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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P00950
|
PMG1_YEAST
|
MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK
|
5.4.2.11
| null |
gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; phosphoglycerate mutase activity [GO:0004619]
|
PF00300;
|
3.40.50.1240;
|
Phosphoglycerate mutase family, BPG-dependent PGAM subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}; Peripheral membrane protein {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}; Cytoplasmic side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:16962558}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000269|PubMed:1386023};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=740 uM for 3-phosphoglycerate {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286}; KM=8.1 uM for 2,3-bisphosphoglycerate (for mutase reaction) {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286}; KM=2.4 uM for 2,3-bisphosphoglycerate (for phosphatase reaction) {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286}; Note=kcat is 490 sec(-1) for the mutase reaction, 0.0074 sec(-1) for the synthase reaction and 0.0087 sec(-1) for the phosphatase reaction with 3-phosphoglycerate as substrate. {ECO:0000269|PubMed:1386023};
|
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
| null | null |
FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. {ECO:0000269|PubMed:1386023, ECO:0000269|PubMed:8240286}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00952
|
SYY_GEOSE
|
MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA
|
6.1.1.1
| null |
regulation of protein complex stability [GO:0061635]; tyrosyl-tRNA aminoacylation [GO:0006437]
|
cytosol [GO:0005829]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; tyrosine-tRNA ligase activity [GO:0004831]
|
PF01479;PF00579;
|
3.40.50.620;3.10.290.10;1.10.240.10;
|
Class-I aminoacyl-tRNA synthetase family, TyrS type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; Evidence={ECO:0000269|PubMed:10630994, ECO:0000269|PubMed:11023793, ECO:0000269|PubMed:11023794, ECO:0000269|PubMed:11401566, ECO:0000269|PubMed:1542120};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.35 mM for ATP {ECO:0000269|PubMed:6315404}; KM=1.8 uM for tyrosine {ECO:0000269|PubMed:6315404};
| null | null | null |
FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000269|PubMed:10630994, ECO:0000269|PubMed:11023793, ECO:0000269|PubMed:11023794, ECO:0000269|PubMed:1542120, ECO:0000269|PubMed:6315404}.
|
Geobacillus stearothermophilus (Bacillus stearothermophilus)
|
P00956
|
SYI_ECOLI
|
MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA
|
6.1.1.5
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
isoleucyl-tRNA aminoacylation [GO:0006428]; response to antibiotic [GO:0046677]
|
cytosol [GO:0005829]
|
aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; isoleucine-tRNA ligase activity [GO:0004822]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
|
PF08264;PF00133;PF06827;
|
1.10.730.20;3.40.50.620;3.90.740.10;
|
Class-I aminoacyl-tRNA synthetase family, IleS type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000269|PubMed:3282306};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for isoleucine {ECO:0000269|PubMed:3282306}; KM=0.4 mM for ATP {ECO:0000269|PubMed:3282306};
| null | null | null |
FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). {ECO:0000269|PubMed:10549284, ECO:0000269|PubMed:10889024, ECO:0000269|PubMed:11782529, ECO:0000269|PubMed:11864608, ECO:0000269|PubMed:12515858, ECO:0000269|PubMed:19557155, ECO:0000269|PubMed:3282306, ECO:0000269|PubMed:9554847}.
|
Escherichia coli (strain K12)
|
P00957
|
SYA_ECOLI
|
MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVLKTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKVDEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAVDAINAGQEAVVVLDQTPFYAESGGQVGDKGELKGANFSFAVEDTQKYGQAIGHIGKLAAGSLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSHNEAMKPEEIRAVEDLVNTQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGDFSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAIATVHADSDRLSEVAHLLKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSGVEPKMLRTMVDDLKNQLGSTIIVLATVVEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVGGKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ
|
6.1.1.7
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit; it is not clear where this binding occurs. {ECO:0000269|PubMed:1712632};
|
alanyl-tRNA aminoacylation [GO:0006419]; negative regulation of DNA-templated transcription [GO:0045892]
|
cytosol [GO:0005829]; membrane [GO:0016020]
|
alanine-tRNA ligase activity [GO:0004813]; aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; Ser-tRNA(Ala) hydrolase activity [GO:0002196]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
|
PF02272;PF01411;PF07973;
|
2.40.30.130;3.10.310.40;3.30.54.20;6.10.250.550;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000269|PubMed:7005211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12541; Evidence={ECO:0000305|PubMed:7005211};
| null | null | null | null |
FUNCTION: Catalyzes the attachment of L-alanine to tRNA(Ala) in a two-step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser (PubMed:28362257). These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step. {ECO:0000269|PubMed:28362257}.; FUNCTION: Edits mischarged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr) (PubMed:12554667, PubMed:18723508). Dtd edits Gly-tRNA(Ala) 4-fold better than does AlaRS (PubMed:28362257). {ECO:0000269|PubMed:12554667, ECO:0000269|PubMed:18723508, ECO:0000269|PubMed:28362257}.; FUNCTION: Attaches Ala to transfer-messenger RNA (tmRNA, also known as 10Sa RNA, the product of the ssrA gene). tmRNA plays a major role in rescue of stalled ribosomes via trans-translation. {ECO:0000269|PubMed:7524073}.
|
Escherichia coli (strain K12)
|
P00958
|
SYMC_YEAST
|
MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLYCPVHNSYLADRYVEGECPKCHYDDARGDQCDKCGALLDPFELINPRCKLDDASPEPKYSDHIFLSLDKLESQISEWVEKASEEGNWSKNSKTITQSWLKDGLKPRCITRDLVWGTPVPLEKYKDKVLYVWFDATIGYVSITSNYTKEWKQWWNNPEHVSLYQFMGKDNVPFHTVVFPGSQLGTEENWTMLHHLNTTEYLQYENGKFSKSRGVGVFGNNAQDSGISPSVWRYYLASVRPESSDSHFSWDDFVARNNSELLANLGNFVNRLIKFVNAKYNGVVPKFDPKKVSNYDGLVKDINEILSNYVKEMELGHERRGLEIAMSLSARGNQFLQENKLDNTLFSQSPEKSDAVVAVGLNIIYAVSSIITPYMPEIGEKINKMLNAPALKIDDRFHLAILEGHNINKAEYLFQRIDEKKIDEWRAKYGGQQV
|
6.1.1.10
| null |
glutamyl-tRNA aminoacylation [GO:0006424]; methionyl-tRNA aminoacylation [GO:0006431]
|
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; methionyl glutamyl tRNA synthetase complex [GO:0017102]
|
ATP binding [GO:0005524]; methionine-tRNA ligase activity [GO:0004825]
|
PF19303;PF09635;PF09334;
|
1.20.1050.110;3.40.30.170;3.40.50.620;2.20.28.20;
|
Class-I aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11726524}. Note=Largely excluded from the nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000269|PubMed:3312199, ECO:0000269|PubMed:8895587, ECO:0000269|PubMed:9659920};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for tRNA(Met) (in the absence of ARC1) {ECO:0000269|PubMed:3312199, ECO:0000269|PubMed:8895587, ECO:0000269|PubMed:9659920}; KM=10 uM for methionine {ECO:0000269|PubMed:3312199, ECO:0000269|PubMed:8895587, ECO:0000269|PubMed:9659920}; Note=The presence of ARC1 reduces the KM for tRNA(Met) to less than 0.1 uM and increases the catalytic efficiency more than 500-fold.;
| null | null | null |
FUNCTION: Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction: methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met). {ECO:0000269|PubMed:8895587}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00959
|
SYM_ECOLI
|
MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK
|
6.1.1.10
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
methionyl-tRNA aminoacylation [GO:0006431]
|
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; membrane [GO:0016020]
|
ATP binding [GO:0005524]; methionine-tRNA ligase activity [GO:0004825]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
|
PF19303;PF09334;PF01588;
|
3.40.50.620;2.20.28.20;2.40.50.140;
|
Class-I aminoacyl-tRNA synthetase family, MetG type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10;
| null | null | null | null |
FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Escherichia coli (strain K12)
|
P00962
|
SYQ_ECOLI
|
MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTWAKVGE
|
6.1.1.18
| null |
glutaminyl-tRNA aminoacylation [GO:0006425]; glutamyl-tRNA aminoacylation [GO:0006424]
|
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; glutamine-tRNA ligase activity [GO:0004819]
|
PF00749;PF03950;PF20974;
|
3.40.50.620;
|
Class-I aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563};
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P00963
|
ASNA_ECOLI
|
MKTAYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGCEKAVQVKVKALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDEDRLSPLHSVYVDQWDWERVMGDGERQFSTLKSTVEAIWAGIKATEAAVSEEFGLAPFLPDQIHFVHSQELLSRYPDLDAKGRERAIAKDLGAVFLVGIGGKLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWNPVLEDAFELSSMGIRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRLTMLLLQLPHIGQVQCGVWPAAVRESVPSLL
|
6.3.1.1
| null |
asparagine biosynthetic process [GO:0006529]; DNA damage response [GO:0006974]; L-asparagine biosynthetic process [GO:0070981]
|
cytosol [GO:0005829]
|
aspartate-ammonia ligase activity [GO:0004071]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF03590;
| null |
Class-II aminoacyl-tRNA synthetase family, AsnA subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine; Xref=Rhea:RHEA:11372, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:456215; EC=6.3.1.1; Evidence={ECO:0000269|PubMed:1369484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11373; Evidence={ECO:0000305|PubMed:1369484};
| null |
PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1.
| null | null |
FUNCTION: May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn. {ECO:0000305|PubMed:17962566}.
|
Escherichia coli (strain K12)
|
P00966
|
ASSY_HUMAN
|
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
|
6.3.4.5
| null |
acute-phase response [GO:0006953]; arginine biosynthetic process [GO:0006526]; argininosuccinate metabolic process [GO:0000053]; aspartate metabolic process [GO:0006531]; cellular response to amine stimulus [GO:0071418]; cellular response to amino acid stimulus [GO:0071230]; cellular response to ammonium ion [GO:0071242]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucagon stimulus [GO:0071377]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oleic acid [GO:0071400]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; circadian rhythm [GO:0007623]; citrulline metabolic process [GO:0000052]; diaphragm development [GO:0060539]; kidney development [GO:0001822]; liver development [GO:0001889]; midgut development [GO:0007494]; negative regulation of leukocyte cell-cell adhesion [GO:1903038]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; response to estradiol [GO:0032355]; response to growth hormone [GO:0060416]; response to mycotoxin [GO:0010046]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; response to zinc ion [GO:0010043]; urea cycle [GO:0000050]
|
cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]
|
amino acid binding [GO:0016597]; argininosuccinate synthase activity [GO:0004055]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; toxic substance binding [GO:0015643]
|
PF20979;PF00764;
|
3.90.1260.10;3.40.50.620;1.20.5.470;
|
Argininosuccinate synthase family, Type 1 subfamily
|
PTM: Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases. {ECO:0000269|PubMed:28985504}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28985504, ECO:0000305|PubMed:27287393}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000269|PubMed:18473344, ECO:0000269|PubMed:27287393, ECO:0000269|PubMed:8792870};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=112 uM for citrulline (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:18473344}; KM=68 uM for aspartate (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:18473344}; Vmax=143 nmol/min/mg enzyme toward citrulline (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:18473344}; Vmax=116 nmol/min/mg enzyme toward aspartate (at pH 7.0 and 37 degrees) {ECO:0000269|PubMed:18473344};
|
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. {ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393, ECO:0000305|PubMed:8792870}.; PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. {ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393, ECO:0000305|PubMed:8792870}.
| null | null |
FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues. {ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393, ECO:0000305|PubMed:8792870}.
|
Homo sapiens (Human)
|
P00967
|
PUR2_DROME
|
MSHRVLVIGSGGREHAICWKLSQSPKVAQIYALPGSHGIQLVEKCRNLDAKTLDPKDFEAIAKWSKENQIALVVVGPEDPLALGLGDVLQSAGIPCFGPGKQGAQIEADKKWAKDFMLRHGIPTARYESFTDTEKAKAFIRSAPYPALVVKAAGLAAGKGVVVAANAKEACQAVDEILGDLKYGQAGATLVVEELLEGEEVSVLAFTDGKSVRAMLPAQDHKRLGNGDTGPNTGGMGAYCPCPLISQPALELVQKAVLERAVQGLIKERINYQGVLYAGLMLTRDGPRVLEFNCRFGDPETQVILPLLESDLFDVMEACCSGKLDKIPLQWRNGVSAVGVILASAGYPETSTKGCIISGLPAANTPTQLVFHSGLAVNAQKEALTNGGRVLIAIALDGSLKEAAAKATKLAGSISFSGSGAQYRTDIAQKAFKIASASTPGLSYKDSGVDIDAGDALVQRIKPLSRGTQRPGVIGGLGGFGGLFRLKELTYKEPVIAEATQGVGAKIHLALTHEFYENVGYDLFALAANDVLEVGAEPVAFLDYIACGKLQVPLAAQLVKGMADGCRDARCALVGGETAEMPSLYAPGQHDMAGYCVGIVEHSRILPRFDLYQPGDLLIGLPSSGLHCAGFNEILTQLAASKVNLRERSPVDGGDDGLTLAHVLATPTQLYVQQLLPHLQKGDEIKSVAHVTHGLLNDILRLLPDGFETTLDFGAVPVPKIFGWLAGKLKLSAQTILERHNCGIGMVLILPQSSQLWRTSLPGAKVLGVLQRRSKVSGSPVQVRNFVEQLEKVASPFGGLGDRELPEELKKLPSNSDLSAPREECFENAAGRRLTRIPTHYKDPILILGTDGVGTKLKIAQQTNRNTSVGIDLVAMCVNDILCNGAEPISFSSYYACGHWQEQLAKGVHSGVQEGARQANSSFIDSHSAALPLLYEPQVYDLAGFALGIAEHTGILPLLAEIQPGDVLIGLPSSGVHSNGFSLVHAVLKRVGLGLHDKAPFSDKTLGEELLVPTKIYVKALSTLLSRGKHGIKALAHITGGGLSENIPRVLRKDLAVRLDANKFQLPPVFAWLAAAGNISSTELQRTYNCGLGMVLVVAPTEVEDVLKELRYPQRAAVVGEVVARKDPKKSQVVVQNFEASLARTQKMLSQRRKRVAVLISGTGSNLQALIDATRDSAQGIHADVVLVISNKPGVLGLQRATQAGIPSLVISHKDFASREVYDAELTRNLKAARVDLICLAGFMRVLSAPFVREWRGRLVNIHPSLLPKYPGLHVQKQALEAGEKESGCTVHFVDEGVDTGAIIVQAAVPILPDDDEDSLTQRIHKAEHWAFPRALAMLVNGTALISPEVSSQ
|
2.1.2.2; 6.3.3.1; 6.3.4.13
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P15640, ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 1 magnesium or manganese ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409};
|
'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleotide biosynthetic process [GO:0006164]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641]; phosphoribosylglycinamide formyltransferase activity [GO:0004644]
|
PF00586;PF02769;PF00551;PF01071;PF02843;PF02844;
|
3.40.50.20;3.30.1490.20;3.30.470.20;3.40.50.170;3.90.600.10;3.90.650.10;3.30.1330.10;
|
GARS family; AIR synthase family; GART family
| null | null |
CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000269|PubMed:3086869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17454; Evidence={ECO:0000305|PubMed:3086869}; CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000269|PubMed:3086869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23033; Evidence={ECO:0000305|PubMed:3086869}; CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366; EC=2.1.2.2; Evidence={ECO:0000269|PubMed:3086869}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15054; Evidence={ECO:0000305|PubMed:3086869};
| null |
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000269|PubMed:3086869}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. {ECO:0000269|PubMed:3086869}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. {ECO:0000269|PubMed:3086869}.
| null | null |
FUNCTION: Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway. {ECO:0000269|PubMed:3086869}.
|
Drosophila melanogaster (Fruit fly)
|
P00968
|
CARB_ECOLI
|
MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQIK
|
6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01210}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:10428826}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:10428826};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; amino acid biosynthetic process [GO:0008652]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856]; UTP biosynthetic process [GO:0006228]
|
carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]
|
PF02786;PF02787;PF02142;
|
3.40.50.20;3.30.470.20;1.10.1030.10;3.40.50.1380;
|
CarB family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:4944634}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase large chain]: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:4944634};
| null |
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000305|Ref.8}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000305|Ref.8}.
| null | null |
FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate. {ECO:0000255|HAMAP-Rule:MF_01210, ECO:0000269|PubMed:2658488, ECO:0000269|PubMed:2868386, ECO:0000269|PubMed:4944634, ECO:0000269|Ref.8}.
|
Escherichia coli (strain K12)
|
P00971
|
RLIG_BPT4
|
MQELFNNLMELCKDSQRKFFYSDDVSASGRTYRIFSYNYASYSDWLLPDALECRGIMFEMDGEKPVRIASRPMEKFFNLNENPFTMNIDLNDVDYILTKEDGSLVSTYLDGDEILFKSKGSIKSEQALMANGILMNINHHRLRDRLKELAEDGFTANFEFVAPTNRIVLAYQEMKIILLNVRENETGEYISYDDIYKDATLRPYLVERYEIDSPKWIEEAKNAENIEGYVAVMKDGSHFKIKSDWYVSLHSTKSSLDNPEKLFKTIIDGASDDLKAMYADDEYSYRKIEAFETTYLKYLDRALFLVLDCHNKHCGKDRKTYAMEAQGVAKGAGMDHLFGIIMSLYQGYDSQEKVMCEIEQNFLKNYKKFIPEGY
|
6.5.1.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04149, ECO:0000269|PubMed:16263720, ECO:0000269|PubMed:28223499}; Note=Binds 2 magnesium ions that perform the catalytic activity via a two-metal mechanism (PubMed:16263720, PubMed:28223499). One of the catalytic Mg(2+), which is coordinated by 5 water molecules, engages the lysine nucleophile and the ATP alpha phosphate while the Mg(2+) orients the PPi leaving group (PubMed:28223499). {ECO:0000255|HAMAP-Rule:MF_04149, ECO:0000269|PubMed:16263720, ECO:0000269|PubMed:28223499};
|
RNA repair [GO:0042245]; virus tail fiber assembly [GO:0098004]
| null |
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; RNA ligase (ATP) activity [GO:0003972]
|
PF09511;PF20819;
|
1.10.3550.20;
|
Tequatrovirus RNA ligase 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_04149, ECO:0000269|PubMed:12766156, ECO:0000269|PubMed:17068206, ECO:0000269|PubMed:3036206};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:16671895};
| null |
FUNCTION: Involved in countering a host defense mechanism which, following viral infection, activates the host anticodon nuclease and shuts off viral translation. Repairs 5'-PO4 and 3'-OH groups in the cleaved host tRNA (PubMed:16671895, PubMed:17068206, PubMed:2444436). The nick ligation reaction entails three nucleotidyl transfer steps (PubMed:12766156). In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate (PubMed:12766156). In step 2, the ligase-AMP binds to the nicked duplex nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated nicked intermediate (PubMed:12766156). In step 3, the RNA ligase directs the attack of the nick 3'-OH on the 5'-phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP (By similarity) (PubMed:12766156). {ECO:0000255|HAMAP-Rule:MF_04149, ECO:0000269|PubMed:12766156, ECO:0000269|PubMed:16671895, ECO:0000269|PubMed:17068206, ECO:0000269|PubMed:2444436}.
|
Enterobacteria phage T4 (Bacteriophage T4)
|
P00973
|
OAS1_HUMAN
|
MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL
|
2.7.7.84
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23319625};
|
antiviral innate immune response [GO:0140374]; cellular response to interferon-alpha [GO:0035457]; cellular response to interferon-beta [GO:0035458]; cellular response to virus [GO:0098586]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; interleukin-27-mediated signaling pathway [GO:0070106]; negative regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000342]; negative regulation of IP-10 production [GO:0071659]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; negative regulation of viral genome replication [GO:0045071]; positive regulation of cellular respiration [GO:1901857]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of monocyte chemotactic protein-1 production [GO:0071639]; positive regulation of tumor necrosis factor production [GO:0032760]; protein complex oligomerization [GO:0051259]; regulation of ribonuclease activity [GO:0060700]; response to virus [GO:0009615]; surfactant homeostasis [GO:0043129]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; type I interferon-mediated signaling pathway [GO:0060337]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribosome [GO:0005840]
|
2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]
|
PF01909;PF10421;
|
1.10.1410.20;3.30.460.10;
|
2-5A synthase family
|
PTM: [Isoform p46]: Prenylated at C-terminal. C-terminal prenylation is necessary to initiate a block to SARS-CoV-2 and is associated with protection from severe COVID-1. The prenylated form is targeted to perinuclear structures rich in viral dsRNA, whereas the non-prenylated form is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication (Probable). C-terminal prenylation is also necessary to initiate a block to cardiovirus EMCV (Probable). {ECO:0000305|PubMed:34581622}.; PTM: [Isoform p42]: Not prenylated at C-terminal. The non-prenylated form is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication. {ECO:0000269|PubMed:34581622}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:3753689, ECO:0000269|PubMed:3754863}. Mitochondrion {ECO:0000269|PubMed:19923450}. Nucleus {ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:3753689}. Microsome {ECO:0000269|PubMed:19923450}. Endoplasmic reticulum {ECO:0000269|PubMed:19923450}. Secreted {ECO:0000250|UniProtKB:Q29599}. Note=Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. {ECO:0000269|PubMed:19923450}.; SUBCELLULAR LOCATION: [Isoform p46]: Note=(Microbial infection) In SARS coronavirus-2/SARS-CoV-2 infected cells, prenylated form localizes to membranous perinuclear structures reminiscent of the endoplasmic reticulum rich in viral dsRNA which are SARS-CoV-2 replicative organelles. {ECO:0000269|PubMed:34581622}.; SUBCELLULAR LOCATION: [Isoform p42]: Note=(Microbial infection) In SARS coronavirus-2/SARS-CoV-2 infected cells, since its not prenylated, is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication. {ECO:0000269|PubMed:34581622}.
|
CATALYTIC ACTIVITY: Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence={ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:12799444, ECO:0000269|PubMed:23319625, ECO:0000269|PubMed:25775560, ECO:0000269|PubMed:3753689, ECO:0000269|PubMed:3754863, ECO:0000269|PubMed:9407111};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for ATP {ECO:0000269|PubMed:12799444};
| null | null | null |
FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:34581622). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:34145065, PubMed:34581622). Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12799444, ECO:0000269|PubMed:18931074, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:23319625, ECO:0000269|PubMed:34145065, ECO:0000269|PubMed:34581622}.; FUNCTION: [Isoform p46]: When prenylated at C-terminal, acts as a double-stranded RNA (dsRNA) sensor specifically targeted to membranous replicative organelles in SARS coronavirus-2/SARS-CoV-2 infected cells where it binds to dsRNA structures in the SARS-CoV-2 5'-UTR and initiates a potent block to SARS-CoV-2 replication. Recognizes short stretches of dsRNA and activates RNase L. The binding is remarkably specific, with two conserved stem loops in the SARS-CoV-2 5'- untranslated region (UTR) constituting the principal viral target (PubMed:34581622). The same mechanism is necessary to initiate a block to cardiovirus EMCV (PubMed:34581622). {ECO:0000269|PubMed:34581622}.; FUNCTION: [Isoform p42]: Not prenylated at C-terminal, is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication. {ECO:0000269|PubMed:34581622}.
|
Homo sapiens (Human)
|
P00974
|
BPT1_BOVIN
|
MKMSRLCLSVALLVLLGTLAASTPGCDTSNQAKAQRPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGAIGPWENL
| null | null |
negative regulation of platelet aggregation [GO:0090331]; negative regulation of serine-type endopeptidase activity [GO:1900004]; negative regulation of thrombin-activated receptor signaling pathway [GO:0070495]; trypsinogen activation [GO:0032023]
|
extracellular space [GO:0005615]; serine protease inhibitor complex [GO:0097180]
|
calcium ion binding [GO:0005509]; molecular function inhibitor activity [GO:0140678]; potassium channel inhibitor activity [GO:0019870]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]; sulfate binding [GO:0043199]; zymogen binding [GO:0035375]
|
PF00014;
|
4.10.410.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
|
Bos taurus (Bovine)
|
P00978
|
AMBP_BOVIN
|
MRSLSGLLLLLTACLAVNASSVPTLPDDIQVQENFDLSRIYGKWFNVAVGSTCPWLKRFKEKMTMSTVVLIAGPTSKEISVTNTHRRKGVCESISGTYEKTSADGKFLYHKAKWNITMESYVVHTNYDEYAIFLTKKLSRRHGPTITVKLYGREPQLRESLLEEFREVALGVGIPEDAIFTMPDRGECVPGEQDPVPTPLSRARRAVLTQEEEGSGAGQPVTNFSKKADSCQLDYSQGPCLGLFKRYFYNGTSMACETFLYGGCMGNGNNFLSEKECLQTCRTVEACNLPIVQGPCRSYIQLWAFDAVKGKCVRFSYGGCKGNGNKFYSEKECKEYCGIPGEADEELLRFSN
|
1.6.2.-
| null | null |
cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]
|
heme binding [GO:0020037]; IgA binding [GO:0019862]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00014;PF00061;
|
2.40.128.20;4.10.410.10;
|
Calycin superfamily, Lipocalin family
|
PTM: The precursor is proteolytically processed into separately functioning proteins. {ECO:0000250|UniProtKB:P02760}.; PTM: [Alpha-1-microglobulin]: 3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'. {ECO:0000250|UniProtKB:P02760}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the C-terminal aspartate. {ECO:0000250|UniProtKB:P02760}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Proteolytically cleaved by PRSS3 at Kunitz domain 2. {ECO:0000250|UniProtKB:P02760}.
|
SUBCELLULAR LOCATION: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.; SUBCELLULAR LOCATION: [Inter-alpha-trypsin inhibitor light chain]: Secreted {ECO:0000250|UniProtKB:P02760}.
| null | null | null | null | null |
FUNCTION: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}.; FUNCTION: [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as a potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}.; FUNCTION: [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
|
Bos taurus (Bovine)
|
P00980
|
VKTHA_DENAN
|
QPRRKLCILHRNPGRCYDKIPAFYYNQKKKQCERFDWSGCGGNSNRFKTIEECRRTCIG
| null | null | null |
extracellular space [GO:0005615]
|
potassium channel regulator activity [GO:0015459]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729]
|
PF00014;
|
4.10.410.10;
|
Venom Kunitz-type family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC(50)=0.4-150 nM) and facilitates neurotransmitter release. {ECO:0000269|PubMed:10936620, ECO:0000269|PubMed:23771044}.
|
Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
|
P00981
|
VKTHK_DENPO
|
SGHLLLLLGLLTLWAELTPVSGAAKYCKLPLRIGPCKRKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG
| null | null | null |
extracellular space [GO:0005615]
|
potassium channel regulator activity [GO:0015459]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729]
|
PF00014;
|
4.10.410.10;
|
Venom Kunitz-type family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor homolog that selectively blocks voltage-gated potassium channels homooligomer Kv1.1/KCNA1 (EC(50)=0.6 nM) and Kv1.1-containing heterooligomer. {ECO:0000269|PubMed:10429207, ECO:0000269|PubMed:8612784, ECO:0000269|PubMed:9134213}.
|
Dendroaspis polylepis polylepis (Black mamba)
|
P00982
|
VKTHD_DENAN
|
AAKYCKLPVRYGPCKKKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG
| null | null | null |
extracellular space [GO:0005615]
|
potassium channel regulator activity [GO:0015459]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729]
|
PF00014;
|
4.10.410.10;
|
Venom Kunitz-type family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv). {ECO:0000269|PubMed:10698633}.
|
Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
|
P00995
|
ISK1_HUMAN
|
MKVTGIFLLSALALLSLSGNTGADSLGREAKCYNELNGCTKIYDPVCGTDGNTYPNECVLCFENRKRQTSILIQKSGPC
| null | null |
cellular response to peptide hormone stimulus [GO:0071375]; negative regulation of calcium ion import [GO:0090281]; negative regulation of nitric oxide mediated signal transduction [GO:0010751]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; nitric oxide mediated signal transduction [GO:0007263]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of pancreatic juice secretion [GO:0090187]; positive regulation of peptide hormone secretion [GO:0090277]; regulation of acrosome reaction [GO:0060046]; regulation of store-operated calcium entry [GO:2001256]; response to ethanol [GO:0045471]; response to nutrient levels [GO:0031667]; sperm capacitation [GO:0048240]
|
extracellular exosome [GO:0070062]
|
endopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00050;
|
3.30.60.30;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7142173}.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:7142173). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (By similarity). {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:7142173}.; FUNCTION: In the male reproductive tract, binds to sperm heads where it modulates sperm capacitance by inhibiting calcium uptake and nitrogen oxide (NO) production. {ECO:0000250|UniProtKB:P09036}.
|
Homo sapiens (Human)
|
P01001
|
ISK6_BOVIN
|
MKTSGVFLLLSLALFCFFSGVFGQGAQVDCAEFKDPKVYCTRESNPHCGSDGQTYGNKCAFCKAVMKSGGKINLKHRGKC
| null | null | null |
extracellular region [GO:0005576]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00050;
|
3.30.60.30;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8BT20}.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor selective for kallikreins. Efficiently inhibits KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14. Doesn't inhibit KLK8. Inhibits acrosin, trypsin, and chymotrypsin. {ECO:0000250|UniProtKB:Q6UWN8}.
|
Bos taurus (Bovine)
|
P01005
|
IOVO_CHICK
|
MAMAGVFVLFSFVLCGFLPDAAFGAEVDCSRFPNATDKEGKDVLVCNKDLRPICGTDGVTYTNDCLLCAYSIEFGTNISKEHDGECKETVPMNCSSYANTTSEDGKVMVLCNRAFNPVCGTDGVTYDNECLLCAHKVEQGASVDKRHDGGCRKELAAVSVDCSEYPKPDCTAEDRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC
| null | null |
response to steroid hormone [GO:0048545]
|
endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
carbohydrate binding [GO:0030246]; IgE binding [GO:0019863]; IgG binding [GO:0019864]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00050;
|
3.30.60.30;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: No decrease in activity observed after incubating at pH 2.5 and pH 7.4 for 1 hour. Retains 20% activity after incubation at pH 12 for 1 hour. {ECO:0000269|PubMed:23075397};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: No decrease in activity observed after heating for 1 hour at up to 80 degrees Celsius. Retains 20% activity after incubation at 95 degrees Celsius for 1 hour. {ECO:0000269|PubMed:23075397};
|
FUNCTION: Serine protease inhibitor. Inhibits trypsin. {ECO:0000269|PubMed:23075397}.
|
Gallus gallus (Chicken)
|
P01006
|
SSI_STRAO
|
MRNTGAGPSPSVSRPPPSAAPLSGAALAAPGDAPSALYAPSALVLTVGKGVSATTAAPERAVTLTCAPGPSGTHPAAGSACADLAAVGGDLNALTRGEDVMCPMVYDPVLLTVDGVWQGKRVSYERVFSNECEMNAHGSSVFAF
| null | null | null |
extracellular region [GO:0005576]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00720;
|
3.30.350.10;
|
Protease inhibitor I16 (SSI) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Strong inhibitor of bacterial serine proteases such as subtilisin.
|
Streptomyces albogriseolus
|
P01008
|
ANT3_HUMAN
|
MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK
| null | null |
blood coagulation [GO:0007596]; regulation of blood coagulation [GO:0030193]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade (PubMed:15140129, PubMed:15853774). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory activity is greatly enhanced in the presence of heparin. {ECO:0000269|PubMed:15140129, ECO:0000269|PubMed:15853774}.
|
Homo sapiens (Human)
|
P01009
|
A1AT_HUMAN
|
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
| null | null |
acute-phase response [GO:0006953]; blood coagulation [GO:0007596]
|
collagen-containing extracellular matrix [GO:0062023]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; platelet alpha granule lumen [GO:0031093]
|
identical protein binding [GO:0042802]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;2.10.310.10;
|
Serpin family
|
PTM: N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23826168}.; PTM: Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.; PTM: (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases. {ECO:0000269|PubMed:3533918}.
|
SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum. Note=The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Short peptide from AAT]: Secreted, extracellular space, extracellular matrix.
| null | null | null | null | null |
FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.; FUNCTION: [Short peptide from AAT]: Reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).
|
Homo sapiens (Human)
|
P01011
|
AACT_HUMAN
|
MERMLPLLALGLLAAGFCPAVLCHPNSPLDEENLTQENQDRGTHVDLGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLSALVETRTIVRFNRPFLMIIVPTDTQNIFFMSKVTNPKQA
| null | null |
acute-phase response [GO:0006953]; inflammatory response [GO:0006954]; maintenance of gastrointestinal epithelium [GO:0030277]; regulation of lipid metabolic process [GO:0019216]
|
azurophil granule lumen [GO:0035578]; blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; platelet alpha granule lumen [GO:0031093]; secretory granule lumen [GO:0034774]
|
DNA binding [GO:0003677]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. {ECO:0000269|PubMed:2404007}.
|
Homo sapiens (Human)
|
P01012
|
OVAL_CHICK
|
MGSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRFDKLPGFGDSIEAQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIVFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDVFSSSANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHIATNAVLFFGRCVSP
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; intracellular amino acid homeostasis [GO:0080144]; monoatomic ion homeostasis [GO:0050801]; monoatomic ion transport [GO:0006811]; response to corticosterone [GO:0051412]; response to estrogen [GO:0043627]; response to progesterone [GO:0032570]; response to steroid hormone [GO:0048545]
|
cytosol [GO:0005829]; early endosome lumen [GO:0031905]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; phagocytic vesicle [GO:0045335]; phagolysosome [GO:0032010]; vesicle [GO:0031982]
|
calcium ion binding [GO:0005509]; protease binding [GO:0002020]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family, Ov-serpin subfamily
|
PTM: Undergoes proteolytic cleavage first at the canonical P1-P1' site, and then at the P8-P7 site by subtilisin. {ECO:0000269|PubMed:11779232, ECO:0000269|PubMed:11931671}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6749856}.
| null | null | null | null | null |
FUNCTION: Non-inhibitory serpin. Storage protein of egg white. {ECO:0000269|PubMed:3732511, ECO:0000269|PubMed:6749856}.
|
Gallus gallus (Chicken)
|
P01015
|
ANGT_RAT
|
MTPTGAGLKATIFCILTWVSLTAGDRVYIHPFHLLYYSKSTCAQLENPSVETLPEPTFEPVPIQAKTSPVDEKTLRDKLVLATEKLEAEDRQRAAQVAMIANFMGFRMYKMLSEARGVASGAVLSPPALFGTLVSFYLGSLDPTASQLQVLLGVPVKEGDCTSRLDGHKVLTALQAVQGLLVTQGGSSSQTPLLQSTVVGLFTAPGLRLKQPFVESLGPFTPAIFPRSLDLSTDPVLAAQKINRFVQAVTGWKMNLPLEGVSTDSTLFFNTYVHFQGKMRGFSQLTGLHEFWVDNSTSVSVPMLSGTGNFQHWSDAQNNFSVTRVPLGESVTLLLIQPQCASDLDRVEVLVFQHDFLTWIKNPPPRAIRLTLPQLEIRGSYNLQDLLAQAKLSTLLGAEANLGKMGDTNPRVGEVLNSILLELQAGEEEQPTESAQQPGSPEVLDVTLSSPFLFAIYERDSGALHFLGRVDNPQNVV
| null | null |
aldosterone secretion [GO:0035932]; angiotensin-activated signaling pathway [GO:0038166]; angiotensin-mediated drinking behavior [GO:0003051]; angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure [GO:0001998]; artery smooth muscle contraction [GO:0014824]; associative learning [GO:0008306]; astrocyte activation [GO:0048143]; blood vessel development [GO:0001568]; brain renin-angiotensin system [GO:0002035]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell growth involved in cardiac muscle cell development [GO:0061049]; cell population proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; cell-matrix adhesion [GO:0007160]; cellular response to angiotensin [GO:1904385]; cellular response to mechanical stimulus [GO:0071260]; drinking behavior [GO:0042756]; ERK1 and ERK2 cascade [GO:0070371]; establishment of blood-nerve barrier [GO:0008065]; extracellular matrix organization [GO:0030198]; female pregnancy [GO:0007565]; fibroblast proliferation [GO:0048144]; G protein-coupled receptor signaling pathway [GO:0007186]; hormone metabolic process [GO:0042445]; intracellular sodium ion homeostasis [GO:0006883]; kidney development [GO:0001822]; maintenance of blood vessel diameter homeostasis by renin-angiotensin [GO:0002034]; MAPK cascade [GO:0000165]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neurotrophin TRK receptor signaling pathway [GO:0051387]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of tissue remodeling [GO:0034104]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; neuron apoptotic process [GO:0051402]; operant conditioning [GO:0035106]; organ growth [GO:0035265]; ovarian follicle rupture [GO:0001543]; peristalsis [GO:0030432]; positive regulation of blood pressure [GO:0045777]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of extracellular matrix constituent secretion [GO:0003331]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gap junction assembly [GO:1903598]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of L-arginine import across plasma membrane [GO:1905589]; positive regulation of L-lysine import across plasma membrane [GO:1905010]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of neuron projection development [GO:0010976]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of organ growth [GO:0046622]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of transforming growth factor beta1 activation [GO:1901394]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein import into nucleus [GO:0006606]; regulation of apoptotic process [GO:0042981]; regulation of blood pressure [GO:0008217]; regulation of calcium ion transport [GO:0051924]; regulation of cardiac conduction [GO:1903779]; regulation of extracellular matrix assembly [GO:1901201]; regulation of gene expression [GO:0010468]; regulation of heart rate [GO:0002027]; regulation of inflammatory response [GO:0050727]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of norepinephrine secretion [GO:0014061]; regulation of renal output by angiotensin [GO:0002019]; regulation of systemic arterial blood pressure by circulatory renin-angiotensin [GO:0001991]; regulation of transmission of nerve impulse [GO:0051969]; renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure [GO:0001999]; renal system process [GO:0003014]; renin-angiotensin regulation of aldosterone production [GO:0002018]; response to angiotensin [GO:1990776]; response to cold [GO:0009409]; response to estradiol [GO:0032355]; response to mechanical stimulus [GO:0009612]; response to muscle activity involved in regulation of muscle adaptation [GO:0014873]; response to salt stress [GO:0009651]; smooth muscle cell differentiation [GO:0051145]; smooth muscle cell proliferation [GO:0048659]; stress-activated MAPK cascade [GO:0051403]; uterine smooth muscle contraction [GO:0070471]; vascular associated smooth muscle cell proliferation [GO:1990874]; vasoconstriction [GO:0042310]; vasodilation [GO:0042311]; vasopressin secretion [GO:0030103]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; serine-type endopeptidase inhibitor activity [GO:0004867]; type 1 angiotensin receptor binding [GO:0031702]; type 2 angiotensin receptor binding [GO:0031703]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4. Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (By similarity). {ECO:0000250|UniProtKB:P01019}.; PTM: The disulfide bond is labile. Angiotensinogen is present in the circulation in a near 40:60 ratio with the oxidized disulfide-bonded form, which preferentially interacts with receptor-bound renin. {ECO:0000269|PubMed:20927107}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:4344907}.
| null | null | null | null | null |
FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. {ECO:0000250|UniProtKB:P01019}.; FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. Acts by binding to angiotensin receptors AGTR1 and AGTR2 (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (PubMed:9508787). {ECO:0000250|UniProtKB:P01019, ECO:0000269|PubMed:9508787}.; FUNCTION: [Angiotensin-3]: Stimulates aldosterone release. {ECO:0000250|UniProtKB:P01019}.; FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (PubMed:18026570). {ECO:0000250|UniProtKB:P11859, ECO:0000269|PubMed:18026570}.
|
Rattus norvegicus (Rat)
|
P01019
|
ANGT_HUMAN
|
MAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA
| null | null |
angiotensin-activated signaling pathway [GO:0038166]; blood vessel remodeling [GO:0001974]; cell-cell signaling [GO:0007267]; G protein-coupled receptor signaling pathway [GO:0007186]; G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger [GO:0007199]; kidney development [GO:0001822]; low-density lipoprotein particle remodeling [GO:0034374]; maintenance of blood vessel diameter homeostasis by renin-angiotensin [GO:0002034]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neurotrophin TRK receptor signaling pathway [GO:0051387]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of activation of Janus kinase activity [GO:0010536]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gap junction assembly [GO:1903598]; positive regulation of inflammatory response [GO:0050729]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transforming growth factor beta1 activation [GO:1901394]; regulation of apoptotic process [GO:0042981]; regulation of blood pressure [GO:0008217]; regulation of blood volume by renin-angiotensin [GO:0002016]; regulation of cardiac conduction [GO:1903779]; regulation of cell growth [GO:0001558]; regulation of cell population proliferation [GO:0042127]; regulation of extracellular matrix assembly [GO:1901201]; regulation of renal output by angiotensin [GO:0002019]; regulation of renal sodium excretion [GO:0035813]; regulation of vasoconstriction [GO:0019229]; renal system process [GO:0003014]; renin-angiotensin regulation of aldosterone production [GO:0002018]; response to angiotensin [GO:1990776]; response to muscle activity involved in regulation of muscle adaptation [GO:0014873]; vasoconstriction [GO:0042310]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; serine-type endopeptidase inhibitor activity [GO:0004867]; type 1 angiotensin receptor binding [GO:0031702]; type 2 angiotensin receptor binding [GO:0031703]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family
|
PTM: Beta-decarboxylation of Asp-25 in angiotensin-2, by mononuclear leukocytes produces alanine (PubMed:17138938). The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor (PubMed:17138938). {ECO:0000269|PubMed:17138938}.; PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1 (PubMed:12045255). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2 (PubMed:10969042, PubMed:4322742). Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4 (PubMed:10969042, PubMed:11815627). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4 (PubMed:10969042, PubMed:11815627). Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (PubMed:15283675). {ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:4322742}.; PTM: The disulfide bond is labile. Angiotensinogen is present in the circulation in a near 40:60 ratio with the oxidized disulfide-bonded form, which preferentially interacts with receptor-bound renin. {ECO:0000269|PubMed:20927107}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:4300938, ECO:0000305|PubMed:7259779, ECO:0000305|PubMed:7539791}.
| null | null | null | null | null |
FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. {ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1132082, ECO:0000269|PubMed:17138938}.; FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone (PubMed:10619573, PubMed:17138938). Acts by binding to angiotensin receptors AGTR1 and AGTR2 (PubMed:1567413). Also binds the DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P01015, ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1567413, ECO:0000269|PubMed:17138938}.; FUNCTION: [Angiotensin-3]: Stimulates aldosterone release. {ECO:0000269|PubMed:1132082}.; FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity). {ECO:0000250|UniProtKB:P11859}.
|
Homo sapiens (Human)
|
P01021
|
BNP_GLOBL
|
MFVSRLAASGLLLLALMALSLDGKPVQQWSQGRPPGPPIPRLVVQQWSQGLPPGPPIPRLVVQQWSQGLPPGPPIPPLVVQQWSQGLPPRPKIPPLVVQQWSQGLPPRPKIPPLVVQKWDPPPVSPPLLLQPHESPAGGTTALREELSLGPEAASGPAAAGADGGRSGSKAPAALHRLSKSKGASATSASASRPMRDLRTDGKQARQNWARMVNPDHHAVGGCCCGGGGGGARRLKGLVKKGVAKGCFGLKLDRIGTMSGLGC
| null | null |
cGMP biosynthetic process [GO:0006182]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311]
|
extracellular region [GO:0005576]
|
hormone activity [GO:0005179]; peptidase inhibitor activity [GO:0030414]; toxin activity [GO:0090729]
|
PF00212;
| null |
Bradykinin-potentiating peptide family; Natriuretic peptide family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10519653, ECO:0000269|PubMed:10866809, ECO:0000269|PubMed:4323853, ECO:0000269|PubMed:4730295, ECO:0000269|Ref.5}.
| null | null | null | null | null |
FUNCTION: [Blomhotin]: Inhibits the rabbit lung angiotensin-converting enzyme (ACE) (IC(50)=15 uM) (PubMed:10866809). Contracts the rat gastric fundus smooth muscle in a rapid and transient manner (PubMed:10519653, PubMed:10866809). {ECO:0000269|PubMed:10519653, ECO:0000269|PubMed:10866809}.; FUNCTION: [Bradykinin-potentiating peptide A]: Causes no contraction of the rat gastric fundus smooth muscle even at high concentrations. Causes very weak contraction of the isolated guinea pig ileum (PubMed:4323853). Causes weak contraction on rat uterus (PubMed:4323853). {ECO:0000269|PubMed:4323853}.; FUNCTION: [Bradykinin-potentiating peptide B]: Inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (Ki=30 nM, IC(50)=1.1 uM) (PubMed:10866809, PubMed:11994001, PubMed:23082758). It binds ACE in a zinc-independent manner (PubMed:23056909). Also potentiates the hypotensive effects of bradykinin. Causes high contraction of the isolated guinea pig ileum and weak contraction on rat uterus (PubMed:4323853). {ECO:0000269|PubMed:10866809, ECO:0000269|PubMed:11994001, ECO:0000269|PubMed:23082758, ECO:0000269|PubMed:4323853}.; FUNCTION: [Bradykinin-potentiating peptide C]: Inhibits the activity of the angiotensin-converting enzyme (ACE) by interacting with the same potency to its C- and N-domains (PubMed:11994001). Inhibits the rabbit lung angiotensin-converting enzyme (ACE) (IC(50)=7.1 uM) (PubMed:10866809). Causes weak contraction of the isolated guinea pig ileum (PubMed:4323853). Causes weak contraction on rat uterus (PubMed:4323853). {ECO:0000269|PubMed:10866809, ECO:0000269|PubMed:11994001, ECO:0000269|PubMed:4323853}.; FUNCTION: [Leu3-blomhotin]: Inhibits the rabbit lung angiotensin-converting enzyme (ACE) (IC(50)=46 uM) (PubMed:10866809). Synthetic Leu3-blomhotin contracts the rat gastric fundus smooth muscle in a rapid and transient manner (PubMed:10866809). Causes moderate contraction of the isolated guinea pig ileum (PubMed:4323853). Causes weak contraction on rat uterus (PubMed:4323853). {ECO:0000269|PubMed:10866809, ECO:0000269|PubMed:4323853}.; FUNCTION: [Bradykinin-potentiating peptide E]: Causes weak contraction of the isolated guinea pig ileum (PubMed:4323853). Causes about 50-fold more potentiating activity on rat uterus than on guinea pig ileum (PubMed:4323853). {ECO:0000269|PubMed:4323853}.; FUNCTION: [Bradykinin-potentiating peptide Ahb1]: Synthetic peptide potentiates the bradykinin in vivo. {ECO:0000269|PubMed:11994001}.; FUNCTION: [Bradykinin-potentiating peptide Ahb2]: Synthetic peptide does not show any bradykinin-potentiating effects. {ECO:0000269|PubMed:11994001}.; FUNCTION: [C-type natriuretic peptide]: has a vasorelaxant activity in rat aortic strips and a diuretic potency in anesthetized rats (By similarity). May act by activating natriuretic receptors (NPR1 and/or NPR2). {ECO:0000250|UniProtKB:P0C7P5}.
|
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
|
P01023
|
A2MG_HUMAN
|
MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFRQGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLTVRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHYILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARLLIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAVDQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDNEDCINRHNVYINGITYTPVSSTNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARLVHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVEKEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVIKPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQNTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKHYDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCFRSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDHGSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQAPSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHALSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEGCVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAIVDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVRDLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA
| null | null |
acute inflammatory response to antigenic stimulus [GO:0002438]; acute-phase response [GO:0006953]; embryonic liver development [GO:1990402]; luteinization [GO:0001553]; negative regulation of complement activation, lectin pathway [GO:0001869]; response to carbon dioxide [GO:0010037]; response to glucocorticoid [GO:0051384]; response to nutrient [GO:0007584]; response to prostaglandin E [GO:0034695]; stem cell differentiation [GO:0048863]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]
|
brain-derived neurotrophic factor binding [GO:0048403]; calcium-dependent protein binding [GO:0048306]; endopeptidase inhibitor activity [GO:0004866]; enzyme binding [GO:0019899]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-1 binding [GO:0019966]; interleukin-8 binding [GO:0019959]; nerve growth factor binding [GO:0048406]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102]; tumor necrosis factor binding [GO:0043120]
|
PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;
|
1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.690;2.60.40.10;
|
Protease inhibitor I39 (alpha-2-macroglobulin) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6203908}.
| null | null | null | null | null |
FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
|
Homo sapiens (Human)
|
P01024
|
CO3_HUMAN
|
MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN
| null | null |
amyloid-beta clearance [GO:0097242]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; complement receptor mediated signaling pathway [GO:0002430]; complement-dependent cytotoxicity [GO:0097278]; complement-mediated synapse pruning [GO:0150062]; fatty acid metabolic process [GO:0006631]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; neuron remodeling [GO:0016322]; oviduct epithelium development [GO:0035846]; positive regulation of activation of membrane attack complex [GO:0001970]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic cell clearance [GO:2000427]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of lipid storage [GO:0010884]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of type IIa hypersensitivity [GO:0001798]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of triglyceride biosynthetic process [GO:0010866]; response to bacterium [GO:0009617]; signal transduction [GO:0007165]; vertebrate eye-specific patterning [GO:0150064]
|
azurophil granule lumen [GO:0035578]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; secretory granule lumen [GO:0034774]
|
C5L2 anaphylatoxin chemotactic receptor binding [GO:0031715]; endopeptidase inhibitor activity [GO:0004866]; signaling receptor binding [GO:0005102]
|
PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null |
PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: (Microbial infection) C3 is cleaved by Staphylococcus aureus aureolysin; this cleavage renders C3a and C3b inactive. C3b is rapidly degraded by host factors CFH and CFI preventing its deposition on the bacterial surface while C3a is further inactivated by aureolysin. {ECO:0000269|PubMed:21502375}.; PTM: (Microbial infection) Complement C3 beta chain is cleaved and inactivated by S.pyogenes SpeB. {ECO:0000269|PubMed:18160402}.; PTM: (Microbial infection) Cleaved by N.meningitidis NalP between Leu-744 and Gly-754, generating a slightly shorter C3 alpha form and a slightly longer C3 beta form. The C3b-like fragment is degraded in the presence of the complement regulators CFH and CFI, preventing its deposition on the bacterial surface. {ECO:0000269|PubMed:24367091}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; FUNCTION: Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. {ECO:0000250}.; FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 (PubMed:10432298, PubMed:15833747, PubMed:16333141, PubMed:19615750, PubMed:2909530, PubMed:8376604, PubMed:9059512). {ECO:0000269|PubMed:10432298, ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:16333141, ECO:0000269|PubMed:19615750, ECO:0000269|PubMed:2909530, ECO:0000269|PubMed:8376604, ECO:0000269|PubMed:9059512}.
|
Homo sapiens (Human)
|
P01025
|
CO3_PIG
|
MGSTSGPRLLLLLLTSLPLALGDPIYTIITPNVLRLESEEMVVLEAHEGQGDIRVSVTVHDFPAKRQVLSSETTTLNNANNYLSTVNIKIPASKEFKSEKGHKFVTVQALFGNVQVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVDHKLLPVGQTIVVTIETPEGIDIKRDSLSSHNQFGILALSWNIPELVNMGQWKIRAHYEDAPQQVFSAEFEVKEYVLPSFEVQVEPSEKFYYIDDPNGLTVNIIARFLYGESVDGTAFVIFGVQDGDQRISLSQSLTRVPIIDGTGEATLSQGVLLNGVHYSSVNDLVGKSIYVSVTVILNSGSDMVEAERTGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVYVTNPDGSPARHIPVVTEDFKVRSLTQEDGVAKLSINTPDNRNSLPITVRTEKDGIPAARQASKTMHVLPYNTQGNSKNYLHLSLPRVELKPGENLNVNFHLRTDPGYQDKIRYFTYLIMNKGKLLKVGRQPRESGQVVVVLPLTITTDFIPSFRLVAYYTLIAANGQREVVADSVWVDVKDSCVGTLVVKGGGKQDKQHRPGQQMTLEIQGERGARVGLVAVDKGVFVLNKKNKLTQRRIWDVVEKADIGCTPGSGKDFAGVFTDAGLAFKSSKGLQTPQRADLECPKPAARKRRSVQLMEKRMDKLGQYSKDVRRCCEHGMRDNPMKFSCQRRAQFIQHGDACVKAFLDCCEYIAKLRQQHSRNKPLGLARSDLDEEIIPEEDIISRSQFPESWLWTIEEFKEPDKNGISTKTMNVFLKDSITTWEILAVSLSDKKGICVADPYEVVVKQDFFIDLRLPYSVVRNEQVEIRAILYNYREAEDLKVRVELLYNPAFCSLATAKKRHQQTLTVPAKSSVPVPYIIVPLKTGLQEVEVKAAVYNHFISDGVKKTLKVVPEGMRVNKTVVTRTLDPEHKGQQGVQREEIPPADLSDQVPDTESETKILLQGTPVAQMVEDAIDGDRLKHLIQTPSGCGEQNMIGMTPTVIAVHYLDSTEQWEKFGLEKRQEALELIKKGYTQQLAFRQKNSAFAAFQDRLSSTLLTAYVVKVFAMAANLIAIDSQVLCGAVKWLILEKQKPDGVFEENGPVIHQEMIGGFKNTEEKDVSLTAFVLIALQEAKDICEPQVNSLLRSINKARDFLADYYLELKRPYTVAIAGYALALSDKLDEPFLNKLLSTAKERNRWEEPGQKLHNVEATSYALLALLVVKDFDSVPPIVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDVPDHKDLNLDVSIHLPSRSAPVRHRILWESASLLRSEETKENEGFTLIAEGKGQGTLSVVTMYHGKAKGKTTCKKFDLKVSIHPAPEPVKKPQEAKSSMVLDICTRYLGNQDATMSILDISMMTGFSPDTEDLKLLSTGVDRYISKYELNKALSNKNTLIIYLDKISHTLEDCISFKVHQYFNVGLIQPGSVKVYSYYNLDESCTRFYHPEKEDGMLNKLCHKEMCRCAEENCFMHHDEEEVTLDDRLERACEPGVDYVYKTRLLKKELSDDFDDYIMVIEQIIKSGSDEVQVGQERRFISHIKCREALKLKEGGHYLVWGVSSDLWGEKPNISYIIGKDTWVELWPDGDVCQDEENQKQCQDLANFSENMVVFGCPN
| null | null |
complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; fatty acid metabolic process [GO:0006631]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of lipid storage [GO:0010884]; positive regulation of protein phosphorylation [GO:0001934]; regulation of triglyceride biosynthetic process [GO:0010866]
|
extracellular space [GO:0005615]
|
C5L2 anaphylatoxin chemotactic receptor binding [GO:0031715]; endopeptidase inhibitor activity [GO:0004866]
|
PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null |
PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxylases to release the C-termianl arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons (By similarity). {ECO:0000250}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01024}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (By similarity). {ECO:0000250}.; FUNCTION: Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). {ECO:0000250}.; FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in post-prandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-internalization and recycling of C5AR2 (By similarity). {ECO:0000250}.
|
Sus scrofa (Pig)
|
P01026
|
CO3_RAT
|
MGPTSGSQLLVLLLLLASSLLALGSPMYSIITPNVLRLESEETFILEAHDAQGDVPVTVTVQDFLKKQVLTSEKTVLTGATGHLNRVFIKIPASKEFNADKGHKYVTVVANFGATVVEKAVLVSFQSGYLFIQTDKTIYTPGSTVFYRIFTVDNNLLPVGKTVVIVIETPDGVPIKRDILSSHNQYGILPLSWNIPELVNMGQWKIRAFYEHAPKQTFSAEFEVKEYVLPSFEVLVEPTEKFYYIHGPKGLEVSITARFLYGKNVDGTAFVIFGVQDEDKKISLALSLTRVLIEDGSGEAVLSRKVLMDGVRPSSPEALVGKSLYVSVTVILHSGSDMVEAERSGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVFVTNPDGSPARRVPVVTQGSDAQALTQDDGVAKLSVNTPNNRQPLTITVSTKKEGIPDARQATRTMQAQPYSTMHNSNNYLHLSVSRVELKPGDNLNVNFHLRTDAGQEAKIRYYTYLVMNKGKLLKAGRQVREPGQDLVVLSLPITPEFIPSFRLVAYYTLIGANGQREVVADSVWVDVKDSCVGTLVVKGDPRDNRQPAPGHQTTLRIEGNQGARVGLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKNYAGVFMDAGLTFKTNQGLQTDQREDPECAKPAARRRRSVQLMERRMDKAGQYTDKGLRKCCEDGMRDIPMPYSCQRRARLITQGESCLKAFMDCCNYITKLREQHRRDHVLGLARSDVDEDIIPEEDIISRSHFPESWLWTIEELKEPEKNGISTKVMNIFLKDSITTWEILAVSLSDKKGICVADPYEITVMQDFFIDLRLPYSVVRNEQVEIRAVLFNYREQEKLKVRVELLHNPAFCSMATAKKRYYQTIEIPPKSSVAVPYVIVPLKIGLQEVEVKAAVFNHFISDGVKKILKVVPEGMRVNKTVAVRTLDPEHLNQGGVQREDVNAADLSDQVPDTDSETRILLQGTPVAQMAEDAVDGERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDQTEQWEKFGLEKRQEALELIKKGYTQQLAFKQPISAYAAFNNRPPSTWLTAMWSRSFSLAANLIAIDSQVLCGAVKWLILEKQKPDGVFQEDGPVIHQEMIGGFRNTKEADVSLTAFVLIALQEARDICEGQVNSLPGSINKAGEYLEASYLNLQRPYTVAIAGYALALMNKLEEPYLTKFLNTAKDRNRWEEPGQQLYNVEATSYALLALLLLKDFDSVPPVVRWLNDERYYGGGYGSTQATFMVFQALAQYRADVPDHKDLNMDVSLHLPSRSSPTVFRLLWESGSLLRSEETKQNEGFSLTAKGKGQGTLSVVTVYHAKVKGKTTCKKFDLRVTIKPAPETAKKPQDAKSSMILDICTRYLGDVDATMSILDISMMTGFIPDTNDLELLSSGVDRYISKYEMDKAFSNKNTLIIYLEKISHSEEDCLSFKVHQFFNVGLIQPGSVKVYSYYNLEESCTRFYHPEKDDGMLSKLCHNEMCRCAEENCFMHQSQDQVSLNERLDKACEPGVDYVYKTKLTTIELSDDFDEYIMTIEQVIKSGSDEVQAGQERRFISHVKCRNALKLQKGKQYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAEERQDQKNQKQCEDLGAFTETMVVFGCPN
| null | null |
amyloid-beta clearance [GO:0097242]; chemotaxis [GO:0006935]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; complement receptor mediated signaling pathway [GO:0002430]; complement-dependent cytotoxicity [GO:0097278]; complement-mediated synapse pruning [GO:0150062]; fatty acid metabolic process [GO:0006631]; inflammatory response [GO:0006954]; neuron remodeling [GO:0016322]; oviduct epithelium development [GO:0035846]; positive regulation of activation of membrane attack complex [GO:0001970]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic cell clearance [GO:2000427]; positive regulation of developmental growth [GO:0048639]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of lipid storage [GO:0010884]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of type IIa hypersensitivity [GO:0001798]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of triglyceride biosynthetic process [GO:0010866]; response to bacterium [GO:0009617]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]; response to glucocorticoid [GO:0051384]; response to magnesium ion [GO:0032026]; response to progesterone [GO:0032570]; response to xenobiotic stimulus [GO:0009410]; retina development in camera-type eye [GO:0060041]; tolerance induction [GO:0002507]; vascular associated smooth muscle cell differentiation [GO:0035886]; vertebrate eye-specific patterning [GO:0150064]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
C5L2 anaphylatoxin chemotactic receptor binding [GO:0031715]; endopeptidase inhibitor activity [GO:0004866]; lipid binding [GO:0008289]
|
PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null |
PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons (By similarity). {ECO:0000250}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01024}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. {ECO:0000269|PubMed:8352775}.; FUNCTION: Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (PubMed:8352775). {ECO:0000269|PubMed:8352775}.; FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000269|PubMed:8352775}.; FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P01027
|
CO3_MOUSE
|
MGPASGSQLLVLLLLLASSPLALGIPMYSIITPNVLRLESEETIVLEAHDAQGDIPVTVTVQDFLKRQVLTSEKTVLTGASGHLRSVSIKIPASKEFNSDKEGHKYVTVVANFGETVVEKAVMVSFQSGYLFIQTDKTIYTPGSTVLYRIFTVDNNLLPVGKTVVILIETPDGIPVKRDILSSNNQHGILPLSWNIPELVNMGQWKIRAFYEHAPKQIFSAEFEVKEYVLPSFEVRVEPTETFYYIDDPNGLEVSIIAKFLYGKNVDGTAFVIFGVQDGDKKISLAHSLTRVVIEDGVGDAVLTRKVLMEGVRPSNADALVGKSLYVSVTVILHSGSDMVEAERSGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVFVTNPDGSPASKVLVVTQGSNAKALTQDDGVAKLSINTPNSRQPLTITVRTKKDTLPESRQATKTMEAHPYSTMHNSNNYLHLSVSRMELKPGDNLNVNFHLRTDPGHEAKIRYYTYLVMNKGKLLKAGRQVREPGQDLVVLSLPITPEFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCIGTLVVKGDPRDNHLAPGQQTTLRIEGNQGARVGLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKNYAGVFMDAGLAFKTSQGLQTEQRADLECTKPAARRRRSVQLMERRMDKAGQYTDKGLRKCCEDGMRDIPMRYSCQRRARLITQGENCIKAFIDCCNHITKLREQHRRDHVLGLARSELEEDIIPEEDIISRSHFPQSWLWTIEELKEPEKNGISTKVMNIFLKDSITTWEILAVSLSDKKGICVADPYEIRVMQDFFIDLRLPYSVVRNEQVEIRAVLFNYREQEELKVRVELLHNPAFCSMATAKNRYFQTIKIPPKSSVAVPYVIVPLKIGQQEVEVKAAVFNHFISDGVKKTLKVVPEGMRINKTVAIHTLDPEKLGQGGVQKVDVPAADLSDQVPDTDSETRIILQGSPVVQMAEDAVDGERLKHLIVTPAGCGEQNMIGMTPTVIAVHYLDQTEQWEKFGIEKRQEALELIKKGYTQQLAFKQPSSAYAAFNNRPPSTWLTAYVVKVFSLAANLIAIDSHVLCGAVKWLILEKQKPDGVFQEDGPVIHQEMIGGFRNAKEADVSLTAFVLIALQEARDICEGQVNSLPGSINKAGEYIEASYMNLQRPYTVAIAGYALALMNKLEEPYLGKFLNTAKDRNRWEEPDQQLYNVEATSYALLALLLLKDFDSVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQTDVPDHKDLNMDVSFHLPSRSSATTFRLLWENGNLLRSEETKQNEAFSLTAKGKGRGTLSVVAVYHAKLKSKVTCKKFDLRVSIRPAPETAKKPEEAKNTMFLEICTKYLGDVDATMSILDISMMTGFAPDTKDLELLASGVDRYISKYEMNKAFSNKNTLIIYLEKISHTEEDCLTFKVHQYFNVGLIQPGSVKVYSYYNLEESCTRFYHPEKDDGMLSKLCHSEMCRCAEENCFMQQSQEKINLNVRLDKACEPGVDYVYKTELTNIELLDDFDEYTMTIQQVIKSGSDEVQAGQQRKFISHIKCRNALKLQKGKKYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAEECQDQKYQKQCEELGAFTESMVVYGCPN
| null | null |
amyloid-beta clearance [GO:0097242]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; complement receptor mediated signaling pathway [GO:0002430]; complement-dependent cytotoxicity [GO:0097278]; complement-mediated synapse pruning [GO:0150062]; fatty acid metabolic process [GO:0006631]; inflammatory response [GO:0006954]; neuron remodeling [GO:0016322]; oviduct epithelium development [GO:0035846]; positive regulation of activation of membrane attack complex [GO:0001970]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic cell clearance [GO:2000427]; positive regulation of developmental growth [GO:0048639]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of lipid storage [GO:0010884]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of type IIa hypersensitivity [GO:0001798]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of triglyceride biosynthetic process [GO:0010866]; response to bacterium [GO:0009617]; vertebrate eye-specific patterning [GO:0150064]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
C5L2 anaphylatoxin chemotactic receptor binding [GO:0031715]; endopeptidase inhibitor activity [GO:0004866]; lipid binding [GO:0008289]
|
PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null |
PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01024}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; FUNCTION: Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity. {ECO:0000250}.; FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2.
|
Mus musculus (Mouse)
|
P01029
|
CO4B_MOUSE
|
MRLLWGLAWVFSFCASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPPGQEVKGSVFLRNPKGGSCSPKKDFKLSSGDDFVLLSLEVPLEDVRSCGLFDLRRAPHIQLVAQSPWLRNTAFKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDFLTITVENSHGLRVLKKEIFTSTSIFQDAFTIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKITPWKPYILMVPSNSDEIQLDIQARYIYGKPVQGVAYTRFALMDEQGKRTFLRGLETQAKLVEGRTHISISKDQFQAALDKINIGVRDLEGLRLYAATAVIESPGGEMEEAELTSWRFVSSAFSLDLSRTKRHLVPGAHFLLQALVQEMSGSEASNVPVKVSATLVSGSDSQVLDIQQSTNGIGQVSISFPIPPTVTELRLLVSAGSLYPAIARLTVQAPPSRGTGFLSIEPLDPRSPSVGDTFILNLQPVGIPAPTFSHYYYMIISRGQIMAMGREPRKTVTSVSVLVDHQLAPSFYFVAYFYHQGHPVANSLLINIQSRDCEGKLQLKVDGAKEYRNADMMKLRIQTDSKALVALGAVDMALYAVGGRSHKPLDMSKVFEVINSYNVGCGPGGGDDALQVFQDAGLAFSDGDRLTQTREDLSCPKEKKSRQKRNVNFQKAVSEKLGQYSSPDAKRCCQDGMTKLPMKRTCEQRAARVPQQACREPFLSCCKFAEDLRRNQTRSQAHLARNNHNMLQEEDLIDEDDILVRTSFPENWLWRVEPVDSSKLLTVWLPDSMTTWEIHGVSLSKSKGLCVAKPTRVRVFRKFHLHLRLPISIRRFEQFELRPVLYNYLNDDVAVSVHVTPVEGLCLAGGGMMAQQVTVPAGSARPVAFSVVPTAAANVPLKVVARGVFDLGDAVSKILQIEKEGAIHREELVYNLDPLNNLGRTLEIPGSSDPNIVPDGDFSSLVRVTASEPLETMGSEGALSPGGVASLLRLPQGCAEQTMIYLAPTLTASNYLDRTEQWSKLSPETKDHAVDLIQKGYMRIQQFRKNDGSFGAWLHRDSSTWLTAFVLKILSLAQEQVGNSPEKLQETASWLLAQQLGDGSFHDPCPVIHRAMQGGLVGSDETVALTAFVVIALHHGLDVFQDDDAKQLKNRVEASITKANSFLGQKASAGLLGAHAAAITAYALTLTKASEDLRNVAHNSLMAMAEETGEHLYWGLVLGSQDKVVLRPTAPRSPTEPVPQAPALWIETTAYALLHLLLREGKGKMADKAASWLTHQGSFHGAFRSTQDTVVTLDALSAYWIASHTTEEKALNVTLSSMGRNGLKTHGLHLNNHQVKGLEEELKFSLGSTISVKVEGNSKGTLKILRTYNVLDMKNTTCQDLQIEVKVTGAVEYAWDANEDYEDYYDMPAADDPSVPLQPVTPLQLFEGRRSRRRREAPKVVEEQESRVQYTVCIWRNGKLGLSGMAIADITLLSGFHALRADLEKLTSLSDRYVSHFETDGPHVLLYFDSVPTTRECVGFGASQEVVVGLVQPSSAVLYDYYSPDHKCSVFYAAPTKSQLLATLCSGDVCQCAEGKCPRLLRSLERRVEDKDGYRMRFACYYPRVEYGFTVKVLREDGRAAFRLFESKITQVLHFRKDTMASIGQTRNFLSRASCRLRLEPNKEYLIMGMDGETSDNKGDPQYLLDSNTWIEEMPSEQMCKSTRHRAACFQLKDFLMEFSSRGCQV
| null | null |
complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; immunoglobulin mediated immune response [GO:0016064]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]
|
axon [GO:0030424]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; synapse [GO:0045202]
|
endopeptidase inhibitor activity [GO:0004866]
|
PF00207;PF07703;PF07677;PF01821;PF21145;PF01835;PF17791;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null |
PTM: Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L5}. Synapse {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L5}.
| null | null | null | null | null |
FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. Catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
P01031
|
CO5_HUMAN
|
MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
| null | null |
cell surface receptor signaling pathway [GO:0007166]; chemotaxis [GO:0006935]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; killing of cells of another organism [GO:0031640]; negative regulation of macrophage chemotaxis [GO:0010760]; positive regulation of chemokine production [GO:0032722]; positive regulation of vascular endothelial growth factor production [GO:0010575]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane attack complex [GO:0005579]
|
chemokine activity [GO:0008009]; endopeptidase inhibitor activity [GO:0004866]; signaling receptor binding [GO:0005102]
|
PF00207;PF07703;PF07677;PF01821;PF21309;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; FUNCTION: [C5a anaphylatoxin]: Derived from proteolytic degradation of complement C5, C5a anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. {ECO:0000269|PubMed:8182049}.
|
Homo sapiens (Human)
|
P01033
|
TIMP1_HUMAN
|
MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA
| null | null |
cartilage development [GO:0051216]; cellular response to UV-A [GO:0071492]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; negative regulation of apoptotic process [GO:0043066]; negative regulation of catalytic activity [GO:0043086]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of metallopeptidase activity [GO:1905049]; negative regulation of trophoblast cell migration [GO:1901164]; positive regulation of cell population proliferation [GO:0008284]; regulation of integrin-mediated signaling pathway [GO:2001044]; response to cytokine [GO:0034097]; response to hormone [GO:0009725]; response to peptide hormone [GO:0043434]
|
basement membrane [GO:0005604]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; metalloendopeptidase inhibitor activity [GO:0008191]; peptidase inhibitor activity [GO:0030414]; protease binding [GO:0002020]; zinc ion binding [GO:0008270]
|
PF00965;
|
2.40.50.120;3.90.370.10;
|
Protease inhibitor I35 (TIMP) family
|
PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds. {ECO:0000269|PubMed:10623524, ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:2163605, ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:3010309}.; PTM: N-glycosylated. {ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:3010309, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3010309, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540}.
| null | null | null | null | null |
FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. {ECO:0000269|PubMed:1420137, ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:17050530, ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.
|
Homo sapiens (Human)
|
P01034
|
CYTC_HUMAN
|
MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA
| null | null |
defense response [GO:0006952]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of collagen catabolic process [GO:0010711]; negative regulation of elastin catabolic process [GO:0060311]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of peptidase activity [GO:0010466]; negative regulation of proteolysis [GO:0045861]; regulation of tissue remodeling [GO:0034103]; supramolecular fiber organization [GO:0097435]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; tertiary granule lumen [GO:1904724]; vesicle [GO:0031982]
|
amyloid-beta binding [GO:0001540]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; identical protein binding [GO:0042802]; peptidase inhibitor activity [GO:0030414]; protease binding [GO:0002020]
|
PF00031;
|
3.10.450.10;
|
Cystatin family
|
PTM: The Thr-25 variant is O-glycosylated with a core 1 or possibly core 8 glycan. The signal peptide of the O-glycosylated Thr-25 variant is cleaved between Ala-20 and Val-21. {ECO:0000269|PubMed:19838169}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20189825}.
| null | null | null | null | null |
FUNCTION: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
|
Homo sapiens (Human)
|
P01036
|
CYTS_HUMAN
|
MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATEDEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWEDRMSLVNSRCQEA
| null | null |
detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; negative regulation of proteolysis [GO:0045861]
|
cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; vesicle [GO:0031982]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]
|
PF00031;
|
3.10.450.10;
|
Cystatin family
|
PTM: Phosphorylated at both its N- and C-terminal regions. {ECO:0000269|PubMed:1741693, ECO:0000269|PubMed:1747107, ECO:0000269|PubMed:1778989, ECO:0000269|PubMed:1898055, ECO:0000269|PubMed:20189825}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20189825}.
| null | null | null | null | null |
FUNCTION: This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively.
|
Homo sapiens (Human)
|
P01037
|
CYTN_HUMAN
|
MAQYLSTLLLLLATLAVALAWSPKEEDRIIPGGIYNADLNDEWVQRALHFAISEYNKATKDDYYRRPLRVLRARQQTVGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWENRRSLVKSRCQES
| null | null |
detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; vesicle [GO:0031982]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]
|
PF00031;
|
3.10.450.10;
|
Cystatin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20189825}.
| null | null | null | null | null |
FUNCTION: Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Cystatin SN, with a pI of 7.5, is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin S, although both inhibit ficin equally well.
|
Homo sapiens (Human)
|
P01040
|
CYTA_HUMAN
|
MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF
| null | null |
cell-cell adhesion [GO:0098609]; keratinocyte differentiation [GO:0030216]; negative regulation of peptidase activity [GO:0010466]; negative regulation of proteolysis [GO:0045861]; peptide cross-linking [GO:0018149]
|
cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; peptidase inhibitor complex [GO:1904090]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; protease binding [GO:0002020]
|
PF00031;
|
3.10.450.10;
|
Cystatin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21944047}.
| null | null | null | null | null |
FUNCTION: This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis. {ECO:0000269|PubMed:21944047}.
|
Homo sapiens (Human)
|
P01042
|
KNG1_HUMAN
|
MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS
| null | null |
blood coagulation [GO:0007596]; inflammatory response [GO:0006954]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell adhesion [GO:0007162]; negative regulation of proteolysis [GO:0045861]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; heparin binding [GO:0008201]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]; zinc ion binding [GO:0008270]
|
PF00031;
|
3.10.450.10;
| null |
PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus. {ECO:0000269|PubMed:4322742, ECO:0000269|PubMed:6055465}.; PTM: Bradykinin is released from kininogen by plasma kallikrein. {ECO:0000305|PubMed:3366244}.; PTM: Hydroxylation of Pro-383 occurs prior to the release of bradykinin. {ECO:0000269|PubMed:3182782, ECO:0000269|PubMed:3366244}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:3484703}.; PTM: (Microbial infection) Bradykinin is generated upon proteolytic cleavage by S.pyogenes SpeB to produce hypotension during septic shock. {ECO:0000269|PubMed:8760820}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.; FUNCTION: [Bradykinin]: The active peptide bradykinin is a potent vasodilatator that is released from HMW-kininogen shows a variety of physiological effects: (A) influence in smooth muscle contraction, (B) induction of hypotension, (C) natriuresis and diuresis, (D) decrease in blood glucose level, (E) it is a mediator of inflammation and causes (E1) increase in vascular permeability, (E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action). {ECO:0000305|PubMed:4322742, ECO:0000305|PubMed:6055465}.
|
Homo sapiens (Human)
|
P01044
|
KNG1_BOVIN
|
MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHGSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
| null | null |
blood coagulation [GO:0007596]; inflammatory response [GO:0006954]; negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]
|
PF00031;
|
3.10.450.10;
| null |
PTM: Bradykinin is released from kininogen by plasma kallikrein.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01042}.; PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus. {ECO:0000250|UniProtKB:P01042}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.; FUNCTION: [Bradykinin]: The active peptide bradykinin is a potent vasodilatator that is released from HMW-kininogen shows a variety of physiological effects: (A) influence in smooth muscle contraction, (B) induction of hypotension, (C) natriuresis and diuresis, (D) decrease in blood glucose level, (E) it is a mediator of inflammation and causes (E1) increase in vascular permeability, (E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action). {ECO:0000250|UniProtKB:P01042}.
|
Bos taurus (Bovine)
|
P01045
|
KNG2_BOVIN
|
MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDTVKKATVQVVGGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHRSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
| null | null |
blood coagulation [GO:0007596]; inflammatory response [GO:0006954]; negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]
|
PF00031;
|
3.10.450.10;
| null |
PTM: Bradykinin is released from kininogen by plasma kallikrein.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.
|
Bos taurus (Bovine)
|
P01048
|
KNT1_RAT
|
MKLITILLLCSRLLPSLAQEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMMISRPPGFSPFRLVRVQETKEGTTRLLNSCEYKGRLSKARAGPAPDHQAEASTVTP
| null | null |
acute-phase response [GO:0006953]; negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]
|
PF00031;
|
3.10.450.10;
| null |
PTM: As T-kinin is preceded by a Met instead of an Arg or Lys, it is not released from its precursor by either tissue or plasma kallikrein.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Kininogens are plasma glycoproteins with a number of functions: (1) as precursor of the active peptide bradykinin they effect smooth muscle contraction, induction of hypotension and increase of vascular permeability. (2) They play a role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII. (3) They are inhibitor of thiol proteases.
|
Rattus norvegicus (Rat)
|
P01050
|
HIRV1_HIRME
|
VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ
| null | null |
negative regulation of serine-type peptidase activity [GO:1902572]
|
extracellular space [GO:0005615]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00713;
|
2.70.10.10;
|
Protease inhibitor I14 (hirudin) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen. {ECO:0000269|PubMed:17585879}.
|
Hirudo medicinalis (Medicinal leech)
|
P01083
|
IAA2_WHEAT
|
MWMKTVFWGLLVFMLVATTMAVEYGARSHNSGPWSWCNPATGYKVSALTGCRAMVKLQCVGSQVPEAVLRDCCQQLADINNEWCRCGDLSSMLRSVYQELGVREGKEVLPGCRKEVMKLTAASVPEVCKVPIPNPSGDRAGVCYGDWAAYPDV
| null | null | null |
extracellular region [GO:0005576]
|
alpha-amylase inhibitor activity [GO:0015066]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00234;
|
1.10.110.10;
|
Protease inhibitor I6 (cereal trypsin/alpha-amylase inhibitor) family
|
PTM: The disulfide bonds are essential for the inhibitor activity.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Alpha-amylase inhibitor.
|
Triticum aestivum (Wheat)
|
P01089
|
2SS_RICCO
|
MAKLIPTIALVSVLLFIIANASFAYRTTITTIEIDESKGEREGSSSQQCRQEVQRKDLSSCERYLRQSSSRRSPGEEVLRMPGDENQQQESQQLQQCCNQVKQVRDECQCEAIKYIAEDQIQQGQLHGEESERVAQRAGEIVSSCGVRCMRQTRTNPSQQGCRGQIQEQQNLRQCQEYIKQQVSGQGPRRSDNQERSLRGCCDHLKQMQSQCRCEGLRQAIEQQQSQGQLQGQDVFEAFRTAANLPSMCGVSPTECRF
| null | null | null | null |
nutrient reservoir activity [GO:0045735]
|
PF00234;
|
1.10.110.10;
|
2S seed storage albumins family
|
PTM: The N-terminus of both large chains is blocked.; PTM: The C-terminus of the allergen Ric c 1 and allergen Ric c 3 small chains are heterogeneous and the length of the chains can vary from 33 to 36 amino acids and from 36 to 40 amino acids respectively.
| null | null | null | null | null | null |
FUNCTION: 2S seed storage proteins.
|
Ricinus communis (Castor bean)
|
P01094
|
IPA3_YEAST
|
MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE
| null | null |
negative regulation of endopeptidase activity [GO:0010951]; protein catabolic process in the vacuole [GO:0007039]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; vacuole [GO:0005773]
|
aspartic-type endopeptidase inhibitor activity [GO:0019828]; endopeptidase inhibitor activity [GO:0004866]; protease binding [GO:0002020]
|
PF10466;
| null |
Protease inhibitor I34 family
| null | null | null | null | null | null | null |
FUNCTION: Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P01096
|
ATIF1_BOVIN
|
MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD
| null | null |
erythrocyte differentiation [GO:0030218]; heme biosynthetic process [GO:0006783]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of hydrolase activity [GO:0051346]; protein homotetramerization [GO:0051289]
|
cell surface [GO:0009986]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
|
angiostatin binding [GO:0043532]; ATPase binding [GO:0051117]; ATPase inhibitor activity [GO:0042030]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:0005198]
|
PF04568;
|
1.20.5.500;
|
ATPase inhibitor family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7397110}.
| null | null | null | null | null |
FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (PubMed:10831597, PubMed:12923572, PubMed:17895376, PubMed:18687699, PubMed:21192948, PubMed:7397110). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (By similarity). {ECO:0000250|UniProtKB:Q9UII2, ECO:0000269|PubMed:10831597, ECO:0000269|PubMed:12923572, ECO:0000269|PubMed:17895376, ECO:0000269|PubMed:18687699, ECO:0000269|PubMed:21192948, ECO:0000269|PubMed:7397110}.
|
Bos taurus (Bovine)
|
P01097
|
ATIF_YEAST
|
MLPRSALARSLQLQRGVAARFYSEGSTGTPRGSGSEDSFVKRERATEDFFVRQREKEQLRHLKEQLEKQRKKIDSLENKIDSMTK
| null | null |
negative regulation of ATP-dependent activity [GO:0032780]
|
mitochondrion [GO:0005739]
|
ATPase inhibitor activity [GO:0042030]; enzyme inhibitor activity [GO:0004857]; molecular function inhibitor activity [GO:0140678]
|
PF04568;
|
1.20.5.500;
|
ATPase inhibitor family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12809520}.
| null | null | null | null | null |
FUNCTION: Endogenous ATPase inhibitor, which inhibits specifically the reverse ATPase reaction of mitochondrial F(1)F(0)-type ATP synthase. It limits ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(0)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(0)-ATP synthase enzyme acts as an ATP hydrolase (PubMed:12167646, PubMed:12809520, PubMed:26420258). Functions through inserting its N-terminal part into the catalytically active F1-ATPase, thereby blocking its rotational movement and subsequently the ATP hydrolase activity (PubMed:23407639). {ECO:0000269|PubMed:12167646, ECO:0000269|PubMed:12809520, ECO:0000269|PubMed:23407639, ECO:0000269|PubMed:26420258}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P01100
|
FOS_HUMAN
|
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to calcium ion [GO:0071277]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to hypoxia [GO:0071456]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; cellular response to prolactin [GO:1990646]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to zinc ion starvation [GO:0034224]; conditioned taste aversion [GO:0001661]; female pregnancy [GO:0007565]; inflammatory response [GO:0006954]; integrated stress response signaling [GO:0140467]; mononuclear cell differentiation [GO:1903131]; myoblast proliferation [GO:0051450]; nervous system development [GO:0007399]; osteoclast differentiation [GO:0030316]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to activity [GO:0014823]; response to cAMP [GO:0051591]; response to corticosterone [GO:0051412]; response to ethanol [GO:0045471]; response to gravity [GO:0009629]; response to immobilization stress [GO:0035902]; response to insulin [GO:0032868]; response to light stimulus [GO:0009416]; response to lipopolysaccharide [GO:0032496]; response to muscle stretch [GO:0035994]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle cell differentiation [GO:0035914]; skeletal muscle cell proliferation [GO:0014856]; SMAD protein signal transduction [GO:0060395]; transcription by RNA polymerase II [GO:0006366]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator binding [GO:0001221]
|
PF00170;
|
1.20.5.170;
|
BZIP family, Fos subfamily
|
PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity). {ECO:0000250}.; PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17709345}.; PTM: In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis. {ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363}.
|
SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30.
| null | null | null | null | null |
FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:7588633, ECO:0000269|PubMed:9732876}.
|
Homo sapiens (Human)
|
P01101
|
FOS_MOUSE
|
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAGMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTELEPLCTPVVTCTPGCTTYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to calcium ion [GO:0071277]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to extracellular stimulus [GO:0031668]; cellular response to hypoxia [GO:0071456]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; cellular response to prolactin [GO:1990646]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to zinc ion starvation [GO:0034224]; conditioned taste aversion [GO:0001661]; female pregnancy [GO:0007565]; mononuclear cell differentiation [GO:1903131]; myoblast proliferation [GO:0051450]; nervous system development [GO:0007399]; osteoclast differentiation [GO:0030316]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; response to activity [GO:0014823]; response to cAMP [GO:0051591]; response to corticosterone [GO:0051412]; response to ethanol [GO:0045471]; response to gravity [GO:0009629]; response to immobilization stress [GO:0035902]; response to insulin [GO:0032868]; response to light stimulus [GO:0009416]; response to lipopolysaccharide [GO:0032496]; response to muscle stretch [GO:0035994]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle cell differentiation [GO:0035914]; skeletal muscle cell proliferation [GO:0014856]; SMAD protein signal transduction [GO:0060395]; transcription by RNA polymerase II [GO:0006366]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription coregulator binding [GO:0001221]
|
PF00170;
|
1.20.5.170;
|
BZIP family, Fos subfamily
|
PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity). {ECO:0000250}.; PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232 (By similarity). {ECO:0000250}.; PTM: In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis. {ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000250, ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069, ECO:0000269|PubMed:21998197, ECO:0000269|PubMed:22105363}.
|
Mus musculus (Mouse)
|
P01106
|
MYC_HUMAN
|
MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
| null | null |
branching involved in ureteric bud morphogenesis [GO:0001658]; cellular response to hypoxia [GO:0071456]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast apoptotic process [GO:0044346]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell division [GO:0051782]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription initiation by RNA polymerase II [GO:0060633]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902255]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of metanephric cap mesenchymal cell proliferation [GO:0090096]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of telomerase activity [GO:0051973]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-DNA complex disassembly [GO:0032986]; regulation of cell cycle process [GO:0010564]; regulation of gene expression [GO:0010468]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of telomere maintenance [GO:0032204]; regulation of transcription by RNA polymerase II [GO:0006357]; response to gamma radiation [GO:0010332]; response to growth factor [GO:0070848]; response to xenobiotic stimulus [GO:0009410]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; Myc-Max complex [GO:0071943]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription repressor complex [GO:0090571]
|
core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SCF ubiquitin ligase complex binding [GO:1905761]; transcription coregulator binding [GO:0001221]; transcription regulator activator activity [GO:0140537]
|
PF00010;PF02344;PF01056;
|
4.10.280.10;
| null |
PTM: Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 (PubMed:22307329). Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25438055, PubMed:25803737). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25803737, ECO:0000269|PubMed:8386367}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17558397, PubMed:17873522). In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:20551172, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:29779948}.
|
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507}. Nucleus {ECO:0000269|PubMed:22719065}. Cytoplasm {ECO:0000269|PubMed:22719065}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:25956029}.
|
Homo sapiens (Human)
|
P01108
|
MYC_MOUSE
|
MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA
| null | null |
acinar cell proliferation [GO:1990863]; amino acid transport [GO:0006865]; B cell apoptotic process [GO:0001783]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell population proliferation [GO:0008283]; cellular response to interferon-alpha [GO:0035457]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; DNA damage response [GO:0006974]; DNA-templated transcription [GO:0006351]; DNA-templated transcription initiation [GO:0006352]; G1/S transition of mitotic cell cycle [GO:0000082]; glucose metabolic process [GO:0006006]; inner mitochondrial membrane organization [GO:0007007]; intracellular iron ion homeostasis [GO:0006879]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lactic acid secretion [GO:0046722]; MAPK cascade [GO:0000165]; middle ear morphogenesis [GO:0042474]; myotube differentiation [GO:0014902]; negative regulation of cell division [GO:0051782]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of gene expression [GO:0010629]; negative regulation of glucose import [GO:0046325]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of transcription by RNA polymerase II [GO:0000122]; NK T cell proliferation [GO:0001866]; pigmentation [GO:0043473]; positive regulation of acinar cell proliferation [GO:1904699]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of B cell apoptotic process [GO:0002904]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular respiration [GO:1901857]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of glycolytic process [GO:0045821]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of metanephric cap mesenchymal cell proliferation [GO:0090096]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of oxidative phosphorylation [GO:1903862]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of telomerase activity [GO:0051973]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein processing [GO:0016485]; pyruvate transport [GO:0006848]; re-entry into mitotic cell cycle [GO:0000320]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle process [GO:0010564]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; regulation of oxidative phosphorylation [GO:0002082]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of telomere maintenance [GO:0032204]; regulation of transcription by RNA polymerase II [GO:0006357]; response to alkaloid [GO:0043279]; response to gamma radiation [GO:0010332]; response to radiation [GO:0009314]; skeletal muscle cell differentiation [GO:0035914]; skeletal system morphogenesis [GO:0048705]; transcription by RNA polymerase II [GO:0006366]; Wnt signaling pathway [GO:0016055]
|
axon [GO:0030424]; euchromatin [GO:0000791]; mitochondrion [GO:0005739]; Myc-Max complex [GO:0071943]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RNA polymerase II transcription repressor complex [GO:0090571]; spindle [GO:0005819]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; ubiquitin protein ligase binding [GO:0031625]
|
PF00010;PF02344;PF01056;
|
4.10.280.10;
| null |
PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (PubMed:18438430). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73. Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:18438430}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex (By similarity). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (PubMed:22328504). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:22328504}.
|
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (PubMed:31005419). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:31005419}.
|
Mus musculus (Mouse)
|
P01109
|
MYC_CHICK
|
MASLRLAAGALEEPAAAAAMPLSASLPSKNYDYDYDSVQPYFYFEEEEENFYLAAQQRGSELQPPAPSEDIWKKFELLPTPPLSPSRRSSLAAASCFPSTADQLEMVTELLGGDMVNQSFICDPDDESFVKSIIIQDCMWSGFSAAAKLEKVVSEKLATYQASRREGGPAAASRPGPPPSGPPPPPAGPAASAGLYLHDLGAAAADCIDPSVVFPYPLSERAPRAAPPGANPAALLGVDTPPTTSSDSEEEQEEDEEIDVVTLAEANESESSTESSTEASEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKRLKLDSGRVLKQISNNRKCSSPRTSDSEENDKRRTHNVLERQRRNELKLSFFALRDQIPEVANNEKAPKVVILKKATEYVLSIQSDEHRLIAEKEQLRRRREQLKHKLEQLRNSRA
| null | null |
cellular response to hypoxia [GO:0071456]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; epidermis morphogenesis [GO:0048730]; ERK1 and ERK2 cascade [GO:0070371]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of cell division [GO:0051782]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of transcription initiation by RNA polymerase II [GO:0060633]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902255]; positive regulation of miRNA transcription [GO:1902895]; protein-DNA complex disassembly [GO:0032986]; regulation of cell cycle process [GO:0010564]; regulation of telomere maintenance [GO:0032204]; regulation of transcription by RNA polymerase II [GO:0006357]; response to gamma radiation [GO:0010332]
|
chromatin [GO:0000785]; Myc-Max complex [GO:0071943]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; RNA polymerase II transcription repressor complex [GO:0090571]
|
core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SCF ubiquitin ligase complex binding [GO:1905761]; transcription coregulator binding [GO:0001221]; transcription regulator activator activity [GO:0140537]
|
PF00010;PF02344;PF01056;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. {ECO:0000250|UniProtKB:P01106}.
|
Gallus gallus (Chicken)
|
P01111
|
RASN_HUMAN
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM
|
3.6.5.2
| null |
MAPK cascade [GO:0000165]; myoblast differentiation [GO:0045445]; positive regulation of endothelial cell proliferation [GO:0001938]; Ras protein signal transduction [GO:0007265]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]; tertiary granule membrane [GO:0070821]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
|
PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex (PubMed:16000296). Depalmitoylated by ABHD17A, ABHD17B and ABHD17C (PubMed:26701913). A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi (PubMed:15705808, PubMed:16000296, PubMed:2661017, PubMed:26701913). {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:16000296, ECO:0000269|PubMed:2661017, ECO:0000269|PubMed:26701913}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.; PTM: Fatty-acylated at Lys-169 and/or Lys-170. {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000305|PubMed:30442762}.; PTM: Phosphorylation at Ser-89 by STK19 enhances NRAS-association with its downstream effectors. {ECO:0000269|PubMed:30712867}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL. {ECO:0000269|PubMed:19744486}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Cytoplasmic side {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}. Golgi apparatus membrane {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}. Note=Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01116};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:30712867}.
|
Homo sapiens (Human)
|
P01112
|
RASH_HUMAN
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS
|
3.6.5.2
| null |
adipose tissue development [GO:0060612]; animal organ morphogenesis [GO:0009887]; cell surface receptor signaling pathway [GO:0007166]; cellular response to gamma radiation [GO:0071480]; cellular senescence [GO:0090398]; chemotaxis [GO:0006935]; defense response to protozoan [GO:0042832]; endocytosis [GO:0006897]; fibroblast proliferation [GO:0048144]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway [GO:0097193]; MAPK cascade [GO:0000165]; myelination [GO:0042552]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of gene expression [GO:0010629]; negative regulation of GTPase activity [GO:0034260]; negative regulation of neuron apoptotic process [GO:0043524]; neuron apoptotic process [GO:0051402]; oncogene-induced cell senescence [GO:0090402]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of GTPase activity [GO:0043547]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of phospholipase C activity [GO:0010863]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of ruffle assembly [GO:1900029]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type II interferon production [GO:0032729]; positive regulation of wound healing [GO:0090303]; Ras protein signal transduction [GO:0007265]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of transcription by RNA polymerase II [GO:0006357]; Schwann cell development [GO:0014044]; signal transduction [GO:0007165]; T cell receptor signaling pathway [GO:0050852]; T-helper 1 type immune response [GO:0042088]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; GTPase complex [GO:1905360]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-membrane adaptor activity [GO:0043495]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
|
PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.; PTM: S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.; PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250}.; PTM: Fatty-acylated at Lys-170. {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000269|PubMed:30442762}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL (PubMed:19744486, PubMed:8626575, PubMed:8626586, PubMed:9632667). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to inhibit Ras signaling (PubMed:8626575, PubMed:8626586, PubMed:9632667). {ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667}.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:9020151};
| null | null | null | null |
FUNCTION: Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:22821884, ECO:0000269|PubMed:9020151}.
|
Homo sapiens (Human)
|
P01116
|
RASK_HUMAN
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM
|
3.6.5.2
| null |
actin cytoskeleton organization [GO:0030036]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; forebrain astrocyte development [GO:0021897]; gene expression [GO:0010467]; glial cell proliferation [GO:0014009]; homeostasis of number of cells within a tissue [GO:0048873]; MAPK cascade [GO:0000165]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of neuron apoptotic process [GO:0043524]; neuron apoptotic process [GO:0051402]; positive regulation of gene expression [GO:0010628]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Rac protein signal transduction [GO:0035022]; Rac protein signal transduction [GO:0016601]; Ras protein signal transduction [GO:0007265]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of synaptic transmission, GABAergic [GO:0032228]; skeletal muscle cell differentiation [GO:0035914]; striated muscle cell differentiation [GO:0051146]; type I pneumocyte differentiation [GO:0060509]; visual learning [GO:0008542]
|
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; protein-membrane adaptor activity [GO:0043495]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
|
PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838, ECO:0000269|Ref.17}.; PTM: Palmitoylated at Lys-182, Lys-184 and Lys-185 (PubMed:29239724). Palmitoylation on lysine residues is promoted by palmitoylation at Cys-180 (PubMed:29239724). Lysine-depalmitoylation by SIRT2 promotes its localization to endomembranes in endocytic pathways (PubMed:29239724). {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000305|PubMed:30442762, ECO:0000305|PubMed:30442766}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL. {ECO:0000269|PubMed:19744486}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor {ECO:0000269|PubMed:29239724, ECO:0000305|PubMed:23698361}; Cytoplasmic side {ECO:0000305|PubMed:23698361}. Endomembrane system {ECO:0000269|PubMed:29239724}. Cytoplasm, cytosol {ECO:0000269|PubMed:23698361}.; SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane {ECO:0000269|PubMed:28619714}; Lipid-anchor {ECO:0000305|PubMed:28619714}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:20949621};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621). Plays an important role in the regulation of cell proliferation (PubMed:22711838, PubMed:23698361). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). {ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000305}.
|
Homo sapiens (Human)
|
P01119
|
RAS1_YEAST
|
MQGNKSTIREYKIVVVGGGGVGKSALTIQFIQSYFVDEYDPTIEDSYRKQVVIDDKVSILDILDTAGQEEYSAMREQYMRTGEGFLLVYSVTSRNSFDELLSYYQQIQRVKDSDYIPVVVVGNKLDLENERQVSYEDGLRLAKQLNAPFLETSAKQAINVDEAFYSLIRLVRDDGGKYNSMNRQLDNTNEIRDSELTSSATADREKKNNGSYVLDNSLTNAGTGSSSKSAVNHNGETTKRTDEKNYVNQNNNNEGNTKYSSNGNGNRSDISRGNQNNALNSRSKQSAEPQKNSSANARKESSGGCCIIC
|
3.6.5.2
| null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; positive regulation of adenylate cyclase activity [GO:0045762]; protein localization to bud neck [GO:0097271]; Ras protein signal transduction [GO:0007265]
|
cell periphery [GO:0071944]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
|
PTM: Farnesylated by RAM1-RAM2, which is required for targeting RAS1 to the cytoplasmic site of the endoplasmic reticulum, where proteolytic processing of the C-terminus by RCE1 and methylation of the resulting carboxyl group by STE14 occurs. {ECO:0000269|PubMed:2050108, ECO:0000269|PubMed:9065405}.; PTM: Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P01120
|
RAS2_YEAST
|
MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSILDILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVVVGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNKTLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKTGLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQAAPGGNTSEASKSGSGGCCIIS
|
3.6.5.2
| null |
ascospore formation [GO:0030437]; cytoplasm to vacuole targeting by the Cvt pathway [GO:0032258]; macroautophagy [GO:0016236]; positive regulation of pseudohyphal growth [GO:2000222]; positive regulation of transcription by galactose [GO:0000411]; protein localization to bud neck [GO:0097271]; Ras protein signal transduction [GO:0007265]; regulation of cytoplasmic mRNA processing body assembly [GO:0010603]; regulation of protein localization [GO:0032880]
|
cell periphery [GO:0071944]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
|
PTM: Farnesylated by RAM1-RAM2, which is required for targeting RAS2 to the cytoplasmic site of the endoplasmic reticulum, where proteolytic processing of the C-terminus by RCE1 and methylation of the resulting carboxyl group by STE14 occurs. {ECO:0000269|PubMed:2050108, ECO:0000269|PubMed:2406252, ECO:0000269|PubMed:2663844, ECO:0000269|PubMed:9065405}.; PTM: Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS2. {ECO:0000269|PubMed:2406252}.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P01123
|
YPT1_YEAST
|
MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQIWDTAGQERFRTITSSYYRGSHGIIIVYDVTDQESFNGVKMWLQEIDRYATSTVLKLLVGNKCDLKDKRVVEYDVAKEFADANKMPFLETSALDSTNVEDAFLTMARQIKESMSQQNLNETTQKKEDKGNVNLKGQSLTNTGGGCC
| null | null |
autophagosome assembly [GO:0000045]; COPII-coated vesicle budding [GO:0090114]; cytoplasm to vacuole targeting by the Cvt pathway [GO:0032258]; early endosome to Golgi transport [GO:0034498]; endocytic recycling [GO:0032456]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi vesicle budding [GO:0048194]; Golgi vesicle docking [GO:0048211]; intracellular protein transport [GO:0006886]; macroautophagy [GO:0016236]; pre-mRNA catabolic process [GO:1990261]; protein localization to phagophore assembly site [GO:0034497]; regulation of endoplasmic reticulum unfolded protein response [GO:1900101]; reticulophagy [GO:0061709]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; SNARE complex assembly [GO:0035493]; SNARE complex disassembly [GO:0035494]
|
cis-Golgi network [GO:0005801]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; mitochondrion [GO:0005739]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; SNARE binding [GO:0000149]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: Prenylation is required for interaction with GDI1 and YIP1. {ECO:0000269|PubMed:10071213}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12802060}; Peripheral membrane protein {ECO:0000269|PubMed:12802060}. Golgi apparatus membrane {ECO:0000269|PubMed:12802060}; Peripheral membrane protein {ECO:0000269|PubMed:12802060}. Cytoplasm {ECO:0000269|PubMed:12802060}. Preautophagosomal structure membrane {ECO:0000269|PubMed:20375281}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=ER and Golgi when GTP-bound. Cytoplasmic when bound to GDI1.
| null | null | null | null | null |
FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. YPT1 regulates the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. Also involved in the recycling of membrane proteins. {ECO:0000269|PubMed:10071213, ECO:0000269|PubMed:11879636, ECO:0000269|PubMed:12189143, ECO:0000269|PubMed:12802060, ECO:0000269|PubMed:15082776, ECO:0000269|PubMed:20375281}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P01127
|
PDGFB_HUMAN
|
MNRCWALFLSLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHGDPGEEDGAELDLNMTRSHSGGELESLARGRRSLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVTRSPGGSQEQRAKTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA
| null | null |
cell chemotaxis [GO:0060326]; cellular response to growth factor stimulus [GO:0071363]; cellular response to mycophenolic acid [GO:0071506]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; embryonic placenta development [GO:0001892]; gene expression [GO:0010467]; heart development [GO:0007507]; interleukin-18-mediated signaling pathway [GO:0035655]; metanephric glomerular mesangial cell development [GO:0072255]; monocyte chemotaxis [GO:0002548]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of phosphatidylinositol biosynthetic process [GO:0010512]; negative regulation of platelet activation [GO:0010544]; negative regulation of protein binding [GO:0032091]; negative regulation of vascular associated smooth muscle cell differentiation [GO:1905064]; paracrine signaling [GO:0038001]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of chemotaxis [GO:0050921]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell proliferation [GO:0001938]; 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 glomerular filtration [GO:0003104]; positive regulation of glomerular mesangial cell proliferation [GO:0072126]; positive regulation of hyaluronan biosynthetic process [GO:1900127]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of metanephric mesenchymal cell migration [GO:2000591]; positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway [GO:0035793]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of vascular associated smooth muscle cell dedifferentiation [GO:1905176]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein kinase C signaling [GO:0070528]; protein phosphorylation [GO:0006468]; reactive oxygen species metabolic process [GO:0072593]; response to wounding [GO:0009611]
|
basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; platelet alpha granule lumen [GO:0031093]; platelet-derived growth factor complex [GO:1990265]
|
chemoattractant activity [GO:0042056]; collagen binding [GO:0005518]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; superoxide-generating NADPH oxidase activator activity [GO:0016176]
|
PF00341;PF04692;
|
2.10.90.10;
|
PDGF/VEGF growth factor family
| null |
SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding.
| null | null | null | null | null |
FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin (PubMed:26599395). Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity). {ECO:0000250|UniProtKB:P31240, ECO:0000269|PubMed:26599395}.
|
Homo sapiens (Human)
|
P01129
|
CDC10_SCHPO
|
MASANFIRQFELGNDSFSYQKRPEDEPSQPLSNRNINKLNDSSTLKDSSSRIFINSQVLRDGRPVELYAVECSGMKYMELSCGDNVALRRCPDSYFNISQILRLAGTSSSENAKELDDIIESGDYENVDSKHPQIDGVWVPYDRAISIAKRYGVYEILQPLISFNLDLFPKFSKQQQIESSSISKNLNTSSFNTRSPLRNHNFSNPSKSSKNGVHTINNMQSSPSPSSSFLLPLTQIDSQNVKRSNNYLSTSPPILEQRLKRHRIDVSDEDLHPSSQLNDNEASSLFPDTPRLNHSLSFVSLVSSLPPLDQNIMQDYHTSKDILTSIFLDVNFADSSALEAKLSDSLDLDVPIDELGHAALHWAAAVAKMPLLQALIHKGANPLRGNLTGETALMRSVLVTNHLNQNSFGDLLDLLYASLPCTDRAGRTVVHHICLTAGIKGRGSASRYYLETLLNWAKKHASGNNGYMLKDFINYLNHQDKNGDTALNIAARIGNKNIVEVLMQAGASAYIPNRAGLSVANFGIFVENALKQPEDSKQTKVSLMSENLSSKEKTAVPPRQKSRDIIASVTDVISSLDKDFQDEMAAKQSMIDSAYTQLRESTKKLSDLREQLHVSETQRTLFLELRQRCKNLMTSIEEQKSELSNLYESFDPNGIHDSLSLDADAPFTVNENNNKNLSIAELKFQVAAYERNEARLNELANKLWQRNSNIKSKCRRVVSLCTGVDESRVDSLLESLLQAVESDGQQGEVDMGRVAGFLRVVKEHQA
| null | null |
cell division [GO:0051301]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; rRNA transcription [GO:0009303]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; MBF transcription complex [GO:0030907]; nucleus [GO:0005634]; SBF transcription complex [GO:0033309]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713]
|
PF00023;PF04383;
|
1.25.40.20;3.10.260.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630, ECO:0000269|PubMed:10759889}.
| null | null | null | null | null |
FUNCTION: Major component of the cell cycle transcription factor complex MBF (MCB binding factor, also known as DSC1), that controls G1-S phase specific gene expression. Involved in the control of rRNA production, via interaction with pol5. May be involved in the transcriptional regulation of the cdc22 and cdt1 genes. In fission yeast, two genes, cdc10 and cdc2, are required for the cell cycle control called start, the point early in the G1 phase at which cells become committed to the mitotic cycle. {ECO:0000269|PubMed:16816948, ECO:0000269|PubMed:8532516}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P01130
|
LDLR_HUMAN
|
MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA
| null | null |
amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; artery morphogenesis [GO:0048844]; cellular response to fatty acid [GO:0071398]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; endocytosis [GO:0006897]; high-density lipoprotein particle clearance [GO:0034384]; intestinal cholesterol absorption [GO:0030299]; lipid metabolic process [GO:0006629]; lipoprotein catabolic process [GO:0042159]; long-term memory [GO:0007616]; low-density lipoprotein particle clearance [GO:0034383]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of astrocyte activation [GO:0061889]; negative regulation of gene expression [GO:0010629]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of receptor recycling [GO:0001920]; phagocytosis [GO:0006909]; phospholipid transport [GO:0015914]; plasma lipoprotein particle clearance [GO:0034381]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of lysosomal protein catabolic process [GO:1905167]; positive regulation of triglyceride biosynthetic process [GO:0010867]; receptor-mediated endocytosis [GO:0006898]; receptor-mediated endocytosis involved in cholesterol transport [GO:0090118]; regulation of cholesterol metabolic process [GO:0090181]; regulation of phosphatidylcholine catabolic process [GO:0010899]; regulation of protein metabolic process [GO:0051246]; response to caloric restriction [GO:0061771]
|
apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated pit [GO:0005905]; early endosome [GO:0005769]; endolysosome membrane [GO:0036020]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; low-density lipoprotein particle [GO:0034362]; lysosome [GO:0005764]; membrane [GO:0016020]; PCSK9-LDLR complex [GO:1990666]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; somatodendritic compartment [GO:0036477]; sorting endosome [GO:0097443]
|
amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; clathrin heavy chain binding [GO:0032050]; identical protein binding [GO:0042802]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein particle receptor activity [GO:0005041]; molecular adaptor activity [GO:0060090]; protease binding [GO:0002020]; very-low-density lipoprotein particle receptor activity [GO:0030229]; virus receptor activity [GO:0001618]
|
PF07645;PF14670;PF00057;PF00058;
|
4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30;
|
LDLR family
|
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:3005267}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000269|PubMed:19520913}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:19520913}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000303|PubMed:6091915}. Golgi apparatus {ECO:0000269|PubMed:17461796}. Early endosome {ECO:0000269|PubMed:17461796}. Late endosome {ECO:0000269|PubMed:17461796}. Lysosome {ECO:0000269|PubMed:17461796}. Note=Rapidly endocytosed upon ligand binding. Localized at cell membrane, probably in lipid rafts, in serum-starved conditions (PubMed:30443021). {ECO:0000269|PubMed:30443021, ECO:0000269|PubMed:3104336}.
| null | null | null | null | null |
FUNCTION: Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization (PubMed:30443021). {ECO:0000269|PubMed:3005267, ECO:0000269|PubMed:30443021, ECO:0000269|PubMed:6091915}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins. {ECO:0000269|PubMed:10535997, ECO:0000269|PubMed:12615904}.; FUNCTION: (Microbial infection) Acts as a receptor for Vesicular stomatitis virus. {ECO:0000269|PubMed:23589850}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. {ECO:0000269|PubMed:11100124}.; FUNCTION: (Microbial infection) Acts as a receptor for Crimean-Congo hemorrhagic fever virus (CCHFV). {ECO:0000269|PubMed:38182887}.; FUNCTION: (Microbial infection) Acts as a receptor for many Alphavirus, including Getah virus (GETV), Ross river virus (RRV) and Semliki Forest virus. {ECO:0000269|PubMed:38182887}.
|
Homo sapiens (Human)
|
P01131
|
LDLR_BOVIN
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MRLAGWGLRWAIALLIAVGEAAVEDNCGRNEFQCQDGKCISYKWVCDGTAECQDGSDESQETCKSVTCKMGDFSCGGRVNRCISGSWRCDGQVDCENGSDEEGCSPKTCSQDEFRCNDGKCIAPKFVCDLDLDCLDGSDEASCPMPTCGPANFQCNSSMCIPQLWACDGDPDCDDGSDEWPKHCGTPHPSGPLQDNNPCSALEFHCGSGECIHSSWHCDHDPDCKDKSDEENCAVATCRPDEFQCSDGTCIHGSRQCDREPDCKDLSDELGCVNVTLCEGPNKFKCQSGECISLDKVCNSVRDCRDWSDEPLKDCGTNECLDNKGGCSHICNDLKIGYECLCPEGFQLVGKHRCEDIDECQNPDTCSQLCVNLEGSYKCECEEGFRLEPLTKACKAVGTIAYLFFTNRHEVRKMTLDRSEYTSLIPNLKNVVALDTEVASNRIYWSDLSQRKIYSAQIDGAPGFSSYDTVIGEDLQAPDGLAVDWIHSNIYWTDSILGTVSVADTKGVKRKTLFQEEGSKPRAIVVDPVHGFMYWTDWGAPAEIKKGGLNGVDVYSLVTEDIQWPNGITLDLSGGRLYWVDSKLHSISSIDVNGGNRKTVLEDKKKLAHPFSLAIFEDKVFWTDVINEAIFSANRLTGSDISLMAENLLSPEDIVLFHNLTQPRGVNWCERTALRNGGCQYLCLPAPQINPRSPKFTCACPDGMLLAKDMRSCLTESESAVTTRGPSTVSSTAVGPKRTASPELTTAESVTMSQQGQGDIASQADTERPGSVGALYIVLPIALLILLAFGTFLLWKNWRLKSINSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA
| null | null |
amyloid-beta clearance by cellular catabolic process [GO:0150094]; artery morphogenesis [GO:0048844]; cellular response to fatty acid [GO:0071398]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:0008203]; high-density lipoprotein particle clearance [GO:0034384]; intestinal cholesterol absorption [GO:0030299]; lipoprotein catabolic process [GO:0042159]; long-term memory [GO:0007616]; low-density lipoprotein particle clearance [GO:0034383]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of astrocyte activation [GO:0061889]; negative regulation of gene expression [GO:0010629]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of receptor recycling [GO:0001920]; phagocytosis [GO:0006909]; phospholipid transport [GO:0015914]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of lysosomal protein catabolic process [GO:1905167]; positive regulation of triglyceride biosynthetic process [GO:0010867]; receptor-mediated endocytosis involved in cholesterol transport [GO:0090118]; regulation of cholesterol metabolic process [GO:0090181]; regulation of phosphatidylcholine catabolic process [GO:0010899]; response to caloric restriction [GO:0061771]
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apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; low-density lipoprotein particle [GO:0034362]; lysosome [GO:0005764]; multivesicular body [GO:0005771]; PCSK9-LDLR complex [GO:1990666]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; somatodendritic compartment [GO:0036477]; sorting endosome [GO:0097443]
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amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein particle receptor activity [GO:0005041]; protease binding [GO:0002020]; very-low-density lipoprotein particle receptor activity [GO:0030229]
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PF07645;PF14670;PF00057;PF00058;
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4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30;
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LDLR family
|
PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P01130}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250|UniProtKB:P01130}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6313699}; Single-pass type I membrane protein {ECO:0000269|PubMed:6313699}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P01130}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000250|UniProtKB:P01130}.
| null | null | null | null | null |
FUNCTION: Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization. {ECO:0000250|UniProtKB:P01130}.
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Bos taurus (Bovine)
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P01132
|
EGF_MOUSE
|
MPWGRRPTWLLLAFLLVFLKISILSVTAWQTGNCQPGPLERSERSGTCAGPAPFLVFSQGKSISRIDPDGTNHQQLVVDAGISADMDIHYKKERLYWVDVERQVLLRVFLNGTGLEKVCNVERKVSGLAIDWIDDEVLWVDQQNGVITVTDMTGKNSRVLLSSLKHPSNIAVDPIERLMFWSSEVTGSLHRAHLKGVDVKTLLETGGISVLTLDVLDKRLFWVQDSGEGSHAYIHSCDYEGGSVRLIRHQARHSLSSMAFFGDRIFYSVLKSKAIWIANKHTGKDTVRINLHPSFVTPGKLMVVHPRAQPRTEDAAKDPDPELLKQRGRPCRFGLCERDPKSHSSACAEGYTLSRDRKYCEDVNECATQNHGCTLGCENTPGSYHCTCPTGFVLLPDGKQCHELVSCPGNVSKCSHGCVLTSDGPRCICPAGSVLGRDGKTCTGCSSPDNGGCSQICLPLRPGSWECDCFPGYDLQSDRKSCAASGPQPLLLFANSQDIRHMHFDGTDYKVLLSRQMGMVFALDYDPVESKIYFAQTALKWIERANMDGSQRERLITEGVDTLEGLALDWIGRRIYWTDSGKSVVGGSDLSGKHHRIIIQERISRPRGIAVHPRARRLFWTDVGMSPRIESASLQGSDRVLIASSNLLEPSGITIDYLTDTLYWCDTKRSVIEMANLDGSKRRRLIQNDVGHPFSLAVFEDHLWVSDWAIPSVIRVNKRTGQNRVRLQGSMLKPSSLVVVHPLAKPGADPCLYRNGGCEHICQESLGTARCLCREGFVKAWDGKMCLPQDYPILSGENADLSKEVTSLSNSTQAEVPDDDGTESSTLVAEIMVSGMNYEDDCGPGGCGSHARCVSDGETAECQCLKGFARDGNLCSDIDECVLARSDCPSTSSRCINTEGGYVCRCSEGYEGDGISCFDIDECQRGAHNCGENAACTNTEGGYNCTCAGRPSSPGLSCPDSTAPSLLGEDGHHLDRNSYPGCPSSYDGYCLNGGVCMHIESLDSYTCNCVIGYSGDRCQTRDLRWWELRHAGYGQKHDIMVVAVCMVALVLLLVLGMWGTYYYRTRKQLSNPPKNPCDEPSGSVSSSGPNSSSGAAVASCPQPWFVVLEKHQDPKNGSLPADGTNGAVVDAGLSPSLQLGSVHLTSWRQKPHIDGMGTGQSCWIPPSSDRGPQEIEGNSHLPSYRPVGPEKLHSLQSANGSCHERAPDLPRQTEPVQ
| 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]; 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 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 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]
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extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
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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]
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PF00008;PF07645;PF14670;PF00058;
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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}.
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Mus musculus (Mouse)
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P01133
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EGF_HUMAN
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MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKLRKGNCSSTVCGQDLQSHLCMCAEGYALSRDRKYCEDVNECAFWNHGCTLGCKNTPGSYYCTCPVGFVLLPDGKRCHQLVSCPRNVSECSHDCVLTSEGPLCFCPEGSVLERDGKTCSGCSSPDNGGCSQLCVPLSPVSWECDCFPGYDLQLDEKSCAASGPQPFLLFANSQDIRHMHFDGTDYGTLLSQQMGMVYALDHDPVENKIYFAHTALKWIERANMDGSQRERLIEEGVDVPEGLAVDWIGRRFYWTDRGKSLIGRSDLNGKRSKIITKENISQPRGIAVHPMAKRLFWTDTGINPRIESSSLQGLGRLVIASSDLIWPSGITIDFLTDKLYWCDAKQSVIEMANLDGSKRRRLTQNDVGHPFAVAVFEDYVWFSDWAMPSVMRVNKRTGKDRVRLQGSMLKPSSLVVVHPLAKPGADPCLYQNGGCEHICKKRLGTAWCSCREGFMKASDGKTCLALDGHQLLAGGEVDLKNQVTPLDILSKTRVSEDNITESQHMLVAEIMVSDQDDCAPVGCSMYARCISEGEDATCQCLKGFAGDGKLCSDIDECEMGVPVCPPASSKCINTEGGYVCRCSEGYQGDGIHCLDIDECQLGEHSCGENASCTNTEGGYTCMCAGRLSEPGLICPDSTPPPHLREDDHHYSVRNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRHAGHGQQQKVIVVAVCVVVLVMLLLLSLWGAHYYRTQKLLSKNPKNPYEESSRDVRSRRPADTEDGMSSCPQPWFVVIKEHQDLKNGGQPVAGEDGQAADGSMQPTSWRQEPQLCGMGTEQGCWIPVSSDKGSCPQVMERSFHMPSYGTQTLEGGVEKPHSLLSANPLWQQRALDPPHQMELTQ
| null | null |
angiogenesis [GO:0001525]; branching morphogenesis of an epithelial tube [GO:0048754]; canonical Wnt signaling pathway [GO:0060070]; 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]; 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-templated transcription [GO:0045893]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial tube formation [GO:1905278]; positive regulation of gene expression [GO:0010628]; positive regulation of hyaluronan biosynthetic process [GO:1900127]; positive regulation of MAP kinase activity [GO:0043406]; 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 protein localization to cell surface [GO:2000008]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]
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clathrin-coated endocytic vesicle membrane [GO:0030669]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]
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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]
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PF00008;PF07645;PF14670;PF00058;
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2.10.25.10;2.120.10.30;
| null |
PTM: O-glycosylated with core 1-like and core 2-like glycans. It is uncertain if Ser-954 or Thr-955 is O-glycosylated. The modification here shows glycan heterogeneity: HexHexNAc (major) and Hex2HexNAc2 (minor). {ECO:0000269|PubMed:22171320}.
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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. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941). {ECO:0000269|PubMed:10964941, ECO:0000269|PubMed:17671655}.
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Homo sapiens (Human)
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P01134
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TGFA_RAT
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MVPAAGQLALLALGILVAVCQALENSTSPLSDSPVAAAVVSHFNKCPDSHTQYCFHGTCRFLVQEEKPACVCHSGYVGVRCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALVCRHEKPSALLKGRTACCHSETVV
| null | null |
angiogenesis [GO:0001525]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB2-EGFR signaling pathway [GO:0038134]; hepatocyte proliferation [GO:0072574]; mammary gland alveolus development [GO:0060749]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; response to xenobiotic stimulus [GO:0009410]
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basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]
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epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
| null |
2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: [Transforming growth factor alpha]: Secreted, extracellular space.; SUBCELLULAR LOCATION: [Protransforming growth factor alpha]: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
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Rattus norvegicus (Rat)
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P01135
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TGFA_HUMAN
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MVPSAGQLALFALGIVLAACQALENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV
| null | null |
angiogenesis [GO:0001525]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB2-EGFR signaling pathway [GO:0038134]; hepatocyte proliferation [GO:0072574]; intracellular signal transduction [GO:0035556]; mammary gland alveolus development [GO:0060749]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]
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basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
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epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
| null |
2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: [Transforming growth factor alpha]: Secreted, extracellular space.; SUBCELLULAR LOCATION: [Protransforming growth factor alpha]: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
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Homo sapiens (Human)
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P01136
|
VGF_VACCW
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MSMKYLMLLFAAMIIRSFADSGNAIETTSPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQHVVLVDYQRSENPNTTTSYIPSPGIMLVLVGIIIITCCLLSVYRFTRRTKLPIQDMVVP
| null | null |
epidermal growth factor receptor signaling pathway [GO:0007173]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of mitotic nuclear division [GO:0045840]
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extracellular space [GO:0005615]; host cell membrane [GO:0033644]; membrane [GO:0016020]
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epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]
| null |
2.10.25.10;
|
Orthopoxvirus OPG019 family
|
PTM: Cleaved at the cell surface by host ADAM10, thereby releasing the secreted form of VGF. {ECO:0000269|PubMed:2410141, ECO:0000269|PubMed:30420785}.
|
SUBCELLULAR LOCATION: [Pro-Viral epidermal growth factor]: Host membrane {ECO:0000269|PubMed:3339713}; Single-pass type I membrane protein {ECO:0000269|PubMed:3339713}.; SUBCELLULAR LOCATION: [Viral epidermal growth factor]: Secreted {ECO:0000269|PubMed:3339713}.
| null | null | null | null | null |
FUNCTION: [Viral epidermal growth factor]: Stimulates cellular proliferation (hyperplasia)and mobility around infected cells to promote rapid and efficient spread of infection. This effect is beneficial for virus replication in vivo, because poxviruses replicate possibly better in proliferating cells than in quiescent cells. Acts by binding host EGFR, inducing its dimerization, autophosphorylation and leading to activation of several cellular pathways regulating cell proliferation or cell survival. The activation by host EGFR of mitogen activated protein kinases (MAPK) and extracellular-signal regulated kinases (ERK) are essential for the positive effect of vaccinia growth factor on poxvirus virulence in vivo. {ECO:0000269|PubMed:15025565, ECO:0000269|PubMed:20512239, ECO:0000269|PubMed:2229050, ECO:0000269|PubMed:3339713}.
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Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P01137
|
TGFB1_HUMAN
|
MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
| null | null |
adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains [GO:0002460]; aortic valve morphogenesis [GO:0003180]; ATP biosynthetic process [GO:0006754]; branch elongation involved in mammary gland duct branching [GO:0060751]; bronchiole development [GO:0060435]; canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; cell-cell junction organization [GO:0045216]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to ionizing radiation [GO:0071479]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to mechanical stimulus [GO:0071260]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to virus [GO:0098586]; chondrocyte differentiation [GO:0002062]; columnar/cuboidal epithelial cell maturation [GO:0002069]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; defense response to fungus [GO:0050832]; digestive tract development [GO:0048565]; embryonic liver development [GO:1990402]; endoderm development [GO:0007492]; epithelial cell proliferation [GO:0050673]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic signaling pathway [GO:0097191]; face morphogenesis [GO:0060325]; female pregnancy [GO:0007565]; frontal suture morphogenesis [GO:0060364]; gene expression [GO:0010467]; germ cell migration [GO:0008354]; heart development [GO:0007507]; heart valve morphogenesis [GO:0003179]; hematopoietic progenitor cell differentiation [GO:0002244]; hyaluronan catabolic process [GO:0030214]; inner ear development [GO:0048839]; intracellular calcium ion homeostasis [GO:0006874]; Langerhans cell differentiation [GO:0061520]; lens fiber cell differentiation [GO:0070306]; liver regeneration [GO:0097421]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; macrophage derived foam cell differentiation [GO:0010742]; mammary gland branching involved in thelarche [GO:0060744]; membrane protein intracellular domain proteolysis [GO:0031293]; muscle cell cellular homeostasis [GO:0046716]; myelination [GO:0042552]; myofibroblast differentiation [GO:0036446]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell differentiation [GO:0045596]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002859]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of ossification [GO:0030279]; negative regulation of phagocytosis [GO:0050765]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of release of sequestered calcium ion into cytosol [GO:0051280]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; neuron apoptotic process [GO:0051402]; Notch signaling pathway [GO:0007219]; odontoblast differentiation [GO:0071895]; odontogenesis of dentin-containing tooth [GO:0042475]; oligodendrocyte development [GO:0014003]; osteoclast differentiation [GO:0030316]; phosphate-containing compound metabolic process [GO:0006796]; phospholipid homeostasis [GO:0055091]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cardiac muscle cell differentiation [GO:2000727]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mesenchymal stem cell proliferation [GO:1902462]; positive regulation of microglia differentiation [GO:0014008]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mononuclear cell migration [GO:0071677]; positive regulation of odontogenesis [GO:0042482]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of primary miRNA processing [GO:2000636]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of receptor signaling pathway via STAT [GO:1904894]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of vascular endothelial growth factor production [GO:0010575]; positive regulation of vascular permeability [GO:0043117]; positive regulation of vasculature development [GO:1904018]; protein export from nucleus [GO:0006611]; receptor catabolic process [GO:0032801]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of blood vessel remodeling [GO:0060312]; regulation of branching involved in mammary gland duct morphogenesis [GO:0060762]; regulation of cartilage development [GO:0061035]; regulation of cell migration [GO:0030334]; regulation of cell population proliferation [GO:0042127]; regulation of enamel mineralization [GO:0070173]; regulation of interleukin-23 production [GO:0032667]; regulation of protein import into nucleus [GO:0042306]; regulation of sodium ion transport [GO:0002028]; regulation of striated muscle tissue development [GO:0016202]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulatory T cell differentiation [GO:0045066]; response to cholesterol [GO:0070723]; response to estradiol [GO:0032355]; response to immobilization stress [GO:0035902]; response to laminar fluid shear stress [GO:0034616]; response to progesterone [GO:0032570]; response to salt [GO:1902074]; response to vitamin D [GO:0033280]; response to wounding [GO:0009611]; response to xenobiotic stimulus [GO:0009410]; retina vasculature development in camera-type eye [GO:0061298]; salivary gland morphogenesis [GO:0007435]; sprouting angiogenesis [GO:0002040]; stem cell proliferation [GO:0072089]; surfactant homeostasis [GO:0043129]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]; tolerance induction to self antigen [GO:0002513]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; vasculogenesis [GO:0001570]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
axon [GO:0030424]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]
|
antigen binding [GO:0003823]; cytokine activity [GO:0005125]; deubiquitinase activator activity [GO:0035800]; enzyme binding [GO:0019899]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein serine/threonine kinase activator activity [GO:0043539]; protein-containing complex binding [GO:0044877]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta receptor binding [GO:0034714]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000269|PubMed:7737999}.; PTM: [Latency-associated peptide]: N-glycosylated (PubMed:2493139, PubMed:28117447, PubMed:3162913). Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear (PubMed:2493139). {ECO:0000269|PubMed:2493139, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:3162913}.
|
SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17827158}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:29483653}.
| null | null | null | null | null |
FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000269|PubMed:29109152, ECO:0000303|PubMed:27252363}.; FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix (PubMed:28117447). Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:19651619, PubMed:19750484, PubMed:2022183, PubMed:22278742, PubMed:8617200, PubMed:8939931). Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (Probable). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (PubMed:19651619, PubMed:19750484, PubMed:22278742). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). {ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931, ECO:0000305|PubMed:29909984}.; FUNCTION: [Transforming growth factor beta-1]: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix (PubMed:29109152). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus (PubMed:19651619, PubMed:19750484, PubMed:2022183, PubMed:22278742, PubMed:8617200, PubMed:8939931). TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (PubMed:20207738). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules' (By similarity). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development (By similarity). At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP) (PubMed:25310401). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus (PubMed:25893292, PubMed:29483653, PubMed:30696809). Positively regulates odontoblastic differentiation in dental papilla cells, via promotion of IPO7-mediated translocation of phosphorylated SMAD2 to the nucleus and subsequent transcription of target genes (By similarity). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (PubMed:25893292, PubMed:30696809). {ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152, ECO:0000269|PubMed:29483653, ECO:0000269|PubMed:30696809, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}.
|
Homo sapiens (Human)
|
P01138
|
NGF_HUMAN
|
MSMLFYTLITAFLIGIQAEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA
| null | null |
extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:0007422]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of DNA binding [GO:0043388]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of Ras protein signal transduction [GO:0046579]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; synaptic vesicle [GO:0008021]
|
growth factor activity [GO:0008083]; lipid binding [GO:0008289]; metalloendopeptidase inhibitor activity [GO:0008191]; nerve growth factor receptor binding [GO:0005163]
|
PF00243;
|
2.10.90.10;
|
NGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20978020}. Endosome lumen {ECO:0000250|UniProtKB:P01139}. Note=ProNGF is endocytosed after binding to the cell surface receptor formed by SORT1 and NGFR. {ECO:0000250|UniProtKB:P01139}.
| null | null | null | null | null |
FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:14976160, PubMed:20978020). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable) (PubMed:20978020). The immature NGF precursor (proNGF) functions as a ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (By similarity). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (PubMed:20164177). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (By similarity). {ECO:0000250|UniProtKB:P01139, ECO:0000269|PubMed:14976160, ECO:0000269|PubMed:20164177, ECO:0000269|PubMed:20978020, ECO:0000305|PubMed:10490030, ECO:0000305|PubMed:15131306}.
|
Homo sapiens (Human)
|
P01139
|
NGF_MOUSE
|
MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG
| null | null |
adult locomotory behavior [GO:0008344]; axon extension [GO:0048675]; circadian rhythm [GO:0007623]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron apoptotic process [GO:0051402]; neuron projection development [GO:0031175]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:0007422]; positive regulation of axon extension [GO:0045773]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of DNA binding [GO:0043388]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron maturation [GO:0014042]; positive regulation of neuron projection development [GO:0010976]; positive regulation of neurotrophin TRK receptor signaling pathway [GO:0051388]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of stem cell proliferation [GO:2000648]; regulation of neuron differentiation [GO:0045664]; regulation of neurotransmitter secretion [GO:0046928]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; sensory perception of pain [GO:0019233]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; dendrite [GO:0030425]; endoplasmic reticulum lumen [GO:0005788]; endosome lumen [GO:0031904]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021]
|
growth factor activity [GO:0008083]; lipid binding [GO:0008289]; metalloendopeptidase inhibitor activity [GO:0008191]; nerve growth factor receptor binding [GO:0005163]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
|
PF00243;
|
2.10.90.10;
|
NGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1284621}. Endosome lumen {ECO:0000269|PubMed:20036257}. Note=ProNGF is endocytosed after binding to the cell surface receptor formed by SORT1 and NGFR. {ECO:0000269|PubMed:20036257}.
| null | null | null | null | null |
FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:20036257). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (PubMed:22649032). The immature NGF precursor (proNGF) functions as a ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse (PubMed:22155786). In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (PubMed:20036257). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (By similarity). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer (PubMed:22649032, PubMed:26144237). The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (PubMed:22649032). {ECO:0000250|UniProtKB:P01138, ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237}.
|
Mus musculus (Mouse)
|
P01142
|
CRF_SHEEP
|
MRLPLLVSVGVLLVALLPSPPCRALLSRGPIPGARQASQHPQPLSFFQPLPQPQEPQALPTLLRVGEEYFLRLGNLDETRAAPLSPAASPLASRSSSRLSPDKVAANFFRALLQPRRPLDSPAGPAKRGTENALGSRQEAPAARKRRSQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIAGK
| null | null |
negative regulation of epinephrine secretion [GO:0032811]; negative regulation of glucagon secretion [GO:0070093]; positive regulation of cortisol secretion [GO:0051464]; regulation of NMDA receptor activity [GO:2000310]; synaptic transmission, dopaminergic [GO:0001963]
|
extracellular space [GO:0005615]; synapse [GO:0045202]
|
corticotropin-releasing hormone activity [GO:0017045]
|
PF00473;
|
6.10.250.1920;
|
Sauvagine/corticotropin-releasing factor/urotensin I family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6273874}.
| null | null | null | null | null |
FUNCTION: Hormone regulating the release of corticotropin from pituitary gland (PubMed:6267699, PubMed:6273874). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). {ECO:0000250|UniProtKB:Q8CIT0, ECO:0000269|PubMed:6267699, ECO:0000269|PubMed:6273874}.
|
Ovis aries (Sheep)
|
P01143
|
CRF_RAT
|
MRLRLLVSAGMLLVALSPCLPCRALLSRGSVSGAPRAPQPLNFLQPEQPQQPQPILIRMGEEYFLRLGNLNRSPAARLSPNSTPLTAGRGSRPSHDQAAANFFRVLLQQLQMPQRPLDSSTELAERGAEDALGGHQGALERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK
| null | null |
adrenal gland development [GO:0030325]; associative learning [GO:0008306]; cellular response to cocaine [GO:0071314]; cellular response to dexamethasone stimulus [GO:0071549]; diterpenoid metabolic process [GO:0016101]; female pregnancy [GO:0007565]; glucocorticoid biosynthetic process [GO:0006704]; hormone-mediated apoptotic signaling pathway [GO:0008628]; hypothalamus development [GO:0021854]; inflammatory response [GO:0006954]; learning or memory [GO:0007611]; locomotory exploration behavior [GO:0035641]; long-term synaptic potentiation [GO:0060291]; lung development [GO:0030324]; monoatomic ion homeostasis [GO:0050801]; negative regulation of epinephrine secretion [GO:0032811]; negative regulation of gene expression [GO:0010629]; negative regulation of glucagon secretion [GO:0070093]; negative regulation of luteinizing hormone secretion [GO:0033685]; negative regulation of norepinephrine secretion [GO:0010700]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuron apoptotic process [GO:0051402]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of corticosterone secretion [GO:2000854]; positive regulation of corticotropin secretion [GO:0051461]; positive regulation of cortisol secretion [GO:0051464]; positive regulation of digestive system process [GO:0060456]; positive regulation of gene expression [GO:0010628]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of protein phosphorylation [GO:0001934]; regulation of NMDA receptor activity [GO:2000310]; regulation of serotonin secretion [GO:0014062]; response to aldosterone [GO:1904044]; response to cocaine [GO:0042220]; response to corticosterone [GO:0051412]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to ether [GO:0045472]; response to immobilization stress [GO:0035902]; response to pain [GO:0048265]; response to xenobiotic stimulus [GO:0009410]; steroid metabolic process [GO:0008202]; synaptic transmission, dopaminergic [GO:0001963]
|
extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; synapse [GO:0045202]; varicosity [GO:0043196]
|
corticotropin-releasing hormone activity [GO:0017045]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; corticotropin-releasing hormone receptor 2 binding [GO:0051431]
|
PF00473;
|
6.10.250.1920;
|
Sauvagine/corticotropin-releasing factor/urotensin I family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6603620}.
| null | null | null | null | null |
FUNCTION: Hormone regulating the release of corticotropin from pituitary gland (PubMed:6603620). Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). {ECO:0000250|UniProtKB:Q8CIT0, ECO:0000269|PubMed:6603620}.
|
Rattus norvegicus (Rat)
|
P01148
|
GON1_HUMAN
|
MKPIQKLLAGLILLTWCVEGCSSQHWSYGLRPGGKRDAENLIDSFQEIVKEVGQLAETQRFECTTHQPRSPLRDLKGALESLIEEETGQKKI
| null | null |
cell-cell signaling [GO:0007267]; negative regulation of neuron migration [GO:2001223]; regulation of gene expression [GO:0010468]; regulation of ovarian follicle development [GO:2000354]; reproduction [GO:0000003]; response to ethanol [GO:0045471]; response to steroid hormone [GO:0048545]; signal transduction [GO:0007165]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
gonadotropin hormone-releasing hormone activity [GO:0005183]; gonadotropin-releasing hormone receptor binding [GO:0031530]; hormone activity [GO:0005179]
|
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 (PubMed:10336644, PubMed:7683654). The mature form of Gonadoliberin-1 is also cleaved and degraded by ACE (PubMed:2983326, PubMed:7683654). {ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:2983326, ECO:0000269|PubMed:7683654}.
|
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.
|
Homo sapiens (Human)
|
P01150
|
TRH_RAT
|
MPGPWLLLALALIFTLTGIPESCALPEAAQEEGAVTPDLPGLENVQVRPERRFLWKDLQRVRGDLGAALDSWITKRQHPGKREEEEKDIEAEERGDLGEGGAWRLHKRQHPGRRANQDKYSWADEEDSDWMPRSWLPDFFLDSWFSDVPQVKRQHPGRRSFPWMESDVTKRQHPGRRFIDPELQRSWEEKEGEGVLMPEKRQHPGKRALGHPCGPQGTCGQTGLLQLLGDLSRGQETLVKQSPQVEPWDKEPLEE
| null | null |
adult walking behavior [GO:0007628]; eating behavior [GO:0042755]; histamine metabolic process [GO:0001692]; hormone-mediated signaling pathway [GO:0009755]; negative regulation of feeding behavior [GO:2000252]; negative regulation of glutamate secretion [GO:0014050]; positive regulation of gamma-aminobutyric acid secretion [GO:0014054]; positive regulation of insulin secretion [GO:0032024]; response to corticosterone [GO:0051412]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to organic cyclic compound [GO:0014070]
|
extracellular region [GO:0005576]; secretory granule [GO:0030141]
|
thyrotropin-releasing hormone activity [GO:0008437]
|
PF05438;
| null |
TRH family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems.
|
Rattus norvegicus (Rat)
|
P01160
|
ANF_HUMAN
|
MSSFSTTTVSFLLLLAFQLLGQTRANPMYNAVSNADLMDFKNLLDHLEEKMPLEDEVVPPQVLSEPNEEAGAALSPLPEVPPWTGEVSPAQRDGGALGRGPWDSSDRSALLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRY
| null | null |
aortic valve morphogenesis [GO:0003180]; cardiac conduction system development [GO:0003161]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of delayed rectifier potassium channel activity [GO:1902261]; positive regulation of heart rate [GO:0010460]; positive regulation of potassium ion export across plasma membrane [GO:1903766]; protein folding [GO:0006457]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of atrial cardiac muscle cell membrane repolarization [GO:0060372]; regulation of blood pressure [GO:0008217]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; regulation of high voltage-gated calcium channel activity [GO:1901841]; response to muscle stretch [GO:0035994]; sodium ion export across plasma membrane [GO:0036376]; vasodilation [GO:0042311]
|
cell projection [GO:0042995]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; protein-containing complex [GO:0032991]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; neuropeptide hormone activity [GO:0005184]; neuropeptide receptor binding [GO:0071855]; signaling receptor binding [GO:0005102]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-123 to produce atrial natriuretic peptide (PubMed:10880574, PubMed:14559895, PubMed:7984506). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (PubMed:2532366, PubMed:7955907, PubMed:7984506). 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 (PubMed:2972874, PubMed:8351194, PubMed:9794555). {ECO:0000250|UniProtKB:P01161, ECO:0000269|PubMed:10880574, ECO:0000269|PubMed:14559895, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:2972874, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:9794555}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity (PubMed:16254193, PubMed:2972276). Degraded by IDE (in vitro) (PubMed:21098034). 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) (PubMed:21098034). {ECO:0000269|PubMed:16254193, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:2972276}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000269|PubMed:21098034}.; PTM: [Urodilatin]: Phosphorylation on Ser-129 decreases vasorelaxant activity. {ECO:0000269|PubMed:2528951}.
|
SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8653797}. Note=Detected in blood. {ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8653797}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8653797}. Note=Detected in blood. {ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8653797}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000269|PubMed:7984506}. Note=Detected in blood. {ECO:0000269|PubMed:7984506}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000269|PubMed:2972874, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:8779891, ECO:0000269|PubMed:8853410, ECO:0000269|PubMed:9794555, ECO:0000269|PubMed:9893117}. Note=Detected in urine (PubMed:2972874, PubMed:8351194, PubMed:8779891, PubMed:9794555). Not detected in blood (PubMed:8351194). Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion (PubMed:8351194, PubMed:8779891, PubMed:8853410, PubMed:9893117). {ECO:0000269|PubMed:2972874, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:8779891, ECO:0000269|PubMed:8853410, ECO:0000269|PubMed:9794555, ECO:0000269|PubMed:9893117}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000269|PubMed:15741263, ECO:0000269|PubMed:18835931, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:2972874, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:8653797, ECO:0000269|PubMed:8779891, ECO:0000269|PubMed:9893117}. Perikaryon {ECO:0000269|PubMed:30534047}. Cell projection {ECO:0000269|PubMed:30534047}. Note=Detected in blood (PubMed:15741263, PubMed:18835931, PubMed:2532366, PubMed:7955907, PubMed:7984506, PubMed:8351194, PubMed:8653797, PubMed:8779891). Detected in urine in one study (PubMed:8351194). However, in another study, was not detected in urine (PubMed:7984506). Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (PubMed:30534047). 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 (PubMed:2532366). In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels (PubMed:9893117). Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (PubMed:8779891). {ECO:0000250|UniProtKB:P01161, ECO:0000269|PubMed:15741263, ECO:0000269|PubMed:18835931, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:30534047, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:7984506, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:8653797, ECO:0000269|PubMed:8779891, ECO:0000269|PubMed:9893117}.; 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 (PubMed:15741263, PubMed:16875975, PubMed:18835931, PubMed:21672517, PubMed:22307324, PubMed:2532366, PubMed:2825692, PubMed:7595132, PubMed:7720651, PubMed:8087923, PubMed:8653797). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (PubMed:1660465, PubMed:1672777, PubMed:21098034, PubMed:2162527, PubMed:22307324, PubMed:25401746, PubMed:2825692, PubMed:7720651, PubMed:8384600, PubMed:9893117). 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 (PubMed:2532366, PubMed:2825692, PubMed:7595132, PubMed:7720651, PubMed:8087923, PubMed:8653797). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (PubMed:16875975). 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 (PubMed:15741263, PubMed:18835931, PubMed:21672517, PubMed:22307324). 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 (PubMed:15741263, PubMed:18835931, PubMed:21672517, PubMed:22307324). Binds the clearance receptor NPR3 which removes the hormone from circulation (PubMed:1672777). {ECO:0000250|UniProtKB:P05125, ECO:0000269|PubMed:15741263, ECO:0000269|PubMed:1660465, ECO:0000269|PubMed:1672777, ECO:0000269|PubMed:16875975, ECO:0000269|PubMed:18835931, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:2162527, ECO:0000269|PubMed:21672517, ECO:0000269|PubMed:22307324, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:25401746, ECO:0000269|PubMed:2825692, ECO:0000269|PubMed:7595132, ECO:0000269|PubMed:7720651, ECO:0000269|PubMed:8087923, ECO:0000269|PubMed:8384600, ECO:0000269|PubMed:8653797, ECO:0000269|PubMed:9893117}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis (PubMed:2532366, PubMed:2825692, PubMed:7595132, PubMed:7955907, PubMed:8087923, PubMed:8653797). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7720651). 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 (PubMed:2162527, PubMed:2825692). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (PubMed:11145122). {ECO:0000250|UniProtKB:P01161, ECO:0000269|PubMed:11145122, ECO:0000269|PubMed:2162527, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:2825692, ECO:0000269|PubMed:7595132, ECO:0000269|PubMed:7720651, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:8087923, ECO:0000269|PubMed:8653797}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation (PubMed:2532366, PubMed:7595132, PubMed:7955907, PubMed:8087923, PubMed:8653797). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7595132, PubMed:7720651). 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 (PubMed:7831500). Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides (PubMed:2162527, PubMed:2825692). 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 (PubMed:11145122). {ECO:0000269|PubMed:11145122, ECO:0000269|PubMed:2162527, ECO:0000269|PubMed:2532366, ECO:0000269|PubMed:2825692, ECO:0000269|PubMed:7595132, ECO:0000269|PubMed:7720651, ECO:0000269|PubMed:7831500, ECO:0000269|PubMed:7955907, ECO:0000269|PubMed:8087923, ECO:0000269|PubMed:8653797}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis (PubMed:2825692, PubMed:7595132, PubMed:8087923). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7595132, PubMed:7720651). May have a role in potassium excretion but not sodium excretion (natriuresis) (PubMed:8087923). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (PubMed:11145122). {ECO:0000269|PubMed:11145122, ECO:0000269|PubMed:2825692, ECO:0000269|PubMed:7595132, ECO:0000269|PubMed:7720651, ECO:0000269|PubMed:8087923}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis (PubMed:8351194, PubMed:8779891, PubMed:8853410). Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance (PubMed:2528951, PubMed:8351194, PubMed:8779891, PubMed:8853410). Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1 (PubMed:8384600, PubMed:9893117). Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney (PubMed:8384600, PubMed:8779891). {ECO:0000269|PubMed:2528951, ECO:0000269|PubMed:8351194, ECO:0000269|PubMed:8384600, ECO:0000269|PubMed:8779891, ECO:0000269|PubMed:8853410, ECO:0000269|PubMed:9893117}.; 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}.
|
Homo sapiens (Human)
|
P01161
|
ANF_RAT
|
MGSFSITKGFFLFLAFWLPGHIGANPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTDEAGAALSSLSEVPPWTGEVNPSQRDGGALGRGPWDPSDRSALLKSKLRALLAGPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR
| null | null |
cardiac muscle hypertrophy in response to stress [GO:0014898]; cell growth involved in cardiac muscle cell development [GO:0061049]; cellular response to angiotensin [GO:1904385]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to mechanical stimulus [GO:0071260]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; heart development [GO:0007507]; multicellular organismal-level water homeostasis [GO:0050891]; negative regulation of blood pressure [GO:0045776]; negative regulation of cell growth [GO:0030308]; negative regulation of collecting lymphatic vessel constriction [GO:1903815]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of cGMP-mediated signaling [GO:0010753]; positive regulation of delayed rectifier potassium channel activity [GO:1902261]; positive regulation of heart rate [GO:0010460]; positive regulation of histamine secretion by mast cell [GO:1903595]; positive regulation of potassium ion export across plasma membrane [GO:1903766]; protein folding [GO:0006457]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of atrial cardiac muscle cell membrane repolarization [GO:0060372]; regulation of blood pressure [GO:0008217]; regulation of body fluid levels [GO:0050878]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; regulation of high voltage-gated calcium channel activity [GO:1901841]; response to 3-methylcholanthrene [GO:1904681]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; sodium ion export across plasma membrane [GO:0036376]; synaptic signaling via neuropeptide [GO:0099538]; vasodilation [GO:0042311]
|
brush border [GO:0005903]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; glycinergic synapse [GO:0098690]; mast cell granule [GO:0042629]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; neuropeptide hormone activity [GO:0005184]; neuropeptide receptor binding [GO:0071855]; signaling receptor binding [GO:0005102]
|
PF00212;
| null |
Natriuretic peptide family
|
PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-122 to produce the atrial natriuretic peptide. 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 (PubMed:3160114, PubMed:6232612, PubMed:6233494, PubMed:6419347). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000269|PubMed:3160114, ECO:0000269|PubMed:6232612, ECO:0000269|PubMed:6233494, ECO:0000269|PubMed:6419347}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity (PubMed:2966343). Degradation by IDE results in reduced activation of NPR1 (in vitro) (By similarity). 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) (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000269|PubMed:2966343}.; 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:0000269|PubMed:2966345, ECO:0000269|PubMed:3160114}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood (PubMed:2966345, PubMed:3160114). Detected in urine in one study (By similarity). However, in another study, was not detected in urine (By similarity). Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (PubMed:3160114). Also likely to be secreted in response to an increase in atrial pressure or atrial stretch (By similarity). In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels (By similarity). 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:0000269|PubMed:2966345, ECO:0000269|PubMed:3160114}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000269|PubMed:3160114}. Note=Detected in blood (PubMed:3160114). Slight increase in secretion in response to the vasopressin AVP (PubMed:3160114). {ECO:0000269|PubMed:3160114}.
| 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 (PubMed:15117952). 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 (PubMed:7831500). 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, ECO:0000269|PubMed:15117952, ECO:0000269|PubMed:7831500}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis (By similarity). In vitro, promotes the production of cGMP and induces vasodilation (By similarity). 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 (PubMed:7831500). 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:0000269|PubMed:7831500}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation (By similarity). In vitro, promotes the production of cGMP and induces vasodilation (By similarity). 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 (PubMed:7831500). Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000269|PubMed:7831500}.; 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:0000269|PubMed:6232612}.; 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:0000269|PubMed:6232612}.; 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:0000269|PubMed:6233494}.; 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:0000269|PubMed:6419347}.; 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:0000269|PubMed:6419347}.
|
Rattus norvegicus (Rat)
|
P01165
|
7B2_PIG
|
MVSTMLSGLVLWLTFGWTPALAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNTPKDFSEDQGYPDPPNPCPIGKTDDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE
| null | null |
intracellular protein transport [GO:0006886]; neuropeptide signaling pathway [GO:0007218]; peptide hormone processing [GO:0016486]; regulation of hormone secretion [GO:0046883]
|
extracellular region [GO:0005576]; secretory granule [GO:0030141]
|
enzyme inhibitor activity [GO:0004857]; enzyme regulator activity [GO:0030234]; unfolded protein binding [GO:0051082]
|
PF05281;
| null |
7B2 family
|
PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides. {ECO:0000250|UniProtKB:P12961}.; PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P12961}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6514132}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000269|PubMed:6514132}.
| null | null | null | null | null |
FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
|
Sus scrofa (Pig)
|
P01175
|
NEU1_BOVIN
|
MAGSSLACCLLGLLALTSACYIQNCPLGGKRAVLDLDVRTCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCSPDGCHEDPACDPEAAFSQH
| null | null |
positive regulation of cold-induced thermogenesis [GO:0120162]; response to estrogen [GO:0043627]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; oxytocin receptor binding [GO:0031855]; V1A vasopressin receptor binding [GO:0031894]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Neurophysin 1 specifically binds oxytocin.; FUNCTION: Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (By similarity). {ECO:0000250|UniProtKB:P01178}.
|
Bos taurus (Bovine)
|
P01178
|
NEU1_HUMAN
|
MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR
| null | null |
drinking behavior [GO:0042756]; eating behavior [GO:0042755]; female pregnancy [GO:0007565]; grooming behavior [GO:0007625]; heart development [GO:0007507]; male mating behavior [GO:0060179]; maternal aggressive behavior [GO:0002125]; maternal behavior [GO:0042711]; memory [GO:0007613]; negative regulation of blood pressure [GO:0045776]; negative regulation of urine volume [GO:0035811]; positive regulation of blood pressure [GO:0045777]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of female receptivity [GO:0045925]; positive regulation of hindgut contraction [GO:0060450]; positive regulation of norepinephrine secretion [GO:0010701]; positive regulation of ossification [GO:0045778]; positive regulation of penile erection [GO:0060406]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of uterine smooth muscle contraction [GO:0070474]; regulation of heart rate [GO:0002027]; response to activity [GO:0014823]; response to amphetamine [GO:0001975]; response to cAMP [GO:0051591]; response to cocaine [GO:0042220]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to ether [GO:0045472]; response to food [GO:0032094]; response to glucocorticoid [GO:0051384]; response to peptide hormone [GO:0043434]; response to progesterone [GO:0032570]; response to prostaglandin E [GO:0034695]; response to retinoic acid [GO:0032526]; response to sucrose [GO:0009744]; signal transduction [GO:0007165]; social behavior [GO:0035176]; sperm ejaculation [GO:0042713]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; terminal bouton [GO:0043195]
|
neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; oxytocin receptor binding [GO:0031855]; V1A vasopressin receptor binding [GO:0031894]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Neurophysin 1 specifically binds oxytocin.; FUNCTION: Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (PubMed:18174156). {ECO:0000269|PubMed:18174156}.
|
Homo sapiens (Human)
|
P01179
|
NEU1_RAT
|
MACPSLACCLLGLLALTSACYIQNCPLGGKRAALDLDMRKCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCATAGICCSPDGCRTDPACDPESAFSER
| null | null |
drinking behavior [GO:0042756]; eating behavior [GO:0042755]; female pregnancy [GO:0007565]; grooming behavior [GO:0007625]; heart development [GO:0007507]; lactation [GO:0007595]; male mating behavior [GO:0060179]; maternal aggressive behavior [GO:0002125]; maternal behavior [GO:0042711]; memory [GO:0007613]; negative regulation of blood pressure [GO:0045776]; negative regulation of urine volume [GO:0035811]; parturition [GO:0007567]; positive regulation of blood pressure [GO:0045777]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of female receptivity [GO:0045925]; positive regulation of hindgut contraction [GO:0060450]; positive regulation of norepinephrine secretion [GO:0010701]; positive regulation of ossification [GO:0045778]; positive regulation of penile erection [GO:0060406]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of uterine smooth muscle contraction [GO:0070474]; regulation of heart rate [GO:0002027]; response to activity [GO:0014823]; response to amphetamine [GO:0001975]; response to cAMP [GO:0051591]; response to cocaine [GO:0042220]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to ether [GO:0045472]; response to external biotic stimulus [GO:0043207]; response to food [GO:0032094]; response to glucocorticoid [GO:0051384]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to progesterone [GO:0032570]; response to prostaglandin E [GO:0034695]; response to retinoic acid [GO:0032526]; response to steroid hormone [GO:0048545]; response to sucrose [GO:0009744]; social behavior [GO:0035176]; sperm ejaculation [GO:0042713]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; terminal bouton [GO:0043195]
|
neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; oxytocin receptor binding [GO:0031855]; V1A vasopressin receptor binding [GO:0031894]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null | null | null | null | null | null | null |
FUNCTION: Neurophysin 1 specifically binds oxytocin.; FUNCTION: Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (By similarity). {ECO:0000250|UniProtKB:P01178}.
|
Rattus norvegicus (Rat)
|
P01180
|
NEU2_BOVIN
|
MPDATLPACFLSLLAFTSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPECREGVGFPRRVRANDRSNATLLDGPSGALLLRLVQLAGAPEPAEPAQPGVY
| null | null |
vasoconstriction [GO:0042310]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; V1A vasopressin receptor binding [GO:0031894]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Neurophysin 2 specifically binds vasopressin.; FUNCTION: Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). {ECO:0000250|UniProtKB:P01185}.
|
Bos taurus (Bovine)
|
P01183
|
NEU2_PIG
|
MPDATLPACFLGLLALTSACYFQNCPKGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPECREGASFLRRARASDRSNATLLDGPSGALLLRLVQLAGAPEPAEPAQPGVY
| null | null |
vasoconstriction [GO:0042310]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; V1A vasopressin receptor binding [GO:0031894]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
|
PTM: A shorter neurophysin molecule (32-123) is called neurophysin-I and is derived from the complete protein (called neurophysin III) by proteolytic degradation (in vivo or after extraction).
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Neurophysin 2 specifically binds vasopressin.; FUNCTION: Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). {ECO:0000250|UniProtKB:P01185}.
|
Sus scrofa (Pig)
|
P01185
|
NEU2_HUMAN
|
MPDTMLPACFLGLLAFSSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAAFGVCCNDESCVTEPECREGFHRRARASDRSNATQLDGPAGALLLRLVQLAGAPEPFEPAQPDAY
| null | null |
cell-cell signaling [GO:0007267]; ERK1 and ERK2 cascade [GO:0070371]; generation of precursor metabolites and energy [GO:0006091]; grooming behavior [GO:0007625]; locomotory behavior [GO:0007626]; maternal aggressive behavior [GO:0002125]; maternal behavior [GO:0042711]; multicellular organismal-level water homeostasis [GO:0050891]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of female receptivity [GO:0007621]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of transmission of nerve impulse [GO:0051970]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular pH reduction [GO:0032849]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of gene expression [GO:0010628]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of vasoconstriction [GO:0045907]; protein kinase C signaling [GO:0070528]; response to ethanol [GO:0045471]; response to nicotine [GO:0035094]; response to testosterone [GO:0033574]; signal transduction [GO:0007165]; social behavior [GO:0035176]; symbiont entry into host cell [GO:0046718]; vasoconstriction [GO:0042310]; water transport [GO:0006833]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; secretory granule [GO:0030141]
|
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; protein kinase activity [GO:0004672]; signaling receptor binding [GO:0005102]; V1A vasopressin receptor binding [GO:0031894]; V1B vasopressin receptor binding [GO:0031895]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: [Neurophysin 2]: Specifically binds vasopressin.; FUNCTION: [Arg-vasopressin]: Has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (PubMed:18174156). {ECO:0000269|PubMed:18174156}.
|
Homo sapiens (Human)
|
P01186
|
NEU2_RAT
|
MLAMMLNTTLSACFLSLLALTSACYFQNCPRGGKRATSDMELRQCLPCGPGGKGRCFGPSICCADELGCFLGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCSDESCVAEPECREGFFRLTRAREQSNATQLDGPARELLLRLVQLAGTQESVDSAKPRVY
| null | null |
ERK1 and ERK2 cascade [GO:0070371]; grooming behavior [GO:0007625]; locomotory behavior [GO:0007626]; maternal aggressive behavior [GO:0002125]; maternal behavior [GO:0042711]; multicellular organismal-level water homeostasis [GO:0050891]; negative regulation of apoptotic process [GO:0043066]; negative regulation of female receptivity [GO:0007621]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of transmission of nerve impulse [GO:0051970]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular pH reduction [GO:0032849]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of gene expression [GO:0010628]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of vasoconstriction [GO:0045907]; protein kinase C signaling [GO:0070528]; response to ethanol [GO:0045471]; response to nicotine [GO:0035094]; response to organic cyclic compound [GO:0014070]; response to testosterone [GO:0033574]; signal transduction [GO:0007165]; social behavior [GO:0035176]; symbiont entry into host cell [GO:0046718]; temperature homeostasis [GO:0001659]; vasoconstriction [GO:0042310]
|
dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; secretory granule [GO:0030141]
|
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; neurohypophyseal hormone activity [GO:0005185]; neuropeptide hormone activity [GO:0005184]; protein kinase activity [GO:0004672]; V1A vasopressin receptor binding [GO:0031894]; V1B vasopressin receptor binding [GO:0031895]; V2 vasopressin receptor binding [GO:0031896]
|
PF00220;PF00184;
|
2.60.9.10;
|
Vasopressin/oxytocin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Neurophysin 2 specifically binds vasopressin.; FUNCTION: Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). {ECO:0000250|UniProtKB:P01185}.
|
Rattus norvegicus (Rat)
|
P01189
|
COLI_HUMAN
|
MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
| null | null |
calcium-mediated signaling [GO:0019722]; cell-cell signaling [GO:0007267]; cellular pigmentation [GO:0033059]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; negative regulation of tumor necrosis factor production [GO:0032720]; neuropeptide signaling pathway [GO:0007218]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; positive regulation of oxytocin production [GO:0140668]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of appetite [GO:0032098]; regulation of blood pressure [GO:0008217]; regulation of corticosterone secretion [GO:2000852]; regulation of glycogen metabolic process [GO:0070873]; response to melanocyte-stimulating hormone [GO:1990680]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; secretory granule lumen [GO:0034774]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. {ECO:0000269|PubMed:2839146}.; PTM: O-glycosylated; reducing sugar is probably N-acetylgalactosamine.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Homo sapiens (Human)
|
P01190
|
COLI_BOVIN
|
MPRLCSSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSSGVGGAAQKREEEVAVGEGPGPRGDDAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Bos taurus (Bovine)
|
P01191
|
COLI_SHEEP
|
MPRLCSSRSGALLLVLLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSFGAGGAAQKREEEVAVGEGPGPRGDGAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ
| null | null |
calcium-mediated signaling [GO:0019722]; cell-cell signaling [GO:0007267]; cellular pigmentation [GO:0033059]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; negative regulation of tumor necrosis factor production [GO:0032720]; neuropeptide signaling pathway [GO:0007218]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; positive regulation of oxytocin production [GO:0140668]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of appetite [GO:0032098]; regulation of blood pressure [GO:0008217]; regulation of corticosterone secretion [GO:2000852]; regulation of glycogen metabolic process [GO:0070873]; response to melanocyte-stimulating hormone [GO:1990680]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
neuropeptide hormone activity [GO:0005184]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Ovis aries (Sheep)
|
P01192
|
COLI_PIG
|
MPRLCGSRSGALLLTLLLQASMGVRGWCLESSQCQDLSTESNLLACIRACKPDLSAETPVFPGNGDAQPLTENPRKYVMGHFRWDRFGRRNGSSSGGGGGGGGAGQKREEEEVAAGEGPGPRGDGVAPGPRQDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDELAEAFPLEFRRELAGAPPEPARDPEAPAEGAAARAELEYGLVAEAEAAEKKDEGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIVKNAHKKGQ
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Sus scrofa (Pig)
|
P01193
|
COLI_MOUSE
|
MPRFCYSRSGALLLALLLQTSIDVWSWCLESSQCQDLTTESNLLACIRACKLDLSLETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGPRNSSSAGSAAQRRAEEEAVWGDGSPEPSPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNVAENESAEAFPLEFKRELEGERPLGLEQVLESDAEKDDGPYRVEHFRWSNPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ
| null | null |
calcium-mediated signaling [GO:0019722]; cell-cell signaling [GO:0007267]; cellular pigmentation [GO:0033059]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; negative regulation of tumor necrosis factor production [GO:0032720]; neuropeptide signaling pathway [GO:0007218]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; positive regulation of oxytocin production [GO:0140668]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of appetite [GO:0032098]; regulation of blood pressure [GO:0008217]; regulation of corticosterone secretion [GO:2000852]; regulation of glycogen metabolic process [GO:0070873]; response to melanocyte-stimulating hormone [GO:1990680]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25707796}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000269|PubMed:25707796}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Mus musculus (Mouse)
|
P01194
|
COLI_RAT
|
MPRFCNSRSGALLLALLLQTSIDVWSWCLESSQCQDLTTESNLLACIRACRLDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGPRNSSSAGGSAQRRAEEETAGGDGRPEPSPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNVAENESAEAFPLEFKRELEGEQPDGLEQVLEPDTEKADGPYRVEHFRWGNPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNVHKKGQ
| null | null |
calcium-mediated signaling [GO:0019722]; cell-cell signaling [GO:0007267]; cellular pigmentation [GO:0033059]; feeding behavior [GO:0007631]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; negative regulation of tumor necrosis factor production [GO:0032720]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of oxytocin production [GO:0140668]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of appetite [GO:0032098]; regulation of blood pressure [GO:0008217]; regulation of corticosterone secretion [GO:2000852]; regulation of glycogen metabolic process [GO:0070873]; response to melanocyte-stimulating hormone [GO:1990680]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; peroxisomal matrix [GO:0005782]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Rattus norvegicus (Rat)
|
P01201
|
COLI_MACNE
|
MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSGSAHQKREDVAAGEDRGLLPEGGPEPRGDGAGPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRPRAGDGPDGPADDGAGPRADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGQ
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Macaca nemestrina (Pig-tailed macaque)
|
P01210
|
PENK_HUMAN
|
MARFLTLCTWLLLLGPGLLATVRAECSQDCATCSYRLVRPADINFLACVMECEGKLPSLKIWETCKELLQLSKPELPQDGTSTLRENSKPEESHLLAKRYGGFMKRYGGFMKKMDELYPMEPEEEANGSEILAKRYGGFMKKDAEEDDSLANSSDLLKELLETGDNRERSHHQDGSDNEEEVSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEALPSDEEGESYSKEVPEMEKRYGGFMRF
| null | null |
aggressive behavior [GO:0002118]; behavioral fear response [GO:0001662]; cellular response to cAMP [GO:0071320]; cellular response to oxidative stress [GO:0034599]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to virus [GO:0098586]; cellular response to vitamin D [GO:0071305]; chemical synaptic transmission [GO:0007268]; G protein-coupled opioid receptor signaling pathway [GO:0038003]; general adaptation syndrome, behavioral process [GO:0051867]; glial cell proliferation [GO:0014009]; locomotory exploration behavior [GO:0035641]; neuropeptide signaling pathway [GO:0007218]; osteoblast differentiation [GO:0001649]; positive regulation of behavioral fear response [GO:2000987]; response to calcium ion [GO:0051592]; response to epinephrine [GO:0071871]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666]; response to immobilization stress [GO:0035902]; response to lipopolysaccharide [GO:0032496]; response to nicotine [GO:0035094]; response to toxic substance [GO:0009636]; sensory perception [GO:0007600]; sensory perception of pain [GO:0019233]; signal transduction [GO:0007165]; startle response [GO:0001964]; synaptic signaling via neuropeptide [GO:0099538]; transmission of nerve impulse [GO:0019226]
|
axon terminus [GO:0043679]; cell body fiber [GO:0070852]; chromaffin granule lumen [GO:0034466]; dendrite [GO:0030425]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0099013]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; symmetric synapse [GO:0032280]; synaptic vesicle lumen [GO:0034592]
|
neuropeptide hormone activity [GO:0005184]; opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin. {ECO:0000250|UniProtKB:P01211}.; PTM: [Met-enkephalin]: Processed and degraded by ACE. {ECO:0000269|PubMed:656131}.; PTM: [Leu-enkephalin]: Processed and degraded by ACE. {ECO:0000269|PubMed:656131}.; PTM: [Met-enkephalin-Arg-Gly-Leu]: Probably cleaved by ACE. {ECO:0000305|PubMed:2982830}.; PTM: [Met-enkephalin-Arg-Phe]: Processed by ACE to generate Met-enkephalin in the nucleus accumbens of the brain. {ECO:0000250|UniProtKB:P04094}.; PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. {ECO:0000269|PubMed:9126357}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. Secreted {ECO:0000250|UniProtKB:P01211}.
| null | null | null | null | null |
FUNCTION: [Met-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. {ECO:0000269|PubMed:7057924}.; FUNCTION: [Leu-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. {ECO:0000269|PubMed:7057924}.; FUNCTION: [Met-enkephalin-Arg-Phe]: Met-enkephalin-Arg-Phe neuropeptide acts as a strong ligand of Mu-type opioid receptor OPRM1. Met-enkephalin-Arg-Phe-binding to OPRM1 in the nucleus accumbens of the brain increases activation of OPRM1, leading to long-term synaptic depression of glutamate release. {ECO:0000250|UniProtKB:P22005}.; FUNCTION: [PENK(114-133)]: Increases glutamate release in the striatum and decreases GABA concentration in the striatum. {ECO:0000250|UniProtKB:P04094}.; FUNCTION: [PENK(237-258)]: Increases glutamate release in the striatum. {ECO:0000250|UniProtKB:P04094}.
|
Homo sapiens (Human)
|
P01211
|
PENK_BOVIN
|
MARFLGLCTWLLALGPGLLATVRAECSQDCATCSYRLARPTDLNPLACTLECEGKLPSLKTWETCKELLQLTKLELPPDATSALSKQEESHLLAKKYGGFMKRYGGFMKKMDELYPLEVEEEANGGEVLGKRYGGFMKKDAEEDDGLGNSSNLLKELLGAGDQREGSLHQEGSDAEDVSKRYGGFMRGLKRSPHLEDETKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEPLPSEEEGESYSKEVPEMEKRYGGFMRF
| null | null |
aggressive behavior [GO:0002118]; behavioral fear response [GO:0001662]; chemical synaptic transmission [GO:0007268]; defense response to bacterium [GO:0042742]; G protein-coupled opioid receptor signaling pathway [GO:0038003]; locomotory behavior [GO:0007626]; neuropeptide signaling pathway [GO:0007218]; sensory perception [GO:0007600]; sensory perception of pain [GO:0019233]; startle response [GO:0001964]; transmission of nerve impulse [GO:0019226]
|
axon terminus [GO:0043679]; chromaffin granule lumen [GO:0034466]; dendrite [GO:0030425]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin. {ECO:0000269|PubMed:12869695}.; PTM: [Met-enkephalin]: Processed and degraded by ACE. {ECO:0000250|UniProtKB:P01210}.; PTM: [Leu-enkephalin]: Processed and degraded by ACE. {ECO:0000250|UniProtKB:P01210}.; PTM: [Met-enkephalin-Arg-Gly-Leu]: Probably cleaved by ACE. {ECO:0000250|UniProtKB:P01210}.; PTM: [Met-enkephalin-Arg-Phe]: Processed by ACE to generate Met-enkephalin in the nucleus accumbens of the brain. {ECO:0000250|UniProtKB:P04094}.; PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. {ECO:0000250|UniProtKB:P01210}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000269|PubMed:12869695}. Secreted {ECO:0000305|PubMed:12869695}.
| null | null | null | null | null |
FUNCTION: [Met-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. {ECO:0000250|UniProtKB:P01210}.; FUNCTION: [Leu-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. {ECO:0000250|UniProtKB:P01210}.; FUNCTION: [Met-enkephalin-Arg-Phe]: Met-enkephalin-Arg-Phe neuropeptide acts as a strong ligand of Mu-type opioid receptor OPRM1. Met-enkephalin-Arg-Phe-binding to OPRM1 in the nucleus accumbens of the brain increases activation of OPRM1, leading to long-term synaptic depression of glutamate release. {ECO:0000250|UniProtKB:P22005}.; FUNCTION: [PENK(111-130)]: Increases glutamate release in the striatum and decreases GABA concentration in the striatum. {ECO:0000250|UniProtKB:P04094}.; FUNCTION: [PENK(233-254)]: Increases glutamate release in the striatum. {ECO:0000250|UniProtKB:P04094}.; FUNCTION: [Enkelytin]: Enkelytin possesses antibacterial activity against Gram-positive bacteria such as Micrococcus luteus and Bacillus megaterium. {ECO:0000269|PubMed:8654396}.
|
Bos taurus (Bovine)
|
P01213
|
PDYN_HUMAN
|
MAWQGLVLAACLLMFPSTTADCLSRCSLCAVKTQDGPKPINPLICSLQCQAALLPSEEWERCQSFLSFFTPSTLGLNDKEDLGSKSVGEGPYSELAKLSGSFLKELEKSKFLPSISTKENTLSKSLEEKLRGLSDGFREGAESELMRDAQLNDGAMETGTLYLAEEDPKEQVKRYGGFLRKYPKRSSEVAGEGDGDSMGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQEDPNAYSGELFDA
| null | null |
chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; sensory perception [GO:0007600]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; extracellular region [GO:0005576]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; plasma membrane [GO:0005886]
|
opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.; FUNCTION: Leumorphin has a typical opioid activity and may have anti-apoptotic effect. {ECO:0000250}.
|
Homo sapiens (Human)
|
P01214
|
PDYN_PIG
|
MAWQGLLLAACLLVLPSTMADCLSGCSLCAVKTQDGPKPINPLICSLECQAALQPAEEWERCQGLLSFLAPLSLGLEGKEDLESKAALEEPSSELVKYMGPFLKELEKNRFLLSTPAEETSLSRSLVEKLRSLPGRLGEETESELMGDAQQNDGAMEAAALDSSVEDPKEQVKRYGGFLRKYPKRSSEVAGEGDGDRDKVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQEDPNAYYEELFDV
| null | null |
chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; sensory perception [GO:0007600]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin.; FUNCTION: Leumorphin has a typical opioid activity and may have anti-apoptotic effect. {ECO:0000250}.
|
Sus scrofa (Pig)
|
P01215
|
GLHA_HUMAN
|
MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
| null | null |
follicle-stimulating hormone secretion [GO:0046884]; follicle-stimulating hormone signaling pathway [GO:0042699]; G protein-coupled receptor signaling pathway [GO:0007186]; hormone-mediated signaling pathway [GO:0009755]; luteinizing hormone secretion [GO:0032275]; negative regulation of organ growth [GO:0046621]; organ growth [GO:0035265]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of steroid biosynthetic process [GO:0010893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of signaling receptor activity [GO:0010469]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; follicle-stimulating hormone complex [GO:0016914]; Golgi lumen [GO:0005796]; pituitary gonadotropin complex [GO:0061696]
|
follicle-stimulating hormone activity [GO:0016913]; hormone activity [GO:0005179]
|
PF00236;
|
2.10.90.10;
|
Glycoprotein hormones subunit alpha family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:2494176}.
| null | null | null | null | null |
FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. {ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:2494176}.
|
Homo sapiens (Human)
|
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