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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P07320
|
CRGD_HUMAN
|
MGKITLYEDRGFQGRHYECSSDHPNLQPYLSRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCRLIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGSWVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS
| null | null |
cellular response to reactive oxygen species [GO:0034614]; lens development in camera-type eye [GO:0002088]; lens fiber cell differentiation [GO:0070306]; 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)
|
P07321
|
EPO_MOUSE
|
MGVPERPTLLLLLSLLLIPLGLPVLCAPPRLICDSRVLERYILEAKEAENVTMGCAEGPRLSENITVPDTKVNFYAWKRMEVEEQAIEVWQGLSLLSEAILQAQALLANSSQPPETLQLHIDKAISGLRSLTSLLRVLGAQKELMSPPDTTPPAPLRTLTVDTFCKLFRVYANFLRGKLKLYTGEVCRRGDR
| null | null |
acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cardiac muscle tissue morphogenesis [GO:0055008]; cellular hyperosmotic response [GO:0071474]; embryo implantation [GO:0007566]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; erythropoietin-mediated signaling pathway [GO:0038162]; heart morphogenesis [GO:0003007]; hemoglobin biosynthetic process [GO:0042541]; myeloid cell apoptotic process [GO:0033028]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of erythrocyte apoptotic process [GO:1902251]; negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902219]; negative regulation of myeloid cell apoptotic process [GO:0033033]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleate erythrocyte development [GO:0048823]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of transcription by RNA polymerase II [GO:0006357]; response to axon injury [GO:0048678]; response to dexamethasone [GO:0071548]; response to electrical stimulus [GO:0051602]; response to estrogen [GO:0043627]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; response to salt stress [GO:0009651]; response to testosterone [GO:0033574]; response to vitamin A [GO:0033189]; vasculogenesis involved in coronary vascular morphogenesis [GO:0060979]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; visceral serous pericardium development [GO:0061032]
|
cell body [GO:0044297]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; erythropoietin receptor binding [GO:0005128]; hormone activity [GO:0005179]; protein kinase activator activity [GO:0030295]
|
PF00758;
|
1.20.1250.10;
|
EPO/TPO family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3. {ECO:0000250|UniProtKB:P01588}.
|
Mus musculus (Mouse)
|
P07323
|
ENOG_RAT
|
MSIQKIWAREILDSRGNPTVEVDLHTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAEKDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRCITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGEEARFAGHNFRNPSVL
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
|
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; multicellular organismal reproductive process [GO:0048609]; response to estradiol [GO:0032355]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]
|
cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; phosphopyruvate hydratase complex [GO:0000015]; photoreceptor inner segment [GO:0001917]; synaptic membrane [GO:0097060]
|
enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein-containing complex binding [GO:0044877]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
| null | null |
FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival.
|
Rattus norvegicus (Rat)
|
P07327
|
ADH1A_HUMAN
|
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF
|
1.1.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945};
|
alcohol metabolic process [GO:0006066]; ethanol oxidation [GO:0006069]; retinoic acid metabolic process [GO:0042573]; retinol metabolic process [GO:0042572]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; butanol dehydrogenase activity [GO:1990362]; NAD-retinol dehydrogenase activity [GO:0004745]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
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:0000269|PubMed:2738060}; 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:0000269|PubMed:2738060}; 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:2738060}; CATALYTIC ACTIVITY: Reaction=1-propanol + NAD(+) = H(+) + NADH + propanal; Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153, ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:2738060};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 uM for butan-1-ol {ECO:0000269|PubMed:2738060}; KM=14 uM for 1-propanol {ECO:0000269|PubMed:2738060}; KM=6100 uM for ethanol {ECO:0000269|PubMed:2738060};
| null | null | null |
FUNCTION: Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060). {ECO:0000269|PubMed:2738060}.
|
Homo sapiens (Human)
|
P07328
|
NIFD_AZOVI
|
MTGMSREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSKKCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQAPWEASEGAEKVAASA
|
1.18.6.1
|
COFACTOR: Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Note=Binds 1 [8Fe-7S] cluster per heterodimer.; COFACTOR: Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409; Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.;
|
nitrogen fixation [GO:0009399]
|
molybdenum-iron nitrogenase complex [GO:0016612]
|
ATP binding [GO:0005524]; carbonyl sulfide nitrogenase activity [GO:0018697]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; nitrogenase activity [GO:0016163]
|
PF00148;
|
3.40.50.1980;
|
NifD/NifK/NifE/NifN family
| null | null |
CATALYTIC ACTIVITY: Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=1.18.6.1;
| null | null | null | null |
FUNCTION: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
|
Azotobacter vinelandii
|
P07329
|
NIFK_AZOVI
|
MSQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKIDEVFQWTTTKEYQELNFQREALTVNPAKACQPLGAVLCALGFEKTMPYVHGSQGCVAYFRSYFNRHFREPVSCVSDSMTEDAAVFGGQQNMKDGLQNCKATYKPDMIAVSTTCMAEVIGDDLNAFINNSKKEGFIPDEFPVPFAHTPSFVGSHVTGWDNMFEGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIKRMLSEMGVGYSLLSDPEEVLDTPADGQFRMYAGGTTQEEMKDAPNALNTVLLQPWHLEKTKKFVEGTWKHEVPKLNIPMGLDWTDEFLMKVSEISGQPIPASLTKERGRLVDMMTDSHTWLHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKRWKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDFMIGNSYGKFIQRDTLHKGKEFEVPLIRIGFPIFDRHHLHRSTTLGYEGAMQILTTLVNSILERLDEETRGMQATDYNHDLVR
|
1.18.6.1
|
COFACTOR: Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Note=Binds 1 [8Fe-7S] cluster per heterodimer.;
|
nitrogen fixation [GO:0009399]
|
molybdenum-iron nitrogenase complex [GO:0016612]
|
ATP binding [GO:0005524]; carbonyl sulfide nitrogenase activity [GO:0018697]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; nitrogenase activity [GO:0016163]
|
PF11844;PF00148;
|
3.40.50.1980;1.20.89.10;
|
NifD/NifK/NifE/NifN family
| null | null |
CATALYTIC ACTIVITY: Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=1.18.6.1;
| null | null | null | null |
FUNCTION: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
|
Azotobacter vinelandii
|
P07330
|
CHEB_ECOLI
|
MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASLAAHKPLSAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMELSRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPREAINMGGVCEVVDLSQVSQQMLAKISAGQAIRI
|
3.1.1.61; 3.5.1.44
| null |
chemotaxis [GO:0006935]; protein deamination [GO:0018277]; protein demethylation [GO:0006482]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
deaminase binding [GO:1990827]; phosphorelay response regulator activity [GO:0000156]; protein-glutamate methylesterase activity [GO:0008984]; protein-glutamine glutaminase activity [GO:0050568]
|
PF01339;PF00072;
|
3.40.50.2300;3.40.50.180;
|
CheB family
|
PTM: Phosphorylated by CheA (PubMed:2188960, PubMed:3280143). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2188960). {ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:3280143}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:358191}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:358191, ECO:0000269|PubMed:392505}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:6300110, ECO:0000269|PubMed:6304723};
| null | null | null | null |
FUNCTION: Involved in chemotaxis (PubMed:2188960, PubMed:324984, PubMed:358191, PubMed:392505). Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli (PubMed:2188960, PubMed:392505). Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR (PubMed:2188960, PubMed:358191, PubMed:392505). Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (PubMed:6300110, PubMed:6304723). Catalyzes its own deactivation by removing the activating phosphoryl group (PubMed:2188960). {ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:324984, ECO:0000269|PubMed:358191, ECO:0000269|PubMed:392505, ECO:0000269|PubMed:6300110, ECO:0000269|PubMed:6304723}.
|
Escherichia coli (strain K12)
|
P07332
|
FES_HUMAN
|
MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR
|
2.7.10.2
| null |
cardiac muscle cell proliferation [GO:0060038]; cell adhesion [GO:0007155]; cellular response to vitamin D [GO:0071305]; centrosome cycle [GO:0007098]; chemotaxis [GO:0006935]; microtubule bundle formation [GO:0001578]; myoblast proliferation [GO:0051450]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of microtubule polymerization [GO:0031116]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of myeloid cell differentiation [GO:0045639]; positive regulation of neuron projection development [GO:0010976]; protein autophosphorylation [GO:0046777]; regulation of cell adhesion [GO:0030155]; regulation of cell differentiation [GO:0045595]; regulation of cell motility [GO:2000145]; regulation of cell population proliferation [GO:0042127]; regulation of cell shape [GO:0008360]; regulation of mast cell degranulation [GO:0043304]; regulation of vesicle-mediated transport [GO:0060627]
|
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]
|
ATP binding [GO:0005524]; immunoglobulin receptor binding [GO:0034987]; microtubule binding [GO:0008017]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol binding [GO:0035091]; protein tyrosine kinase activity [GO:0004713]
|
PF00611;PF07714;PF00017;
|
1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily
|
PTM: Autophosphorylated on Tyr-713. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK. {ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:18046454, ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19382747, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:7687763}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:11509660, ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:15867340, ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:2656706, ECO:0000269|PubMed:7687763};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. {ECO:0000269|PubMed:11509660, ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:18046454, ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19051325, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:2656706, ECO:0000269|PubMed:8955135}.
|
Homo sapiens (Human)
|
P07333
|
CSF1R_HUMAN
|
MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC
|
2.7.10.1
| null |
axon guidance [GO:0007411]; cell population proliferation [GO:0008283]; cell-cell junction maintenance [GO:0045217]; cellular response to cytokine stimulus [GO:0071345]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cytokine-mediated signaling pathway [GO:0019221]; forebrain neuron differentiation [GO:0021879]; hemopoiesis [GO:0030097]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; macrophage colony-stimulating factor signaling pathway [GO:0038145]; macrophage differentiation [GO:0030225]; mammary gland duct morphogenesis [GO:0060603]; microglial cell proliferation [GO:0061518]; monocyte differentiation [GO:0030224]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; olfactory bulb development [GO:0021772]; osteoclast differentiation [GO:0030316]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation by host of viral process [GO:0044794]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemokine production [GO:0032722]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage proliferation [GO:0120041]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of bone resorption [GO:0045124]; regulation of cell shape [GO:0008360]; regulation of macrophage migration [GO:1905521]; regulation of MAPK cascade [GO:0043408]; response to ischemia [GO:0002931]; ruffle organization [GO:0031529]; signal transduction [GO:0007165]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell surface [GO:0009986]; CSF1-CSF1R complex [GO:1990682]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; macrophage colony-stimulating factor receptor activity [GO:0005011]; protein homodimerization activity [GO:0042803]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]
|
PF00047;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
|
PTM: Autophosphorylated in response to CSF1 or IL34 binding (PubMed:20489731, PubMed:23408870, PubMed:24336230). Phosphorylation at Tyr-561 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-561 and Tyr-809 is important for interaction with SRC family members, including FYN, YES1 and SRC, and for subsequent activation of these protein kinases. Phosphorylation at Tyr-699 and Tyr-923 is important for interaction with GRB2. Phosphorylation at Tyr-723 is important for interaction with PIK3R1. Phosphorylation at Tyr-708 is important for normal receptor degradation. Phosphorylation at Tyr-723 and Tyr-809 is important for interaction with PLCG2. Phosphorylation at Tyr-969 is important for interaction with CBL. Dephosphorylation by PTPN2 negatively regulates downstream signaling and macrophage differentiation. {ECO:0000269|PubMed:16170366, ECO:0000269|PubMed:20489731, ECO:0000269|PubMed:23408870, ECO:0000269|PubMed:24336230}.; PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation. {ECO:0000269|PubMed:16170366}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:16170366, ECO:0000269|PubMed:16648572, ECO:0000269|PubMed:17121910, ECO:0000269|PubMed:18342505, ECO:0000269|PubMed:19193011, ECO:0000269|PubMed:20137931};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for CSF1 and IL34 and 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 in response to IL34 and CSF1, 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 and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding, including the ERK1/2 and the JNK pathway (PubMed:20504948, PubMed:30982609). Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. In the central nervous system, may play a role in the development of microglia macrophages (PubMed:30982608). {ECO:0000269|PubMed:12882960, ECO:0000269|PubMed:15117969, ECO:0000269|PubMed:16170366, ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:16648572, ECO:0000269|PubMed:17121910, ECO:0000269|PubMed:18467591, ECO:0000269|PubMed:18814279, ECO:0000269|PubMed:19193011, ECO:0000269|PubMed:19934330, ECO:0000269|PubMed:20489731, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061, ECO:0000269|PubMed:30982608, ECO:0000269|PubMed:30982609, ECO:0000269|PubMed:7683918}.
|
Homo sapiens (Human)
|
P07334
|
CDR1_SCHPO
|
MVKRHKNTIGVWRLGKTLGTGSTSCVRLAKHAKTGDLAAIKIIPIRYASIGMEILMMRLLRHPNILRLYDVWTDHQHMYLALEYVPDGELFHYIRKHGPLSEREAAHYLSQILDAVAHCHRFRFRHRDLKLENILIKVNEQQIKIADFGMATVEPNDSCLENYCGSLHYLAPEIVSHKPYRGAPADVWSCGVILYSLLSNKLPFGGQNTDVIYNKIRHGAYDLPSSISSAAQDLLHRMLDVNPSTRITIPEVFSHPFLMGCTSLSSMDSTTPPTPSLSIDEIDPLVVDCMCVLWKKSSSKKVVRRLQQRDDNDEKYVYKVLSEILRDDMLKKQRFDENKYLSLYDLIHDNNLFTKASISTTSLVKSNVSTNSRKSSNFEDELARRVSSPLSALNQMSQSPIPIRVSSDKDYDSYACHEVVSNPSTLDDDYNYMFVCPPEEYTYSTDNVRTDSLDLQSLPTPTLEQLESVPFNRYGYVRIFPSTTLSSTASGYYTPDSLSTPEPSIDGLTNLDDVQVGGFVQGSGNQNRRPISFPVISNMQPNITNVRSASAPLCSSPVPSRRYSQYATNARYTPRKVSSGSVLRKISSFFRKD
|
2.7.11.1
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; signaling [GO:0023052]
|
Cdr2 medial cortical node complex [GO:0110115]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; medial cortical node [GO:0071341]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: This protein, a dose-dependent mitotic inducer, appears to function as a negative regulator of mitosis inhibitor wee1 by phosphorylating and inactivating it.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P07335
|
KCRB_RAT
|
MPFSNSHNTQKLRFPAEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIEDRHGGYQPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQPIDDLMPAQK
|
2.7.3.2
| null |
cellular response to estrogen stimulus [GO:0071391]; cellular response to wortmannin [GO:1904568]; cerebellum development [GO:0021549]; futile creatine cycle [GO:0140651]; intracellular chloride ion homeostasis [GO:0030644]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310]
|
cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; ubiquitin protein ligase binding [GO:0031625]
|
PF00217;PF02807;
|
1.10.135.10;3.30.590.10;
|
ATP:guanido phosphotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04447}. Mitochondrion {ECO:0000250|UniProtKB:Q04447}. Cell membrane {ECO:0000250|UniProtKB:P12277}. Note=Localizes to the mitochondria of thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. {ECO:0000250|UniProtKB:Q04447}.
|
CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000250|UniProtKB:Q04447, ECO:0000255|PROSITE-ProRule:PRU10029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158; Evidence={ECO:0000250|UniProtKB:Q04447};
| null | null | null | null |
FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation. During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work. {ECO:0000250|UniProtKB:Q04447}.
|
Rattus norvegicus (Rat)
|
P07338
|
CTRB1_RAT
|
MAFLWLVSCFALVGATFGCGVPTIQPVLTGLSRIVNGEDAIPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVKTSDVVVAGEFDQGSDEENIQVLKIAQVFKNPKFNMFTVRNDITLLKLATPAQFSETVSAVCLPNVDDDFPPGTVCATTGWGKTKYNALKTPEKLQQAALPIVSEADCKKSWGSKITDVMTCAGASGVSSCMGDSGGPLVCQKDGVWTLAGIVSWGSGVCSTSTPAVYSRVTALMPWVQQILEAN
|
3.4.21.1
| null |
digestion [GO:0007586]; positive regulation of apoptotic process [GO:0043065]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; response to cytokine [GO:0034097]; response to food [GO:0032094]; response to nutrient [GO:0007584]; response to peptide hormone [GO:0043434]; response to toxic substance [GO:0009636]
|
extracellular region [GO:0005576]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079};
| null | null | null | null | null |
Rattus norvegicus (Rat)
|
P07339
|
CATD_HUMAN
|
MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL
|
3.4.23.5
| null |
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; autophagosome assembly [GO:0000045]; insulin catabolic process [GO:1901143]; insulin receptor recycling [GO:0038020]; lipoprotein catabolic process [GO:0042159]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; proteolysis [GO:0006508]; regulation of establishment of protein localization [GO:0070201]
|
collagen-containing extracellular matrix [GO:0062023]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
|
aspartic-type endopeptidase activity [GO:0004190]; aspartic-type peptidase activity [GO:0070001]; cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233]
|
PF07966;PF00026;
|
2.40.70.10;
|
Peptidase A1 family
|
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000269|PubMed:27333034}.; PTM: As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified (PubMed:1426530). An additional form starting at Ala-168 has also been identified (PubMed:27333034). {ECO:0000269|PubMed:1426530, ECO:0000269|PubMed:27333034}.
|
SUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted, extracellular space. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380). {ECO:0000269|PubMed:20551380}.
|
CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5;
| null | null | null | null |
FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed:27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. {ECO:0000269|PubMed:27333034}.
|
Homo sapiens (Human)
|
P07340
|
AT1B1_RAT
|
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIIRFLEKYKDSAQKDDMIFEDCGSMPSEPKERGEFNHERGERKVCRFKLDWLGNCSGLNDESYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPLTMKYNPNVLPVQCTGKRDEDKDKVGNIEYFGMGGFYGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTLDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
| null | null |
ATP metabolic process [GO:0046034]; blastocyst development [GO:0001824]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; innate immune response [GO:0045087]; intracellular calcium ion homeostasis [GO:0006874]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; membrane repolarization [GO:0086009]; metal ion transport [GO:0030001]; monoatomic cation transmembrane transport [GO:0098655]; positive regulation of potassium ion import across plasma membrane [GO:1903288]; positive regulation of sodium ion export across plasma membrane [GO:1903278]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; regulation of calcium ion transmembrane transport [GO:1903169]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of gene expression [GO:0010468]; relaxation of cardiac muscle [GO:0055119]; response to hypoxia [GO:0001666]; sodium ion export across plasma membrane [GO:0036376]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; sperm flagellum [GO:0036126]; T-tubule [GO:0030315]
|
ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674]
|
PF00287;
|
1.20.5.170;2.60.40.1660;
|
X(+)/potassium ATPases subunit beta family
|
PTM: Glutathionylated. N-glycosylated (PubMed:14749213). {ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:14749213}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:14749213}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. {ECO:0000250|UniProtKB:P14094}.
| null | null | null | null | null |
FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (PubMed:22328500). Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1 (By similarity). {ECO:0000250|UniProtKB:P05026, ECO:0000269|PubMed:22328500}.; FUNCTION: Involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000269|PubMed:22328500}.
|
Rattus norvegicus (Rat)
|
P07341
|
ALDOB_CHICK
|
MTHQFPALSPEQKKALSDIAQRIVASGKGILAADESVGTMGNRLQRINVENTEENRRAFREILFSSDASISKSIGGVILFHETLYQKDSSGKPFPAIIKEKGMVVGIKLDAGTAPLAGTNGETTIQGLDKLAERCAQYKKDGADFGKWRAVLKISSTTPSQLAIQENANTLARYASICQQNGLVPIVEPEVLPDGDHDLQRCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHSCPKKYTPQDVAVATVTTLLRTVPAAVPGICFLSGGQSEEEASLNLNAMNQSPLPKPWKLTFSYGRALQASALAAWLGKSENKKAAQEAFCKRAQINSLACRGQYVTSGKTDTAATQSLFTASYTY
|
4.1.2.13
| null |
fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate [GO:0061624]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; liver development [GO:0001889]; NADH oxidation [GO:0006116]; negative regulation of pentose-phosphate shunt [GO:1905856]; positive regulation of ATP-dependent activity [GO:0032781]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]
|
centriolar satellite [GO:0034451]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815]
|
ATPase binding [GO:0051117]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-1-phosphate aldolase activity [GO:0061609]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]
|
PF00274;
|
3.20.20.70;
|
Class I fructose-bisphosphate aldolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
| null | null | null |
Gallus gallus (Chicken)
|
P07342
|
ILVB_YEAST
|
MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH
|
2.2.1.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
|
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
|
acetolactate synthase complex [GO:0005948]; mitochondrion [GO:0005739]
|
acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976]
|
PF02775;PF00205;PF02776;
|
3.40.50.970;3.40.50.1220;
|
TPP enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10213630}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; Evidence={ECO:0000269|PubMed:10213630}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25250; Evidence={ECO:0000269|PubMed:10213630}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + H(+) + pyruvate = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + CO2; Xref=Rhea:RHEA:27654, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16763, ChEBI:CHEBI:49256; EC=2.2.1.6; Evidence={ECO:0000305|PubMed:10213630}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27655; Evidence={ECO:0000305|PubMed:10213630};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.6 mM for pyruvate (catalytic subunit only) {ECO:0000269|PubMed:10213630}; KM=18.1 mM for pyruvate (reconstituted into the acetolactate synthase complex with the regulatory subunit) {ECO:0000269|PubMed:10213630};
|
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. {ECO:0000305|PubMed:10213630}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. {ECO:0000305|PubMed:10213630}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:10213630};
| null |
FUNCTION: Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine. {ECO:0000305|PubMed:10213630}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07347
|
ARD1_YEAST
|
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQDENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV
|
2.3.1.255
| null |
N-terminal protein amino acid acetylation [GO:0006474]; N-terminal protein amino acid propionylation [GO:0061606]
|
NatA complex [GO:0031415]
|
identical protein binding [GO:0042802]; peptide-glutamate-alpha-N-acetyltransferase activity [GO:1990190]; peptide-serine-alpha-N-acetyltransferase activity [GO:1990189]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family, ARD1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, ChEBI:CHEBI:133371; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, ChEBI:CHEBI:133375; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
| null | null | null | null |
FUNCTION: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07355
|
ANXA2_HUMAN
|
MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
| null | null |
angiogenesis [GO:0001525]; cell-matrix adhesion [GO:0007160]; collagen fibril organization [GO:0030199]; epithelial cell apoptotic process [GO:1904019]; fibrinolysis [GO:0042730]; lung development [GO:0030324]; membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of low-density lipoprotein particle receptor catabolic process [GO:0032804]; negative regulation of receptor internalization [GO:0002091]; osteoclast development [GO:0036035]; positive regulation of exocytosis [GO:0045921]; positive regulation of low-density lipoprotein particle clearance [GO:1905581]; positive regulation of low-density lipoprotein particle receptor binding [GO:1905597]; positive regulation of low-density lipoprotein receptor activity [GO:1905599]; positive regulation of plasma membrane repair [GO:1905686]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of receptor recycling [GO:0001921]; positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vacuole organization [GO:0044090]; positive regulation of vesicle fusion [GO:0031340]; regulation of neurogenesis [GO:0050767]; response to activity [GO:0014823]; vesicle budding from membrane [GO:0006900]
|
adherens junction [GO:0005912]; AnxA2-p11 complex [GO:1990665]; azurophil granule lumen [GO:0035578]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; myelin sheath adaxonal region [GO:0035749]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; PCSK9-AnxA2 complex [GO:1990667]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; RNA polymerase II transcription regulator complex [GO:0090575]; sarcolemma [GO:0042383]; Schmidt-Lanterman incisure [GO:0043220]; vesicle [GO:0031982]
|
cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; protease binding [GO:0002020]; RNA binding [GO:0003723]; S100 protein binding [GO:0044548]; serine-type endopeptidase inhibitor activity [GO:0004867]; virion binding [GO:0046790]
|
PF00191;
|
1.10.220.10;
|
Annexin family
|
PTM: Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface. {ECO:0000269|PubMed:15302870, ECO:0000269|PubMed:2946940}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism.
| null | null | null | null | null |
FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640). {ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.; FUNCTION: (Microbial infection) Binds M.pneumoniae CARDS toxin, probably serves as one receptor for this pathogen. When ANXA2 is down-regulated by siRNA, less toxin binds to human cells and less vacuolization (a symptom of M.pneumoniae infection) is seen. {ECO:0000269|PubMed:25139904}.
|
Homo sapiens (Human)
|
P07356
|
ANXA2_MOUSE
|
MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAVKTKGVDEVTIVNILTNRSNVQRQDIAFAYQRRTKKELPSALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
| null | null |
angiogenesis [GO:0001525]; body fluid secretion [GO:0007589]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; collagen fibril organization [GO:0030199]; epithelial cell apoptotic process [GO:1904019]; fibrinolysis [GO:0042730]; lung development [GO:0030324]; membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of low-density lipoprotein particle receptor catabolic process [GO:0032804]; negative regulation of receptor internalization [GO:0002091]; osteoclast development [GO:0036035]; positive regulation of exocytosis [GO:0045921]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of low-density lipoprotein particle clearance [GO:1905581]; positive regulation of low-density lipoprotein particle receptor binding [GO:1905597]; positive regulation of low-density lipoprotein receptor activity [GO:1905599]; positive regulation of plasma membrane repair [GO:1905686]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor recycling [GO:0001921]; positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vacuole organization [GO:0044090]; positive regulation of vesicle fusion [GO:0031340]; protein localization to plasma membrane [GO:0072659]; regulation of neurogenesis [GO:0050767]; response to activity [GO:0014823]; vesicle budding from membrane [GO:0006900]
|
AnxA2-p11 complex [GO:1990665]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; macropinosome [GO:0044354]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; midbody [GO:0030496]; myelin sheath adaxonal region [GO:0035749]; nuclear matrix [GO:0016363]; PCSK9-AnxA2 complex [GO:1990667]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]; ruffle [GO:0001726]; sarcolemma [GO:0042383]; Schmidt-Lanterman incisure [GO:0043220]; vesicle [GO:0031982]
|
bone sialoprotein binding [GO:0044730]; cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; protease binding [GO:0002020]; S100 protein binding [GO:0044548]; serine-type endopeptidase inhibitor activity [GO:0004867]; small GTPase binding [GO:0031267]; virion binding [GO:0046790]
|
PF00191;
|
1.10.220.10;
|
Annexin family
|
PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
| null | null | null | null | null |
FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:22848640). {ECO:0000250|UniProtKB:P07355, ECO:0000269|PubMed:22848640}.
|
Mus musculus (Mouse)
|
P07357
|
CO8A_HUMAN
|
MFAVVFFILSLMTCQPGVTAQEKVNQRVRRAATPAAVTCQLSNWSEWTDCFPCQDKKYRHRSLLQPNKFGGTICSGDIWDQASCSSSTTCVRQAQCGQDFQCKETGRCLKRHLVCNGDQDCLDGSDEDDCEDVRAIDEDCSQYEPIPGSQKAALGYNILTQEDAQSVYDASYYGGQCETVYNGEWRELRYDSTCERLYYGDDEKYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKDKSDSFGVTIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRKDDIMLDEGMLQSLMELPDQYNYGMYAKFINDYGTHYITSGSMGGIYEYILVIDKAKMESLGITSRDITTCFGGSLGIQYEDKINVGGGLSGDHCKKFGGGKTERARKAMAVEDIISRVRGGSSGWSGGLAQNRSTITYRSWGRSLKYNPVVIDFEMQPIHEVLRHTSLGPLEAKRQNLRRALDQYLMEFNACRCGPCFNNGVPILEGTSCRCQCRLGSLGAACEQTQTEGAKADGSWSCWSSWSVCRAGIQERRRECDNPAPQNGGASCPGRKVQTQAC
| null | null |
complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886]
|
complement binding [GO:0001848]; protein-containing complex binding [GO:0044877]
|
PF21195;PF00057;PF01823;PF00090;
|
4.10.400.10;2.20.100.10;
|
Complement C6/C7/C8/C9 family
| null |
SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane protein. Note=Secreted as soluble protein. Inserts into the cell membrane of target cells.
| null | null | null | null | null |
FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself. {ECO:0000269|PubMed:17872444, ECO:0000269|PubMed:7440581}.
|
Homo sapiens (Human)
|
P07358
|
CO8B_HUMAN
|
MKNSRTWAWRAPVELFLLCAALGCLSLPGSRGERPHSFGSNAVNKSFAKSRQMRSVDVTLMPIDCELSSWSSWTTCDPCQKKRYRYAYLLQPSQFHGEPCNFSDKEVEDCVTNRPCGSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRRIYKKCQHEMDQYWGIGSLASGINLFTNSFEGPVLDHRYYAGGCSPHYILNTRFRKPYNVESYTPQTQGKYEFILKEYESYSDFERNVTEKMASKSGFSFGFKIPGIFELGISSQSDRGKHYIRRTKRFSHTKSVFLHARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIYEYTLVMNKEAMERGDYTLNNVHACAKNDFKIGGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDTMVEDLVVLVRGGASEHITTLAYQELPTADLMQEWGDAVQYNPAIIKVKVEPLYELVTATDFAYSSTVRQNMKQALEEFQKEVSSCHCAPCQGNGVPVLKGSRCDCICPVGSQGLACEVSYRKNTPIDGKWNCWSNWSSCSGRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS
| null | null |
complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; membrane [GO:0016020]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886]
|
protein-containing complex binding [GO:0044877]
|
PF21195;PF00057;PF01823;PF00090;
|
4.10.400.10;2.20.100.10;
|
Complement C6/C7/C8/C9 family
|
PTM: N-glycosylated; contains one or two bound glycans. Not O-glycosylated. {ECO:0000269|PubMed:10551839, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2820472}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
|
Homo sapiens (Human)
|
P07359
|
GP1BA_HUMAN
|
MPLLLLLLLLPSPLHPHPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHTTPWGLFYSWSTASLDSQMPSSLHPTQESTKEQTTFPPRWTPNFTLHMESITFSKTPKSTTEPTPSPTTSEPVPEPAPNMTTLEPTPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTPIPTIATSPTILVSATSLITPKSTFLTTTKPVSLLESTKKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDFCCLLPLGFYVLGLFWLLFASVVLILLLSWVGHVKPQALDSGQGAALTTATQTTHLELQRGRQVTVPRAWLLFLRGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLSTVSIRYSGHSL
| null | null |
blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; cell surface receptor signaling pathway [GO:0007166]; fibrinolysis [GO:0042730]; megakaryocyte development [GO:0035855]; platelet activation [GO:0030168]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of platelet activation [GO:0010572]; regulation of blood coagulation [GO:0030193]; release of sequestered calcium ion into cytosol [GO:0051209]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glycoprotein Ib-IX-V complex [GO:1990779]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
thrombin-activated receptor activity [GO:0015057]
|
PF13855;PF01462;
|
3.80.10.10;
| null |
PTM: Glycocalicin is the product of a proteolytic cleavage/shedding, catalyzed by ADAM17, which releases most of the extracellular domain. Binding sites for vWF and thrombin are in this part of the protein. {ECO:0000269|PubMed:17445093}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
|
Homo sapiens (Human)
|
P07360
|
CO8G_HUMAN
|
MLPPGTATLLTLLLAAGSLGQKPQRPRRPASPISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHVAPQGTAMAVSTFRKLDGICWQVRQLYGDTGVLGRFLLQARDARGAVHVVVAETDYQSFAVLYLERAGQLSVKLYARSLPVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFHVLDEVRR
| null | null |
complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886]
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complement binding [GO:0001848]; protein-containing complex binding [GO:0044877]; retinol binding [GO:0019841]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol.
|
Homo sapiens (Human)
|
P07363
|
CHEA_ECOLI
|
MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYICQALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA
|
2.7.13.3
| null |
aerotaxis [GO:0009454]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935]; establishment of localization in cell [GO:0051649]; negative regulation of protein modification process [GO:0031400]; phosphorelay signal transduction system [GO:0000160]; phosphorylation [GO:0016310]; positive regulation of post-translational protein modification [GO:1901875]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of chemotaxis [GO:0050920]; signal transduction [GO:0007165]; thermotaxis [GO:0043052]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673]
|
PF01584;PF09078;PF02895;PF02518;PF01627;
|
3.30.70.400;1.10.287.560;3.30.565.10;1.20.120.160;2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
| null | null | null | null |
FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
|
Escherichia coli (strain K12)
|
P07371
|
CB22_PEA
|
MAASSSSSMALSSPTLAGKQLKLNPSSQELGAARFTMRKSATTKKVASSGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFSKNRELEVIHSRWAMLGALGCVFPELLSRNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWSYATNFVPGK
| null |
COFACTOR: Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin. {ECO:0000305|PubMed:15719016};
|
photosynthesis, light harvesting in photosystem I [GO:0009768]; response to light stimulus [GO:0009416]
|
chloroplast envelope [GO:0009941]; chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522]; photosystem II [GO:0009523]; plastoglobule [GO:0010287]
|
chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872]
|
PF00504;
|
1.10.3460.10;
|
Light-harvesting chlorophyll a/b-binding (LHC) protein family
|
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
|
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. {ECO:0000269|PubMed:2174365}.; FUNCTION: May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen. {ECO:0000269|PubMed:2174365}.
|
Pisum sativum (Garden pea) (Lathyrus oleraceus)
|
P07374
|
UREA_CANEN
|
MKLSPREVEKLGLHNAGYLAQKRLARGVRLNYTEAVALIASQIMEYARDGEKTVAQLMCLGQHLLGRRQVLPAVPHLLNAVQVEATFPDGTKLVTVHDPISRENGELQEALFGSLLPVPSLDKFAETKEDNRIPGEILCEDECLTLNIGRKAVILKVTSKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGTAVRFEPGDCKSVTLVSIEGNKVIRGGNAIADGPVNETNLEAAMHAVRSKGFGHEEEKDASEGFTKEDPNCPFNTFIHRKEYANKYGPTTGDKIRLGDTNLLAEIEKDYALYGDECVFGGGKVIRDGMGQSCGHPPAISLDTVITNAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFSNMIIGANTEVIAGEGLIVTAGAIDCHVHYICPQLVYEAISSGITTLVGGGTGPAAGTRATTCTPSPTQMRLMLQSTDDLPLNFGFTGKGSSSKPDELHEIIKAGAMGLKLHEDWGSTPAAIDNCLTIAEHHDIQINIHTDTLNEAGFVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGIKNVLPSSTNPTRPLTSNTIDEHLDMLMVCHHLDREIPEDLAFAHSRIRKKTIAAEDVLNDIGAISIISSDSQAMGRVGEVISRTWQTADKMKAQTGPLKCDSSDNDNFRIRRYIAKYTINPAIANGFSQYVGSVEVGKLADLVMWKPSFFGTKPEMVIKGGMVAWADIGDPNASIPTPEPVKMRPMYGTLGKAGGALSIAFVSKAALDQRVNVLYGLNKRVEAVSNVRKLTKLDMKLNDALPEITVDPESYTVKADGKLLCVSEATTVPLSRNYFLF
|
3.5.1.5
|
COFACTOR: Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000269|PubMed:11696010, ECO:0000269|PubMed:20471401}; Note=Binds 2 nickel ions per subunit. {ECO:0000269|PubMed:20471401};
|
nitrogen compound metabolic process [GO:0006807]; urea catabolic process [GO:0043419]
|
urease complex [GO:0035550]
|
nickel cation binding [GO:0016151]; toxin activity [GO:0090729]; urease activity [GO:0009039]
|
PF01979;PF00449;PF00699;PF00547;PF18473;
|
3.20.20.140;2.10.150.10;3.30.280.10;2.30.40.10;
|
Metallo-dependent hydrolases superfamily, Urease alpha subunit family
|
PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000269|PubMed:20471401}.
| null |
CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000269|PubMed:11696010}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20558; Evidence={ECO:0000269|PubMed:11696010};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for urea (at 37 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:11696010}; KM=2.9 mM for urea (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:11696010}; KM=7.1 mM for urea (at 37 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:11696010}; Vmax=6000 umol/min/mg enzyme (at 37 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:11696010}; Vmax=13700 umol/min/mg enzyme (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:11696010}; Vmax=26700 umol/min/mg enzyme (at 37 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:11696010};
|
PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000305}.
| null | null |
FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism (PubMed:26690979). Is known to be highly toxic and lethal when given by intravenous route, producing convulsions and other signs of central nervous system intoxication associated with the high levels of ammonia formed in the blood of mice and rabbits (PubMed:26690979). Is neurotoxic in mammals, when directly injected into hippocampus (PubMed:33631299). It may induce seizures by acting at a neuronal network level, thereby disturbing electroencephalographic rhythms and causing metabolic alterations in key areas related to epileptogenesis and to neurogenic pulmonary edema (PubMed:33631299). It increases calcium influx and neuronal firing rate in the hippocampus (PubMed:33631299). Is able to insert itself into lipid bilayers, altering physicochemical properties of artificial membranes, and forming cation-selective ion channels (PubMed:24583269). In vitro, has the ability to induce platelet aggregation, platelet granules secretion and release of ATP (PubMed:11696010). In contrast to canatoxin, another urease from C.ensiformis, is not lethal to mice when intraperitoneally injected (PubMed:11696010). {ECO:0000269|PubMed:11696010, ECO:0000269|PubMed:24583269, ECO:0000269|PubMed:33631299, ECO:0000305|PubMed:26690979}.
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Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
|
P07379
|
PCKGC_RAT
|
MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALTDPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIELTDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCAHPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPKEDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
|
2.7.11.-; 4.1.1.32
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895};
|
cellular hyperosmotic response [GO:0071474]; cellular hyperosmotic salinity response [GO:0071475]; cellular hypotonic response [GO:0071476]; cellular hypotonic salinity response [GO:0071477]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to fructose stimulus [GO:0071332]; cellular response to glucagon stimulus [GO:0071377]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to interleukin-1 [GO:0071347]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; cellular response to potassium ion starvation [GO:0051365]; cellular response to raffinose [GO:0097403]; cellular response to retinoic acid [GO:0071300]; cellular response to tumor necrosis factor [GO:0071356]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol biosynthetic process from pyruvate [GO:0046327]; hepatocyte differentiation [GO:0070365]; lipid metabolic process [GO:0006629]; oxaloacetate metabolic process [GO:0006107]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of transcription by RNA polymerase II [GO:0045944]; propionate catabolic process [GO:0019543]; regulation of lipid biosynthetic process [GO:0046890]; response to activity [GO:0014823]; response to bacterium [GO:0009617]; response to insulin [GO:0032868]; response to interleukin-6 [GO:0070741]; response to lipid [GO:0033993]; response to lipopolysaccharide [GO:0032496]; response to methionine [GO:1904640]; response to nutrient levels [GO:0031667]; response to starvation [GO:0042594]; tricarboxylic acid metabolic process [GO:0072350]
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cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]
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carboxylic acid binding [GO:0031406]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; nucleoside diphosphate kinase activity [GO:0004550]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; phosphoenolpyruvate carboxykinase activity [GO:0004611]; protein serine kinase activity (using GTP as donor) [GO:0106264]
|
PF00821;PF17297;
|
3.90.228.20;3.40.449.10;2.170.8.10;
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Phosphoenolpyruvate carboxykinase [GTP] family
|
PTM: Acetylated (PubMed:30193097). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5; acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.; PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation (PubMed:30193097). Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2 (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.; PTM: Ubiquitination by UBR5 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P35558}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:4186849}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.
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CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:31461616}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:30193097}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390; Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:30193097}; CATALYTIC ACTIVITY: Reaction=GTP + L-seryl-[protein] = GDP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P35558}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021; Evidence={ECO:0000250|UniProtKB:P35558};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for oxaloacetate {ECO:0000269|PubMed:30193097}; KM=161 uM for GTP {ECO:0000269|PubMed:30193097}; KM=301 uM for phosphoenolpyruvate {ECO:0000269|PubMed:30193097}; KM=79 uM for GDP {ECO:0000269|PubMed:30193097}; KM=475 uM for phosphoenolpyruvate (for phosphoenolpyruvate carboxykinase in the backward reaction) {ECO:0000269|PubMed:26709450}; KM=207 uM for GDP (for phosphoenolpyruvate carboxykinase in the backward reaction) {ECO:0000269|PubMed:26709450}; KM=435 uM for CO2 (for phosphoenolpyruvate carboxykinase in the backward reaction) {ECO:0000269|PubMed:26709450}; KM=51 uM for oxaloacetate (for phosphoenolpyruvate carboxykinase in the forward reaction) {ECO:0000269|PubMed:26709450}; KM=55 uM for GTP (for phosphoenolpyruvate carboxykinase in the forward reaction) {ECO:0000269|PubMed:26709450}; Note=kcat is 76 sec(-1) with oxaloacetate as substrate (PubMed:30193097). kcat is 27 sec(-1) with phosphoenolpyruvate as substrate (PubMed:30193097). kcat is 65 sec(-1) with GTP as substrate (PubMed:30193097). kcat is 25 sec(-1) with GDP as substrate (PubMed:30193097). kcat is 52 sec(-1) with phosphoenolpyruvate carboxykinase in the forward reaction (PubMed:26709450). kcat is 19 sec(-1) with phosphoenolpyruvate carboxykinase in the backward forward reaction (PubMed:26709450). {ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:30193097};
|
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000269|PubMed:30193097}.
| null | null |
FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:26322521, PubMed:26709450, PubMed:28345895, PubMed:30193097, PubMed:31461616, PubMed:4186849). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:30193097). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProtKB:Q9Z2V4, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:31461616, ECO:0000269|PubMed:4186849}.
|
Rattus norvegicus (Rat)
|
P07384
|
CAN1_HUMAN
|
MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
|
3.4.22.52
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8954105, ECO:0000269|PubMed:9271093}; Note=Binds 4 Ca(2+) ions. {ECO:0000269|PubMed:9271093};
|
mammary gland involution [GO:0060056]; positive regulation of cell population proliferation [GO:0008284]; proteolysis [GO:0006508]; receptor catabolic process [GO:0032801]; regulation of catalytic activity [GO:0050790]; regulation of macroautophagy [GO:0016241]; regulation of NMDA receptor activity [GO:2000310]; self proteolysis [GO:0097264]
|
calpain complex [GO:0110158]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; peptidase activity [GO:0008233]
|
PF01067;PF13833;PF00648;
|
2.60.120.380;3.90.70.10;1.10.238.10;
|
Peptidase C2 family
|
PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms. {ECO:0000269|PubMed:8769305, ECO:0000269|PubMed:8954105}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:8769305}. Cell membrane {ECO:0000269|PubMed:8769305}. Note=Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719). {ECO:0000269|PubMed:21531719}.
|
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000269|PubMed:16411745, ECO:0000269|PubMed:19617626, ECO:0000269|PubMed:21531719};
| null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:19617626, PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). Cleaves and activates caspase-7 (CASP7) (PubMed:19617626). {ECO:0000269|PubMed:19617626, ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:23707407, ECO:0000269|PubMed:2400579}.
|
Homo sapiens (Human)
|
P07395
|
SYFB_ECOLI
|
MKFSELWLREWVNPAIDSDALANQITMAGLEVDGVEPVAGSFHGVVVGEVVECAQHPNADKLRVTKVNVGGDRLLDIVCGAPNCRQGLRVAVATIGAVLPGDFKIKAAKLRGEPSEGMLCSFSELGISDDHSGIIELPADAPIGTDIREYLKLDDNTIEISVTPNRADCLGIIGVARDVAVLNQLPLVQPEIVPVGATIDDTLPITVEAPEACPRYLGRVVKGINVKAPTPLWMKEKLRRCGIRSIDAVVDVTNYVLLELGQPMHAFDKDRIEGGIVVRMAKEGETLVLLDGTEAKLNADTLVIADHNKALAMGGIFGGEHSGVNDETQNVLLECAFFSPLSITGRARRHGLHTDASHRYERGVDPALQHKAMERATRLLIDICGGEAGPVIDITNEATLPKRATITLRRSKLDRLIGHHIADEQVTDILRRLGCEVTEGKDEWQAVAPSWRFDMEIEEDLVEEVARVYGYNNIPDEPVQASLIMGTHREADLSLKRVKTLLNDKGYQEVITYSFVDPKVQQMIHPGVEALLLPSPISVEMSAMRLSLWTGLLATVVYNQNRQQNRVRIFESGLRFVPDTQAPLGIRQDLMLAGVICGNRYEEHWNLAKETVDFYDLKGDLESVLDLTGKLNEVEFRAEANPALHPGQSAAIYLKGERIGFVGVVHPELERKLDLNGRTLVFELEWNKLADRVVPQAREISRFPANRRDIAVVVAENVPAADILSECKKVGVNQVVGVNLFDVYRGKGVAEGYKSLAISLILQDTSRTLEEEEIAATVAKCVEALKERFQASLRD
|
6.1.1.20
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
|
phenylalanyl-tRNA aminoacylation [GO:0006432]
|
cytosol [GO:0005829]; membrane [GO:0016020]; phenylalanine-tRNA ligase complex [GO:0009328]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049]
|
PF03483;PF03484;PF03147;PF01588;PF17759;
|
3.30.56.10;3.30.70.380;2.40.50.140;3.50.40.10;
|
Phenylalanyl-tRNA synthetase beta subunit family, Type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P07396
|
PG062_VACCW
|
MNSHFASAHTPFYINTKEGRYLVLKAVKVCDVRTVECEGSKASCVLKVDKPSSPACERRPSSPSRCERMNNPRKQVPFMRTDMLQNMFAANRDNVASRLLN
| null | null |
suppression by virus of host type I interferon production [GO:0039501]; symbiont-mediated suppression of host innate immune response [GO:0052170]; viral protein processing [GO:0019082]
|
host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
|
DNA binding [GO:0003677]; molecular sequestering activity [GO:0140313]
|
PF04767;
| null |
Orthopoxvirus OPG062 family
|
PTM: Phosphorylated on two serines. While these phosphorylations do not play a role in virion assembly; they are essential for the interaction with host RICTOR and RPTOR. {ECO:0000269|PubMed:20392848, ECO:0000269|PubMed:30078703}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000305|PubMed:16877059}. Note=Major component of the virion comprising about 10% of the virion mass. {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays an essential role in virion assembly and morphogenesis (PubMed:20392848). Also plays a role in the inhibition of host immune response by dysregulating mTOR. Sequesters host RICTOR and RPTOR, thereby disrupting mTORC1 and mTORC2 crosstalk. In turn, blocks the host antiviral response in part through mTOR-dependent degradation of cGAS, the primary poxvirus sensor (PubMed:30078703). {ECO:0000269|PubMed:20392848, ECO:0000269|PubMed:30078703}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07399
|
GLYC_LYCVW
|
MGQIVTMFEALPHIIDEVINIVIIVLIIITSIKAVYNFATCGILALVSFLFLAGRSCGMYGLNGPDIYKGVYQFKSVEFDMSHLNLTMPNACSVNNSHHYISMGSSGLEPTFTNDSILNHNFCNLTSALNKKSFDHTLMSIVSSLHLSIRGNSNYKAVSCDFNNGITIQYNLSSSDPQSAMSQCRTFRGRVLDMFRTAFGGKYMRSGWGWTGSDGKTTWCSQTSYQYLIIQNRTWENHCRYAGPFGMSRILFAQEKTKFLTRRLSGTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDEEFCDMLRLIDYNKAALSKFKQDVESALHVFKTTLNSLISDQLLMRNHLRDLMGVPYCNYSKFWYLEHAKTGETSVPKCWLVTNGSYLNETHFSDQIEQEADNMITEMLRKDYIKRQGSTPLALMDLLMFSTSAYLISIFLHFVRIPTHRHIKGGSCPKPHRLTNKGICSCGAFKVPGVKTIWKRR
| null | null |
fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062]
|
host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
metal ion binding [GO:0046872]
|
PF00798;
|
6.10.140.1590;2.20.28.180;
|
Arenaviridae GPC protein family
|
PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase. {ECO:0000255|HAMAP-Rule:MF_04084}.
|
SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. {ECO:0000255|HAMAP-Rule:MF_04084}.
| null | null | null | null | null |
FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: [Glycoprotein G1]: Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface. Down-modulates host DAG1. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: [Glycoprotein G2]: Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification. {ECO:0000255|HAMAP-Rule:MF_04084}.
|
Lymphocytic choriomeningitis virus (strain WE) (LCMV)
|
P07410
|
HBB_UROTO
|
VHLTDGEKNAISTAWGKVNAAEIGAEALGRLLVVYPWTQRFFDSFGDLSSASAVMGNAKVKAHGKKVIDSFSNGLKHLDNLKGTFASLSELHCDKLHVDPENFKLLGNMIVIVMAHHLGKDFTPEAQAAFQKVVAGVANALSHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Urocitellus townsendii (Townsend's ground squirrel) (Spermophilus townsendii)
|
P07412
|
HBB_FELCA
|
GFLTAEEKGLVNGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSSADAIMSNAKVKAHGKKVLNSFSDGLKNIDDLKGAFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGHDFNPQVQAAFQKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Felis catus (Cat) (Felis silvestris catus)
|
P07428
|
HBA_XENTR
|
MHLTADDKKHIKAIWPSVAAHGDKYGGEALHRMFMCAPKTKTYFPDFDFSEHSKHILAHGKKVSDALNEACNHLDNIAGCLSKLSDLHAYDLRVDPGNFPLLAHQILVVVAIHFPKQFDPATHKALDKFLVSVSNVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
P07429
|
HBB1_XENTR
|
MVNLTAKERQLITGTWSKICAKTLGKQALGSMLYTYPWTQRYFSSFGNLSSIEAIFHNAAVATHGEKVLTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPYNFKRFCSCTIISMAQTLQEDFTPELQAAFEKLFAAIADALGKGYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
P07432
|
HBB1_XENBO
|
MGLTAHDRQLINSTWGKVCAKTIGKEALGRLLWTYPWTQRYFSSFGNLNSADAVFHNEAVAAHGEKVVTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPCNFKRFGGCLSISLARQFHEEYTPELHAAYEHLFDAIADALGKGYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus borealis (Kenyan clawed frog)
|
P07433
|
HBB2_XENBO
|
MGLTAHEKQLITGSWGKINAKAIGKEALGRLLNTFPWTQRYFSSFGNLGSAEAIFHNEAVAAHGEKVVTSVGEAIKHMDDIKGYYAELSKYHSETLHVDPNNFKRFGGCLSITLGHHFGEEYTPELHAAYEHLFDAIADALGKGYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus borealis (Kenyan clawed frog)
|
P07437
|
TBB5_HUMAN
|
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
cell division [GO:0051301]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule cytoskeleton organization [GO:0000226]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; natural killer cell mediated cytotoxicity [GO:0042267]; odontoblast differentiation [GO:0071895]; regulation of synapse organization [GO:0050807]; spindle assembly [GO:0051225]
|
azurophil granule lumen [GO:0035578]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intercellular bridge [GO:0045171]; membrane raft [GO:0045121]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; nuclear envelope lumen [GO:0005641]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; MHC class I protein binding [GO:0042288]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]; ubiquitin protein ligase binding [GO:0031625]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866, PubMed:28576883). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P99024, ECO:0000269|PubMed:26875866, ECO:0000269|PubMed:28576883}.; PTM: Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility (Probable) (PubMed:28576883). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally (Probable) (PubMed:28576883). {ECO:0000269|PubMed:28576883, ECO:0000305|PubMed:19524510}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000269|PubMed:16371510}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26637975}.
| null | null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Homo sapiens (Human)
|
P07438
|
MT1B_HUMAN
|
MDPNCSCTTGGSCACAGSCKCKECKCTSCKKCCCSCCPVGCAKCAQGCVCKGSSEKCRCCA
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]
|
PF00131;
|
4.10.10.10;
|
Metallothionein superfamily, Type 1 family
| null | null | null | null | null | null | null |
FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
|
Homo sapiens (Human)
|
P07445
|
SDIS_PSEPU
|
MNLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVEDPFGQPPIHGREQIAAFYRQGLGGGKVRACLTGPVRASHNGCGAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYWSEVNLSVREPQ
|
5.3.3.1
| null |
steroid metabolic process [GO:0008202]
| null |
steroid delta-isomerase activity [GO:0004769]
|
PF12680;
|
3.10.450.50;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid; Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909; EC=5.3.3.1;
| null | null | null | null | null |
Pseudomonas putida (Arthrobacter siderocapsulatus)
|
P07451
|
CAH3_HUMAN
|
MAKEWGYASHNGPDHWHELFPNAKGENQSPVELHTKDIRHDPSLQPWSVSYDGGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLPGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFKEALKQRDGIAVIGIFLKIGHENGEFQIFLDALDKIKTKGKEAPFTKFDPSCLFPACRDYWTYQGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLLSSAENEPPVPLVSNWRPPQPINNRVVRASFK
|
4.2.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958};
|
one-carbon metabolic process [GO:0006730]; response to bacterium [GO:0009617]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
carbonate dehydratase activity [GO:0004089]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
|
PTM: S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione. {ECO:0000250|UniProtKB:P14141}.; PTM: S-glutathionylated in hepatocytes under oxidative stress. {ECO:0000250|UniProtKB:P14141}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618712}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52 mM for CO(2) {ECO:0000269|PubMed:18618712};
| null | null | null |
FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712}.
|
Homo sapiens (Human)
|
P07455
|
IGF1_BOVIN
|
MGKISSLPTQLFKCCFCDFLKQVKMPITSSSHLFYLALCLLAFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKAQKEVHLKNTSRGSAGNKNYRM
| null | null |
cell population proliferation [GO:0008283]; hyperosmotic salinity response [GO:0042538]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903407]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903408]; regulation of protein phosphorylation [GO:0001932]; response to electrical stimulus [GO:0051602]; response to food [GO:0032094]; response to growth hormone [GO:0060416]; response to insulin [GO:0032868]; response to magnetism [GO:0071000]
|
alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation. Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (By similarity). As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250|UniProtKB:P05017, ECO:0000250|UniProtKB:P05019, ECO:0000250|UniProtKB:P08025}.
|
Bos taurus (Bovine)
|
P07456
|
IGF2_BOVIN
|
MGITAGKSVLVLLAFLAFASCCYAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSASTTVLPDDVTAYPVGKFFQYDIWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHGGASSKASSD
| null | null |
embryonic placenta development [GO:0001892]; embryonic placenta morphogenesis [GO:0060669]; glucose metabolic process [GO:0006006]; in utero embryonic development [GO:0001701]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ossification [GO:0001503]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; regulation of muscle cell differentiation [GO:0051147]; response to insulin [GO:0032868]
|
extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF08365;PF00049;
|
1.10.100.10;
|
Insulin family
|
PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000250|UniProtKB:P01344}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
| null | null | null | null | null |
FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver. Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity). {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.; FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as a physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
|
Bos taurus (Bovine)
|
P07463
|
CALM_PARTE
|
MAEQLTEEQIAEFKEAFALFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLSLMARKMKEQDSEEELIEAFKVFDRDGNGLISAAELRHVMTNLGEKLTDDEVDEMIREADIDGDGHINYEEFVRMMVSK
| null | null | null | null |
calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234]
|
PF13499;
|
1.10.238.10;
|
Calmodulin family
|
PTM: The pantophobiac mutant CAM2 is undermethylated on Lys-116.
| null | null | null | null | null | null |
FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
|
Paramecium tetraurelia
|
P07464
|
THGA_ECOLI
|
MNMPMTERIRAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRDKHYYFKDYKVESSV
|
2.3.1.18
| null |
lactose biosynthetic process [GO:0005989]
|
cytoplasm [GO:0005737]
|
galactoside O-acetyltransferase activity [GO:0008870]; identical protein binding [GO:0042802]
|
PF00132;PF12464;
|
2.160.10.10;
|
Transferase hexapeptide repeat family
|
PTM: The N-terminus of this protein is heterogeneous because the initiator methionine is only partially cleaved. {ECO:0000269|PubMed:3922433}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3922433}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactoside + acetyl-CoA = a 6-acetyl-beta-D-galactoside + CoA; Xref=Rhea:RHEA:15713, ChEBI:CHEBI:28034, ChEBI:CHEBI:28250, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.18; Evidence={ECO:0000269|PubMed:14009486, ECO:0000269|PubMed:4630409};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for acetyl-CoA {ECO:0000269|PubMed:4630409}; KM=0.104 mM for acetyl-CoA {ECO:0000269|PubMed:7592843}; KM=0.77 M for isopropyl beta-D-1-thiogalactopyranoside {ECO:0000269|PubMed:4630409}; KM=63.4 mM for p-nitrophenyl-b-D-galactopyranoside {ECO:0000269|PubMed:7592843};
| null | null | null |
FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to the 6-O-methyl position of a range of galactosides, glucosides, and lactosides (PubMed:14009486, PubMed:4630409, PubMed:7592843). May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into the cell (Probable). {ECO:0000269|PubMed:14009486, ECO:0000269|PubMed:4630409, ECO:0000269|PubMed:7592843, ECO:0000305|PubMed:11937062}.
|
Escherichia coli (strain K12)
|
P07470
|
CX7A1_BOVIN
|
MRALRVSQALVRSFSSTARNRFENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFPHKK
| null | null |
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial respirasome assembly [GO:0097250]; regulation of oxidative phosphorylation [GO:0002082]
|
mitochondrial respirasome [GO:0005746]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277]
|
oxidoreductase activity [GO:0016491]
|
PF02238;
|
4.10.91.10;
|
Cytochrome c oxidase VIIa family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
| null | null |
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P10174}.
| 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 subunit 2 and heme A of subunit 1 to the active site in subunit 1, 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:0000250|UniProtKB:P10174}.
|
Bos taurus (Bovine)
|
P07471
|
CX6A2_BOVIN
|
MALPLKSLSRGLASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPFSWGDGNHTFFHNPRVNPLPTGYEKP
| null | null |
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]
|
mitochondrial respiratory chain complex IV [GO:0005751]; respiratory chain complex IV [GO:0045277]
|
enzyme regulator activity [GO:0030234]; oxidoreductase activity [GO:0016491]
|
PF02046;
|
4.10.95.10;
|
Cytochrome c oxidase subunit 6A family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
| null | null |
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P32799}.
| 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 subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in the assembly and stabilization of complex IV (By similarity). {ECO:0000250|UniProtKB:P32799, ECO:0000250|UniProtKB:P43023}.
|
Bos taurus (Bovine)
|
P07476
|
INVO_HUMAN
|
MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQEGQPKHLEQQEGQLEQLEEQEGQLKHLEQQEGQLEHLEHQEGQLGLPEQQVLQLKQLEKQQGQPKHLEEEEGQLKHLVQQEGQLKHLVQQEGQLEQQERQVEHLEQQVGQLKHLEEQEGQLKHLEQQQGQLEVPEQQVGQPKNLEQEEKQLELPEQQEGQVKHLEKQEAQLELPEQQVGQPKHLEQQEKHLEHPEQQDGQLKHLEQQEGQLKDLEQQKGQLEQPVFAPAPGQVQDIQPALPTKGEVLLPVEHQQQKQEVQWPPKHK
| null | null |
isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine [GO:0018153]; keratinization [GO:0031424]; keratinocyte differentiation [GO:0030216]; peptide cross-linking [GO:0018149]; response to UV-B [GO:0010224]
|
centrosome [GO:0005813]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear body [GO:0016604]
| null |
PF00904;PF10583;
| null |
Involucrin family
|
PTM: Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other involucrin molecules, to other proteins such as keratin, desmoplakin, periplakin and envoplakin, and to lipids like omega-hydroxyceramide.
|
SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope.
| null | null | null | null | null |
FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
|
Homo sapiens (Human)
|
P07477
|
TRY1_HUMAN
|
MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
|
digestion [GO:0007586]; extracellular matrix disassembly [GO:0022617]; proteolysis [GO:0006508]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
|
PTM: Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.; PTM: Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins. {ECO:0000269|PubMed:25010489}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null |
FUNCTION: Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. {ECO:0000269|PubMed:7945238}.
|
Homo sapiens (Human)
|
P07478
|
TRY2_HUMAN
|
MNLLLILTFVAAAVAAPFDDDDKIVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS
|
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};
|
antimicrobial humoral response [GO:0019730]; collagen catabolic process [GO:0030574]; digestion [GO:0007586]; extracellular matrix disassembly [GO:0022617]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; proteolysis [GO:0006508]
|
azurophil granule lumen [GO:0035578]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
|
PTM: Sulfated on tyrosine. {ECO:0000269|PubMed:17087724}.; PTM: Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins. {ECO:0000269|PubMed:25010489}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null |
FUNCTION: In the ileum, may be involved in defensin processing, including DEFA5. {ECO:0000269|PubMed:12021776}.
|
Homo sapiens (Human)
|
P07483
|
FABPH_RAT
|
MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTHSTFKNTEISFQLGVEFDEVTADDRKVKSVVTLDGGKLVHVQKWDGQETTLTRELSDGKLILTLTHGNVVSTRTYEKEA
| null | null |
brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; intracellular lipid transport [GO:0032365]; long-chain fatty acid transport [GO:0015909]; phospholipid homeostasis [GO:0055091]; positive regulation of long-chain fatty acid import into cell [GO:0140214]; regulation of fatty acid oxidation [GO:0046320]; regulation of phosphatidylcholine biosynthetic process [GO:2001245]; response to fatty acid [GO:0070542]; response to insulin [GO:0032868]; response to xenobiotic stimulus [GO:0009410]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]; sarcoplasm [GO:0016528]
|
cytoskeletal protein binding [GO:0008092]; fatty acid binding [GO:0005504]; icosatetraenoic acid binding [GO:0050543]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]
|
PF00061;
|
2.40.128.20;
|
Calycin superfamily, Fatty-acid binding protein (FABP) family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
|
Rattus norvegicus (Rat)
|
P07486
|
G3P1_DROME
|
MSKIGINGFGRIGRLVLRAAIDKGASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYVVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPAATGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGATYDEIKAKVEEASKGPLKGILGYTDEEVVSTDFFSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNRVIDLIKYMQSKD
|
1.2.1.12
| null |
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycolytic process [GO:0006096]
|
cytosol [GO:0005829]; M band [GO:0031430]; Z disc [GO:0030018]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
| null | null | null |
Drosophila melanogaster (Fruit fly)
|
P07487
|
G3P2_DROME
|
MSKIGINGFGRIGRLVLRAAIDKGANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNRVIDLIKYMQSKD
|
1.2.1.12
| null |
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycolytic process [GO:0006096]
|
cytosol [GO:0005829]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
| null | null | null |
Drosophila melanogaster (Fruit fly)
|
P07490
|
GON1_RAT
|
METIPKLMAAVVLLTVCLEGCSSQHWSYGLRPGGKRNTEHLVDSFQEMGKEEDQMAEPQNFECTVHWPRSPLRDLRGALERLIEEEAGQKKM
| null | null |
estrous cycle [GO:0044849]; female pregnancy [GO:0007565]; male sex determination [GO:0030238]; negative regulation of apoptotic process [GO:0043066]; negative regulation of immature T cell proliferation [GO:0033087]; negative regulation of neuron migration [GO:2001223]; ovulation cycle [GO:0042698]; regulation of gene expression [GO:0010468]; regulation of ovarian follicle development [GO:2000354]; reproduction [GO:0000003]; response to ethanol [GO:0045471]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to potassium ion [GO:0035864]; response to prolactin [GO:1990637]; response to prostaglandin E [GO:0034695]; response to steroid hormone [GO:0048545]; response to testosterone [GO:0033574]
|
axon terminus [GO:0043679]; cytoplasmic side of rough endoplasmic reticulum membrane [GO:0098556]; dendrite [GO:0030425]; extracellular space [GO:0005615]; Golgi-associated vesicle [GO:0005798]; neurosecretory vesicle [GO:1990008]; perikaryon [GO:0043204]
|
gonadotropin hormone-releasing hormone activity [GO:0005183]; gonadotropin-releasing hormone receptor binding [GO:0031530]
|
PF00446;
| null |
GnRH family
|
PTM: [Gonadoliberin-1]: The precursor is cleaved by ACE, which removes the Gly-Lys-Arg peptide at the C-terminus, leading to mature hormone. The mature form of Gonadoliberin-1 is also cleaved and degraded by ACE. {ECO:0000250|UniProtKB:P01148}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
|
Rattus norvegicus (Rat)
|
P07492
|
GRP_HUMAN
|
MRGRELPLVLLALVLCLAPRGRAVPLPAGGGTVLTKMYPRGNHWAVGHLMGKKSTGESSSVSERGSLKQQLREYIRWEEAARNLLGLIEAKENRNHQPPQPKALGNQQPSWDSEDSSNFKDVGSKGKVGRLSAPGSQREGRNPQLNQQ
| null | null |
cellular response to sodium phosphate [GO:1904384]; mast cell degranulation [GO:0043303]; negative regulation of voltage-gated potassium channel activity [GO:1903817]; negative regulation of voltage-gated sodium channel activity [GO:1905151]; neuropeptide signaling pathway [GO:0007218]; ossification [GO:0001503]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway [GO:1900738]; positive regulation of respiratory gaseous exchange [GO:1903942]; positive regulation of vascular associated smooth muscle cell apoptotic process [GO:1905461]; psychomotor behavior [GO:0036343]; regulation of gene expression [GO:0010468]; response to external biotic stimulus [GO:0043207]; signal transduction [GO:0007165]; social behavior [GO:0035176]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuron projection [GO:0043005]; neuronal dense core vesicle [GO:0098992]; secretory granule lumen [GO:0034774]
|
neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]
|
PF02044;
| null |
Bombesin/neuromedin-B/ranatensin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3211139}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q863C3}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q8R1I2}.
| null | null | null | null | null |
FUNCTION: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By similarity). In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to act on vasoactive intestinal peptide (VIP)-expressing cells in the auditory cortex, most likely via extrasynaptic diffusion from local and long-range sources, to mediate disinhibition of glutamatergic cells via VIP cell-specific GRPR signaling which leads to enhanced auditory fear memories (By similarity). Contributes to the regulation of food intake (By similarity). Inhibits voltage-gated sodium channels but enhances voltage-gated potassium channels in hippocampal neurons (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). {ECO:0000250|UniProtKB:P24393, ECO:0000250|UniProtKB:P63153, ECO:0000250|UniProtKB:Q8R1I2}.; FUNCTION: [Neuromedin-C]: Induces an itch response through activation of receptors present on mast cells, triggering mast cell degranulation. {ECO:0000250|UniProtKB:Q8R1I2}.
|
Homo sapiens (Human)
|
P07498
|
CASK_HUMAN
|
MKSFLLVVNALALTLPFLAVEVQNQKQPACHENDERPFYQKTAPYVPMYYVPNSYPYYGTNLYQRRPAIAINNPYVPRTYYANPAVVRPHAQIPQRQYLPNSHPPTVVRRPNLHPSFIAIPPKKIQDKIIIPTINTIATVEPTPAPATEPTVDSVVTPEAFSESIITSTPETTTVAVTPPTA
| null | null |
lactation [GO:0007595]; protein stabilization [GO:0050821]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
| null |
PF00997;
| null |
Kappa-casein family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
|
Homo sapiens (Human)
|
P07499
|
ANF_CANLF
|
MGSPIAASFLLFLAVQLLGQTGANPVYGSVSNADLLDFKNLLDRLEDKMPLEDEAESPQALSEQNAEAGAALSPLPEVPPWTGEVSPAQRDGGALGRSPWDSSDRSALLKSKLRALLAAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRY
| null | null |
cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-121 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing gives rise to the auriculin and atriopeptin peptides (By similarity). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). During IDE degradation, the resulting products can temporarily stimulate NPR2 to produce cGMP, before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Phosphorylation on Ser-127 decreases vasorelaxant activity. {ECO:0000250|UniProtKB:P01160}.
|
SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. {ECO:0000250|UniProtKB:P01161}.
| null | null | null | null | null |
FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (By similarity). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P07500
|
ANF_RABIT
|
MGPFSTITVSFLFCLAFWHPDQIGANPVYNAMSNADLMDFKNLLDHLEDRMPFEDEAVPPQALSEQSDEAGAALSPLPEVPPWTGEVSPAQRDGEALGRSTWEASERSALLKSKLRALLTAPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR
| null | null |
cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-123 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing gives rise to the auriculin and atriopeptin peptides (By similarity). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). During IDE degradation, the resulting products can temporarily stimulate NPR2 to produce cGMP, before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Phosphorylation on Ser-129 decreases vasorelaxant activity. {ECO:0000250|UniProtKB:P01160}.
|
SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. {ECO:0000250|UniProtKB:P01161}.
| null | null | null | null | null |
FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (By similarity). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
|
Oryctolagus cuniculus (Rabbit)
|
P07501
|
ANF_BOVIN
|
MGSSAITVSFLLFLAFQLPGQTGANPVYGSVSNADLMDFKNLLDRLEDKMPLEDEAVPSQVLSEQNEEAGAPLSPLSEMPPWMGEVNPAQREGGVLGRGPWESSDRSALLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRYRR
| null | null |
cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-122 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing gives rise to the auriculin and atriopeptin peptides (By similarity). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). During IDE degradation, the resulting products can temporarily stimulate NPR2 to produce cGMP, before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Phosphorylation on Ser-128 decreases vasorelaxant activity. {ECO:0000250|UniProtKB:P01160}.
|
SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. {ECO:0000250|UniProtKB:P01161}.
| null | null | null | null | null |
FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (By similarity). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
|
Bos taurus (Bovine)
|
P07505
|
SODCP_SPIOL
|
MAAHTILASAPSHTTFSLISPFSSTPTNALSSSLQSSSFNGLSFKLSPTTQSLSLSTSAASKPLTIVAATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:1880134}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:1880134}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1880134}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1880134};
| null |
chloroplast [GO:0009507]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]
|
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Spinacia oleracea (Spinach)
|
P07507
|
MGP_BOVIN
|
MKSLLLLSILAALAVAALCYESHESLESYEINPFINRRNANSFISPQQRWRAKAQERIRELNKPQYELNREACDDFKLCERYAMVYGYNAAYDRYFRQRRGAK
| null | null |
cartilage development [GO:0051216]; cell differentiation [GO:0030154]; ossification [GO:0001503]; regulation of bone mineralization [GO:0030500]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Requires vitamin K-dependent gamma-carboxylation for its function.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation.
|
Bos taurus (Bovine)
|
P07510
|
ACHG_HUMAN
|
MHGGQGPLLLLLLLAVCLGAQGRNQEERLLADLMQNYDPNLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYEGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQSQTYSTNEIDLQLSQEDGQTIEWIFIDPEAFTENGEWAIQHRPAKMLLDPAAPAQEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIHFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIVVNAVVVLNVSLRSPHTHSMARGVRKVFLRLLPQLLRMHVRPLAPAAVQDTQSRLQNGSSGWSITTGEEVALCLPRSELLFQQWQRQGLVAAALEKLEKGPELGLSQFCGSLKQAAPAIQACVEACNLIACARHQQSHFDNGNEEWFLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNRVPALPFPGDPRPYLPSPD
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; muscle contraction [GO:0006936]; signal transduction [GO:0007165]
|
acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; channel activity [GO:0015267]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536};
| null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Homo sapiens (Human)
|
P07511
|
GLYC_RABIT
|
MATAVNGAPRDAALWSSHEQMLAQPLKDSDAEVYDIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEHIDELETLCQKRALQAYGLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMAYKVNPDTGYIDYDRLEENARLFHPKLIIAGTSCYSRNLDYGRLRKIADENGAYLMADMAHISGLVVAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRRGVRSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTPEFKEYQRQVVANCRALSAALVELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDKSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTVQIQDDTGPRATLKEFKEKLAGDEKHQRAVRALRQEVESFAALFPLPGLPGF
|
2.1.2.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10387080};
|
cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to tetrahydrofolate [GO:1904482]; folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; glycine metabolic process [GO:0006544]; L-serine catabolic process [GO:0006565]; L-serine metabolic process [GO:0006563]; protein homotetramerization [GO:0051289]; purine nucleobase biosynthetic process [GO:0009113]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; mRNA 5'-UTR binding [GO:0048027]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270]
|
PF00464;
|
3.90.1150.10;3.40.640.10;
|
SHMT family
|
PTM: Deamidation of asparagine produces alternatively aspartate or isoaspartate, which in turn can be converted to aspartate through carboxylmethylation/demethylation. {ECO:0000269|PubMed:2318867}.
|
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000269|PubMed:1381582};
| null |
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000305}.
| null | null |
FUNCTION: Interconversion of serine and glycine. {ECO:0000269|PubMed:1381582}.
|
Oryctolagus cuniculus (Rabbit)
|
P07514
|
NB5R3_BOVIN
|
MGAQLSTLGHVVLSPVWFLYSLIMKLFQRSTPAITLENPDIKYPLRLIDKEVISHDTRRFRFALPSPEHILGLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVYQGKGKFAIRPDKKSDPVIKTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSARFKLWYTVDKAPEAWDYSQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDRVGHPKERCFAF
|
1.6.2.2
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P00387};
|
cholesterol biosynthetic process [GO:0006695]
|
endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; FAD binding [GO:0071949]
|
PF00970;PF00175;
|
3.40.50.80;2.40.30.10;
|
Flavoprotein pyridine nucleotide cytochrome reductase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniProtKB:P20070}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniProtKB:P20070}.
|
CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; Evidence={ECO:0000269|PubMed:1370824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46681; Evidence={ECO:0000305|PubMed:1370824};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor. {ECO:0000269|PubMed:1370824}.
|
Bos taurus (Bovine)
|
P07516
|
PPR1B_BOVIN
|
MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRSNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEEDEEEEEDSQAEVLKGSRGSAGQKTTYGQGLEGPWERPPPLDGPQRDGSSEDQVEDPALNEPGEEPQRPAHPEPGT
| null | null |
behavioral response to cocaine [GO:0048148]; cellular response to cocaine [GO:0071314]; DNA-templated transcription [GO:0006351]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; negative regulation of female receptivity [GO:0007621]; response to amphetamine [GO:0001975]; response to morphine [GO:0043278]; visual learning [GO:0008542]
|
axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; dendrite cytoplasm [GO:0032839]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]
|
molecular function inhibitor activity [GO:0140678]; protein phosphatase inhibitor activity [GO:0004864]
|
PF05395;
| null |
Protein phosphatase inhibitor 1 family
|
PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein.; PTM: Phosphorylation of Thr-34 is required for activity. {ECO:0000269|PubMed:3511054}.
|
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Inhibitor of protein-phosphatase 1.
|
Bos taurus (Bovine)
|
P07519
|
CBP1_HORVU
|
MARCRRRSGCTAGAALLLLLALALSGGGGAAPQGAEVTGLPGFDGALPSKHYAGYVTVDEGHGRNLFYYVVESERDPGKDPVVLWLNGGPGCSSFDGFVYEHGPFNFESGGSVKSLPKLHLNPYAWSKVSTMIYLDSPAGVGLSYSKNVSDYETGDLKTATDSHTFLLKWFQLYPEFLSNPFYIAGESYAGVYVPTLSHEVVKGIQGGAKPTINFKGYMVGNGVCDTIFDGNALVPFAHGMGLISDEIYQQASTSCHGNYWNATDGKCDTAISKIESLISGLNIYDILEPCYHSRSIKEVNLQNSKLPQSFKDLGTTNKPFPVRTRMLGRAWPLRAPVKAGRVPSWQEVASGVPCMSDEVATAWLDNAAVRSAIHAQSVSAIGPWLLCTDKLYFVHDAGSMIAYHKNLTSQGYRAIIFSGDHDMCVPFTGSEAWTKSLGYGVVDSWRPWITNGQVSGYTEGYEHGLTFATIKGAGHTVPEYKPQEAFAFYSRWLAGSKL
|
3.4.16.5
| null |
proteolysis [GO:0006508]; secondary metabolic process [GO:0019748]
|
extracellular region [GO:0005576]
|
acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; serine-type carboxypeptidase activity [GO:0004185]
|
PF00450;
|
3.40.50.12670;3.40.50.1820;
|
Peptidase S10 family
|
PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
|
SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
|
CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074, ECO:0000255|PROSITE-ProRule:PRU10075};
| null | null | null | null |
FUNCTION: May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo.
|
Hordeum vulgare (Barley)
|
P07522
|
EGF_RAT
|
MLFSLTFLSVFLKITVLSVTAQQTRNCQSGPLERSGTTTYAAAGPPRFLIFLQGNSIFRINTDGTNHQQLVVDAGVSVVMDFHYKEERLYWVDLERQLLQRVFFNGSGQETVCKVDKNVSGLAINWIDGEILRTDRWKGVITVTDMNGNNSRVLLSSLKRPANILVDPTERLIFWSSVVTGNLHRADLGGMDVKTLLEAPERISVLILDILDKRLFWAQDGREGSHGYIHSCDYNGGSIHHIRHQARHDLLTMAIFGDKILYSALKEKAIWIADKHTGKNVVRVNLDPASVPPRELRVVHLHAQPGTENRAQASDSERCKQRRGQCLYSLSERDPNSDSSACAEGYTLSRDRKYCEDVNECALQNHGCTLGCENIPGSYYCTCPTGFVLLPDGKRCHELVACPGNRSECSHDCILTSDGPLCICPAGSVLGKDGKTCTGCSFSDNGGCSQICLPLSLASWECDCFPGYDLQLDRKSCAASMGPQPFLLFANSQDIRHMHFDGTDYKTLLSRQMGMVFALDYDPVESKIYFAQTALKWIERANLDGSQRERRITEGVDTPEGLAVDWIGRRIYWTDSGKSVIEGSDLSGKHHQIIIKESISRPRGIAVHPKARRLFWTDTGMSPRIESSSLQGSDRTLIASSNLLEPSGIAIDYLTDTLYWCDTKLSVIEMADLDGSKRRRLTQNDVGHPFSLAVFEDHVWFSDWAIPSVIRVNKRTGQNRVRLRGSMLKPSSLVVVHPLAKPGADPCLHRNGGCEHICQESLGTAQCLCREGFVKAPDGKMCLTRKDDQILAGDNADLSKEVASLDNSPKAYVPDDDRTESSTLVAEIMVSGLNYEDDCGPGGCGSHAHCISEGEAAVCQCLKGFAGDGNLCSDIDECELGSSDCPPTSSRCINTEGGYVCQCSEGYEGDGIYCLDVDECQQGSHGCSENATCTNTEGGYNCTCAGCPSAPGLPCPDSTSPSLLGKDGCHWVRNSNTGCPPSYDGYCLNGGVCMYVESVDRYVCNCVIGYIGERCQHRDLRWWKLRHADYGQRHDITVVSVCVVALALLLLLGMWGTYYYRTRKQLSESSKKPSEESSSNVSSNGPDSSGAGVSSGPQPWFVVLEEHQQPKNGRLPAAGTNGAVVEAGLSSSL
| null | null |
angiogenesis [GO:0001525]; branching morphogenesis of an epithelial tube [GO:0048754]; canonical Wnt signaling pathway [GO:0060070]; cell population proliferation [GO:0008283]; cerebellar granule cell precursor proliferation [GO:0021930]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation [GO:0050673]; ERBB2-EGFR signaling pathway [GO:0038134]; ERK1 and ERK2 cascade [GO:0070371]; intracellular signal transduction [GO:0035556]; kidney development [GO:0001822]; mammary gland alveolus development [GO:0060749]; negative regulation of cholesterol efflux [GO:0090370]; negative regulation of secretion [GO:0051048]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cerebellar granule cell precursor proliferation [GO:0021940]; positive regulation of DNA binding [GO:0043388]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of epithelial tube formation [GO:1905278]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of hyaluronan biosynthetic process [GO:1900127]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein localization to early endosome [GO:1902966]; positive regulation of receptor internalization [GO:0002092]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; regulation of calcium ion import [GO:0090279]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of protein localization to cell surface [GO:2000008]; regulation of protein transport [GO:0051223]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]
|
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; guanyl-nucleotide exchange factor activity [GO:0005085]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF00008;PF07645;PF14670;PF00058;
|
2.10.25.10;2.120.10.30;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P07527
|
WEE1_SCHPO
|
MSSSSNTSSHRSYGLRRSQRSMNLNRATLLAPPTPSSLYDANNSTSSTSSQKPNTSFTSLFGPRKQTTSSPSFSHAAPLHPLSPPSFTHSQPQIQAQPVPRRPSLFDRPNLVSRSSSRLGDSPSLSPVAQVANPIHHTAPSPSDVRAFPIHKNASTGVKRSFFSSSMSNGAMSPPSHSPSPFLQSSQHIPPSTPAQKLRKKNNFDSFRISNSHISPFASGSFSPFATSSPNFLSTSTPAPPNSNNANPSTLFSSIPSSRHTTSNHFPSNSAQSSLFSPTARPLTARKLGFASSQTKSAVSNNHSRNSSKDASFMMKSFIPSNRSHPQTQQNESSLFSDNSMVNSSSNSFSLFPNATLPNPPSSELLTTPFQQIKPPSQVFMSTGLLSKQHRPRKNINFTPLPPSTPSKPSTFVRPHSSSTDSPPSPSTPSNTQTDSYFIQRENTPTNHNSIPTIQLEKSSMDFLRFDPPPSAVKTSHNYGLPFLSNQRCPATPTRNPFAFENTVSIHMDGRQPSPIKSRNNNQMSFAMEEEADVSQPSSSSFTLSFPSALTSSKVSSSTSHLLTRFRNVTLLGSGEFSEVFQVEDPVEKTLKYAVKKLKVKFSGPKERNRLLQEVSIQRALKGHDHIVELMDSWEHGGFLYMQVELCENGSLDRFLEEQGQLSRLDEFRVWKILVEVALGLQFIHHKNYVHLDLKPANVMITFEGTLKIGDFGMASVWPVPRGMEREGDCEYIAPEVLANHLYDKPADIFSLGITVFEAAANIVLPDNGQSWQKLRSGDLSDAPRLSSTDNGSSLTSSSRETPANSIIGQGGLDRVVEWMLSPEPRNRPTIDQILATDEVCWVEMRRKAGAIIYEGIHGSSSNPQGDQMMEDWQVNV
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
|
cell division [GO:0051301]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 cell size control checkpoint signaling [GO:0031569]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; phosphorylation [GO:0016310]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]
|
Cdr2 medial cortical node complex [GO:0110115]; cytoplasm [GO:0005737]; medial cortical node [GO:0071341]; mitotic spindle pole body [GO:0044732]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily
|
PTM: Phosphorylated in the C-terminal by NIM1/CDR1.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
| null | null | null | null |
FUNCTION: Protein kinase that acts both on serines and on tyrosines. It acts as a dosage-dependent negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2. {ECO:0000269|PubMed:1825699}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P07547
|
ARO1_EMENI
|
MSNPTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTPSFEEAFRKAAAEITPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQNPPCGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEENAETILKAVRREVRPGEHRFEGIEEILKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNMALDKKNDGPKKKIVLLSAIGTPYETRASVVANEDIRVVLAPSIEVHPGVAQSSNVICAPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGNLQASSSPLYLGNAGTASRFLTTVATLANSSTVDSSVLTGNNRMKQRPIGDLVDALTANGASIEYVERTGSLPLKIAASGGFAGGNINLAAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVIESDASSATYPLAVAAVTGTTCTVPNIGSASLQGDARFAVEVLRPMGCTVEQTETSTTVTGPSDGILRPLPNVDMEPMTDAFLGASVLAAIARGKESNHTTRIYGIANQRVKECNRIKAMKDELAKFGVICREHDDGLEIDGIDRSNLRQPVGGVFCYDDHRVAFSFSVLSLVTPQPTLILEKECVGKTWPGWWDTLRQLFKVKLEGKELEEEPVAASGPDRANASIYIIGMRGAGKSTAGNWVSKALNRPFVDLDTELETVEGMTIPDIIKTRGWQGFRNAELEILKRTLKERSRGYVFACGGGVVEMPEARKLLTDYHKTKGNVLLLMRDIKKIMDFLSIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSRDASPSGLARASEDFNRFLQVATGQIDSLSIIKEKEHSFFASLTLPDLREAGDILEEVCVGSDAVELRVDLLKDPASNNDIPSVDYVVEQLSFLRSRVTLPIIFTIRTQSQGGRFPDNAHDAALELYRLAFRSGCEFVDLEIAFPEDMLRAVTEMKGFSKIIASHHDPKGELSWANMSWIKFYNKALEYGDIIKLVGVARNIDDNTALRKFKNWAAEAHDVPLIAINMGDQGQLSRILNGFMTPVSHPSLPFKAAPGQLSATEIRKGLSLMGEIKPKKFAIFGSPISQSRSPALHNTLFAQVGLPHNYTRLETTNAQDVQEFIRSPDFGGASVTIPLKLDIMPLLDEVAAEAEIIGAVNTIIPVSTGKNTPSRLVGRNTDWQGMILSLRKAGVYGPKRKDQEQSALVVGGGGTARAAIYALHNMGYSPIYIVGRTPSKLENMVSTFPSSYNIRIVESPSSFESVPHVAIGTIPADQPIDPTMRETLCHMFERAQEADAEAVKAIEHAPRILLEMAYKPQVTALMRLASDSGWKTIPGLEVLVGQGWYQFKYWTGISPLYESARACSSPLI
|
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
|
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
|
PF01761;PF01487;PF00275;PF18317;PF08501;PF01202;
|
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
|
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
| null |
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
| null | null |
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
|
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
|
P07548
|
DFD_DROME
|
MSSFLMGYPHAPHHVQSPMSMGNGLDPKFPPLADDYHHYNGHYSMTASTGHMSGAVGGGAGVGSVGGGGAGGMTGHPHSMHPADMVSDYMAHHHNPHSHSHSHTHSLPHHHSNSAISGHHQASAGGYSSNYANATPPSHPHSHPHAHPHQSLGYYVHHAPEFISAGAVHSDPTNGYGPAANVPNTSNGGGGGGSGAVLGGGAVGGSANGYYGGYGGGYGTANGSVGSTHSQGHSPHSQMMDLPLQCSSTEPPTNTALGLQELGLKLEKRIEEAVPAGQQLQELGMRLRCDDMGSENDDMSEEDRLMLDRSPDELGSNDNDDDLGDSDSDEDLMAETTDGERIIYPWMKKIHVAGVANGSYQPGMEPKRQRTAYTRHQILELEKEFHYNRYLTRRRRIEIAHTLVLSERQIKIWFQNRRMKWKKDNKLPNTKNVRKKTVDANGNPTPVAKKPTKRAASKKQQQAQQQQQSQQQQTQQTPVMNECIRSDSLESIGDVSSSLGNPPYIPAAPETTSSYPGSQQHLSNNNNNGSGNNNNNNNNNNSNLNNNNNNNQMGHTNLHGHLQQQQSDLMTNLQLHIKQDYDLTAL
| null | null |
anterior/posterior pattern specification [GO:0009952]; embryonic brain development [GO:1990403]; head development [GO:0060322]; head morphogenesis [GO:0060323]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process involved in morphogenesis [GO:1902339]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior head segmentation [GO:0035289]; regulation of gene expression [GO:0010468]; specification of segmental identity, head [GO:0007380]
|
neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; molecular adaptor activity [GO:0060090]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
|
Antp homeobox family, Deformed subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Homeotic protein controlling Drosophila head development. Transcriptional activator of the apoptotic activator protein rpr in cells at the maxillary/mandibular boundary. {ECO:0000269|PubMed:12202035, ECO:0000269|PubMed:16453752}.
|
Drosophila melanogaster (Fruit fly)
|
P07550
|
ADRB2_HUMAN
|
MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL
| null | null |
activation of adenylate cyclase activity [GO:0007190]; activation of transmembrane receptor protein tyrosine kinase activity [GO:0007171]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; adrenergic receptor signaling pathway [GO:0071875]; bone resorption [GO:0045453]; brown fat cell differentiation [GO:0050873]; cell surface receptor signaling pathway [GO:0007166]; cellular response to amyloid-beta [GO:1904646]; desensitization of G protein-coupled receptor signaling pathway by arrestin [GO:0002032]; diet induced thermogenesis [GO:0002024]; endosome to lysosome transport [GO:0008333]; heat generation [GO:0031649]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of smooth muscle contraction [GO:0045986]; norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0002025]; positive regulation of AMPA receptor activity [GO:2000969]; positive regulation of autophagosome maturation [GO:1901098]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of lipophagy [GO:1904504]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mini excitatory postsynaptic potential [GO:0061885]; positive regulation of protein kinase A signaling [GO:0010739]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of transcription by RNA polymerase II [GO:0045944]; receptor-mediated endocytosis [GO:0006898]; regulation of sodium ion transport [GO:0002028]; response to cold [GO:0009409]; response to psychosocial stress [GO:1990911]; smooth muscle contraction [GO:0006939]; transcription by RNA polymerase II [GO:0006366]
|
apical plasma membrane [GO:0016324]; clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal dense core vesicle [GO:0098992]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
adenylate cyclase binding [GO:0008179]; amyloid-beta binding [GO:0001540]; beta2-adrenergic receptor activity [GO:0004941]; identical protein binding [GO:0042802]; norepinephrine binding [GO:0051380]; potassium channel regulator activity [GO:0015459]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB2 sub-subfamily
|
PTM: Palmitoylated (PubMed:11146000, PubMed:17962520, PubMed:18547522, PubMed:2540197, PubMed:27481942). Mainly palmitoylated at Cys-341 (PubMed:17962520, PubMed:18547522, PubMed:2540197). Palmitoylation may reduce accessibility of phosphorylation sites by anchoring the receptor to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (PubMed:11146000). Also undergoes transient, ligand-induced palmitoylation at Cys-265 probably by ZDHHC9, ZDHHC14 and ZDHHC18 within the Golgi (PubMed:27481942). Palmitoylation at Cys-265 requires phosphorylation by PKA and receptor internalization and stabilizes the receptor (PubMed:27481942). Could be depalmitoylated by LYPLA1 at the plasma membrane (PubMed:27481942). {ECO:0000269|PubMed:11146000, ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942}.; PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.; PTM: Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor. {ECO:0000269|PubMed:8521811}.; PTM: Polyubiquitinated (PubMed:23166351). Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation (PubMed:19424180, PubMed:20559325, PubMed:23166351). Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent. {ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23166351}.; PTM: Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2. {ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:19584355}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23166351, ECO:0000269|PubMed:25220262, ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}; Multi-pass membrane protein {ECO:0000269|PubMed:19584355}. Early endosome {ECO:0000269|PubMed:20559325}. Golgi apparatus {ECO:0000269|PubMed:27481942}. Note=Colocalizes with VHL at the cell membrane (PubMed:19584355). Activated receptors are internalized into endosomes prior to their degradation in lysosomes (PubMed:20559325). Activated receptors are also detected within the Golgi apparatus (PubMed:27481942). {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:27481942}.
| null | null | null | null | null |
FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}.
|
Homo sapiens (Human)
|
P07560
|
SEC4_YEAST
|
MSGLRTVSASSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFTNIKQWFKTVNEHANDEAQLLLVGNKSDMETRVVTADQGEALAKELGIPFIESSAKNDDNVNEIFFTLAKLIQEKIDSNKLVGVGNGKEGNISINSGSGNSSKSNCC
| null | null |
ascospore-type prospore assembly [GO:0031321]; autophagy [GO:0006914]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; Golgi vesicle fusion to target membrane [GO:0048210]; membrane addition at site of cytokinesis [GO:0007107]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; regulation of exocytosis [GO:0017157]; vesicle docking involved in exocytosis [GO:0006904]; vesicle fusion [GO:0006906]
|
cellular bud neck [GO:0005935]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; trans-Golgi network transport vesicle [GO:0030140]; transport vesicle [GO:0030133]; transport vesicle membrane [GO:0030658]; vesicle [GO:0031982]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note=A small fraction is soluble.
| null | null | null | null | null |
FUNCTION: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle. {ECO:0000269|PubMed:16390997}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P07564
|
POLG_DEN2J
|
MNNQRKKARSTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGVIIMLIPTAMAFHLTTRNGEPHMIVGRQEKGKSLLFKTEDGVNMCTLMAIDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCATTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFLCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKVVLPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGVVTLYLGAMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLRPQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKMEKASFIEVKSCHWPKSHTLWSNGVLESEMIIPKNFAGPVSQHNYRPGYHTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQIDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMATIGIALLSQSTIPETILELTDALALGMMVLKIVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAAVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGVFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQRGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNTGTIGAVSLDFSPGTSGSPIVDRKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKKRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRANDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGIKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGKGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDLGLGSITTQESESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKIHIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLILCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTNTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGESSPNPTIEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMKHKKATYETDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDRERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRGNSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIFKSIQHLTVTEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELVMKDGRVLVVPCRNQDELIGRARISQGAGWSLKETACLGKSYAQMWTLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLAVWNRVWIQENPWMEDKTPVESWEEVPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW
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2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
| null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
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extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
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ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
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PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
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1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10;
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Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
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PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication. {ECO:0000250|UniProtKB:P29990}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.
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SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P29990}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
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CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: 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: 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; 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=3.6.4.13; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
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FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). Mediates complement activation, which may contribute to the pathogenesis of the vascular leakage that occurs in severe dengue disease. Activates autophagy through the AMPK/ERK/mTOR signaling pathway. Mechanistically, acts as the assembly platform for STK11-AMPK interactions and promotes STK11-AMPK interactions. In turn, promotes phosphorylation of the AMPK kinase structural domain and activates AMPK, thereby positively regulating the AMPK/ERK/mTOR signaling pathway and inducing autophagy. {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
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Dengue virus type 2 (strain Jamaica/1409/1983) (DENV-2)
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P07566
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POLS_RUBVT
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MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
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host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036]
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metal ion binding [GO:0046872]; RNA binding [GO:0003723]
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PF05750;PF05748;PF05749;
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2.60.98.30;3.30.67.20;2.60.40.2650;3.10.50.50;
| null |
PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidase. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism. {ECO:0000250|UniProtKB:P08563}.; PTM: [Spike glycoprotein E1]: Contains three N-linked oligosaccharides. {ECO:0000250|UniProtKB:P08563}.; PTM: Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity (By similarity). Dephosphorylated by human PP1A (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08563}.
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SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated around Golgi region (By similarity). In the virion, it is probably associated to the viral membrane (By similarity). {ECO:0000250|UniProtKB:P08563}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. {ECO:0000250|UniProtKB:P08563}.; SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. {ECO:0000250|UniProtKB:P08563}.
| null | null | null | null | null |
FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. {ECO:0000250|UniProtKB:P08563}.; FUNCTION: [Spike glycoprotein E2]: Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement. {ECO:0000250|UniProtKB:P08563}.; FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein (By similarity). Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:15557740). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity). {ECO:0000250|UniProtKB:P08563, ECO:0000269|PubMed:15557740}.
|
Rubella virus (strain Therien) (RUBV)
|
P07567
|
GAG_MPMV
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDFAVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPHQGNGWRGQPQAPKQAYGAVSFVPANKNNPFQSLPEPPQEVQDWTSVPPPTQY
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell cytoplasm [GO:0030430]; viral nucleocapsid [GO:0019013]
|
metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF02337;PF00607;PF19317;PF14787;
|
1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10;
| null |
PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:3927012}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
|
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
|
P07570
|
PRO_MPMV
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDFAVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPHQGNRVEGPAPGPETSLWGSQLCSSQQKQPISKLTRATPGSAGLDLCSTSHTVLTPEMGPQALSTGIYGPLPPNTFGLILGRSSITMKGLQVYPGVIDNDYTGEIKIMAKAVNNIVTVSQGNRIAQLILLPLIETDNKVQQPYRGQGSFGSSDIYWVQPITCQKPSLTLWLDDKMFTGLIDTGADVTIIKLEDWPPNWPITDTLTNLRGIGQSNNPKQSSKYLTWRDKENNSGLIKPFVIPNLPVNLWGRDLLSQMKIMMCSPNDIVTAQMLAQGYSPGKGLGKKENGILHPIPNQGQSNKKGFGNF
|
3.4.23.-; 3.6.1.23
| null |
nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; viral process [GO:0016032]
|
viral nucleocapsid [GO:0019013]
|
aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF00692;PF01585;PF02337;PF00607;PF19317;PF00077;PF14787;
|
1.10.1200.30;2.70.40.10;2.40.70.10;1.10.375.10;1.10.150.490;4.10.60.10;
| null |
PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric. {ECO:0000269|PubMed:14568536, ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.; PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:9636364}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000269|PubMed:9636364}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000269|PubMed:9636364}.
|
CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:17169987};
| null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364}.; FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364}.; FUNCTION: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000269|PubMed:22171253}.
|
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
|
P07572
|
POL_MPMV
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDFAVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPHQGNRVEGPAPGPETSLWGSQLCSSQQKQPISKLTRATPGSAGLDLCSTSHTVLTPEMGPQALSTGIYGPLPPNTFGLILGRSSITMKGLQVYPGVIDNDYTGEIKIMAKAVNNIVTVSQGNRIAQLILLPLIETDNKVQQPYRGQGSFGSSDIYWVQPITCQKPSLTLWLDDKMFTGLIDTGADVTIIKLEDWPPNWPITDTLTNLRGIGQSNNPKQSSKYLTWRDKENNSGLIKPFVIPNLPVNLWGRDLLSQMKIMMCSPNDIVTAQMLAQGYSPGKGLGKKENGILHPIPNQGQSNKKGFGNFLTAAIDILAPQQCAEPITWKSDEPVWVDQWPLTNDKLAAAQQLVQEQLEAGHITESSSPWNTPIFVIKKKSGKWRLLQDLRAVNATMVLMGALQPGLPSPVAIPQGYLKIIIDLKDCFFSIPLHPSDQKRFAFSLPSTNFKEPMQRFQWKVLPQGMANSPTLCQKYVATAIHKVRHAWKQMYIIHYMDDILIAGKDGQQVLQCFDQLKQELTAAGLHIAPEKVQLQDPYTYLGFELNGPKITNQKAVIRKDKLQTLNDFQKLLGDINWLRPYLKLTTGDLKPLFDTLKGDSDPNSHRSLSKEALASLEKVETAIAEQFVTHINYSLPLIFLIFNTALTPTGLFWQDNPIMWIHLPASPKKVLLPYYDAIADLIILGRDHSKKYFGIEPSTIIQPYSKSQIDWLMQNTEMWPIACASFVGILDNHYPPNKLIQFCKLHTFVFPQIISKTPLNNALLVFTDGSSTGMAAYTLTDTTIKFQTNLNSAQLVELQALIAVLSAFPNQPLNIYTDSAYLAHSIPLLETVAQIKHISETAKLFLQCQQLIYNRSIPFYIGHVRAHSGLPGPIAQGNQRADLATKIVASNINTNLESAQNAHTLHHLNAQTLRLMFNIPREQARQIVKQCPICVTYLPVPHLGVNPRGLFPNMIWQMDVTHYSEFGNLKYIHVSIDTFSGFLLATLQTGETTKHVITHLLHCFSIIGLPKQIKTDNGPGYTSKNFQEFCSTLQIKHITGIPYNPQGQGIVERAHLSLKTTIEKIKKGEWYPRKGTPRNILNHALFILNFLNLDDQNKSAADRFWHNNPKKQFAMVKWKDPLDNTWHGPDPVLIWGRGSVCVYSQTYDAARWLPERLVRQVSNNNQSRE
|
2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.-; 3.6.1.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405};
|
DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]
|
viral nucleocapsid [GO:0019013]
|
aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF00692;PF01585;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF14787;
|
1.10.10.200;1.10.1200.30;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;2.30.30.10;1.10.150.490;3.30.420.10;4.10.60.10;
|
Retroviral Pol polyprotein family
|
PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa. {ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:9636364}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000269|PubMed:9636364}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000269|PubMed:9636364}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:22171253}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:22171253}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000250|UniProtKB:P07570};
| null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364}.; FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364}.; FUNCTION: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000269|PubMed:22171253}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000255|PROSITE-ProRule:PRU00405}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. {ECO:0000305|PubMed:28458055}.
|
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
|
P07575
|
ENV_MPMV
|
MNFNYHFIWSLVILSQISQVQAGFGDPREALAEIQQKHGKPCDCAGGYVSSPPINSLTTVSCSTHTAYSVTNSLKWQCVSTPTTPSNTHIGSCPGECNTISYDSVHASCYNHYQQCNIGNKTYLTATITGDRTPAIGDGNVPTVLGTSHNLITAGCPNGKKGQVVCWNSRPSVHISDGGGPQDKARDIIVNKKFEELHRSLFPELSYHPLALPEARGKEKIDAHTLDLLATVHSLLNASQPSLAEDCWLCLQSGDPVPLALPYNDTLCSNFACLSNHSCPLTPPFLVQPFNFTDSNCLYAHYQNNSFDIDVGLASFTNCSSYYNVSTASKPSNSLCAPNSSVFVCGNNKAYTYLPTNWTGSCVLATLLPDIDIIPGSEPVPIPAIDHFLGKAKRAIQLIPLFVGLGITTAVSTGAAGLGVSITQYTKLSHQLISDVQAISSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIKNLQDDLERRRRQLIDNPFWTSFHGFLPYVMPLLGPLLCLLLVLSFGPIIFNKLMTFIKHQIESIQAKPIQVHYHRLEQEDSGGSYLTLT
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; syncytium formation by plasma membrane fusion [GO:0000768]; virion attachment to host cell [GO:0019062]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00429;
|
1.10.287.210;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity). {ECO:0000250}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.
|
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
|
P07583
|
LEG4_CHICK
|
MSCQGPVCTNLGLKPGQRLTVKGIIAPNAKSFVMNLGKDSTHLGLHFNPRFDAHGDVNLIVCNSKKMEEWGTEQRETVFPFQKGAPIEITFSINPSDLTVHLPGHQFSFPNRLGLSVFDYFDTHGDFTLRSVSWE
| null | null | null |
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
galactoside binding [GO:0016936]; lactose binding [GO:0030395]; laminin binding [GO:0043236]
|
PF00337;
|
2.60.120.200;
| null | null | null | null | null | null | null | null |
FUNCTION: This protein binds beta-galactoside. May participate in host antiviral defense through specific interaction with glycans on the viral envelope glycoproteins. {ECO:0000269|PubMed:28978647}.
|
Gallus gallus (Chicken)
|
P07584
|
ASTA_ASTAS
|
MQCAVLLVLLGVVAASPIIPEAARALYYNDGMFEGDIKLRAGRQPARVGAAILGDEYLWSGGVIPYTFAGVSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFTSGSGCWSYVGRISGAQQVSLQANGCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRYVGEDYQYYSIMHYGKYSFSIQWGVLETIVPLQNGIDLTDPYDKAHMLQTDANQINNLYTNECSLRH
|
3.4.24.21
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323, ECO:0000269|Ref.3}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323, ECO:0000269|Ref.3};
|
cell adhesion [GO:0007155]; fertilization [GO:0009566]; negative regulation of binding of sperm to zona pellucida [GO:2000360]; positive regulation of protein processing [GO:0010954]; prevention of polyspermy [GO:0060468]; proteolysis [GO:0006508]
|
cortical granule [GO:0060473]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
aspartic-type peptidase activity [GO:0070001]; glutamic-type peptidase activity [GO:0070002]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]
|
PF01400;
|
3.40.390.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.; EC=3.4.24.21; Evidence={ECO:0000269|PubMed:2261483, ECO:0000269|Ref.3};
| null | null | null | null |
FUNCTION: Metalloprotease. This protease prefers to cleave in front of small aliphatic residues (P1'). The presence of Lys or Arg in the P1 and P2 position yields high-turnover substrates. In the P3 position the enzyme prefers Pro > Val > Leu > Ala > Gly. {ECO:0000269|PubMed:2261483}.
|
Astacus astacus (Noble crayfish) (Astacus fluviatilis)
|
P07585
|
PGS2_HUMAN
|
MKATIILLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK
| null | null |
animal organ morphogenesis [GO:0009887]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of vascular endothelial growth factor signaling pathway [GO:1900747]; positive regulation of autophagy [GO:0010508]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]
|
extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent conferring compression resistance [GO:0030021]; glycosaminoglycan binding [GO:0005539]; RNA binding [GO:0003723]
|
PF13855;PF01462;
|
3.80.10.10;
|
Small leucine-rich proteoglycan (SLRP) family, SLRP class I subfamily
|
PTM: The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
| null | null | null | null | null |
FUNCTION: May affect the rate of fibrils formation.
|
Homo sapiens (Human)
|
P07589
|
FINC_BOVIN
|
MLGGPGPGLLLLLAVLSLGTAVPSAGASKSRRQAQQIVQPQSPLTVSQSKPGCYDNGKHYQINQQWERTYLGSALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDQAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSLQTTSAGSGSFTDVRTAIYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGKTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCVAYSQLRDQCIVDGITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETRTFYQIGDSWEKYLQGVRYQCYCYGRGIGEWACQPLQTYPDTSGPVQVIITETPSQPNSHPIQWSAPESSHISKYILRWKPKNSPDRWKEATIPGHLNSYTIKGLRPGVVYEGQLISVQHYGQREVTRFDFTTTSTSPAVTSNTVTGETTPLSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYTVNVYEISEEGEQNLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPRAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGVPRSDKVPPPRDLQFVEVTDVKITIMWTPPESPVTGYRVDVIPVNLPGEHGQRLPVSRNTFAEVTGLSPGVTYHFKVFAVNQGRESKPLTAQQATKLDAPTNLQFINETDTTVIVTWTPPRARIVGYRLTVGLTRGGQPKQYNVGPAASQYPLRNLQPGSEYAVSLVAVKGNQQSPRVTGVFTTLQPLGSIPHYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSESGSIVVSGLTPGVEYVYTISVLRDGQERDAPIVKKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGYSLEEVVHADQSSCTFENLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNVGPDTMRVTWAPPSSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTALDSPSGIDFSDITANSFTVHWIAPRATITGYRIRHHPENMGGRPREDRVPPSRNSITLTNLNPGTEYVVSIVALNSKEESLPLVGQQSTVSDVPRDLEVIAATPTSLLISWDAPAVTVRYYRITYGETGGSSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPVSINYRTEIDKPSQMQVTDVQDNSISVRWLPSSSPVTGYRVTTAPKNGPGPSKTKTVGPDQTEMTIEGLQPTVEYVVSVYAQNQNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEETAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTTIPAPTNLKFTQVTPTSLTAQWTAPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPIQRTIRPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIQVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTGNGIQLPGTSGQQPSLGQQMIFEEHGFRRTTPPTTATPVRHRPRPYPPNVNEEIQIGHVPRGDVDHHLYPHVVGLNPNASTGQEALSQTTISWTPFQESSEYIISCHPVGIDEEPLQFRVPGTSASATLTGLTRGATYNIIVEAVKDQQRQKVREEVVTVGNSVDQGLSQPTDDSCFDPYTVSHYAIGEEWERLSDSGFKLSCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAEPGNEGSTAHSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE
| null | null |
acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; heart development [GO:0007507]; nervous system development [GO:0007399]; regulation of cell shape [GO:0008360]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
disordered domain specific binding [GO:0097718]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; proteoglycan binding [GO:0043394]
|
PF00039;PF00040;PF00041;
|
2.10.70.10;2.10.10.10;2.60.40.10;
| null |
PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11276}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000250|UniProtKB:P11276}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000269|PubMed:25128524}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11276}. Secreted {ECO:0000250|UniProtKB:P11276}.
| null | null | null | null | null |
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). {ECO:0000250|UniProtKB:P02751, ECO:0000250|UniProtKB:P11276}.; FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.; FUNCTION: Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. {ECO:0000250|UniProtKB:P11276}.
|
Bos taurus (Bovine)
|
P07591
|
TRXM_SPIOL
|
MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP
| null | null | null |
chloroplast [GO:0009507]
|
enzyme activator activity [GO:0008047]; protein-disulfide reductase activity [GO:0015035]
|
PF00085;
|
3.40.30.10;
|
Thioredoxin family, Plant M-type subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast.
| null | null | null | null | null |
FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
|
Spinacia oleracea (Spinach)
|
P07602
|
SAP_HUMAN
|
MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; epithelial cell differentiation involved in prostate gland development [GO:0060742]; ganglioside GM1 transport to membrane [GO:1905572]; lysosomal transport [GO:0007041]; positive regulation of beta-galactosidase activity [GO:1903771]; prostate gland growth [GO:0060736]; regulation of autophagy [GO:0010506]; regulation of lipid metabolic process [GO:0019216]; sphingolipid metabolic process [GO:0006665]
|
azurophil granule membrane [GO:0035577]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; plasma membrane [GO:0005886]
|
enzyme activator activity [GO:0008047]; ganglioside GM1 binding [GO:1905573]; ganglioside GM2 binding [GO:1905574]; ganglioside GM3 binding [GO:1905575]; ganglioside GP1c binding [GO:1905577]; ganglioside GT1b binding [GO:1905576]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; scaffold protein binding [GO:0097110]
|
PF02199;PF05184;PF03489;
|
1.10.225.10;
| null |
PTM: The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.; PTM: N-linked glycans show a high degree of microheterogeneity. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329}.; PTM: The one residue extended Saposin-B-Val is only found in 5% of the chains.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:21835174, ECO:0000269|PubMed:22431521}.; SUBCELLULAR LOCATION: [Prosaposin]: Secreted {ECO:0000250|UniProtKB:Q61207}. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000250|UniProtKB:Q61207}.
| null | null | null | null | null |
FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.; FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.; FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; FUNCTION: [Prosaposin]: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling. {ECO:0000250|UniProtKB:Q61207, ECO:0000269|PubMed:10383054}.; FUNCTION: Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.
|
Homo sapiens (Human)
|
P07604
|
TYRR_ECOLI
|
MRLEVFCEDRLGLTRELLDLLVLRGIDLRGIEIDPIGRIYLNFAELEFESFSSLMAEIRRIAGVTDVRTVPWMPSEREHLALSALLEALPEPVLSVDMKSKVDMANPASCQLFGQKLDRLRNHTAAQLINGFNFLRWLESEPQDSHNEHVVINGQNFLMEITPVYLQDENDQHVLTGAVVMLRSTIRMGRQLQNVAAQDVSAFSQIVAVSPKMKHVVEQAQKLAMLSAPLLITGDTGTGKDLFAYACHQASPRAGKPYLALNCASIPEDAVESELFGHAPEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGMFREDLYYRLNVLTLNLPPLRDCPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYAWPGNVRQLKNAIYRALTQLDGYELRPQDILLPDYDAATVAVGEDAMEGSLDEITSRFERSVLTQLYRNYPSTRKLAKRLGVSHTAIANKLREYGLSQKKNEE
| null | null |
aromatic compound catabolic process [GO:0019439]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]
|
PF18024;PF13188;PF00158;
|
1.10.8.60;3.30.70.260;1.10.10.60;3.40.50.300;3.30.450.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Dual transcriptional regulator of the TyrR regulon, which includes a number of genes coding for proteins involved in the biosynthesis or transport of the three aromatic amino acids, phenylalanine, tyrosine and tryptophan (PubMed:14614536, PubMed:15049824, PubMed:1860819, PubMed:334742, PubMed:4399341, PubMed:4887504, PubMed:7798138, PubMed:7961453, PubMed:8449883). These three aromatic amino acids act as effectors which bind to the TyrR protein to form an active regulatory protein (PubMed:1860819, PubMed:334742, PubMed:4399341, PubMed:7961453, PubMed:8106498). Modulates the expression of at least eight unlinked transcription units, including aroF, aroG, aroLM, aroP, mtr, tyrA, tyrB and tyrP (PubMed:14614536, PubMed:15049824, PubMed:1860819, PubMed:334742, PubMed:4399341, PubMed:4887504, PubMed:7798138, PubMed:7961453, PubMed:8449883). In most cases TyrR acts as a repressor, but positive effects have been observed on the tyrP gene, which is repressed in the presence of tyrosine and activated at high phenylalanine concentrations (PubMed:15049824, PubMed:1860819, PubMed:334742, PubMed:7798138, PubMed:8407813, PubMed:8449883). Is also involved in activation, but not repression, of mtr expression in association with phenylalanine or tyrosine (PubMed:2061290, PubMed:8407813, PubMed:8449883). Acts by binding specifically to TyrR boxes in the promoter region of the target genes (PubMed:10197993, PubMed:1860819, PubMed:7961453, PubMed:8449883, PubMed:8947567). {ECO:0000269|PubMed:10197993, ECO:0000269|PubMed:14614536, ECO:0000269|PubMed:15049824, ECO:0000269|PubMed:1860819, ECO:0000269|PubMed:2061290, ECO:0000269|PubMed:334742, ECO:0000269|PubMed:4399341, ECO:0000269|PubMed:4887504, ECO:0000269|PubMed:7798138, ECO:0000269|PubMed:7961453, ECO:0000269|PubMed:8106498, ECO:0000269|PubMed:8407813, ECO:0000269|PubMed:8449883, ECO:0000269|PubMed:8947567}.
|
Escherichia coli (strain K12)
|
P07607
|
TYSY_MOUSE
|
MLVVGSELQSDAQQLSAEAPRHGELQYLRQVEHILRCGFKKEDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVRIWDANGSRDFLDSLGFSARQEGDLGPVYGFQWRHFGAEYKDMDSDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV
|
2.1.1.45
| null |
cartilage development [GO:0051216]; circadian rhythm [GO:0007623]; developmental growth [GO:0048589]; dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; intestinal epithelial cell maturation [GO:0060574]; liver regeneration [GO:0097421]; methylation [GO:0032259]; regulation of translation [GO:0006417]; response to cytokine [GO:0034097]; response to ethanol [GO:0045471]; response to folic acid [GO:0051593]; response to glucocorticoid [GO:0051384]; response to organophosphorus [GO:0046683]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; tetrahydrofolate interconversion [GO:0035999]; uracil metabolic process [GO:0019860]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
dihydrofolate reductase activity [GO:0004146]; folic acid binding [GO:0005542]; heterocyclic compound binding [GO:1901363]; mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; sequence-specific mRNA binding [GO:1990825]; thymidylate synthase activity [GO:0004799]
|
PF00303;
|
3.30.572.10;
|
Thymidylate synthase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04818}. Cytoplasm {ECO:0000250|UniProtKB:P04818}. Mitochondrion {ECO:0000250|UniProtKB:P04818}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04818}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P04818}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000250|UniProtKB:P45352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12105; Evidence={ECO:0000250|UniProtKB:P45352};
| null |
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000250|UniProtKB:P45352}.
| null | null |
FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:0000250|UniProtKB:P04818}.
|
Mus musculus (Mouse)
|
P07611
|
PG094_VACCW
|
MGGGVSVELPKRDPPPGVPTDEMLLNVDKMHDVIAPAKLLEYVHIGPLAKDKEDKVKKRYPEFRLVNTGPGGLSALLRQSYNGTAPNCCRTFNRTHYWKKDGKISDKYEEGAVLESCWPDVHDTGKCDVDLFDWCQGDTFDRNICHQWIGSAFNRSNRTVEGQQSLINLYNKMQTLCSKDASVPICESFLHHLRAHNTEDSKEMIDYILRQQSADFKQKYMRCSYPTRDKLEESLKYAEPRECWDPECSNANVNFLLTRNYNNLGLCNIVRCNTSVNNLQMDKTSSLRLSCGLSNSDRFSTVPVNRAKVVQHNIKHSFDLKLHLISLLSLLVIWILIVAI
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF03003;
| null |
Orthopoxvirus OPG086 family
|
PTM: Unglycosylated because produced in viral factories instead of the classic ER -Golgi route. {ECO:0000305|PubMed:34076488}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:34076488}; Single-pass type II membrane protein {ECO:0000305}. Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. {ECO:0000269|PubMed:16973586, ECO:0000305|PubMed:34076488}.
| null | null | null | null | null |
FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. {ECO:0000269|PubMed:16339313, ECO:0000269|PubMed:16973586, ECO:0000269|PubMed:34076488}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07612
|
PG095_VACCW
|
MGAAASIQTTVNTLSERISSKLEQEANASAQTKCDIEIGNFYIRQNHGCNLTVKNMCSADADAQLDAVLSAATETYSGLTPEQKAYVPAMFTAALNIQTSVNTVVRDFENYVKQTCNSSAVVDNKLKIQNVIIDECYGAPGSPTNLEFINTGSSKGNCAIKALMQLTTKATTQIAPKQVAGTGVQFYMIVIGVIILAALFMYYAKRMLFTSTNDKIKLILANKENVHWTTYMDTFFRTSPMVIATTDMQN
| null | null |
symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF02442;
| null |
Orthopoxvirus OPG095 family
|
PTM: Myristoylated. {ECO:0000269|PubMed:2243383, ECO:0000269|PubMed:9188589}.; PTM: Disulfid bonds are oxidized in the cytoplasm by OPG088 protein. {ECO:0000269|PubMed:11983854}.; PTM: Unglycosylated because produced in viral factories instead of the classic ER -Golgi route. {ECO:0000305|PubMed:34076488}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305|PubMed:34076488}. Note=Localizes to the membrane surrounding the core of mature virus particles (MV). {ECO:0000269|PubMed:9188589, ECO:0000305|PubMed:34076488}.
| null | null | null | null | null |
FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. {ECO:0000269|PubMed:34076488}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07617
|
MCE_VACCW
|
MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQRKISSKNSMSKNRNSKRSVRSNK
|
2.1.1.57
| null |
7-methylguanosine mRNA capping [GO:0006370]; regulation of mRNA 3'-end processing [GO:0031440]
|
virion component [GO:0044423]
|
mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746]
|
PF01358;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Poxvirus/kinetoplastid 2'-O-MTase family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Localizes to the virion core. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57;
| null | null | null | null |
FUNCTION: Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates. {ECO:0000269|PubMed:12359447, ECO:0000269|PubMed:1313572, ECO:0000269|PubMed:1670500}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P07623
|
METAS_ECOLI
|
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLTRGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDAQTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYDLRHMNPTLD
|
2.3.1.46
| null |
L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine [GO:0019281]
|
cytoplasm [GO:0005737]
|
homoserine O-acetyltransferase activity [GO:0004414]; homoserine O-succinyltransferase activity [GO:0008899]; protein homodimerization activity [GO:0042803]
|
PF04204;
|
3.40.50.880;
|
MetA family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine; Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46; Evidence={ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:10572016, ECO:0000269|PubMed:17302437, ECO:0000269|PubMed:17442255, ECO:0000269|PubMed:28581482};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for succinyl-CoA {ECO:0000269|PubMed:10572016}; KM=0.13 mM for succinyl-CoA {ECO:0000269|PubMed:17302437}; KM=0.28 mM for succinyl-CoA {ECO:0000269|PubMed:17442255}; KM=1.6 mM for L-homoserine {ECO:0000269|PubMed:10572016}; KM=0.72 mM for L-homoserine {ECO:0000269|PubMed:17302437}; KM=0.38 mM for L-homoserine {ECO:0000269|PubMed:17442255}; KM=0.64 mM for CoA {ECO:0000269|PubMed:10572016}; KM=3.5 mM for O-succinylhomoserine {ECO:0000269|PubMed:10572016}; Note=kcat is 24 sec(-1) with succinyl-CoA as substrate. kcat is 24 sec(-1) with L-homoserine as substrate. kcat is 5.23 sec(-1) with CoA as substrate. kcat is 5.23 sec(-1) with O-succinylhomoserine as substrate. {ECO:0000269|PubMed:10572016};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:10572016}.
| null | null |
FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine (PubMed:10572016, PubMed:17302437, PubMed:17442255, PubMed:28581482). Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-succinylhomoserine (PubMed:10572016, PubMed:17302437, PubMed:17442255). Cannot use acetyl-CoA (PubMed:10572016). {ECO:0000269|PubMed:10572016, ECO:0000269|PubMed:17302437, ECO:0000269|PubMed:17442255, ECO:0000269|PubMed:28581482}.
|
Escherichia coli (strain K12)
|
P07630
|
CAH2_CHICK
|
MSHHWGYDSHNGPAHWHEHFPIANGERQSPIAISTKAARYDPALKPLSFSYDAGTAKAIVNNGHSFNVEFDDSSDKSVLQGGALDGVYRLVQFHIHWGSCEGQGSEHTVDGVKYDAELHIVHWNVKYGKFAEALKHPDGLAVVGIFMKVGNAKPEIQKVVDALNSIQTKGKQASFTNFDPTGLLPPCRDYWTYPGSLTTPPLHECVIWHVLKEPITVSSEQMCKLRGLCFSAENEPVCRMVDNWRPCQPLKSREVRASFQ
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00921};
|
carbon dioxide transport [GO:0015670]; cellular response to carbon dioxide [GO:0071244]; one-carbon metabolic process [GO:0006730]; regulation of intracellular pH [GO:0051453]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00918};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can also hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00918}.
|
Gallus gallus (Chicken)
|
P07632
|
SODC_RAT
|
MAMKAVCVLKGDGPVQGVIHFEQKASGEPVVVSGQITGLTEGEHGFHVHQYGDNTQGCTTAGPHFNPHSKKHGGPADEERHVGDLGNVAAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
action potential initiation [GO:0099610]; anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; auditory receptor cell stereocilium organization [GO:0060088]; cellular response to ATP [GO:0071318]; cellular response to cadmium ion [GO:0071276]; cellular response to oxidative stress [GO:0034599]; cellular response to potassium ion [GO:0035865]; determination of adult lifespan [GO:0008340]; ectopic germ cell programmed cell death [GO:0035234]; embryo implantation [GO:0007566]; gene expression [GO:0010467]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide biosynthetic process [GO:0050665]; intracellular iron ion homeostasis [GO:0006879]; locomotory behavior [GO:0007626]; muscle cell cellular homeostasis [GO:0046716]; myeloid cell homeostasis [GO:0002262]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of developmental process [GO:0051093]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of reproductive process [GO:2000242]; neurofilament cytoskeleton organization [GO:0060052]; neuronal action potential [GO:0019228]; ovarian follicle development [GO:0001541]; peripheral nervous system myelin maintenance [GO:0032287]; positive regulation of catalytic activity [GO:0043085]; positive regulation of cytokine production [GO:0001819]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of phagocytosis [GO:0050766]; positive regulation of superoxide anion generation [GO:0032930]; reactive oxygen species metabolic process [GO:0072593]; regulation of blood pressure [GO:0008217]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of multicellular organism growth [GO:0040014]; regulation of protein kinase activity [GO:0045859]; relaxation of vascular associated smooth muscle [GO:0060087]; removal of superoxide radicals [GO:0019430]; response to amphetamine [GO:0001975]; response to antipsychotic drug [GO:0097332]; response to axon injury [GO:0048678]; response to carbon monoxide [GO:0034465]; response to copper ion [GO:0046688]; response to ethanol [GO:0045471]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to nutrient levels [GO:0031667]; response to organic substance [GO:0010033]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; response to superoxide [GO:0000303]; response to xenobiotic stimulus [GO:0009410]; retina homeostasis [GO:0001895]; retrograde axonal transport [GO:0008090]; sensory perception of sound [GO:0007605]; spermatogenesis [GO:0007283]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]; transmission of nerve impulse [GO:0019226]
|
axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; dense core granule [GO:0031045]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]; secretory granule [GO:0030141]
|
copper ion binding [GO:0005507]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein phosphatase 2B binding [GO:0030346]; protein-folding chaperone binding [GO:0051087]; small GTPase binding [GO:0031267]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
|
PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000250}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:2703531}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697; Evidence={ECO:0000305|PubMed:2703531};
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Rattus norvegicus (Rat)
|
P07634
|
ANFB_PIG
|
MGPRMALPRVLLLLFLHLLLLGCRSHPLGGAGLASELPGIQELLDRLRDRVSELQAERTDLEPLRQDRGLTEAWEAREAAPTGVLGPRSSIFQVLRGIRSPKTMRDSGCFGRRLDRIGSLSGLGCNVLRRY
| null | null |
blood vessel diameter maintenance [GO:0097746]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-99 to produce the active brain natriuretic peptide 32 and the inactive NT-proBNP. CORIN also cleaves the precursor molecule at additional residues including Arg-96 and possibly Lys-102 (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to Brain natriuretic peptide 26 (PubMed:3421965). {ECO:0000250|UniProtKB:P16860, ECO:0000269|PubMed:3421965}.; PTM: [Brain natriuretic peptide 32]: Undergoes further proteolytic cleavage by various proteases such as DPP4, MME and possibly FAP, to give rise to a variety of shorter peptides. Cleaved at Pro-101 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Degraded by IDE. During IDE degradation, the resulting products initially increase the activation of NPR1 and can also stimulate NPR2 to produce cGMP before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P16860}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16860}. Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}.; SUBCELLULAR LOCATION: [Brain natriuretic peptide 32]: Secreted {ECO:0000250|UniProtKB:P16860}. Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}.
| null | null | null | null | null |
FUNCTION: [Brain natriuretic peptide 32]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (By similarity). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses. Involved in regulating the extracellular fluid volume and maintaining the fluid-electrolyte balance through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Binds the clearance receptor NPR3 (By similarity). {ECO:0000250|UniProtKB:P16860, ECO:0000250|UniProtKB:P40753}.; FUNCTION: [Brain natriuretic peptide 26]: Plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion (PubMed:2964562). In vivo, induces vasodilation (PubMed:2964562). {ECO:0000269|PubMed:2964562}.; FUNCTION: [NT-proBNP]: May affect cardio-renal homeostasis. Able to promote the production of cGMP although its potency is very low compared to brain natriuretic peptide 32. {ECO:0000250|UniProtKB:P16860}.
|
Sus scrofa (Pig)
|
P07636
|
TNPA_BPMU
|
MELWVSPKECANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFEIARPTLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKFAKPDWAAALVDGRGASRRNVHKSEFDEDAWQFLIADYLRPEKPAFRKCYERLELAAREHGWSIPSRATAFRRIQQLDEAMVVACREGEHALMHLIPAQQRTVEHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMDVVTRYGIPEDFHITIDNTRGAANKWLTGGAPNRYRFKVKEDDPKGLFLLMGAKMHWTSVVAGKGWGQAKPVERAFGVGGLEEYVDKHPALAGAYTGPNPQAKPDNYGDRAVDAELFLKTLAEGVAMFNARTGRETEMCGGKLSFDDVFEREYARTIVRKPTEEQKRMLLLPAEAVNVSRKGEFTLKVGGSLKGAKNVYYNMALMNAGVKKVVVRFDPQQLHSTVYCYTLDGRFICEAECLAPVAFNDAAAGREYRRRQKQLKSATKAAIKAQKQMDALEVAELLPQIAEPAAPESRIVGIFRPSGNTERVKNQERDDEYETERDEYLNHSLDILEQNRRKKAI
|
3.1.22.-; 6.5.1.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14661976, ECO:0000269|PubMed:7912831};
|
DNA integration [GO:0015074]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA transposition [GO:0006313]; latency-replication decision [GO:0098689]; viral DNA genome replication [GO:0039693]
|
host cell cytoplasm [GO:0030430]
|
DNA binding [GO:0003677]; double-stranded DNA endonuclease activity [GO:1990238]; ligase activity [GO:0016874]; metal ion binding [GO:0046872]; transposase activity [GO:0004803]
|
PF02914;PF02316;PF09039;PF09299;
|
6.10.250.2550;1.10.10.60;3.30.420.10;2.30.30.130;1.10.10.10;
|
Mulikevirus repressor c protein family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair.; FUNCTION: Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE-recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target-primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome.; FUNCTION: Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication.
|
Escherichia phage Mu (Bacteriophage Mu)
|
P07639
|
AROB_ECOLI
|
MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQAGVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELASGLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRAGLPVNGPREMSAQAYLPHMLRDKKVLAGEMRLILPLAIGKSEVRSGVSHELVLNAIADCQSA
|
4.2.3.4
|
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; Note=Binds 1 divalent metal cation per subunit. Displays higher activity with Co(2+), however, Zn(2+) may be the physiological metal cofactor. {ECO:0000269|PubMed:2514789};
|
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]
|
cytoplasm [GO:0005737]
|
3-dehydroquinate synthase activity [GO:0003856]; NAD+ binding [GO:0070403]; zinc ion binding [GO:0008270]
|
PF01761;
|
3.40.50.1970;1.20.1090.10;
|
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
|
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 6.5) {ECO:0000269|PubMed:2514789}; KM=5.5 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 8.5) {ECO:0000269|PubMed:2514789};
|
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}.
| null | null |
FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}.
|
Escherichia coli (strain K12)
|
P07647
|
KLK9_RAT
|
MWFLILFLALSLGQIDAAPPGQSRVVGGYNCETNSQPWQVAVIGTTFCGGVLIDPSWVITAAHCYSKNYRVLLGRNNLVKDEPFAQRRLVSQSFQHPDYIPVFMRNHTRQRAYDHNNDLMLLHLSKPADITGGVKVIDLPTEEPKVGSICLASGWGMTNPSEMKLSHDLQCVNIHLLSNEKCIETYKNIETDVTLCAGEMDGGKDTCTGDSGGPLICDGVLQGLTSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP
|
3.4.21.35
| null |
positive regulation of vasoconstriction [GO:0045907]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
secretory granule [GO:0030141]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a trypsin-like properties.
|
Rattus norvegicus (Rat)
|
P07648
|
RECC_ECOLI
|
MLRVYHSNRLDVLEALMEFIVERERLDDPFEPEMILVQSTGMAQWLQMTLSQKFGIAANIDFPLPASFIWDMFVRVLPEIPKESAFNKQSMSWKLMTLLPQLLEREDFTLLRHYLTDDSDKRKLFQLSSKAADLFDQYLVYRPDWLAQWETGHLVEGLGEAQAWQAPLWKALVEYTHQLGQPRWHRANLYQRFIETLESATTCPPGLPSRVFICGISALPPVYLQALQALGKHIEIHLLFTNPCRYYWGDIKDPAYLAKLLTRQRRHSFEDRELPLFRDSENAGQLFNSDGEQDVGNPLLASWGKLGRDYIYLLSDLESSQELDAFVDVTPDNLLHNIQSDILELENRAVAGVNIEEFSRSDNKRPLDPLDSSITFHVCHSPQREVEVLHDRLLAMLEEDPTLTPRDIIVMVADIDSYSPFIQAVFGSAPADRYLPYAISDRRARQSHPVLEAFISLLSLPDSRFVSEDVLALLDVPVLAARFDITEEGLRYLRQWVNESGIRWGIDDDNVRELELPATGQHTWRFGLTRMLLGYAMESAQGEWQSVLPYDESSGLIAELVGHLASLLMQLNIWRRGLAQERPLEEWLPVCRDMLNAFFLPDAETEAAMTLIEQQWQAIIAEGLGAQYGDAVPLSLLRDELAQRLDQERISQRFLAGPVNICTLMPMRSIPFKVVCLLGMNDGVYPRQLAPLGFDLMSQKPKRGDRSRRDDDRYLFLEALISAQQKLYISYIGRSIQDNSERFPSVLVQELIDYIGQSHYLPGDEALNCDESEARVKAHLTCLHTRMPFDPQNYQPGERQSYAREWLPAASQAGKAHSEFVQPLPFTLPETVPLETLQRFWAHPVRAFFQMRLQVNFRTEDSEIPDTEPFILEGLSRYQINQQLLNALVEQDDAERLFRRFRAAGDLPYGAFGEIFWETQCQEMQQLADRVIACRQPGQSMEIDLACNGVQITGWLPQVQPDGLLRWRPSLLSVAQGMQLWLEHLVYCASGGNGESRLFLRKDGEWRFPPLAAEQALHYLSQLIEGYREGMSAPLLVLPESGGAWLKTCYDAQNDAMLDDDSTLQKARTKFLQAYEGNMMVRGEGDDIWYQRLWRQLTPETMEAIVEQSQRFLLPLFRFNQS
| null | null |
clearance of foreign intracellular DNA [GO:0044355]; DNA recombination [GO:0006310]; double-strand break repair via homologous recombination [GO:0000724]; recombinational repair [GO:0000725]; response to radiation [GO:0009314]
|
exodeoxyribonuclease V complex [GO:0009338]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; exodeoxyribonuclease V activity [GO:0008854]
|
PF04257;PF17946;
|
1.10.10.160;1.10.10.990;3.40.50.10930;3.40.50.300;
|
RecC family
| null | null | null | null | null | null | null |
FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination (PubMed:123277, PubMed:4552016, PubMed:4562392). In the holoenzyme this subunit almost certainly recognizes the wild-type Chi sequence, when added to isolated RecB increases its ATP-dependent helicase processivity. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions. {ECO:0000269|PubMed:10197988, ECO:0000269|PubMed:10884344, ECO:0000269|PubMed:123277, ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438, ECO:0000269|PubMed:1535156, ECO:0000269|PubMed:16041061, ECO:0000269|PubMed:1618858, ECO:0000269|PubMed:20852646, ECO:0000269|PubMed:23851395, ECO:0000269|PubMed:4268693, ECO:0000269|PubMed:4552016, ECO:0000269|PubMed:4562392, ECO:0000269|PubMed:7608206, ECO:0000269|PubMed:9192629, ECO:0000269|PubMed:9230304, ECO:0000269|PubMed:9448271, ECO:0000269|PubMed:9790841}.
|
Escherichia coli (strain K12)
|
P07649
|
TRUA_ECOLI
|
MSDQQQPPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPITVFCAGRTDAGVHGTGQVVHFETTALRKDAAWTLGVNANLPGDIAVRWVKTVPDDFHARFSATARRYRYIIYNHRLRPAVLSKGVTHFYEPLDAERMHRAAQCLLGENDFTSFRAVQCQSRTPWRNVMHINVTRHGPYVVVDIKANAFVHHMVRNIVGSLMEVGAHNQPESWIAELLAAKDRTLAAATAKAEGLYLVAVDYPDRYDLPKPPMGPLFLAD
|
5.4.99.12
| null |
tRNA pseudouridine synthesis [GO:0031119]
| null |
protein homodimerization activity [GO:0042803]; pseudouridine synthase activity [GO:0009982]; tRNA binding [GO:0000049]; tRNA pseudouridine synthase activity [GO:0106029]
|
PF01416;
|
3.30.70.660;3.30.70.580;
|
TRNA pseudouridine synthase TruA family
| null | null |
CATALYTIC ACTIVITY: Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA; Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12; Evidence={ECO:0000269|PubMed:17466622};
| null | null | null | null |
FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. {ECO:0000269|PubMed:17466622}.
|
Escherichia coli (strain K12)
|
P07658
|
FDHF_ECOLI
|
MKKVVTVCPYCASGCKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDTQILTPRLKTPMIRRQRGGKLEPVSWDEALNYVAERLSAIKEKYGPDAIQTTGSSRGTGNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYRKIVEGYTPESVEDITGVSASEIRQAARMYAQAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPHAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKDPANREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVFTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGFIQWPCRDTSDADQGTSYLFKEKFDTPNGLAQFFTCDWVAPIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPGYAQINTEDAKRLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYKYCAVRVEPIADQRAAEQYVIDEYNKLKTRLREAALA
|
1.17.98.4
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; COFACTOR: Name=Mo-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60539; Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.;
|
anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; cellular respiration [GO:0045333]; formate oxidation [GO:0015944]; glucose catabolic process [GO:0006007]; urate catabolic process [GO:0019628]
|
cytosol [GO:0005829]; formate dehydrogenase complex [GO:0009326]; membrane [GO:0016020]; plasma membrane respiratory chain complex I [GO:0045272]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; formate dehydrogenase (NAD+) activity [GO:0008863]; metal ion binding [GO:0046872]; molybdopterin cofactor binding [GO:0043546]; oxidoreductase activity, acting on the aldehyde or oxo group of donors [GO:0016903]
|
PF04879;PF00384;PF01568;
|
2.40.40.20;3.40.50.740;2.20.25.90;3.40.228.10;1.20.5.460;
|
Prokaryotic molybdopterin-containing oxidoreductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=A + formate + H(+) = AH2 + CO2; Xref=Rhea:RHEA:27290, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499; EC=1.17.98.4; Evidence={ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0000269|PubMed:9521673};
| null | null | null | null |
FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.
|
Escherichia coli (strain K12)
|
P07662
|
G7AC_PSEU7
|
MLRVLHRAASALVMATVIGLAPAVAFALAEPTSTPQAPIAAYKPRSNEILWDGYGVPHIYGVDAPSAFYGYGWAQARSHGDNILRLYGEARGKGAEYWGPDYEQTTVWLLTNGVPERAQQWYAQQSPDFRANLDAFAAGINAYAQQNPDDISPEVRQVLPVSGADVVAHAHRLMNFLYVASPGRTLGEGDPPDLADQGSNSWAVAPGKTANGNALLLQNPHLSWTTDYFTYYEAHLVTPDFEIYGATQIGLPVIRFAFNQRMGITNTVNGMVGATNYRLTLQDGGYLYDGQVRPFERPQASYRLRQADGTTVDKPLEIRSSVHGPVFERADGTAVAVRVAGLDRPGMLEQYFDMITADSFDDYEAALARMQVPTFNIVYADREGTINYSFNGVAPKRAEGDIAFWQGLVPGDSSRYLWTETHPLDDLPRVTNPPGGFVQNSNDPPWTPTWPVTYTPKDFPSYLAPQTPHSLRAQQSVRLMSENDDLTLERFMALQLSHRAVMADRTLPDLIPAALIDPDPEVQAAARLLAAWDREFTSDSRAALLFEEWARLFAGQNFAGQAGFATPWSLDKPVSTPYGVRDPKAAVDQLRTAIANTKRKYGAIDRPFGDASRMILNDVNVPGAAGYGNLGSFRVFTWSDPDENGVRTPVHGETWVAMIEFSTPVRAYGLMSYGNSRQPGTTHYSDQIERVSRADFRELLLRREQVEAAVQERTPFNFKP
|
3.5.1.93
| null |
antibiotic biosynthetic process [GO:0017000]; response to antibiotic [GO:0046677]
|
periplasmic space [GO:0042597]
|
glutaryl-7-aminocephalosporanic-acid acylase activity [GO:0033968]
|
PF01804;
|
1.10.1400.10;2.30.120.10;3.60.20.10;1.10.439.10;
|
Peptidase S45 family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2993240}.
|
CATALYTIC ACTIVITY: Reaction=(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate; Xref=Rhea:RHEA:23508, ChEBI:CHEBI:15377, ChEBI:CHEBI:30921, ChEBI:CHEBI:58501, ChEBI:CHEBI:58693; EC=3.5.1.93;
| null | null | null | null |
FUNCTION: Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). {ECO:0000269|PubMed:2993240}.
|
Pseudomonas sp. (strain SY-77)
|
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