269|Ref.7}.; PTM: After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, but the alpha-amino group is free and is not N-palmitoylated. {ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4}.
|
SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:9351808}; Lipid-anchor {ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4}.
| null | null | null | null | null |
FUNCTION: The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. {ECO:0000269|PubMed:10736158}.
|
Blastochloris viridis (Rhodopseudomonas viridis)
|
P07174
|
TNR16_RAT
|
MRRAGAACSAMDRLRLLLLLILGVSSGGAKETCSTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDNVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCAYGYYQDEETGHCEACSVCEVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEEIPGRWIPRSTPPEGSDSTAPSTQEPEVPPEQDLVPSTVADMVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQTHTQTASGQALKGDGNLYSSLPLTKREEVEKLLNGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWGAQDSATLDALLAALRRIQRADIVESLCSESTATSPV
| null | null |
axon guidance [GO:0007411]; cellular response to amyloid-beta [GO:1904646]; cellular response to oxidative stress [GO:0034599]; central nervous system development [GO:0007417]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; detection of temperature stimulus [GO:0016048]; dorsal aorta development [GO:0035907]; fibroblast growth factor receptor signaling pathway [GO:0008543]; fibroblast proliferation [GO:0048144]; glucose homeostasis [GO:0042593]; hair follicle development [GO:0001942]; hair follicle morphogenesis [GO:0031069]; intracellular glucose homeostasis [GO:0001678]; intracellular protein transport [GO:0006886]; negative regulation of angiogenesis [GO:0016525]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration [GO:0030336]; negative regulation of dendritic spine development [GO:0061000]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of hair follicle development [GO:0051799]; negative regulation of mitochondrial depolarization [GO:0051902]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron projection development [GO:0010977]; nerve development [GO:0021675]; neuron apoptotic process [GO:0051402]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of myelination [GO:0031643]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron projection development [GO:0010976]; positive regulation of odontogenesis of dentin-containing tooth [GO:0042488]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of synaptic transmission, cholinergic [GO:0032224]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of gene expression [GO:0010468]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to lipopolysaccharide [GO:0032496]; Rho protein signal transduction [GO:0007266]; skeletal muscle cell differentiation [GO:0035914]; skin development [GO:0043588]
|
cell surface [GO:0009986]; cell-cell junction [GO:0005911]; clathrin-coated endocytic vesicle [GO:0045334]; cytoplasm [GO:0005737]; dendrite membrane [GO:0032590]; dendritic spine [GO:0043197]; external side of plasma membrane [GO:0009897]; growth cone [GO:0030426]; neuromuscular junction [GO:0031594]; neuronal cell body membrane [GO:0032809]; nuclear envelope [GO:0005635]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]
|
amyloid-beta binding [GO:0001540]; calmodulin binding [GO:0005516]; coreceptor activity [GO:0015026]; death receptor activity [GO:0005035]; identical protein binding [GO:0042802]; nerve growth factor binding [GO:0048406]; neurotrophin binding [GO:0043121]; neurotrophin TRKA receptor binding [GO:0005168]; preprotein binding [GO:0070678]; protein-containing complex binding [GO:0044877]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625]
|
PF00531;PF18422;PF00020;
|
6.10.250.1780;1.10.533.10;2.10.50.10;
| null |
PTM: Subject to intramembrane proteolytic cleavage by the gamma-secretase complex, giving rise to an intracellular fragment that is rapidly degraded via the proteasome. {ECO:0000269|PubMed:27056327}.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:20036257}.; PTM: Phosphorylated on serine residues.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:3027580}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:22155786}. Cell projection, growth cone {ECO:0000269|PubMed:22155786}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9Z0W1}.
| null | null | null | null | null |
FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4 (PubMed:15131306, PubMed:18596692, PubMed:3027580). Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:22155786, PubMed:24908487). In response to proNGF binding, the heterodimeric receptor with SORCS2 activates a signaling cascade that leads to decreased Rac activity, reorganization of the actin cytoskeleton and neuronal growth cone collapse (PubMed:22155786). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells (PubMed:10514511, PubMed:10985348, PubMed:24908487). Plays a role in the inactivation of RHOA (By similarity). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (By similarity). {ECO:0000250|UniProtKB:P08138, ECO:0000250|UniProtKB:Q9Z0W1, ECO:0000269|PubMed:10514511, ECO:0000269|PubMed:10985348, ECO:0000269|PubMed:15131306, ECO:0000269|PubMed:18596692, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:3027580}.
|
Rattus norvegicus (Rat)
|
P07195
|
LDHB_HUMAN
|
MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
|
1.1.1.27
| null |
lactate metabolic process [GO:0006089]; NAD metabolic process [GO:0019674]; pyruvate metabolic process [GO:0006090]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; oxidoreductase complex [GO:1990204]
|
identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; NAD binding [GO:0051287]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, LDH family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion inner membrane {ECO:0000269|PubMed:27618187}; Peripheral membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000269|PubMed:11276087, ECO:0000269|PubMed:27618187}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; Evidence={ECO:0000269|PubMed:11276087}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446; Evidence={ECO:0000269|PubMed:11276087};
| null |
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000305|PubMed:27618187}.
| null | null |
FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:27618187}.
|
Homo sapiens (Human)
|
P07196
|
NFL_HUMAN
|
MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKDKEEAEEEEAAEEEEAAKEESEEAKEEEEGGEGEEGEETKEAEEEEKKVEGAGEEQAAKKKD
| null | null |
anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cerebral cortex development [GO:0021987]; hippocampus development [GO:0021766]; intermediate filament organization [GO:0045109]; intermediate filament polymerization or depolymerization [GO:0045105]; locomotion [GO:0040011]; microtubule cytoskeleton organization [GO:0000226]; motor neuron apoptotic process [GO:0097049]; negative regulation of motor neuron apoptotic process [GO:2000672]; neurofilament bundle assembly [GO:0033693]; neurofilament cytoskeleton organization [GO:0060052]; neuromuscular process controlling balance [GO:0050885]; peripheral nervous system axon regeneration [GO:0014012]; positive regulation of axonogenesis [GO:0050772]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; protein polymerization [GO:0051258]; regulation of axon diameter [GO:0031133]; regulation of synapse maturation [GO:0090128]; response to acrylamide [GO:1903937]; response to corticosterone [GO:0051412]; response to peptide hormone [GO:0043434]; response to sodium arsenite [GO:1903935]; response to toxic substance [GO:0009636]; retrograde axonal transport [GO:0008090]; spinal cord development [GO:0021510]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; intermediate filament [GO:0005882]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; postsynaptic intermediate filament cytoskeleton [GO:0099160]; presynaptic intermediate filament cytoskeleton [GO:0099182]; Schaffer collateral - CA1 synapse [GO:0098685]
|
identical protein binding [GO:0042802]; phospholipase binding [GO:0043274]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic intermediate filament cytoskeleton [GO:0099184]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000269|PubMed:8621664}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}.
| null | null | null | null | null |
FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08551}.
|
Homo sapiens (Human)
|
P07197
|
NFM_HUMAN
|
MSYTLDSLGNPSAYRRVTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYKRSMLAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGPGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTFAGSITGPLYTHRPPITISSKIQKPKVEAPKLKVQHKFVEEIIEETKVEDEKSEMEEALTAITEELAVSMKEEKKEAAEEKEEEPEAEEEEVAAKKSPVKATAPEVKEEEGEKEEEEGQEEEEEEDEGAKSDQAEEGGSEKEGSSEKEEGEQEEGETEAEAEGEEAEAKEEKKVEEKSEEVATKEELVADAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVSKSPVEEKAKSPVPKSPVEEAKSKAEVGKGEQKEEEEKEVKEAPKEEKVEKKEEKPKDVPEKKKAESPVKEEAVAEVVTITKSVKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSDKGAKGSRKEDIAVNGEVEGKEEVEQETKEKGSGREEEKGVVTNGLDLSPADEKKGGDKSEEKVVVTKTVEKITSEGGDGATKYITKSVTVTQKVEEHEETFEEKLVSTKKVEKVTSHAIVKEVTQSD
| null | null |
neurofilament bundle assembly [GO:0033693]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neurofibrillary tangle [GO:0097418]; neurofilament [GO:0005883]; postsynaptic intermediate filament cytoskeleton [GO:0099160]
|
microtubule binding [GO:0008017]; structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08553}. Cell projection, axon {ECO:0000250|UniProtKB:P08553}.
| null | null | null | null | null |
FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}.
|
Homo sapiens (Human)
|
P07199
|
CENPB_HUMAN
|
MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLTEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTSLKSEGEEEEEEEEEEEEEEGEGEEEEEEGEEEEEEGGEGEELGEEEEVEEEGDVDSDEEEEEDEESSSEGLEAEDWAQGVVEAGGSFGAYGAQEEAQCPTLHFLEGGEDSDSDSEEEDDEEEDDEDEDDDDDEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS
| null | null | null |
chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
centromeric DNA binding [GO:0019237]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; satellite DNA binding [GO:0003696]; sequence-specific DNA binding [GO:0043565]
|
PF09026;PF04218;PF03184;PF03221;
|
1.10.287.1090;1.10.10.60;
| null |
PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:P27790}.; PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is stimulated in response to extracellular stimuli, including increased cell density and heat shock, and seems to facilitate binding to CENP-B boxes. Chromatin-bound CENP-B is primarily trimethylated. {ECO:0000269|PubMed:23978223}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583, ECO:0000269|PubMed:18072184}. Chromosome, centromere {ECO:0000269|PubMed:18072184}.
| null | null | null | null | null |
FUNCTION: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box (PubMed:11726497). May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes (Probable). {ECO:0000269|PubMed:11726497, ECO:0000305}.
|
Homo sapiens (Human)
|
P07200
|
TGFB1_PIG
|
MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGDVPPGPLPEAVLALYNSTRDRVAGESVEPEPEPEADYYAKEVTRVLMVESGNQIYDKFKGTPHSLYMLFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNDSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTRREAIEGFRLSAHCSCDSKDNTLHVEINGFNSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
| null | null |
ATP biosynthetic process [GO:0006754]; cell-cell junction organization [GO:0045216]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic signaling pathway [GO:0097191]; hematopoietic progenitor cell differentiation [GO:0002244]; hyaluronan catabolic process [GO:0030214]; inflammatory response [GO:0006954]; lymph node development [GO:0048535]; membrane protein intracellular domain proteolysis [GO:0031293]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of skeletal muscle tissue development [GO:0048642]; odontoblast differentiation [GO:0071895]; phosphate-containing compound metabolic process [GO:0006796]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of microglia differentiation [GO:0014008]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein phosphorylation [GO:0006468]; receptor catabolic process [GO:0032801]; regulation of binding [GO:0051098]; regulation of cell population proliferation [GO:0042127]; regulation of DNA binding [GO:0051101]; regulation of protein import into nucleus [GO:0042306]; regulation of striated muscle tissue development [GO:0016202]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to cholesterol [GO:0070723]; response to estradiol [GO:0032355]; response to progesterone [GO:0032570]; response to wounding [GO:0009611]; salivary gland morphogenesis [GO:0007435]; transforming growth factor beta receptor signaling pathway [GO:0007179]
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blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleus [GO:0005634]
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antigen binding [GO:0003823]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta receptor binding [GO:0034714]
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PF00019;PF00688;
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2.60.120.970;2.10.90.10;
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TGF-beta family
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PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: [Latency-associated peptide]: N-glycosylated. Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear. {ECO:0000250|UniProtKB:P01137}.
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SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}.
| null | null | null | null | null |
FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia. Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Transforming growth factor beta-1]: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus. Positively regulates odontoblastic differentiation in dental papilla cells, via promotion of IPO7-mediated translocation of phosphorylated SMAD2 to the nucleus and subsequent transcription of target genes (By similarity). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.
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Sus scrofa (Pig)
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P07202
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PERT_HUMAN
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MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRNLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALSEDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQLTCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVDSGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQAVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
|
1.11.1.8
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COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
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embryonic hemopoiesis [GO:0035162]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thyroid hormone generation [GO:0006590]
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cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
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calcium ion binding [GO:0005509]; heme binding [GO:0020037]; iodide peroxidase activity [GO:0004447]; peroxidase activity [GO:0004601]
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PF03098;PF07645;PF00084;
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2.10.70.10;1.10.640.10;2.10.25.10;
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Peroxidase family, XPO subfamily
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PTM: Glycosylated.; PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface.; PTM: Cleaved in its N-terminal part.
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SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell surface.
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CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956, Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O; Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277, Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine + [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278, Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873, ChEBI:CHEBI:90874; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933};
| null |
PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
| null | null |
FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}.
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Homo sapiens (Human)
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P07203
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GPX1_HUMAN
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MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA
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1.11.1.12; 1.11.1.9
| null |
angiogenesis involved in wound healing [GO:0060055]; arachidonic acid metabolic process [GO:0019369]; biological process involved in interaction with symbiont [GO:0051702]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to glucose stimulus [GO:0071333]; cellular response to oxidative stress [GO:0034599]; endothelial cell development [GO:0001885]; epigenetic regulation of gene expression [GO:0040029]; fat cell differentiation [GO:0045444]; fibroblast proliferation [GO:0048144]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide catabolic process [GO:0042744]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; lipoxygenase pathway [GO:0019372]; myoblast differentiation [GO:0045445]; myoblast proliferation [GO:0051450]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neuron apoptotic process [GO:0051402]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of supramolecular fiber organization [GO:1902905]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of proteasomal protein catabolic process [GO:0061136]; response to estradiol [GO:0032355]; response to folic acid [GO:0051593]; response to gamma radiation [GO:0010332]; response to hormone [GO:0009725]; response to hydrogen peroxide [GO:0042542]; response to hydroperoxide [GO:0033194]; response to nicotine [GO:0035094]; response to selenium ion [GO:0010269]; response to symbiotic bacterium [GO:0009609]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; skeletal muscle fiber development [GO:0048741]; skeletal muscle tissue regeneration [GO:0043403]; temperature homeostasis [GO:0001659]; triglyceride metabolic process [GO:0006641]; UV protection [GO:0009650]; vasodilation [GO:0042311]
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cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
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glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; SH3 domain binding [GO:0017124]
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PF00255;
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3.40.30.10;
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Glutathione peroxidase family
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PTM: During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250|UniProtKB:P11352}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}.
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CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000305|PubMed:11115402}; CATALYTIC ACTIVITY: Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O; Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019; EC=1.11.1.12; Evidence={ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412, ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:64090; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413; Evidence={ECO:0000269|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673, ChEBI:CHEBI:131607; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652; Evidence={ECO:0000269|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76687, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:60955, ChEBI:CHEBI:77852; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76688; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90680; Evidence={ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000305|PubMed:11115402}; CATALYTIC ACTIVITY: Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76691, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:75230, ChEBI:CHEBI:83343; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76695, ChEBI:CHEBI:15377, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76699, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:195399, ChEBI:CHEBI:195400; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76700; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76703, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90772, ChEBI:CHEBI:195401; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76704; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76707, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:132087, ChEBI:CHEBI:194369; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76708; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76711, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:144832, ChEBI:CHEBI:195402; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76712; Evidence={ECO:0000305|PubMed:36608588}; CATALYTIC ACTIVITY: Reaction=(17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + 2 glutathione = (17S)-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76715, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:133795, ChEBI:CHEBI:195403; Evidence={ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76716; Evidence={ECO:0000305|PubMed:36608588};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:11115402, PubMed:36608588). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway (PubMed:11115402). {ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:36608588}.
|
Homo sapiens (Human)
|
P07204
|
TRBM_HUMAN
|
MLGVLVLGALALAGLGFPAPAEPQPGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGVGRRRLWIGLQLPPGCGDPKRLGPLRGFQWVTGDNNTSYSRWARLDLNGAPLCGPLCVAVSAAEATVPSEPIWEEQQCEVKADGFLCEFHFPATCRPLAVEPGAAAAAVSITYGTPFAARGADFQALPVGSSAAVAPLGLQLMCTAPPGAVQGHWAREAPGAWDCSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSCTASATQSCNDLCEHFCVPNPDQPGSYSCMCETGYRLAADQHRCEDVDDCILEPSPCPQRCVNTQGGFECHCYPNYDLVDGECVEPVDPCFRANCEYQCQPLNQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQASCECPEGYILDDGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALARHIGTDCDSGKVDGGDSGSGEPPPSPTPGSTLTPPAVGLVHSGLLIGISIASLCLVVALLALLCHLRKKQGAARAKMEYKCAAPSKEVVLQHVRTERTPQRL
| null | null |
blood coagulation [GO:0007596]; blood coagulation, common pathway [GO:0072377]; female pregnancy [GO:0007565]; negative regulation of blood coagulation [GO:0030195]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of platelet activation [GO:0010544]; proteolysis [GO:0006508]; response to cAMP [GO:0051591]; response to lipopolysaccharide [GO:0032496]; response to X-ray [GO:0010165]; zymogen activation [GO:0031638]
|
apicolateral plasma membrane [GO:0016327]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; serine-type endopeptidase complex [GO:1905370]; vacuolar membrane [GO:0005774]
|
calcium ion binding [GO:0005509]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
|
PF12662;PF07645;PF14670;PF00059;PF09064;
|
2.10.25.10;3.10.100.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:8216207}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:8390446}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.
|
Homo sapiens (Human)
|
P07205
|
PGK2_HUMAN
|
MSLSKKLTLDKLDVRGKRVIMRVDFNVPMKKNQITNNQRIKASIPSIKYCLDNGAKAVVLMSHLGRPDGVPMPDKYSLAPVAVELKSLLGKDVLFLKDCVGAEVEKACANPAPGSVILLENLRFHVEEEGKGQDPSGKKIKAEPDKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPHKASGFLMKKELDYFAKALENPVRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAYTFLKVLNNMEIGASLFDEEGAKIVKDIMAKAQKNGVRITFPVDFVTGDKFDENAQVGKATVASGISPGWMGLDCGPESNKNHAQVVAQARLIVWNGPLGVFEWDAFAKGTKALMDEIVKATSKGCITVIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKILPGVEALSNM
|
2.7.2.3
| null |
canonical glycolysis [GO:0061621]; flagellated sperm motility [GO:0030317]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618]
|
PF00162;
|
3.40.50.1260;
|
Phosphoglycerate kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
| null | null |
FUNCTION: Essential for sperm motility and male fertility (PubMed:26677959). Not required for the completion of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:P09041, ECO:0000269|PubMed:26677959}.
|
Homo sapiens (Human)
|
P07207
|
NOTCH_DROME
|
MQSQRSRRRSRAPNTWICFWINKMHAVASLPASLPLLLLTLAFANLPNTVRGTDTALVAASCTSVGCQNGGTCVTQLNGKTYCACDSHYVGDYCEHRNPCNSMRCQNGGTCQVTFRNGRPGISCKCPLGFDESLCEIAVPNACDHVTCLNGGTCQLKTLEEYTCACANGYTGERCETKNLCASSPCRNGATCTALAGSSSFTCSCPPGFTGDTCSYDIEECQSNPCKYGGTCVNTHGSYQCMCPTGYTGKDCDTKYKPCSPSPCQNGGICRSNGLSYECKCPKGFEGKNCEQNYDDCLGHLCQNGGTCIDGISDYTCRCPPNFTGRFCQDDVDECAQRDHPVCQNGATCTNTHGSYSCICVNGWAGLDCSNNTDDCKQAACFYGATCIDGVGSFYCQCTKGKTGLLCHLDDACTSNPCHADAICDTSPINGSYACSCATGYKGVDCSEDIDECDQGSPCEHNGICVNTPGSYRCNCSQGFTGPRCETNINECESHPCQNEGSCLDDPGTFRCVCMPGFTGTQCEIDIDECQSNPCLNDGTCHDKINGFKCSCALGFTGARCQINIDDCQSQPCRNRGICHDSIAGYSCECPPGYTGTSCEININDCDSNPCHRGKCIDDVNSFKCLCDPGYTGYICQKQINECESNPCQFDGHCQDRVGSYYCQCQAGTSGKNCEVNVNECHSNPCNNGATCIDGINSYKCQCVPGFTGQHCEKNVDECISSPCANNGVCIDQVNGYKCECPRGFYDAHCLSDVDECASNPCVNEGRCEDGINEFICHCPPGYTGKRCELDIDECSSNPCQHGGTCYDKLNAFSCQCMPGYTGQKCETNIDDCVTNPCGNGGTCIDKVNGYKCVCKVPFTGRDCESKMDPCASNRCKNEAKCTPSSNFLDFSCTCKLGYTGRYCDEDIDECSLSSPCRNGASCLNVPGSYRCLCTKGYEGRDCAINTDDCASFPCQNGGTCLDGIGDYSCLCVDGFDGKHCETDINECLSQPCQNGATCSQYVNSYTCTCPLGFSGINCQTNDEDCTESSCLNGGSCIDGINGYNCSCLAGYSGANCQYKLNKCDSNPCLNGATCHEQNNEYTCHCPSGFTGKQCSEYVDWCGQSPCENGATCSQMKHQFSCKCSAGWTGKLCDVQTISCQDAADRKGLSLRQLCNNGTCKDYGNSHVCYCSQGYAGSYCQKEIDECQSQPCQNGGTCRDLIGAYECQCRQGFQGQNCELNIDDCAPNPCQNGGTCHDRVMNFSCSCPPGTMGIICEINKDDCKPGACHNNGSCIDRVGGFECVCQPGFVGARCEGDINECLSNPCSNAGTLDCVQLVNNYHCNCRPGHMGRHCEHKVDFCAQSPCQNGGNCNIRQSGHHCICNNGFYGKNCELSGQDCDSNPCRVGNCVVADEGFGYRCECPRGTLGEHCEIDTLDECSPNPCAQGAACEDLLGDYECLCPSKWKGKRCDIYDANYPGWNGGSGSGNDRYAADLEQQRAMCDKRGCTEKQGNGICDSDCNTYACNFDGNDCSLGINPWANCTANECWNKFKNGKCNEECNNAACHYDGHDCERKLKSCDSLFDAYCQKHYGDGFCDYGCNNAECSWDGLDCENKTQSPVLAEGAMSVVMLMNVEAFREIQAQFLRNMSHMLRTTVRLKKDALGHDIIINWKDNVRVPEIEDTDFARKNKILYTQQVHQTGIQIYLEIDNRKCTECFTHAVEAAEFLAATAAKHQLRNDFQIHSVRGIKNPGDEDNGEPPANVKYVITGIILVIIALAFFGMVLSTQRKRAHGVTWFPEGFRAPAAVMSRRRRDPHGQEMRNLNKQVAMQSQGVGQPGAHWSDDESDMPLPKRQRSDPVSGVGLGNNGGYASDHTMVSEYEEADQRVWSQAHLDVVDVRAIMTPPAHQDGGKHDVDARGPCGLTPLMIAAVRGGGLDTGEDIENNEDSTAQVISDLLAQGAELNATMDKTGETSLHLAARFARADAAKRLLDAGADANCQDNTGRTPLHAAVAADAMGVFQILLRNRATNLNARMHDGTTPLILAARLAIEGMVEDLITADADINAADNSGKTALHWAAAVNNTEAVNILLMHHANRDAQDDKDETPLFLAAREGSYEACKALLDNFANREITDHMDRLPRDVASERLHHDIVRLLDEHVPRSPQMLSMTPQAMIGSPPPGQQQPQLITQPTVISAGNGGNNGNGNASGKQSNQTAKQKAAKKAKLIEGSPDNGLDATGSLRRKASSKKTSAASKKAANLNGLNPGQLTGGVSGVPGVPPTNSAAQAAAAAAAAVAAMSHELEGSPVGVGMGGNLPSPYDTSSMYSNAMAAPLANGNPNTGAKQPPSYEDCIKNAQSMQSLQGNGLDMIKLDNYAYSMGSPFQQELLNGQGLGMNGNGQRNGVGPGVLPGGLCGMGGLSGAGNGNSHEQGLSPPYSNQSPPHSVQSSLALSPHAYLGSPSPAKSRPSLPTSPTHIQAMRHATQQKQFGGSNLNSLLGGANGGGVVGGGGGGGGGVGQGPQNSPVSLGIISPTGSDMGIMLAPPQSSKNSAIMQTISPQQQQQQQQQQQQQHQQQQQQQQQQQQQQQQQLGGLEFGSAGLDLNGFCGSPDSFHSGQMNPPSIQSSMSGSSPSTNMLSPSSQHNQQAFYQYLTPSSQHSGGHTPQHLVQTLDSYPTPSPESPGHWSSSSPRSNSDWSEGVQSPAANNLYISGGHQANKGSEAIYI
| null | null |
actin filament organization [GO:0007015]; asymmetric cell division [GO:0008356]; axon guidance [GO:0007411]; border follicle cell migration [GO:0007298]; cell dedifferentiation [GO:0043697]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; chaeta development [GO:0022416]; chaeta morphogenesis [GO:0008407]; compartment boundary maintenance [GO:0060289]; compound eye development [GO:0048749]; compound eye morphogenesis [GO:0001745]; compound eye retinal cell programmed cell death [GO:0046667]; crystal cell differentiation [GO:0042688]; defense response to insect [GO:0002213]; determination of adult lifespan [GO:0008340]; dorsal appendage formation [GO:0046843]; dorsal closure [GO:0007391]; dorsal/ventral axis specification [GO:0009950]; embryonic hemopoiesis [GO:0035162]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; epithelial cell type specification, open tracheal system [GO:0035153]; eye-antennal disc development [GO:0035214]; eye-antennal disc morphogenesis [GO:0007455]; female germ-line stem cell population maintenance [GO:0036099]; follicle cell of egg chamber development [GO:0030707]; follicle cell of egg chamber migration [GO:0007297]; follicle cell of egg chamber stalk formation [GO:0030713]; foregut morphogenesis [GO:0007440]; formation of a compartment boundary [GO:0060288]; germ-line stem cell population maintenance [GO:0030718]; germ-line stem-cell niche homeostasis [GO:0060250]; germarium-derived egg chamber formation [GO:0007293]; glial cell differentiation [GO:0010001]; glial cell fate determination [GO:0007403]; glial cell migration [GO:0008347]; hemocyte proliferation [GO:0035172]; imaginal disc-derived leg joint morphogenesis [GO:0016348]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived leg segmentation [GO:0036011]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; imaginal disc-derived wing morphogenesis [GO:0007476]; imaginal disc-derived wing vein specification [GO:0007474]; intestinal stem cell homeostasis [GO:0036335]; lamellocyte differentiation [GO:0035171]; larval lymph gland hemopoiesis [GO:0035167]; lateral inhibition [GO:0046331]; leg disc morphogenesis [GO:0007478]; long-term memory [GO:0007616]; lymph gland development [GO:0048542]; Malpighian tubule tip cell differentiation [GO:0061382]; mesoderm development [GO:0007498]; morphogenesis of an epithelial fold [GO:0060571]; motor neuron axon guidance [GO:0008045]; muscle cell cellular homeostasis [GO:0046716]; muscle cell fate determination [GO:0007521]; myoblast development [GO:0048627]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; negative regulation of compound eye photoreceptor development [GO:0045316]; negative regulation of gene expression [GO:0010629]; negative regulation of lamellocyte differentiation [GO:0035204]; negative regulation of neurogenesis [GO:0050768]; negative regulation of Notch signaling pathway [GO:0045746]; nervous system process [GO:0050877]; neuroblast development [GO:0014019]; neuroblast fate determination [GO:0007400]; neuroblast fate specification [GO:0014018]; neuroblast proliferation [GO:0007405]; neuron fate determination [GO:0048664]; neuron fate specification [GO:0048665]; neuronal stem cell population maintenance [GO:0097150]; Notch signaling pathway [GO:0007219]; ommatidial rotation [GO:0016318]; oocyte localization involved in germarium-derived egg chamber formation [GO:0030720]; oogenesis [GO:0048477]; peripheral nervous system development [GO:0007422]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of crystal cell differentiation [GO:0042691]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; R1/R6 cell differentiation [GO:0048052]; R3/R4 cell differentiation [GO:0048056]; R7 cell differentiation [GO:0045466]; regulation of cardioblast cell fate specification [GO:0042686]; regulation of cell differentiation [GO:0045595]; regulation of filopodium assembly [GO:0051489]; regulation of glycolytic process [GO:0006110]; regulation of growth [GO:0040008]; regulation of mitotic cell cycle [GO:0007346]; regulation of neuroblast proliferation [GO:1902692]; regulation of neurogenesis [GO:0050767]; regulation of stem cell division [GO:2000035]; response to symbiont [GO:0009608]; retinal cell programmed cell death [GO:0046666]; second mitotic wave involved in compound eye morphogenesis [GO:0016330]; sensory organ development [GO:0007423]; sensory organ precursor cell fate determination [GO:0016360]; stem cell differentiation [GO:0048863]; wing disc dorsal/ventral pattern formation [GO:0048190]; wing disc pattern formation [GO:0035222]
|
adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; CSL-Notch-Mastermind transcription factor complex [GO:1990433]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endosome [GO:0005768]; Golgi lumen [GO:0005796]; late endosome [GO:0005770]; membrane [GO:0016020]; multivesicular body [GO:0005771]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; chromatin binding [GO:0003682]; histone acetyltransferase binding [GO:0035035]; Notch binding [GO:0005112]; transcription coactivator activity [GO:0003713]; transmembrane signaling receptor activity [GO:0004888]; WW domain binding [GO:0050699]
|
PF00023;PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066;
|
3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10;
|
NOTCH family
|
PTM: Upon binding its ligands such as Delta or Serrate, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain. S2 cleavage is probably mediated by Kuz. It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane. S3 cleavage requires Psn.; PTM: O-glycosylated (PubMed:27268051). Three forms of O-glycosylation (O-fucosylation, O-glucosylation and O-GlcNAcylation) are detected (PubMed:27268051). O-fucosylated by O-fut1 and fng in the EGF repeat domain inhibits both Serrate/Ser- and Delta/Dl-binding (PubMed:10935637, PubMed:12909620). O-glucosylation by rumi in the endoplasmic reticulum is necessary for correct folding and signaling (PubMed:18243100). {ECO:0000269|PubMed:10935637, ECO:0000269|PubMed:12909620, ECO:0000269|PubMed:18243100, ECO:0000269|PubMed:27268051}.; PTM: Ubiquitinated by various ubiquitin ligases; which promotes ligand-independent endocytosis and proteasomal degradation (PubMed:15620649, PubMed:22162134). Ubiquitinated by Nedd4 (PubMed:15620649). May also be ubiquitinated by Su(dx) and Cbl (PubMed:29309414). Mono-ubiquitinated, possibly by dx/deltex; this may be involved in the ESCRT-III mediated targeting to multivesicular bodies (PubMed:22162134). {ECO:0000269|PubMed:15620649, ECO:0000269|PubMed:22162134, ECO:0000269|PubMed:29309414}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17329366}; Single-pass type I membrane protein {ECO:0000269|PubMed:17329366}. Endosome {ECO:0000269|PubMed:17329366}. Endosome, multivesicular body {ECO:0000269|PubMed:22162134}. Note=Transported to early endosomes by O-fut1 (PubMed:17329366). Targeting to the endolysosomal pathway is regulated by protein ubiquitination and reliant on the ESCRT-III complex (PubMed:22162134). Colocalizes with dx/deltex on multivesicular bodies (PubMed:22162134). {ECO:0000269|PubMed:22162134}.; SUBCELLULAR LOCATION: [Processed neurogenic locus Notch protein]: Nucleus. Note=Upon activation and S3 cleavage, it is released from the cell membrane and enters into the nucleus in conjunction with Su(H).
| null | null | null | null | null |
FUNCTION: Essential signaling protein which has a major role in many developmental processes (PubMed:3935325). Functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination (PubMed:10935637, PubMed:12909620, PubMed:15620650, PubMed:18243100). Upon ligand activation, and releasing from the cell membrane, the Notch intracellular domain (NICD) forms a transcriptional activator complex with Su(H) (Suppressor of hairless) and activates genes of the E(spl) complex (PubMed:7671825). Regulates oogenesis, the differentiation of the ectoderm and the development of the central and peripheral nervous system, eye, wing disk, muscles and segmental appendages such as antennae and legs, through lateral inhibition or induction (PubMed:11719214, PubMed:12369105, PubMed:3935325). Regulates neuroblast self-renewal, identity and proliferation through the regulation of bHLH-O proteins; in larval brains, involved in the maintenance of type II neuroblast self-renewal and identity by suppressing erm expression together with pnt; might also regulate dpn expression through the activation of the transcriptional regulator Su(H) (PubMed:18342578, PubMed:20152183, PubMed:21262215, PubMed:23056424, PubMed:27151950, PubMed:28899667). Targeted for ESCRT-mediated endosomal sequestration and lysosomal degradation by various E3 ubiquitin ligases to regulate the Notch signaling pathway (PubMed:17084358, PubMed:22162134, PubMed:33349255). Can undergo ligand-dependent and non-canonical ligand-independent activation (PubMed:22162134). Ligand-independent activation is dependent on endosome acidification and probably occurs in late endosomes or lysosome (PubMed:23178945). Ectopic ligand-independent activation occurs when disruption of the endolysosomal pathway, particularly of the ESCRT-III complex, prevents sequestration of the receptor in intraluminal vesicles of multivesicular bodies (PubMed:17084357, PubMed:17084358, PubMed:17088062, PubMed:23178945). {ECO:0000269|PubMed:10935637, ECO:0000269|PubMed:11719214, ECO:0000269|PubMed:12369105, ECO:0000269|PubMed:12909620, ECO:0000269|PubMed:15620650, ECO:0000269|PubMed:17084357, ECO:0000269|PubMed:17084358, ECO:0000269|PubMed:17088062, ECO:0000269|PubMed:18243100, ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:20152183, ECO:0000269|PubMed:21262215, ECO:0000269|PubMed:22162134, ECO:0000269|PubMed:23056424, ECO:0000269|PubMed:23178945, ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:28899667, ECO:0000269|PubMed:33349255, ECO:0000269|PubMed:7671825, ECO:0000303|PubMed:3935325}.
|
Drosophila melanogaster (Fruit fly)
|
P07210
|
POLG_HRV8A
|
MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPTVEACGYSDRLIQITRGDSTITSQDTANAVVAYGVWPSYLTPDDATAIDKPTQPDTSSNRFYTLDSRSWTSASSGWWWKLPDALKNMGIFGENMFYHFLGRSGYTIHVQCNSSKFHQGLLIVAAIPEHQLASATSGNVSVGYNHTHPGEQGREVVPSRTSSDNKRPSDDSWLNFDGTLLGNLPIYPHQYINLRTNNSATLILPYVNAVPMDSMLRHNNWSLVIIPICPLQVQPGGTQSIPITVSISPMFSEFSGPRSKVVFSTTQGLPVMLTPGSGQFLTTDDTQSPSAFPYFHPTKEIFIPGQVRNLIEMCQVDTLIPVNNTQENVRSVNMYTVDLRTQVDLAKEVFSIPVDIASQPLATTLIGELASYYTHWTGSLRFSFMFCGSASSTLKLLIAYTPPGVGKPKSRREAMLGTHLVWDVGLQSTASLVVPWVSASHFRFTTPDTYSSAGYITCWYQTNFVVPDSTPDNAKMVCMVSACKDFCLRLARDTNLHTQEGVLTQNPVENYIDSVLNEVLVVPNIQPSTSVSSHAAPALDAAETGHTSSVQPEDMIETRYVITDQTRDETSIESFLGRSGCIAMIEFNTSSDKTEHDKIGKGFKTWKVSLQEMAQIRRKYELFTYTRFDSEITIVTAAAAQGNDSGHIVLQFMYVPPGAPVPEKRDDYTWQSGTNASVFWQEGQPYPRFTIPFMSIASAYYMFYDGYDGDSAASKYGSVVTNDMGTICVRIVTSNQKHDSNIVCRIYHKAKHIKAWCPRPPRAVAYQHTHSTNYIPSNGEATTQIKTRPDVFTVTNVGPSSMFVHVGNLIYRNLHLFNSDLDDSILVSYSSDLIIYRTNTEGNDVIPNCDCTECTYYCHHKDRYFPIRVTAHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKLLCKHGVIGMITAGGEGHVAFIDLRKFQCAEEQGLSDYVEHLGQVFGVGFVDSIKQQVNFINPTSKIGSKVIKWLLRIVSAMIIMVRNSSDPQTVIATLTLLGCSGSPWRFLKEKLCAWLQLSYVHKQSDSWLKKFTEACNAARGLEWIGQKISKFIDWIKSMLPQAQLKIDYLTKLKQLNLLEKQIETIRLAPASVQEKIFIEINTLHDLSLKFLPLYASEARRIKNLYIKCSNVIKGGKRNEPVAVLIHGSPGTGKSLATSVLARMLTVETDIYSLPPDPKYFDGYDQQSVVIMDDIMQNPSGEDMTLFCQMVSSVPFIPPMADLPDKGKPFTSKFVLASTNHTLLTPPTVSSLPAMARRFYFDLDIQVKKEYLLDGKLDIAKSFRPCDVNIKIGNAKCCPFICGKAVEFKDRNSCTTLSLSQLYSHIKEEDRRRSSAAQAMEAIFQGIDLQSPPPPAIADLLRSVKTPEIIKYCQDNNWIVPAECSIERDLGIANMTIGIIANVVSIVGVIYIIYKLFCTLQGPYSGEPKPKSRAPERRVVTQGPEEEFGRSLLKHNCCVVTTDKGKFTGLGIYDQVMVLPTHSDPGSEILVDGVKVKVSDSYDLHNHEGVKLEITVVKLIRNEKFKDIRKYLPSREDDYPACNLALLANQDEPTIISVGDAVSYGNILLSGTNTARMIKYHYPTKAGYCGGVLYKVGSILGIHVGGNGRDGFSAMLLKSYFGETQGLITKELPVSVKNLPSVHVSSKTRLQPSVFHDVFPGTKEPAVLSSNDPRLETDFDSALFSKYKGNPACQVTPHMKIAVAHYAAQLSTLDINPQPLSLEESVFGIEGLEALDLNTSAGFPYVSLGIKKKDLIDKKTKDITKLRKAIDEYGIDLPMVTFLKDELRKKEKIKDGKTRVIEANSVNDTVLFRSVFGNLFSAFHKNPGIVTGSAVGCDPEVFWSTIPLMLDGECLMAFDYSNYDGSLHPVWFKCLSMLLEDIGFSSQLINQICNSKHIYKSKYYEVEGGMPSGCAGTSIFNTIINNIIIRTLVLDAYKNIDLDKLKILAYGDDVIFSYNFKLDMAVLAKEGEKYGLTITPADKSDVFQELTYKNVTFLKRGFRADERHSFLIHPTFPVAEIHDSIRWTKNPSCMQEHVLSLCHLMWHNGRHAYQEFIKGIRSVSAGRALYIPAYEVLEHEWYEKF
|
2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15
|
COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313};
|
DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; 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]
|
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
|
PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910;
|
1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10;
|
Picornaviruses polyprotein family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
|
SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.; SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
|
CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [Protease 2A]: Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
| null | null | null | null |
FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor 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 (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03301, ECO:0000250|UniProtKB:P04936}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P04936}.; 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}.
|
Human rhinovirus A serotype 89 (strain 41467-Gallo) (HRV-89)
|
P07213
|
TOM70_YEAST
|
MKSFITRNKTAILATVAATGTAIGAYYYYNQLQQQQQRGKKNTINKDEKKDTKDSQKETEGAKKSTAPSNPPIYPVSSNGEPDFSNKANFTAEEKDKYALALKDKGNQFFRNKKYDDAIKYYNWALELKEDPVFYSNLSACYVSVGDLKKVVEMSTKALELKPDYSKVLLRRASANEGLGKFADAMFDLSVLSLNGDFNDASIEPMLERNLNKQAMSKLKEKFGDIDTATATPTELSTQPAKERKDKQENLPSVTSMASFFGIFKPELTFANYDESNEADKELMNGLSNLYKRSPESYDKADESFTKAARLFEEQLDKNNEDEKLKEKLAISLEHTGIFKFLKNDPLGAHEDIKKAIELFPRVNSYIYMALIMADRNDSTEYYNYFDKALKLDSNNSSVYYHRGQMNFILQNYDQAGKDFDKAKELDPENIFPYIQLACLAYRENKFDDCETLFSEAKRKFPEAPEVPNFFAEILTDKNDFDKALKQYDLAIELENKLDGIYVGIAPLVGKATLLTRNPTVENFIEATNLLEKASKLDPRSEQAKIGLAQMKLQQEDIDEAITLFEESADLARTMEEKLQAITFAEAAKVQQRIRSDPVLAKKIQETLAKLREQGLM
| null | null |
protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial inner membrane [GO:0045039]; protein insertion into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626]
|
mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]
|
mitochondrion targeting sequence binding [GO:0030943]; protein-transporting ATPase activity [GO:0015450]
|
PF00515;PF13432;PF14559;PF13181;
|
1.25.40.10;
|
Tom70 family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11502169}; Single-pass membrane protein {ECO:0000269|PubMed:11502169}.
| null | null | null | null | null |
FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore. {ECO:0000269|PubMed:11054285}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07214
|
SPRC_MOUSE
|
MRAWIFFLLCLAGRALAAPQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI
| null | null |
bone development [GO:0060348]; cellular response to growth factor stimulus [GO:0071363]; lung development [GO:0030324]; pigmentation [GO:0043473]; regulation of cell population proliferation [GO:0042127]; regulation of synapse organization [GO:0050807]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; synapse [GO:0045202]; vesicle [GO:0031982]
|
calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]
|
PF09289;PF00050;PF10591;
|
3.30.60.30;1.10.238.10;
|
SPARC family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:3427055}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:3427055}. Note=In or around the basement membrane.
| null | null | null | null | null |
FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
|
Mus musculus (Mouse)
|
P07221
|
CASQ1_RABIT
|
MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD
| null | null |
positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of store-operated calcium channel activity [GO:1901341]; protein polymerization [GO:0051258]; regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014809]; regulation of store-operated calcium entry [GO:2001256]; sarcomere organization [GO:0045214]
|
mitochondrial matrix [GO:0005759]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018]
|
calcium ion binding [GO:0005509]; ion binding [GO:0043167]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803]
|
PF01216;
|
3.40.30.10;
|
Calsequestrin family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:22170046}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141, ECO:0000269|PubMed:8227022}. Mitochondrion matrix {ECO:0000250|UniProtKB:O09165}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000269|PubMed:15731387}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells (PubMed:15731387). Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:15731387}.
| null | null | null | null | null |
FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141, ECO:0000269|PubMed:19398037, ECO:0000269|PubMed:22170046, ECO:0000269|PubMed:3427087, ECO:0000269|PubMed:8227022, ECO:0000303|PubMed:22337878}.
|
Oryctolagus cuniculus (Rabbit)
|
P07222
|
NPM_XENLA
|
MEDSMDMDNIAPLRPQNFLFGCELKADKKEYSFKVEDDENEHQLSLRTVSLGASAKDELHVVEAEGINYEGKTIKIALASLKPSVQPTVSLGGFEITPPVILRLKSGSGPVYVSGQHLVALEDLESSDDEDEEHEPSPKNAKRIAPDSASKVPRKKTRLEEEEEDSDEDDDDDEDDDDEDDDEEEEETPVKKTDSTKSKAAQKLNHNGKASALSTTQKTPKTPEQKGKQDTKPQTPKTPKTPLSSEEIKAKMQTYLEKGNVLPKVEVKFANYVKNCFRTENQKVIEDLWKWRQSLKDGK
| null | null |
chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of centrosome duplication [GO:0010824]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of endoribonuclease activity [GO:0060699]; ribosomal large subunit biogenesis [GO:0042273]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal small subunit export from nucleus [GO:0000056]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:1990904]
|
chromatin binding [GO:0003682]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF16276;PF03066;
|
1.10.10.2100;2.60.120.340;
|
Nucleoplasmin family
|
PTM: Phosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a chaperonin for the core histones H3, H2B and H4. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. It may function in the assembly and/or transport of ribosome. May stimulate endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA. May inhibit endonuclease activity on AP single-stranded RNA (By similarity). {ECO:0000250}.
|
Xenopus laevis (African clawed frog)
|
P07224
|
PROS_BOVIN
|
MRVLGGRTGTLLACLALVLPVLEANFLSRQHASQVLIRRRRANTLLEETKKGNLERECIEELCNKEEAREIFENNPETEYFYPKYLGCLGSFRAGLFTAARLSTNAYPDLRSCVNAISDQCNPLPCNEDGFMTCKDGQATFTCICKSGWQGEKCESDINECKDPVNINGGCSQICENTPGSYHCSCKNGFVMLSNKKDCKDVDECVLKPSICGTAVCKNIPGDFECECAEGYKYNPVSKSCDDVDECAENLCAQLCVNYPGGYSCYCDGKKGFKLAQDQKSCEAVPVCLPLDLDKNYELLYLAEQFVGVVLYLKFRLPETTRFSAEFDFRTYDSEGVILYAESSDHSAWFLIALREGKIEIQFKNEKTTKMTTGGKVINDGLWHMVSVEELEQSISVKIAKEAVMNINKPGSLFKPTNGFLETKVYFAGVPRKMENALIRPINPRLDGCIRGWNLMNQGTSGVKEIIQEKQNKHCLVNVEKGSYYPGTGVAQFSINYKNESNPEAWQINVSLNIRPSAGTGVMLALVSDNTVPFALSLVDSATEKLQDILVSVESMVIGRIEAISLCSDQQTFLEIRVNRNNLELSTQLRKDSFHSEDFQRQFAILDEAMKGTVVTYLGGLPDVPFSATPVNAFYQGCMEVNINGVQVDLDEAISKHNDIRAHSCPSVWQKTKHT
| null | null |
blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]
|
PF00008;PF07645;PF14670;PF00594;PF00054;PF02210;
|
2.60.120.200;4.10.740.10;2.10.25.10;
| null |
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2937785}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
|
Bos taurus (Bovine)
|
P07225
|
PROS_HUMAN
|
MRVLGGRCGALLACLLLVLPVSEANFLSKQQASQVLVRKRRANSLLEETKQGNLERECIEELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQCSPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPGSYHCSCKNGFVMLSNKKDCKDVDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKSCEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKSCEVVSVCLPLNLDTKYELLYLAEQFAGVVLYLKFRLPEISRFSAEFDFRTYDSEGVILYAESIDHSAWLLIALRGGKIEVQLKNEHTSKITTGGDVINNGLWNMVSVEELEHSISIKIAKEAVMDINKPGPLFKPENGLLETKVYFAGFPRKVESELIKPINPRLDGCIRSWNLMKQGASGIKEIIQEKQNKHCLVTVEKGSYYPGSGIAQFHIDYNNVSSAEGWHVNVTLNIRPSTGTGVMLALVSGNNTVPFAVSLVDSTSEKSQDILLSVENTVIYRIQALSLCSDQQSHLEFRVNRNNLELSTPLKIETISHEDLQRQLAVLDKAMKAKVATYLGGLPDVPFSATPVNAFYNGCMEVNINGVQLDLDEAISKHNDIRAHSCPSVWKKTKNS
| null | null |
blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]
|
blood microparticle [GO:0072562]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]
|
calcium ion binding [GO:0005509]; endopeptidase inhibitor activity [GO:0004866]
|
PF07645;PF14670;PF00594;PF12661;PF00054;PF02210;
|
2.60.120.200;4.10.740.10;2.10.25.10;
| null |
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
|
Homo sapiens (Human)
|
P07228
|
ITB1_CHICK
|
MAETNLTLLTWAGILCCLIWSGSAQQGGSDCIKANAKSCGECIQAGPNCGWCKKTDFLQEGEPTSARCDDLAALKSKGCPEQDIENPRGSKRVLEDREVTNRKIGAAEKLKPEAITQIQPQKLVLQLRVGEPQTFSLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTALMREMEKITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTGDQNCTSPFSYKNVLSLTSEGNKFNELVGKQHISGNLDSPEGGFDAIMQVAVCGDQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGKCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQAVYKELKNLIPKSAVGTLSSNSSNVIQLIIDAYNSLSSEVILENSKLPKEVTISYKSYCKNGVNDTQEDGRKCSNISIGDEVRFEINVTANECPKKGQNETIKIKPLGFTEEVEIHLQFICDCLCQSEGEPNSPACHDGNGTFECGACRCNEGRIGRLCECSTDEVNSEDMDAYCRRENSTEICSNNGECICGQCVCKKRENTNEVYSGKYCECDNFNCDRSNGLICGGNGICKCRVCECFPNFTGSACDCSLDTTPCMAGNGQICNGRGTCECGTCNCTDPKFQGPTCEMCQTCLGVCAEHKDCVQCRAFEKGEKKETCSQECMHFNMTRVESRGKLPQPVHPDPLSHCKEKDVGDCWFYFTYSVNSNGEASVHVVETPECPSGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK
| null | null |
cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]
|
cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; synapse [GO:0045202]
|
C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]
|
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
|
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
|
Integrin beta chain family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05556}.
| null | null | null | null | null |
FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-1 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (PubMed:34427057). {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P09055}.
|
Gallus gallus (Chicken)
|
P07231
|
CKG_CONGE
|
MHLYTYLYLLVPLVTFHLILGTGTLDDGGALTERRSADATALKAEPVLLQKSAARSTDDNGKDRLTQMKRILKQRGNKARGEEELQENQELIREKSNGKR
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10406223}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10406223, ECO:0000269|PubMed:26048991}; Note=Divalent cations stabilize the toxin the in alpha-helix conformation. {ECO:0000269|PubMed:10406223, ECO:0000269|PubMed:26048991};
| null |
extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792]
|
ion channel regulator activity [GO:0099106]; metal ion binding [GO:0046872]; toxin activity [GO:0090729]
| null | null |
Conotoxin B superfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6501296}.
| null | null | null | null | null |
FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice. {ECO:0000269|PubMed:2165278}.
|
Conus geographus (Geography cone) (Nubecula geographus)
|
P07237
|
PDIA1_HUMAN
|
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
|
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]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-23-mediated signaling pathway [GO:0038155]; peptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]; 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]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; 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-disulfide reductase activity [GO:0015035]; RNA binding [GO:0003723]; thiol oxidase activity [GO:0016972]
|
PF00085;PF13848;
|
3.40.30.10;
|
Protein disulfide isomerase family
|
PTM: Phosphorylation of Ser-357 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone (PubMed:32149426). It also promotes interaction with ERN1 (PubMed:32149426). {ECO:0000269|PubMed:32149426}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:32149426}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:23475612}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:21670307}; 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 (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces (PubMed:11181151). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:10636893). Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:11181151, ECO:0000269|PubMed:23475612, ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000269|PubMed:32149426};
| 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 (PubMed:32149426). 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 (PubMed:21670307). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:32149426}.
|
Homo sapiens (Human)
|
P07239
|
DUSP_VACCW
|
MDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHIPLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHCAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVENPSFKRQIIEKYVIDKN
|
3.1.3.-; 3.1.3.48
| null |
dephosphorylation [GO:0016311]; negative regulation of MAPK cascade [GO:0043409]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
cytoplasm [GO:0005737]; host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
|
MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; phosphatase activity [GO:0016791]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine/threonine phosphatase activity [GO:0008330]
|
PF00782;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:21362620}. Host cytoplasm {ECO:0000269|PubMed:21362620}. Note=Approximately 200 molecules of OPG106 are packaged within the virion and are essential for the viability of the virus.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:1848923}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87 uM for 3-O-methylfluorescein phosphate {ECO:0000269|PubMed:21362620};
| null | null | null |
FUNCTION: Serine/tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the OPG144 protein. {ECO:0000269|PubMed:10438817, ECO:0000269|PubMed:11238845, ECO:0000269|PubMed:1848923, ECO:0000269|PubMed:18593332, ECO:0000269|PubMed:21362620}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07242
|
PG110_VACCW
|
MAWSITNKADTSSFTKMAEIRAHLKNSAENKDKNEDIFPEDVIIPSTKPKTKRATTPRKPAATKRSTKKEEVEEEVVIEEYHQTTEKNSPSPGVSDIVESVAAVELDDSDGDDEPMVQVEAGKVNHSARSDLSDLKVATDNIVKDLKKIITRISAVSTVLEDVQAAGISRQFTSMTKAITTLSDLVTEGKSKVVRKKVKTCKK
| null | null |
viral DNA genome replication [GO:0039693]; viral transcription [GO:0019083]
|
host cell cytoplasm [GO:0030430]; viral envelope [GO:0019031]
|
translation elongation factor activity [GO:0003746]
|
PF03286;
| null |
Orthopoxvirus OPG110 family
|
PTM: Phosphorylated at multiple sites. Phosphorylation is necessary for cleavage activity. Phosphorylated by the viral B1R and F10 kinases (Probable). {ECO:0000305|PubMed:11001589, ECO:0000305|PubMed:18089571}.
|
SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000269|PubMed:25855734}. Note=Early during viral infection, diffusely localizes within the cytoplasm. Following DNA replication, localizes specifically to virus factories. {ECO:0000269|PubMed:25855734}.
| null | null | null | null | null |
FUNCTION: Involved in the co-transcriptional or post-transcriptional endoribonucleolytic cleavage that generates sequence-homogeneous 3' ends during late transcription. Involved in postreplicative transcription elongation on intermediate and late genes. Also involved in DNA replication and in multiple steps of virion morphogenesis (PubMed:25855734). Required both for inclusion of virosoplasm into crescents as well as for maturation of immature virions (IV) into mature virions (MV). {ECO:0000269|PubMed:17376501, ECO:0000269|PubMed:18089571, ECO:0000269|PubMed:20206959, ECO:0000269|PubMed:25855734}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07244
|
PUR2_YEAST
|
MLNILVLGNGAREHVLVTKLAQSPTVGKIYVAPGNGGTATMDPSRVINWDITPDVANFARLQSMAVEHKINLVVPGPELPLVNGITSVFHSVGIPVFGPSVKAAQLEASKAFSKRFMSKHNIPTASYDVFTNPEEAISFLQAHTDKAFVIKADGIAAGKGVIIPSSIDESVQAIKDIMVTKQFGEEAGKQVVIEQFLEGDEISLLTIVDGYSHFNLPVAQDHKRIFDGDKGLNTGGMGAYAPAPVATPSLLKTIDSQIVKPTIDGMRRDGMPFVGVLFTGMILVKDSKTNQLVPEVLEYNVRFGDPETQAVLSLLDDQTDLAQVFLAAAEHRLDSVNIGIDDTRSAVTVVVAAGGYPESYAKGDKITLDTDKLPPHTQIFQAGTKYDSATDSLLTNGGRVLSVTSTAQDLRTAVDTVYEAVKCVHFQNSYYRKDIAYRAFQNSESSKVAITYADSGVSVDNGNNLVQTIKEMVRSTRRPGADSDIGGFGGLFDLAQAGFRQNEDTLLVGATDGVGTKLIIAQETGIHNTVGIDLVAMNVNDLVVQGAEPLFFLDYFATGALDIQVASDFVSGVANGCIQSGCALVGGETSEMPGMYPPGHYDTNGTAVGAVLRQDILPKINEMAAGDVLLGLASSGVHSNGFSLVRKIIQHVALPWDAPCPWDESKTLGEGILEPTKIYVKQLLPSIRQRLLLGLAHITGGGLVENIPRAIPDHLQARVDMSTWEVPRVFKWFGQAGNVPHDDILRTFNMGVGMVLIVKRENVKAVCDSLTEEGEIIWELGSLQERPKDAPGCVIENGTKLY
|
6.3.3.1; 6.3.4.13
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305};
|
'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641]
|
PF00586;PF02769;PF01071;PF02843;PF02844;
|
3.40.50.20;3.30.1490.20;3.30.470.20;3.90.600.10;3.90.650.10;3.30.1330.10;
|
GARS family; AIR synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000250|UniProtKB:P20772}; CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000250|UniProtKB:P20772};
| null |
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
| null | null |
FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities. {ECO:0000250|UniProtKB:P20772}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07245
|
C1TC_YEAST
|
MAGQVLDGKACAQQFRSNIANEIKSIQGHVPGFAPNLAIIQVGNRPDSATYVRMKRKAAEEAGIVANFIHLDESATEFEVLRYVDQLNEDPHTHGIIVQLPLPAHLDEDRITSRVLAEKDVDGFGPTNIGELNKKNGHPFFLPCTPKGIIELLHKANVTIEGSRSVVIGRSDIVGSPVAELLKSLNSTVTITHSKTRDIASYLHDADIVVVAIGQPEFVKGEWFKPRDGTSSDKKTVVIDVGTNYVADPSKKSGFKCVGDVEFNEAIKYVHLITPVPGGVGPMTVAMLMQNTLIAAKRQMEESSKPLQIPPLPLKLLTPVPSDIDISRAQQPKLINQLAQELGIYSHELELYGHYKAKISPKVIERLQTRQNGKYILVSGITPTPLGEGKSTTTMGLVQALTAHLGKPAIANVRQPSLGPTLGVKGGAAGGGYSQVIPMDEFNLHLTGDIHAIGAANNLLAAAIDTRMFHETTQKNDATFYNRLVPRKNGKRKFTPSMQRRLNRLGIQKTNPDDLTPEEINKFARLNIDPDTITIKRVVDINDRMLRQITIGQAPTEKNHTRVTGFDITVASELMAILALSKDLRDMKERIGRVVVAADVNRSPVTVEDVGCTGALTALLRDAIKPNLMQTLEGTPVLVHAGPFANISIGASSVIADRVALKLVGTEPEAKTEAGYVVTEAGFDFTMGGERFFNIKCRSSGLTPNAVVLVATVRALKSHGGAPDVKPGQPLPSAYTEENIEFVEKGAANMCKQIANIKQFGVPVVVAINKFETDTEGEIAAIRKAALEAGAFEAVTSNHWAEGGKGAIDLAKAVIEASNQPVDFHFLYDVNSSVEDKLTTIVQKMYGGAAIDILPEAQRKIDMYKEQGFGNLPICIAKTQYSLSHDATLKGVPTGFTFPIRDVRLSNGAGYLYALAAEIQTIPGLATYAGYMAVEVDDDGEIDGLF
|
1.5.1.5; 3.5.4.9; 6.3.4.3
| null |
folic acid-containing compound metabolic process [GO:0006760]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]
|
PF01268;PF00763;PF02882;
|
3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300;
|
Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22813; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22814; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000269|PubMed:3514599, ECO:0000305|PubMed:8464869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23701; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23702; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; EC=6.3.4.3; Evidence={ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20222; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20223; Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
| null |
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
| null | null |
FUNCTION: Cytoplasmic isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-methylenetetrahydrofolate dehydrogenase. Involved in the generation of one-carbon intermediates in the biosynthesis of the purine bases. {ECO:0000269|PubMed:329838, ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07246
|
ADH3_YEAST
|
MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLMEKGKILGRYVVDTSK
|
1.1.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00330}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00330};
|
amino acid catabolic process to alcohol via Ehrlich pathway [GO:0000947]; NADH oxidation [GO:0006116]
|
cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
alcohol dehydrogenase (NAD+) activity [GO:0004022]; butanol dehydrogenase activity [GO:1990362]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:1101965, ECO:0000269|PubMed:2188098, ECO:0000269|PubMed:2943982}. Mitochondrion inner membrane {ECO:0000269|PubMed:2937632}.
|
CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:12702265}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:12702265}; CATALYTIC ACTIVITY: Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH; Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292; Evidence={ECO:0000269|PubMed:3546317}; CATALYTIC ACTIVITY: Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH; Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743, ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33200; Evidence={ECO:0000269|PubMed:3546317}; CATALYTIC ACTIVITY: Reaction=hexan-1-ol + NAD(+) = H(+) + hexanal + NADH; Xref=Rhea:RHEA:60972, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60973; Evidence={ECO:0000269|PubMed:3546317};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 uM for NAD(+) {ECO:0000269|PubMed:3546317}; KM=12 mM for ethanol {ECO:0000269|PubMed:3546317}; KM=0.44 mM for acetaldehyde {ECO:0000269|PubMed:3546317}; KM=70 uM for NADH {ECO:0000269|PubMed:3546317}; KM=11 mM for propanol {ECO:0000269|PubMed:3546317}; KM=7.7 mM for butanol {ECO:0000269|PubMed:3546317}; KM=5.2 mM for pentanol {ECO:0000269|PubMed:3546317}; KM=1.9 mM for hexanol {ECO:0000269|PubMed:3546317};
| null | null | null |
FUNCTION: Mitochondrial isozyme that reduces acetaldehyde to ethanol during the fermentation of glucose (Probable) (PubMed:22094012). Involved in the shuttling of mitochondrial reducing equivalents to the cytosol, where the redox balance is restored by NADH dehydrogenases on the external side of the mitochondrial inner membrane (PubMed:10940011). Shows a high affinity for alcohols with a double bond conjugated to the alcohol group (PubMed:1101965). {ECO:0000269|PubMed:10940011, ECO:0000269|PubMed:1101965, ECO:0000269|PubMed:22094012, ECO:0000305|PubMed:12702265}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07247
|
KRUP_DROME
|
MSISMLQDAQTRTLAAALAGIKQEDVHLDRSMSLSPPMSANTSATSAAAIYPAMGLQQAAAASAFGMLSPTQLLAANRQAAAFMAQLPMSTLANTLFPHNPAALFGAWAAQQSLPPQGTHLHSPPASPHSPLSTPLGSGKHPLNSPNSTPQHHEPAKKARKLSVKKEFQTEISMSVNDMYHTSGGPISPPSSGSSPNSTHDGAGGNAGCVGVSKDPSRDKSFTCKICSRSFGYKHVLQNHERTHTGEKPFECPECHKRFTRDHHLKTHMRLHTGEKPYHCSHCDRQFVQVANLRRHLRVHTGERPYTCEICDGKFSDSNQLKSHMLVHNGEKPFECERCHMKFRRRHHLMNHKCGIQSPPTPALSPAMSGDYPVAISAIAIEASTNRFAAMCATYGGSNESVDMEKATPEDDGPLDLSEDGASSVDGHCSNIARRKAQDIRRVFRLPPPQIPHVPSDMPEQTEPEDLSMHSPRSIGSHEQTDDIDLYDLDDAPASYMGHQQH
| null | null |
axon guidance [GO:0007411]; compound eye development [GO:0048749]; heterochromatin formation [GO:0031507]; Malpighian tubule bud morphogenesis [GO:0061332]; muscle organ development [GO:0007517]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast fate determination [GO:0007400]; regulation of development, heterochronic [GO:0040034]; regulation of hemocyte proliferation [GO:0035206]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357]; trunk segmentation [GO:0035290]; zygotic determination of anterior/posterior axis, embryo [GO:0007354]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3112773}. Note=Chromatin associated.
| null | null | null | null | null |
FUNCTION: Krueppel is a gap class segmentation protein. It is involved in the segmentation of the embryo and in the differentiation of the Malpighian tubules.
|
Drosophila melanogaster (Fruit fly)
|
P07248
|
ADR1_YEAST
|
MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGDRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS
| null | null |
chromatin organization [GO:0006325]; peroxisome organization [GO:0007031]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by oleic acid [GO:0061429]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; nucleic acid binding [GO:0003676]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; TFIIB-class transcription factor binding [GO:0001093]; TFIID-class transcription factor complex binding [GO:0001094]; transcription coactivator activity [GO:0003713]
|
PF00096;
|
3.30.160.60;
| null |
PTM: Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression. {ECO:0000269|PubMed:1549108}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07249
|
ARGR1_YEAST
|
MTSNSDGSSTSPVEKPITGDVETNEPTKPIRRLSTPSPEQDQEGDFDEEDDDDKFSVSTSTPTPTITKTKDSSDTSTVTRRKQPIRYIENKTRRHVTFSKRRHGIMKKAYELSVLTGANILLLILANSGLVYTFTTPKLEPVVREDEGKSLIRACINASDTPDATDTSPAQEQSPAN
| null | null |
arginine metabolic process [GO:0006525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of arginine biosynthetic process [GO:1900079]; regulation of arginine catabolic process [GO:1900081]; regulation of arginine metabolic process [GO:0000821]
|
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; serum response element binding [GO:0010736]
|
PF00319;
|
3.40.1810.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3311884}.
| null | null | null | null | null |
FUNCTION: With ARG81, ARG82 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine. {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:2274024, ECO:0000269|PubMed:3298999}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07250
|
IPMK_YEAST
|
MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSSMSLIDFAHSEITPGKGYDENVIEGVETLLDIFMKF
|
2.7.1.127; 2.7.1.151
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17050532};
|
arginine metabolic process [GO:0006525]; inositol phosphate biosynthetic process [GO:0032958]; macroautophagy [GO:0016236]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein stabilization [GO:0050821]; regulation of arginine metabolic process [GO:0000821]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; ATP binding [GO:0005524]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol tetrakisphosphate 3-kinase activity [GO:0000824]; inositol tetrakisphosphate 6-kinase activity [GO:0000825]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827]; inositol-1,4,5-trisphosphate 3-kinase activity [GO:0008440]; inositol-1,4,5-trisphosphate 6-kinase activity [GO:0000823]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]
|
PF03770;
|
3.30.470.160;
|
Inositol phosphokinase (IPK) family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:3311884}.
|
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151; Evidence={ECO:0000269|PubMed:10574768}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:17717, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331, ECO:0000269|PubMed:7945194}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17718; Evidence={ECO:0000305|PubMed:10683435, ECO:0000305|PubMed:10720331, ECO:0000305|PubMed:7945194}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127; Evidence={ECO:0000269|PubMed:10683435}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021; Evidence={ECO:0000305|PubMed:10683435}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11856, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11857; Evidence={ECO:0000305|PubMed:10683435, ECO:0000305|PubMed:10720331}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16123124}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; Evidence={ECO:0000269|PubMed:16123124};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.3 uM for 1D-myo-inositol 1,4,5-trisphosphate {ECO:0000269|PubMed:11311242}; KM=7.1 uM for 1D-myo-inositol 1,4,5-trisphosphate {ECO:0000269|PubMed:7945194}; KM=62 uM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:11311242}; KM=30 uM for phosphatidylinositol 4,5-bisphosphate {ECO:0000269|PubMed:11311242}; KM=2.1 mM for ATP {ECO:0000269|PubMed:7945194}; Vmax=6272 nmol/min/mg enzyme for 1D-myo-inositol 1,4,5-trisphosphate {ECO:0000269|PubMed:11311242}; Vmax=4.9 nmol/min/mg enzyme for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:11311242};
| null | null | null |
FUNCTION: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:10574768, PubMed:10683435, PubMed:11311242). Its predominant in vivo catalytic function is to convert Ins(1,4,5)P3 to Ins(1,4,5,6)P4 to Ins(1,3,4,5,6)P5 via 6- and 3-kinase activities (PubMed:15944147). It can also use Ins(1,3,4,5,6)P5 as a substrate and act as a diphosphoinositol polyphosphate synthase to generate two different isomers of PP-InsP4 (PubMed:11311242). Has also a role in transcription regulation. Forms a complex with ARG80, ARG81 and MCM1 (ArgR-MCM1), which coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruits ARG80 and MCM21 to stabilize them (PubMed:10632874, PubMed:3298999, PubMed:8043104). Neither the kinase activity nor inositol phosphates are required for the formation of ArgR-MCM1 transcriptional complexes on DNA promoter elements and the control of arginine metabolism (PubMed:10720331, PubMed:11119723, PubMed:12828642, PubMed:22992733). In contrast, only the catalytic activity is required for PHO gene repression by phosphate and for NCR gene activation in response to nitrogen availability, indicating a role for inositol pyrophosphates in these controls (PubMed:12828642). Inositol polyphosphates may be involved in the regulation of chromatin remodeling of transcription (PubMed:12434012). Regulates nuclear mRNA export via inositol phosphate metabolism (PubMed:10390371, PubMed:10683435). Also has lipid kinase activity, transforming the lipid inositol phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) in the nucleus (PubMed:16123124). Its kinase activity is necessary for the propagation of most [PSI+] prion variants (PubMed:28923943). {ECO:0000269|PubMed:10390371, ECO:0000269|PubMed:10574768, ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331, ECO:0000269|PubMed:11119723, ECO:0000269|PubMed:11311242, ECO:0000269|PubMed:12434012, ECO:0000269|PubMed:12828642, ECO:0000269|PubMed:15944147, ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:22992733, ECO:0000269|PubMed:28923943, ECO:0000269|PubMed:3298999, ECO:0000269|PubMed:8043104}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07251
|
ATPA_YEAST
|
MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF
| null | null |
proton motive force-driven ATP synthesis [GO:0015986]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase, catalytic core [GO:0005754]; mitochondrion [GO:0005739]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF00006;PF00306;PF02874;
|
2.40.30.20;1.20.150.20;3.40.50.300;
|
ATPase alpha/beta chains family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}. Note=Peripheral membrane protein.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). {ECO:0000250}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07255
|
COX9_YEAST
|
MTIAPITGTIKRRVIMDIVLGFSLGGVMASYWWWGFHMDKINKREKFYAELAERKKQEN
| null | null |
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]
|
mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
|
cytochrome-c oxidase activity [GO:0004129]
| null | null |
Fungal cytochrome c oxidase subunit 7a family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
| null | null |
PATHWAY: Energy metabolism; oxidative phosphorylation.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000305|PubMed:30598554}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07256
|
QCR1_YEAST
|
MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW
| null | null |
aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; protein processing involved in protein targeting to mitochondrion [GO:0006627]; proton transmembrane transport [GO:1902600]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF00675;PF05193;
|
3.30.830.10;
|
Peptidase M16 family, UQCRC1/QCR1 subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000305|PubMed:11880631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07257
|
QCR2_YEAST
|
MLSAARLQFAQGSVRRLTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL
| null | null |
aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; proteolysis [GO:0006508]; proton transmembrane transport [GO:1902600]
|
mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF00675;
|
3.30.830.10;
|
Peptidase M16 family, UQCRC2/QCR2 subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000305|PubMed:11880631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07258
|
CARA_YEAST
|
MSSAATKATFCIQNGPSFEGISFGANKSVAGETVFTTSLVGYPESMTDPSYRGQILVFTQPLIGNYGVPSGEARDEYNLLKYFESPHIHVVGIVVAEYAYQYSHWTAVESLAQWCQREGVAAITGVDTRELVQYLREQGSSLGRITLADHDPVPYVNPMKTNLVAQVTTKKPFHVSALPGKAKANVALIDCGVKENIIRCLVKRGANVTVFPYDYRIQDVASEFDGIFLSNGPGNPELCQATISNVRELLNNPVYDCIPIFGICLGHQLLALASGASTHKLKYGNRAHNIPAMDLTTGQCHITSQNHGYAVDPETLPKDQWKPYFVNLNDKSNEGMIHLQRPIFSTQFHPEAKGGPLDTAILFDKFFDNIEKYQLQSQAKSSISLKVTYSTDKSRLQSINVTKLAKERVLF
|
6.3.5.5
| null |
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221]
|
carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]
|
ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; glutaminase activity [GO:0004359]
|
PF00988;PF00117;
|
3.40.50.880;3.50.30.20;
|
CarA family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:200419, ECO:0000269|PubMed:205532}.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000269|PubMed:206535, ECO:0000269|PubMed:206652, ECO:0000269|PubMed:5856369}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific small chain]: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000269|PubMed:206535, ECO:0000269|PubMed:206652};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.25 mM for glutamine {ECO:0000269|PubMed:206535};
|
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|PubMed:5856369}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:206652};
| null |
FUNCTION: Small subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia. {ECO:0000269|PubMed:206535, ECO:0000269|PubMed:4594376, ECO:0000269|PubMed:5856369, ECO:0000269|Ref.8}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07259
|
PYR1_YEAST
|
MATIAPTAPITPPMESTGDRLVTLELKDGTVLQGYSFGAEKSVAGELVFQTGMVGYPESVTDPSYEGQILVITYPLVGNYGVPDMHLRDELVEELPRYFESNRIHIAGLVISHYTDEYSHYLAKSSLGKWLQNEGIPAVYGVDTRSLTKHLRDAGSMLGRLSLEKSGSDRTISRSSSWRSAFDVPEWVDPNVQNLVSKVSINEPKLYVPPADNKHIELQTGPDGKVLRILAIDVGMKYNQIRCFIKRGVELKVVPWNYDFTKEDYDGLFISNGPGDPSVLDDLSQRLSNVLEAKKTPVFGICLGHQLIARAAGASTLKLKFGNRGHNIPCTSTISGRCYITSQNHGFAVDVDTLTSGWKPLFVNANDDSNEGIYHSELPYFSVQFHPESTPGPRDTEFLFDVFIQAVKEFKYTQVLKPIAFPGGLLEDNVKAHPRIEAKKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTILINPNIATIQTSKGLADKVYFVPVTAEFVRKVILHERPDAIYVTFGGQTALSVGIAMKDEFEALGVKVLGTPIDTIITTEDRELFSNAIDEINEKCAKSQAANSVDEALAAVKEIGFPVIVRAAYALGGLGSGFANNEKELVDLCNVAFSSSPQVLVEKSMKGWKEVEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPVSKDYCIIEVNARLSRSSALASKATGYPLAYTAAKLGLNIPLNEVKNSVTKSTCACFEPSLDYCVVKMPRWDLKKFTRVSTELSSSMKSVGEVMSIGRTFEEAIQKAIRSTEYANLGFNETDLDIDIDYELNNPTDMRVFAIANAFAKKGYSVDKVWEMTRIDKWFLNKLHDLVQFAEKISSFGTKEELPSLVLRQAKQLGFDDRQIARFLDSNEVAIRRLRKEYGITPFVKQIDTVAAEFPAYTNYLYMTYNADSHDLSFDDHGVMVLGSGVYRIGSSVEFDWCAVTAVRTLRANNIKTIMVNYNPETVSTDYDEADRLYFETINLERVLDIYEIENSSGVVVSMGGQTSNNIAMTLHRENVKILGTSPDMIDSAENRYKFSRMLDQIGVDQPAWKELTSMDEAESFAEKVGYPVLVRPSYVLSGAAMNTVYSKNDLESYLNQAVEVSRDYPVVITKYIENAKEIEMDAVARNGELVMHVVSEHVENAGVHSGDATLIVPPQDLAPETVDRIVVATAKIGKALKITGPYNIQFIAKDNEIKVIECNVRASRSFPFISKVVGVNLIELATKAIMGLPLTPYPVEKLPDDYVAVKVPQFSFPRLAGADPVLGVEMASTGEVATFGHSKYEAYLKSLLATGFKLPKKNILLSIGSYKEKQELLSSVQKLYNMGYKLFATSGTADFLSEHGIAVQYLEVLNKDDDDQKSEYSLTQHLANNEIDLYINLPSANRFRRPASYVSKGYKTRRLAVDYSVPLVTNVKCAKLLIEAISRNITLDVSERDAQTSHRTITLPGLINIATYVPNASHVIKGPAELKETTRLFLESGFTYCQLMPRSISGPVITDVASLKAANSVSQDSSYTDFSFTIAGTAHNAHSVTQSASKVTALFLPLRELKNKITAVAELLNQWPTEKQVIAEAKTADLASVLLLTSLQNRSIHITGVSNKEDLALIMTVKAKDPRVTCDVNIYSLFIAQDDYPEAVFLPTKEDQEFFWNNLDSIDAFSVGALPVALANVTGNKVDVGMGIKDSLPLLLAAVEEGKLTIDDIVLRLHDNPAKIFNIPTQDSVVEIDLDYSFRRNKRWSPFNKDMNGGIERVVYNGETLVLSGELVSPGAKGKCIVNPSPASITASAELQSTSAKRRFSITEEAIADNLDAAEDAIPEQPLEQKLMSSRPPRELVAPGAIQNLIRSNNPFRGRHILSIKQFKRSDFHVLFAVAQELRAAVAREGVLDLMKGHVITTIFFEPSTRTCSSFIAAMERLGGRIVNVNPLVSSVKKGETLQDTIRTLACYSDAIVMRHSEEMSVHIAAKYSPVPIINGGNGSREHPTQAFLDLFTIREEIGTVNGITVTFMGDLKHGRTVHSLCRLLMHYQVRINLVSPPELRLPEGLREELRKAGLLGVESIELTPHIISKTDVLYCTRVQEERFNSPEEYARLKDTYIVDNKILAHAKENMAIMHPLPRVNEIKEEVDYDHRAAYFRQMKYGLFVRMALLAMVMGVDM
|
2.1.3.2; 3.5.1.2; 6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; negative regulation of pyrimidine nucleobase metabolic process [GO:0045984]; UTP biosynthetic process [GO:0006228]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]
|
amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:0004359]; metal ion binding [GO:0046872]
|
PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729;
|
3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380;
|
CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11015727, ECO:0000269|PubMed:14562095}. Note=Associates with membranes. {ECO:0000269|PubMed:11921093}.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000269|PubMed:182284, ECO:0000269|PubMed:237624, ECO:0000269|PubMed:5552824, ECO:0000305|PubMed:5856369}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000305|PubMed:5856369}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000269|PubMed:237624, ECO:0000269|PubMed:3281587, ECO:0000305|PubMed:5856369}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000269|PubMed:4575349, ECO:0000269|PubMed:5552824, ECO:0000269|PubMed:6354093};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for NH4(+) {ECO:0000269|PubMed:3281587}; KM=0.5 mM for glutamine {ECO:0000269|PubMed:182284}; KM=3 mM for hydrogencarbonate {ECO:0000269|PubMed:182284}; KM=16.6 mM for aspartate {ECO:0000269|PubMed:4575349, ECO:0000269|PubMed:6354093}; KM=1.18 mM for carbamoyl phosphate {ECO:0000269|PubMed:4575349, ECO:0000269|PubMed:6354093};
|
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000305|PubMed:5856369}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000305|PubMed:5856369}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (for the CPSase reaction) (PubMed:3281587). Optimum pH is 8-9 (fro the ATCase reaction) (PubMed:4575349). {ECO:0000269|PubMed:3281587, ECO:0000269|PubMed:4575349};
| null |
FUNCTION: Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. {ECO:0000269|PubMed:10446140, ECO:0000269|PubMed:15128434, ECO:0000269|PubMed:3281587, ECO:0000269|PubMed:5856369, ECO:0000269|PubMed:8449292}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07260
|
IF4E_YEAST
|
MSVEEVSKKFEENVSVDDTTATPKTVLSDSAHFDVKHPLNTKWTLWYTKPAVDKSESWSDLLRPVTSFQTVEEFWAIIQNIPEPHELPLKSDYHVFRNDVRPEWEDEANAKGGKWSFQLRGKGADIDELWLRTLLAVIGETIDEDDSQINGVVLSIRKGGNKFALWTKSEDKEPLLRIGGKFKQVLKLTDDGHLEFFPHSSANGRHPQPSITL
| null | null |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of formation of translation preinitiation complex [GO:1901195]; regulation of cell cycle [GO:0051726]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]; ribosome [GO:0005840]
|
mRNA cap binding [GO:0098808]; phosphatidylinositol-3-phosphate binding [GO:0032266]; RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]
|
PF01652;
|
3.30.760.10;
|
Eukaryotic initiation factor 4E family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8119957}. Nucleus {ECO:0000269|PubMed:8119957}.
| null | null | null | null | null |
FUNCTION: Recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. {ECO:0000269|PubMed:2685552, ECO:0000269|PubMed:8119957}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07261
|
GCR1_YEAST
|
MVCTSTSSNFYSIAQYILQSYFKVNVDSLNSLKLVDLIVDQTYPDSLTLRKLNEGATGQPYDYFNTVSRDADISKCPIFALTIFFVIRWSHPNPPISIENFTTVPLLDSNFISLNSNPLLYIQNQNPNSNSSVKVSRSQTFEPSKELIDLVFPWLSYLKQDMLLIDRTNYKLYSLCELFEFMGRVAIQDLRYLSQHPLLLPNIVTFISKFIPELFQNEEFKGIGSIKNSNNNALNNVTGIETQFLNPSTEEVSQKVDSYFMELSKKLTTENIRLSQEITQLKADMNSVGNVCNQILLLQRQLLSGNQAIGSKSENIVSSTGGGILILDKNSINSNVLSNLVQSIDPNHSKPNGQAQTHQRGPKGQSHAQVQSTNSPALAPINMFPSLSNSIQPMLGTLAPQPQDIVQKRKLPLPGSIASAATGSPFSPSPVGESPYSKRFKLDDKPTPSQTALDSLLTKSISSPRLPLSTLANTAVTESFRSPQQFQHSPDFVVGGSSSSTTENNSKKVNEDSPSSSSKLAERPRLPNNDSTTSMPESPTEVAGDDVDREKPPESSKSEPNDNSPESKDPEKNGKNSNPLGTDADKPVPISNIHNSTEAANSSGTVTKTAPSFPQSSSKFEIINKKDTKAGPNEAIKYKLSRENKTIWDLYAEWYIGLNGKSSIKKLIENYGWRRWKVSEDSHFFPTRRIIMDYIETECDRGIKLGRFTNPQQPREDIRKILVGDLEKFRINNGLTLNSLSLYFRNLTKNNKEICIFENFKNWNVRSMTEEEKLKYCKRRHNTPS
| null | null |
carbon catabolite repression of transcription from RNA polymerase II promoter by glucose [GO:0000433]; nucleosome organization [GO:0034728]; positive regulation of ribosomal protein gene transcription by RNA polymerase II [GO:0060963]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from a mobile element promoter [GO:0061435]; regulation of glycolytic process [GO:0006110]
|
nuclear envelope [GO:0005635]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF12550;
| null | null |
PTM: Phosphorylated in a GCR2-dependent manner. {ECO:0000269|PubMed:9335588}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional activator required for the expression of glycolytic and ribosomal genes. Forms a transcriptional activation complex with RAP1, RAP1 providing the specific DNA-binding function and GCR1 providing the activation function. Can also bind itself to DNA to a core 5'-CTTCC-3' sequence (CT box). CT box-binding is not essential, but enhances the activation function of the RAP1-GCR1 complex in promoters that contain both DNA signals (only glycolytic genes). CT box-dependent transcriptional activation requires GCR2. {ECO:0000269|PubMed:11333224, ECO:0000269|PubMed:1508187, ECO:0000269|PubMed:3025612, ECO:0000269|PubMed:3547083, ECO:0000269|PubMed:8508768, ECO:0000269|PubMed:9335588}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07263
|
SYH_YEAST
|
MLSRSLNKVVTSIKSSSIIRMSSATAAATSAPTANAANALKASKAPKKGKLQVSLKTPKGTKDWADSDMVIREAIFSTLSGLFKKHGGVTIDTPVFELREILAGKYGEDSKLIYNLEDQGGELCSLRYDLTVPFARYVAMNNIQSIKRYHIAKVYRRDQPAMTKGRMREFYQCDFDVAGTFESMVPDSECLSILVEGLTSLGIKDFKIKLNHRKILDGIFQIAGVKDEDVRKISSAVDKLDKSPWEAVKKEMTEEKGQSEETADKIGEYVKLNGSLKEIHAVLSADANITSNEKAKQGLDDIATLMKYTEAFDIDSFISFDLSLARGLDYYTGLIYEVVTSASAPPENASELKKKAKSAEDASEFVGVGSIAAGGRYDNLVNMFSEASGKKSTQIPCVGISFGVERIFSLIKQRINSSTTIKPTATQVFVMAFGGGKDWTGYLPERMKVTKQLWDAGIEAEYVYKAKANPRKQFDAAEKAGCHIAVILGKEEYLEGKLRVKRLGQEFADDDGELVSAADIVPIVQEKLSQIHEDGLNEVTRLIKGL
|
6.1.1.21
| null |
histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial translation [GO:0032543]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
aminoacyl-tRNA ligase activity [GO:0004812]; ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF03129;PF13393;
|
3.40.50.800;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
| null | null | null | null |
FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion. {ECO:0000269|PubMed:1459448, ECO:0000269|PubMed:3521891}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07264
|
LEUC_YEAST
|
MVYTPSKGPRTLYDKVFDAHVVHQDENGSFLLYIDRHLVHEVTSPQAFEGLENAGRKVRRVDCTLATVDHNIPTESRKNFKSLDTFIKQTDSRLQVKTLENNVKQFGVPYFGMSDARQGIVHTIGPEEGFTLPGTTVVCGDSHTSTHGAFGSLAFGIGTSEVEHVLATQTIIQAKSKNMRITVNGKLSPGITSKDLILYIIGLIGTAGGTGCVIEFAGEAIEALSMEARMSMCNMAIEAGARAGMIKPDETTFQYTKGRPLAPKGAEWEKAVAYWKTLKTDEGAKFDHEINIEAVDVIPTITWGTSPQDALPITGSVPDPKNVTDPIKKSGMERALAYMGLEPNTPLKSIKVDKVFIGSCTNGRIEDLRSAAAVVRGQKLASNIKLAMVVPGSGLVKKQAEAEGLDKIFQEAGFEWREAGCSICLGMNPDILDAYERCASTSNRNFEGRQGALSRTHLMSPAMAAAAGIAGHFVDIREFEYKDQDQSSPKVEVTSEDEKELESAAYDHAEPVQPEDAPQDIANDELKDIPVKSDDTPAKPSSSGMKPFLTLEGISAPLDKANVDTDAIIPKQFLKTIKRTGLKKGLFYEWRFRKDDQGKDQETDFVLNVEPWREAEILVVTGDNFGCGSSREHAPWALKDFGIKSIIAPSYGDIFYNNSFKNGLLPIRLDQQIIIDKLIPIANKGGKLCVDLPNQKILDSDGNVLVDHFEIEPFRKHCLVNGLDDIGITLQKEEYISRYEALRREKYSFLEGGSKLLKFDNVPKRKAVTTTFDKVHQDW
|
4.2.1.33
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
|
amino acid biosynthetic process [GO:0008652]; leucine biosynthetic process [GO:0009098]
|
3-isopropylmalate dehydratase complex [GO:0009316]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]
|
3-isopropylmalate dehydratase activity [GO:0003861]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]
|
PF00330;PF00694;
|
3.30.499.10;3.20.19.10;
|
Aconitase/IPM isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33;
| null |
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
| null | null |
FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07267
|
CARP_YEAST
|
MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEKANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI
|
3.4.23.25
| null |
autophagy [GO:0006914]; cytoplasm to vacuole targeting by the Cvt pathway [GO:0032258]; macroautophagy [GO:0016236]; microautophagy [GO:0016237]; pexophagy [GO:0000425]; proteolysis involved in protein catabolic process [GO:0051603]
|
endoplasmic reticulum [GO:0005783]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
|
aspartic-type endopeptidase activity [GO:0004190]; disordered domain specific binding [GO:0097718]; oligosaccharide binding [GO:0070492]; peptidase activity [GO:0008233]
|
PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.; EC=3.4.23.25;
| null | null | null | null |
FUNCTION: Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07268
|
PRZN_SERME
|
MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEAQSSDFIHFVDHFSGAAGEALLSYNASNNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV
|
3.4.24.40
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 7 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00353;PF00413;PF08548;
|
3.40.390.10;2.150.10.10;
|
Peptidase M10B family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with hydrophobic residues in P1'.; EC=3.4.24.40;
| null | null | null | null |
FUNCTION: Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon.
|
Serratia marcescens (strain ATCC 21074 / E-15)
|
P07269
|
PHO2_YEAST
|
MMEEFSYDHDFNTHFATDLDYLQHDQQQQQQQQHDQQHNQQQQPQPQPIQTQNLEHDHDQHTNDMSASSNASDSGPQRPKRTRAKGEALDVLKRKFEINPTPSLVERKKISDLIGMPEKNVRIWFQNRRAKLRKKQHGSNKDTIPSSQSRDIANDYDRGSTDNNLVTTTSTSSIFHDEDLTFFDRIPLNSNNNYYFFDICSITVGSWNRMKSGALQRRNFQSIKELRNLSPIKINNIMSNATDLMVLISKKNSEINYFFSAMANNTKILFRIFFPLSSVTNCSLTLETDDDIINSNNTSDKNNSNTNNDDDNDDNSNEDNDNSSEDKRNAKDNFGELKLTVTRSPTFAVYFLNNAPDEDPNLNNQWSICDDFSEGRQVNDAFVGGSNIPHTLKGLQKSLRFMNSLILDYKSSNEILPTINTAIPTAAVPQQNIAPPFLNTNSSATDSNPNTNLEDSLFFDHDLLSSSITNTNNGQGSNNGRQASKDDTLNLLDTTVNSNNNHNANNEENHLAQEHLSNDADIVANPNDHLLSLPTDSELPNTPDFLKNTNELTDEHRWI
| null | null |
cell differentiation [GO:0030154]; chromatin remodeling [GO:0006338]; positive regulation of DNA binding [GO:0043388]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; regulation of histidine biosynthetic process [GO:0120213]; regulation of purine nucleobase metabolic process [GO:0006141]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Regulator in phosphate metabolism and acts as a derepressor of another central regulator PHO5. Binds to the upstream activator sequence (UAS) of PHO5. It also binds to the TRP4, HIS4, and CYC1 promoters. {ECO:0000269|PubMed:3049251}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07270
|
PHO4_YEAST
|
MGRTTSEGIHGFVDDLEPKSSILDKVGDFITVNTKRHDGREDFNEQNDELNSQENHNSSENGNENENEQDSLALDDLDRAFELVEGMDMDWMMPSHAHHSPATTATIKPRLLYSPLIHTQSAVPVTISPNLVATATSTTSANKVTKNKSNSSPYLNKRRGKPGPDSATSLFELPDSVIPTPKPKPKPKQYPKVILPSNSTRRVSPVTAKTSSSAEGVVVASESPVIAPHGSSHSRSLSKRRSSGALVDDDKRESHKHAEQARRNRLAVALHELASLIPAEWKQQNVSAAPSKATTVEAACRYIRHLQQNVST
| null | null |
cellular response to phosphate starvation [GO:0016036]; chromatin remodeling [GO:0006338]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565]
|
PF00010;
|
4.10.280.10;
| null |
PTM: Phosphorylated by the cyclin-CDK PHO80-PHO85 at five residues under high-phosphate conditions, preventing PHO4 from activating the structural PHO genes. Phosphorylation of Ser-114 and Ser-128 promotes nuclear export. Phosphorylation of Ser-152 decreases nuclear import. Phosphorylation of Ser-223 decreases the binding affinity for PHO2. {ECO:0000269|PubMed:10320381, ECO:0000269|PubMed:8108735, ECO:0000269|PubMed:8539622}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8539622}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8539622}. Note=Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07271
|
PIF1_YEAST
|
MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNNSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYKKVRRSRKHLRRWENIGALVVDEISMLDAELLDKLDFIARKIRKNHQPFGGIQLIFCGDFFQLPPVSKDPNRPTKFAFESKAWKEGVKMTIMLQKVFRQRGDVKFIDMLNRMRLGNIDDETEREFKKLSRPLPDDEIIPAELYSTRMEVERANNSRLSKLPGQVHIFNAIDGGALEDEELKERLLQNFLAPKELHLKVGAQVMMVKNLDATLVNGSLGKVIEFMDPETYFCYEALTNDPSMPPEKLETWAENPSKLKAAMEREQSDGEESAVASRKSSVKEGFAKSDIGEPVSPLDSSVFDFMKRVKTDDEVVLENIKRKEQLMQTIHQNSAGKRRLPLVRFKASDMSTRMVLVEPEDWAIEDENEKPLVSRVQLPLMLAWSLSIHKSQGQTLPKVKVDLRRVFEKGQAYVALSRAVSREGLQVLNFDRTRIKAHQKVIDFYLTLSSAESAYKQLEADEQVKKRKLDYAPGPKYKAKSKSKSNSPAPISATTQSNNGIAAMLQRHSRKRFQLKKESNSNQVHSLVSDEPRGQDTEDHILE
|
3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734}; Note=Mg(2+). To a lesser extent, can also use Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734};
|
chromosome organization [GO:0051276]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; G-quadruplex DNA unwinding [GO:0044806]; mitochondrial genome maintenance [GO:0000002]; negative regulation of telomere maintenance via telomerase [GO:0032211]; replication fork reversal [GO:0071932]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; replication fork [GO:0005657]
|
5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; G-quadruplex DNA binding [GO:0051880]; single-stranded DNA binding [GO:0003697]; telomerase inhibitor activity [GO:0010521]
|
PF05970;PF21530;
|
3.40.50.300;
|
Helicase family, PIF1 subfamily
|
PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA. {ECO:0000269|PubMed:22927468}.
|
SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16816432}. Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. {ECO:0000269|PubMed:16816432}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16816432, ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:20655619}; Peripheral membrane protein {ECO:0000269|PubMed:20655619}; Matrix side {ECO:0000269|PubMed:20655619}. Note=Bound to the mitochondrial inner membrane either directly or indirectly via a protein complex. {ECO:0000269|PubMed:20655619}.
|
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=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596008};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for ATP {ECO:0000269|PubMed:8253734}; KM=0.4 mM for dATP {ECO:0000269|PubMed:8253734};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:8253734};
| null |
FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing. {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:10693764, ECO:0000269|PubMed:10926538, ECO:0000269|PubMed:11429610, ECO:0000269|PubMed:12024022, ECO:0000269|PubMed:15907372, ECO:0000269|PubMed:15923634, ECO:0000269|PubMed:16121131, ECO:0000269|PubMed:16537895, ECO:0000269|PubMed:16816432, ECO:0000269|PubMed:16878131, ECO:0000269|PubMed:17257907, ECO:0000269|PubMed:17590086, ECO:0000269|PubMed:17720711, ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:19424434, ECO:0000269|PubMed:20225162, ECO:0000269|PubMed:21620135, ECO:0000269|PubMed:23175612, ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596008, ECO:0000269|PubMed:23657261, ECO:0000269|PubMed:3038524, ECO:0000269|PubMed:8287473}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07272
|
PPR1_YEAST
|
MKQKKFNSKKSNRTDLSKRGDSPNIGISKSRTACKRCRLKKIKCDQEFPSCKRCAKLEVPCVSLDPATGKDVPRSYVFFLEDRLAVMMRVLKEYGVDPTKIRGNIPATSDDEPFDLKKYSSVSSLGEEGILPHNGLLADYLVQKGNSMASSAITSKSMASPQTINVQRKEFLVNSKKQDGSALLPETGSPMTSDARAEELRRCNKEISALGTMRESSFNSFLGDSSGISFAKLVFTATNFRQDSGDDVLDEDIKQREQKYNGYAEAENNPHFDPLELPPRHAAEVMISRFFVDTNSQLPLLHRELFLKKYFEPIYGPWNPNIALASDQTGINSAFEIPITSAFSAHTEPKRENVTEKIDVCSSVDVPWYDTWETSQKVNMRPIVELPTKFHIPYFFLNIIFAIGHATQVLKSDITTVATYKRRATKYIASLFSSSDRLEALAGTLLMVIYSIMRPNVPGVWYTMGSVLRLTVDLGLHSEKINKNYDAFTREIRRRLFWCVYSLDRQICSYFGRPFGIPEESITTRYPSLLDDSFITLTNREIDDYSDLPSPNPSSKVIALAMYKIRRIQASIVRILYAPGAELPRRFMDLESWRIETYNELERWFQVDVPKNFEMMNCKFNSIWFDLNYHYSKSILYGLSPKFPTLNDTAFKIVLDSTKGTIDVFYNLCVNKKIGYTWVAVHNMFMTGMTYLYVNFYSKNNINDCQEKVSEYTEKVLIVLKNLIGFCESAKTCYTSYKILSSVVIKLKFMQINDAKGIFSDSNPLTSQANRMSSYDKKTNVLGFDDGTFDNKVFNRTNFEEKAPFDIPLDEFFTELEKHSNVSQFNTLDVSEGNQVINESASTNTSSALNCQSYTNNQDIMDILFQVTSGSVWDEFFVRSGNGNEGESSYDISKGKNSESGGIF
| null | null |
DNA-templated transcription [GO:0006351]; positive regulation of pyrimidine nucleotide biosynthetic process [GO:1900399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pyrimidine nucleotide biosynthetic process [GO:0006221]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
|
PF04082;PF00172;
|
4.10.240.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Positive regulator of URA1 and URA3 expression.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07273
|
TFS2_YEAST
|
MDSKEVLVHVKNLEKNKSNDAAVLEILHVLDKEFVPTEKLLRETKVGVEVNKFKKSTNVEISKLVKKMISSWKDAINKNKRSRQAQQHHQDHAPGNAEDKTTVGESVNGVQQPASSQSDAMKQDKYVSTKPRNSKNDGVDTAIYHHKLRDQVLKALYDVLAKESEHPPQSILHTAKAIESEMNKVNNCDTNEAAYKARYRIIYSNVISKNNPDLKHKIANGDITPEFLATCDAKDLAPAPLKQKIEEIAKQNLYNAQGATIERSVTDRFTCGKCKEKKVSYYQLQTRSADEPLTTFCTCEACGNRWKFS
| null | null |
DNA-templated transcription [GO:0006351]; maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II [GO:0001193]; positive regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0045899]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of mRNA 3'-end processing [GO:0031440]; transcription antitermination [GO:0031564]; transcription by RNA polymerase III [GO:0006383]; transcription elongation by RNA polymerase I [GO:0006362]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367]; tRNA transcription by RNA polymerase III [GO:0042797]
|
nucleus [GO:0005634]
|
RNA polymerase II complex binding [GO:0000993]; RNA polymerase II complex recruiting activity [GO:0001139]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270]
|
PF08711;PF01096;PF07500;
|
2.20.25.10;1.20.930.10;1.10.472.30;
|
TFS-II family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.; FUNCTION: Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07274
|
PROF_YEAST
|
MSWQAYTDNLIGTGKVDKAVIYSRAGDAVWATSGGLSLQPNEIGEIVQGFDNPAGLQSNGLHIQGQKFMLLRADDRSIYGRHDAEGVVCVRTKQTVIIAHYPPTVQAGEATKIVEQLADYLIGVQY
| null | null |
intracellular transport [GO:0046907]; mitotic actomyosin contractile ring assembly [GO:1903475]; positive regulation of formin-nucleated actin cable assembly [GO:0090338]; sequestering of actin monomers [GO:0042989]
|
cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]
|
actin monomer binding [GO:0003785]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; proline-rich region binding [GO:0070064]
|
PF00235;
|
3.30.450.30;
|
Profilin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
| null | null | null | null | null |
FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07276
|
RAD2_YEAST
|
MGVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQEGNAVKNSHITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPSSGSSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEELPKATQYLILSSLRLKSRLRMGYSKEQLETIFPNSMDFSRFQIDMVKRRNFFTQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDGSDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECEWEEVELKPKNVKFVEDFSLKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEVQELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVFLFGGTKIYKNMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTNGLKGMGPVSSIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKKLVNNEIILDDDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM
|
3.1.-.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000250};
|
nucleotide-excision repair [GO:0006289]; transcription by RNA polymerase II [GO:0006366]
|
nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634]
|
DNA endonuclease activity [GO:0004520]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]
|
PF00867;PF00752;
|
1.10.150.20;3.40.50.1010;
|
XPG/RAD2 endonuclease family, XPG subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair. {ECO:0000269|PubMed:8247134}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07277
|
ERG12_YEAST
|
MSLPFLTSAPGKVIIFGEHSAVYNKPAVAASVSALRTYLLISESSAPDTIELDFPDISFNHKWSINDFNAITEDQVNSQKLAKAQQATDGLSQELVSLLDPLLAQLSESFHYHAAFCFLYMFVCLCPHAKNIKFSLKSTLPIGAGLGSSASISVSLALAMAYLGGLIGSNDLEKLSENDKHIVNQWAFIGEKCIHGTPSGIDNAVATYGNALLFEKDSHNGTINTNNFKFLDDFPAIPMILTYTRIPRSTKDLVARVRVLVTEKFPEVMKPILDAMGECALQGLEIMTKLSKCKGTDDEAVETNNELYEQLLELIRINHGLLVSIGVSHPGLELIKNLSDDLRIGSTKLTGAGGGGCSLTLLRRDITQEQIDSFKKKLQDDFSYETFETDLGGTGCCLLSAKNLNKDLKIKSLVFQLFENKTTTKQQIDDLLLPGNTNLPWTS
|
2.7.1.36
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P17256};
|
ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process, mevalonate pathway [GO:0010142]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; mevalonate kinase activity [GO:0004496]
|
PF00288;
|
3.30.230.10;3.30.70.890;
|
GHMP kinase family, Mevalonate kinase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:1645230}.
|
CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+); Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.1.36; Evidence={ECO:0000269|PubMed:1645230}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066; Evidence={ECO:0000269|PubMed:1645230};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for mevalonate {ECO:0000269|PubMed:1645230}; Vmax=27 nmol/min/mg enzyme {ECO:0000269|PubMed:1645230};
|
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. {ECO:0000269|PubMed:1645230}.
| null | null |
FUNCTION: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:1645230). ERG12 converts mevalonate into 5-phosphomevalonate (PubMed:1645230). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:32679672). {ECO:0000269|PubMed:1645230, ECO:0000303|PubMed:32679672}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07278
|
KAPR_YEAST
|
MVSSLPKESQAELQLFQNEINAANPSDFLQFSANYFNKRLEQQRAFLKAREPEFKAKNIVLFPEPEESFSRPQSAQSQSRSRSSVMFKSPFVNEDPHSNVFKSGFNLDPHEQDTHQQAQEEQQHTREKTSTPPLPMHFNAQRRTSVSGETLQPNNFDDWTPDHYKEKSEQQLQRLEKSIRNNFLFNKLDSDSKRLVINCLEEKSVPKGATIIKQGDQGDYFYVVEKGTVDFYVNDNKVNSSGPGSSFGELALMYNSPRAATVVATSDCLLWALDRLTFRKILLGSSFKKRLMYDDLLKSMPVLKSLTTYDRAKLADALDTKIYQPGETIIREGDQGENFYLIEYGAVDVSKKGQGVINKLKDHDYFGEVALLNDLPRQATVTATKRTKVATLGKSGFQRLLGPAVDVLKLNDPTRH
| null | null |
negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to bud neck [GO:0097271]; regulation of cytoplasmic mRNA processing body assembly [GO:0010603]; regulation of protein phosphorylation [GO:0001932]
|
cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; identical protein binding [GO:0042802]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF02197;
|
2.60.120.10;
|
CAMP-dependent kinase regulatory chain family
|
PTM: Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clustered in several groups, all localized in the N-terminal part. The first cluster termed cluster I (CI) is located close to the N-terminus and includes Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and Ser-84. This cluster of phosphorylation sites, termed cluster II (CII), is important for BCY1 cytoplasmic localization and function (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-150, and Thr-160. This cluster falls within or near the so-called autoinhibitory domain where the catalytic subunit of PKA autophosphorylates the highly conserved Ser-145 to inhibit BCY1 (PubMed:20702584). A last cluster of phosphorylated residues included Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites in CIII (and to a lesser extent in CII) are hyperphosphorylated in response to rapamycin (PubMed:20702584). {ECO:0000269|PubMed:11134339, ECO:0000269|PubMed:12704202, ECO:0000269|PubMed:20702584}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic when phosphorylated. Nuclear when not phosphorylated.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1. {ECO:0000269|PubMed:12704202, ECO:0000269|PubMed:2823100, ECO:0000269|PubMed:3037314, ECO:0000269|PubMed:6243658}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07280
|
RS19A_YEAST
|
MPGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE
| null | null |
ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal subunit export from nucleus [GO:0000054]; translation [GO:0006412]
|
cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF01090;
|
1.10.10.10;
|
Eukaryotic ribosomal protein eS19 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874, PubMed:17726054). {ECO:0000269|PubMed:16159874, ECO:0000269|PubMed:17726054, ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07281
|
RS19B_YEAST
|
MAGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE
| null | null |
ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal subunit export from nucleus [GO:0000054]; translation [GO:0006412]
|
cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF01090;
|
1.10.10.10;
|
Eukaryotic ribosomal protein eS19 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874). {ECO:0000269|PubMed:16159874, ECO:0000305|PubMed:22096102}.; FUNCTION: Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA. {ECO:0000269|PubMed:16159874}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07283
|
PMM_YEAST
|
MSIAEFAYKEKPETLVLFDVDGTLTPARLTVSEEVRKTLAKLRNKCCIGFVGGSDLSKQLEQLGPNVLDEFDYSFSENGLTAYRLGKELASQSFINWLGEEKYNKLAVFILRYLSEIDLPKRRGTFLEFRNGMINVSPIGRNASTEERNEFERYDKEHQIRAKFVEALKKEFPDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKDGFKEIHFFGDKTMVGGNDYEIFVDERTIGHSVQSPDDTVKILTELFNL
|
5.4.2.8
| null |
GDP-mannose biosynthetic process [GO:0009298]; mannose metabolic process [GO:0006013]; protein N-linked glycosylation [GO:0006487]
|
cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]
|
metal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615]
|
PF03332;
|
3.30.1240.20;3.40.50.1000;
|
Eukaryotic PMM family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3905826}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:3288631}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11142; Evidence={ECO:0000305|PubMed:3288631};
| null |
PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. {ECO:0000305|PubMed:3288631}.
| null | null |
FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen. {ECO:0000269|PubMed:3288631}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07284
|
SYSC_YEAST
|
MLDINQFIEDKGGNPELIRQSQKARNASVEIVDEIISDYKDWVKTRFELDELNKKFNKLQKDIGLKFKNKEDASGLLAEKEKLTQQKKELTEKEQQEDKDLKKKVFQVGNIVHPSVVVSNDEENNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGYDPDRGVKICGHRGYFFRNYGVFLNQALINYGLQFLAAKGYIPLQAPVMMNKELMSKTAQLSEFDEELYKVIDGEDEKYLIATSEQPISAYHSGEWFEKPQEQLPIHYVGYSSCFRREAGSHGKDAWGVFRVHAFEKIEQFVITEPEKSWEEFEKMISYSEEFYKSLKLPYRIVGIVSGELNNAAAKKYDLEAWFPYQKEYKELVSCSNCTDYQSRNLEIRCGIKKMGDREKKYVHCLNSTLAATQRALCCILENYQTEDGLVVPEVLRKYIPGEPEFLPFVNELPKNSTSSKDKKKKN
|
6.1.1.11
| null |
cytoplasmic translation [GO:0002181]; mitochondrial seryl-tRNA aminoacylation [GO:0070158]; seryl-tRNA aminoacylation [GO:0006434]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; serine-tRNA ligase activity [GO:0004828]; tRNA binding [GO:0000049]
|
PF02403;PF00587;
|
1.10.287.40;
|
Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49591}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence={ECO:0000269|PubMed:3031581}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12293; Evidence={ECO:0000269|PubMed:3031581};
| null | null | null | null |
FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). {ECO:0000269|PubMed:3031581}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07286
|
GPT_YEAST
|
MLRLFSLALITCLIYYSKNQGPSALVAAVGFGIAGYLATDMLIPRVGKSFIKIGLFGKDLSKPGRPVLPETIGAIPAAVYLFVMFIYIPFIFYKYMVITTSGGGHRDVSVVEDNGMNSNIFPHDKLSEYLSAILCLESTVLLGIADDLFDLRWRHKFFLPAIAAIPLLMVYYVDFGVTHVLIPGFMERWLKKTSVDLGLWYYVYMASMAIFCPNSINILAGVNGLEVGQCIVLAILALLNDLLYFSMGPLATRDSHRFSAVLIIPFLGVSLALWKWNRWPATVFVGDTYCYFAGMVFAVVGILGHFSKTMLLLFIPQIVNFIYSCPQLFKLVPCPRHRLPKFNEKDGLMYPSRANLKEEPPKSIFKPILKLLYCLHLIDLEFDENNEIISTSNMTLINLTLVWFGPMREDKLCNTILKLQFCIGILALLGRHAIGAIIFGHDNLWTVR
|
2.7.8.15
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H3H5};
|
aerobic respiration [GO:0009060]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; protein N-linked glycosylation [GO:0006487]
|
endoplasmic reticulum [GO:0005783]; UDP-N-acetylglucosamine transferase complex [GO:0043541]
|
glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity [GO:0003975]
|
PF00953;
| null |
Glycosyltransferase 4 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}.
|
CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP; Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519, ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:58427; EC=2.7.8.15; Evidence={ECO:0000269|PubMed:6096695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13290; Evidence={ECO:0000305|PubMed:6096695};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:6096695}.
| null | null |
FUNCTION: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane. {ECO:0000269|PubMed:6096695}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07288
|
KLK3_HUMAN
|
MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP
|
3.4.21.77
| null |
negative regulation of angiogenesis [GO:0016525]; positive regulation of antibacterial peptide production [GO:0002803]; protein metabolic process [GO:0019538]; proteolysis [GO:0006508]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; secretory granule [GO:0030141]
|
endopeptidase activity [GO:0004175]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Tyr-|-Xaa-.; EC=3.4.21.77;
| null | null | null | null |
FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
|
Homo sapiens (Human)
|
P07293
|
CAC1S_RABIT
|
MEPSSPQDEGLRKKQPKKPLPEVLPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLTVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNVIQSNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYYIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVEDLREGKLSLEEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSRVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDIANRVLLSLFTIEMLLKMYGLGLRQYFMSIFNRFDCFVVCSGILELLLVESGAMTPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPSYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSRGLPDKTEEEKSVMAKKLEQKPKGEGIPTTAKLKVDEFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKVRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRAESVRNQILGYFDIAFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSTISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFFSCNDLSKMTEEECRGYYYVYKDGDPTQMELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYRAIDSNEEDMGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYHQSEEMNHISDILNVAFTIIFTLEMILKLLAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIRRTISGDLTAEEELERAMVEAAMEERIFRRTGGLFGQVDTFLERTNSLPPVMANQRPLQFAEIEMEELESPVFLEDFPQDARTNPLARANTNNANANVAYGNSNHSNNQMFSSVHCEREFPGEAETPAAGRGALSHSHRALGPHSKPCAGKLNGQLVQPGMPINQAPPAPCQQPSTDPPERGQRRTSLTGSLQDEAPQRRSSEGSTPRRPAPATALLIQEALVRGGLDTLAADAGFVTATSQALADACQMEPEEVEVAATELLKARESVQGMASVPGSLSRRSSLGSLDQVQGSQETLIPPRP
| null | null |
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cellular response to caffeine [GO:0071313]; muscle contraction [GO:0006936]; positive regulation of muscle contraction [GO:0045933]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; release of sequestered calcium ion into cytosol [GO:0051209]
|
L-type voltage-gated calcium channel complex [GO:1990454]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]
|
calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; transmembrane transporter binding [GO:0044325]; voltage-gated calcium channel activity [GO:0005245]
|
PF08763;PF16885;PF16905;PF00520;
|
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1S subfamily
|
PTM: The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690. {ECO:0000305|PubMed:3037387}.; PTM: Phosphorylated. Phosphorylation by PKA activates the calcium channel. Both the minor and major forms are phosphorylated in vitro by PKA (PubMed:2549550, PubMed:2844809). Phosphorylation at Ser-1575 is involved in beta-adrenergic-mediated regulation of the channel (PubMed:20937870). {ECO:0000269|PubMed:20937870, ECO:0000269|PubMed:2549550, ECO:0000269|PubMed:2844809}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036, ECO:0000269|PubMed:27621462, ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29467163, ECO:0000269|PubMed:9465115, ECO:0000305|PubMed:3037387}; Multi-pass membrane protein {ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:3037387}.
| null | null | null | null | null |
FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle (PubMed:15201141, PubMed:25548159, PubMed:27621462, PubMed:29078335, PubMed:29467163, PubMed:9465115). Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction (PubMed:15201141, PubMed:27621462, PubMed:9465115). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. {ECO:0000250|UniProtKB:Q13698, ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:27621462, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29467163, ECO:0000269|PubMed:9465115, ECO:0000305}.
|
Oryctolagus cuniculus (Rabbit)
|
P07305
|
H10_HUMAN
|
MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK
| null | null |
chromosome condensation [GO:0030261]; heterochromatin formation [GO:0031507]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; positive regulation of transcription regulatory region DNA binding [GO:2000679]
|
actin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; nucleosomal DNA binding [GO:0031492]; nucleosome binding [GO:0031491]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
|
PTM: Phosphorylated on Ser-17 in RNA edited version. {ECO:0000269|PubMed:18993075}.; PTM: ADP-ribosylated on Ser-104 in response to DNA damage. {ECO:0000269|PubMed:27723750}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Note=The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes.
| null | null | null | null | null |
FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division.
|
Homo sapiens (Human)
|
P07306
|
ASGR1_HUMAN
|
MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
| null | null |
cellular response to extracellular stimulus [GO:0031668]; receptor-mediated endocytosis [GO:0006898]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
asialoglycoprotein receptor activity [GO:0004873]; fucose binding [GO:0042806]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]; signaling receptor activity [GO:0038023]
|
PF00059;PF03954;
|
3.10.100.10;
| null |
PTM: Phosphorylated on a cytoplasmic Ser residue.
|
SUBCELLULAR LOCATION: [Isoform H1a]: Membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform H1b]: Secreted {ECO:0000269|PubMed:20886072}.
| null | null | null | null | null |
FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
|
Homo sapiens (Human)
|
P07307
|
ASGR2_HUMAN
|
MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFSLLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGSVGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVNWVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDSDGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVCEKRRNATGEVA
| null | null |
cell surface receptor signaling pathway [GO:0007166]; endocytosis [GO:0006897]
|
endoplasmic reticulum quality control compartment [GO:0044322]; external side of plasma membrane [GO:0009897]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
asialoglycoprotein receptor activity [GO:0004873]; fucose binding [GO:0042806]; mannose binding [GO:0005537]; signaling receptor activity [GO:0038023]
|
PF00059;PF03954;
|
3.10.100.10;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
| null | null | null | null | null |
FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
|
Homo sapiens (Human)
|
P07308
|
ACOD1_RAT
|
MPAHMLQEISSSYTTTTTITEPPSGNLQNGREKMKKVPLYLEEDIRPEMREDIHDPSYQDEEGPPPKLEYVWRNIILMALLHVGALYGITLIPSSKVYTLLWGIFYYLISALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFLHSLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHAFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAVLARIKRTGDGSHKSS
|
1.14.19.1
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:2892838, ECO:0000305|PubMed:7947684}; Note=Expected to bind 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P13516};
|
brown fat cell differentiation [GO:0050873]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; lipid homeostasis [GO:0055088]; monounsaturated fatty acid biosynthetic process [GO:1903966]; positive regulation of cold-induced thermogenesis [GO:0120162]; response to bacterium [GO:0009617]; response to fatty acid [GO:0070542]; response to nutrient [GO:0007584]; sebaceous gland development [GO:0048733]; sterol homeostasis [GO:0055092]; tarsal gland development [GO:1903699]; triglyceride metabolic process [GO:0006641]; unsaturated fatty acid biosynthetic process [GO:0006636]; white fat cell differentiation [GO:0050872]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
iron ion binding [GO:0005506]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768]
| null | null |
Fatty acid desaturase type 1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:2892838}; Multi-pass membrane protein {ECO:0000269|PubMed:2892838}.
|
CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000269|PubMed:2892838, ECO:0000269|PubMed:7947684};
| null | null | null | null |
FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:2892838, PubMed:7947684). Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:2892838, PubMed:7947684). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:7947684). Required for normal development of sebaceous glands. Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland. Required for normal production of meibum, an oily material that prevents drying of the cornea (By similarity). {ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:2892838, ECO:0000269|PubMed:7947684}.
|
Rattus norvegicus (Rat)
|
P07313
|
MYLK2_RABIT
|
MATENGAVELGIQSLSTDEASKGAASEESLAAEKDPAPPDPEKGPGPSDTKQDPDPSTPKKDANTPAPEKGDVVPAQPSAGGSQGPAGEGGQVEAPAEGSAGKPAALPQQTATAEASEKKPEAEKGPSGHQDPGEPTVGKKVAEGQAAARRGSPAFLHSPSCPAIIASTEKLPAQKPLSEASELIFEGVPATPGPTEPGPAKAEGGVDLLAESQKEAGEKAPGQADQAKVQGDTSRGIEFQAVPSERPRPEVGQALCLPAREEDCFQILDDCPPPPAPFPHRIVELRTGNVSSEFSMNSKEALGGGKFGAVCTCTEKSTGLKLAAKVIKKQTPKDKEMVMLEIEVMNQLNHRNLIQLYAAIETPHEIVLFMEYIEGGELFERIVDEDYHLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSLGVITYMLLSGLSPFLGDDDTETLNNVLSGNWYFDEETFEAVSDEAKDFVSNLIVKEQGARMSAAQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV
|
2.7.11.18
| null |
cardiac muscle tissue morphogenesis [GO:0055008]; phosphorylation [GO:0016310]; regulation of muscle filament sliding [GO:0032971]; striated muscle contraction [GO:0006941]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain binding [GO:0032027]; myosin light chain kinase activity [GO:0004687]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11733062}. Note=Colocalizes with phosphorylated myosin light chain (RLCP) at filaments of the myofibrils.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900, Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.18;
| null | null | null | null |
FUNCTION: Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain. {ECO:0000250}.
|
Oryctolagus cuniculus (Rabbit)
|
P07314
|
GGT1_RAT
|
MKNRFLVLGLVAVVLVFVIIGLCIWLPTTSGKPDHVYSRAAVATDAKRCSEIGRDMLQEGGSVVDAAIASLLCMGLINAHSMGIGGGLFFTIYNSTTRKAEVINAREMAPRLANTSMFNNSKDSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARHGFPVGKGLARALDKKRDIIEKTPALCEVFCRQGKVLQEGETVTMPKLADTLQILAQEGARAFYNGSLTAQIVKDIQEAGGIMTVEDLNNYRAEVIEHPMSIGLGDSTLYVPSAPLSGPVLILILNILKGYNFSPKSVATPEQKALTYHRIVEAFRFAYAKRTMLGDPKFVDVSQVIRNMSSEFYATQLRARITDETTHPTAYYEPEFYLPDDGGTAHLSVVSEDGSAVAATSTINLYFGSKVLSRVSGILFNDEMDDFSSPNFTNQFGVAPSPANFIKPGKQPLSSMCPSIIVDKDGKVRMVVGASGGTQITTSVALAIINSLWFGYDVKRAVEEPRLHNQLLPNTTTVEKNIDQVVTAGLKTRHHHTEVTPDFIAVVQAVVRTSGGWAAASDSRKGGEPAGY
|
2.3.2.2; 3.4.19.13; 3.4.19.14
| null |
amino acid metabolic process [GO:0006520]; cellular response to oxidative stress [GO:0034599]; cysteine biosynthetic process [GO:0019344]; fatty acid metabolic process [GO:0006631]; glutamate metabolic process [GO:0006536]; glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; hepatoblast differentiation [GO:0061017]; hepatocyte differentiation [GO:0070365]; leukotriene D4 biosynthetic process [GO:1901750]; leukotriene metabolic process [GO:0006691]; liver regeneration [GO:0097421]; peptide modification [GO:0031179]; proteolysis [GO:0006508]; regulation of immune system process [GO:0002682]; regulation of inflammatory response [GO:0050727]; response to alcohol [GO:0097305]; response to estradiol [GO:0032355]; response to lipopolysaccharide [GO:0032496]; response to tumor necrosis factor [GO:0034612]; spermatogenesis [GO:0007283]; zymogen activation [GO:0031638]
|
extracellular space [GO:0005615]; plasma membrane [GO:0005886]; vesicle [GO:0031982]
|
aminoacyltransferase activity [GO:0016755]; glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068]; leukotriene-C(4) hydrolase [GO:0002951]; peptidyltransferase activity [GO:0000048]
|
PF01019;
|
1.10.246.130;3.60.20.40;
|
Gamma-glutamyltransferase family
|
PTM: N-glycosylated on both chains; contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. {ECO:0000269|PubMed:6142889}.; PTM: O-glycosylated; close to the membrane anchor on the heavy chain and on the light chain. The sugar moieties are localized to the stretch Thr-28 to Ser-30. Contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. {ECO:0000269|PubMed:2573604}.; PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000250|UniProtKB:P19440}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000305|PubMed:6136502}.
|
CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000269|PubMed:6122208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905; Evidence={ECO:0000305|PubMed:6122208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23906; Evidence={ECO:0000305|PubMed:6122208}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; Evidence={ECO:0000269|PubMed:6122208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808; Evidence={ECO:0000305|PubMed:6122208}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P19440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4; Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14; Evidence={ECO:0000269|PubMed:6122208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564; Evidence={ECO:0000305|PubMed:6122208}; CATALYTIC ACTIVITY: Reaction=(13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + H2O = (13R)-S-cysteinylglycyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + L-glutamate; Xref=Rhea:RHEA:53512, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:137407, ChEBI:CHEBI:137408; Evidence={ECO:0000250|UniProtKB:P19440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53513; Evidence={ECO:0000250|UniProtKB:P19440};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 uM for leukotriene C(4) {ECO:0000269|PubMed:6122208}; KM=5.7 uM for glutathione {ECO:0000269|PubMed:6122208}; KM=5.8 uM for gamma-glutamyl-p-anilide {ECO:0000269|PubMed:6122208};
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PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000305|PubMed:6122208}.; PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. {ECO:0000305|PubMed:6122208}.
| null | null |
FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (By similarity) (PubMed:6122208). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:6122208). In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:6122208). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4 (PubMed:6122208). {ECO:0000250|UniProtKB:P19440, ECO:0000269|PubMed:6122208}.
|
Rattus norvegicus (Rat)
|
P07315
|
CRGC_HUMAN
|
MGKITFYEDRAFQGRSYETTTDCPNLQPYFSRCNSIRVESGCWMLYERPNYQGQQYLLRRGEYPDYQQWMGLSDSIRSCCLIPQTVSHRLRLYEREDHKGLMMELSEDCPSIQDRFHLSEIRSLHVLEGCWVLYELPNYRGRQYLLRPQEYRRCQDWGAMDAKAGSLRRVVDLY
| null | null |
lens development in camera-type eye [GO:0002088]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
structural constituent of eye lens [GO:0005212]
|
PF00030;
|
2.60.20.10;
|
Beta/gamma-crystallin family
| null | null | null | null | null | null | null |
FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.
|
Homo sapiens (Human)
|
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