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 |
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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}. Mit... | 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 reac... | 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 | MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISE... | 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; Ev... | 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|Pu... | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P00956 | SYI_ECOLI | MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILG... | 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|Pu... | 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 ... | Escherichia coli (strain K12) |
P00957 | SYA_ECOLI | MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRH... | 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 bindin... | 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:7... | 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;... | Escherichia coli (strain K12) |
P00958 | SYMC_YEAST | MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLY... | 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|P... | 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 AR... | 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 | MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSN... | 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 | MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQD... | 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|H... | null | null | null | null | null | Escherichia coli (strain K12) |
P00963 | ASNA_ECOLI | MKTAYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGCEKAVQVKVKALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDEDRLSPLHSVYVDQWDWERVMGDGERQFSTLKSTVEAIWAGIKATEAAVSEEFGLAPFLPDQIHFVHSQELLSRYPDLDAKGRERAIAKDLGAVFLVGIGGKLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWNPVLEDAFELSSMGIRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRLTMLLLQLPHIGQVQCGVWPA... | 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}; PhysiologicalD... | 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 | MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAEL... | 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:007124... | 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|PubMe... | 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:00... | 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: s... | 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 biosynth... | Homo sapiens (Human) |
P00967 | PUR2_DROME | MSHRVLVIGSGGREHAICWKLSQSPKVAQIYALPGSHGIQLVEKCRNLDAKTLDPKDFEAIAKWSKENQIALVVVGPEDPLALGLGDVLQSAGIPCFGPGKQGAQIEADKKWAKDFMLRHGIPTARYESFTDTEKAKAFIRSAPYPALVVKAAGLAAGKGVVVAANAKEACQAVDEILGDLKYGQAGATLVVEELLEGEEVSVLAFTDGKSVRAMLPAQDHKRLGNGDTGPNTGGMGAYCPCPLISQPALELVQKAVLERAVQGLIKERINYQGVLYAGLMLTRDGPRVLEFNCRFGDPETQVILPLLESDLFDVMEACC... | 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; Evid... | 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-phosp... | 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 | MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA... | 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 bios... | 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];... | 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... | 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:000... | 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... | Escherichia coli (strain K12) |
P00971 | RLIG_BPT4 | MQELFNNLMELCKDSQRKFFYSDDVSASGRTYRIFSYNYASYSDWLLPDALECRGIMFEMDGEKPVRIASRPMEKFFNLNENPFTMNIDLNDVDYILTKEDGSLVSTYLDGDEILFKSKGSIKSEQALMANGILMNINHHRLRDRLKELAEDGFTANFEFVAPTNRIVLAYQEMKIILLNVRENETGEYISYDDIYKDATLRPYLVERYEIDSPKWIEEAKNAENIEGYVAVMKDGSHFKIKSDWYVSLHSTKSSLDNPEKLFKTIIDGASDDLKAMYADDEYSYRKIEAFETTYLKYLDRALFLVLDCHNKHCGKDRKT... | 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 coordin... | 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 nucleot... | Enterobacteria phage T4 (Bacteriophage T4) |
P00973 | OAS1_HUMAN | MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLA... | 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 met... | 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 i... | 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:199234... | 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... | 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'-... | 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 | MRSLSGLLLLLTACLAVNASSVPTLPDDIQVQENFDLSRIYGKWFNVAVGSTCPWLKRFKEKMTMSTVVLIAGPTSKEISVTNTHRRKGVCESISGTYEKTSADGKFLYHKAKWNITMESYVVHTNYDEYAIFLTKKLSRRHGPTITVKLYGREPQLRESLLEEFREVALGVGIPEDAIFTMPDRGECVPGEQDPVPTPLSRARRAVLTQEEEGSGAGQPVTNFSKKADSCQLDYSQGPCLGLFKRYFYNGTSMACETFLYGGCMGNGNNFLSEKECLQTCRTVEACNLPIVQGPCRSYIQLWAFDAVKGKCVRFSYGGC... | 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 polycyc... | 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... | 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 regulato... | 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]... | 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 whe... | 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 | MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKP... | 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... | Homo sapiens (Human) |
P01009 | A1AT_HUMAN | MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGT... | 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 regi... | 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-... | 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 proteolyt... | Homo sapiens (Human) |
P01011 | AACT_HUMAN | MERMLPLLALGLLAAGFCPAVLCHPNSPLDEENLTQENQDRGTHVDLGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISR... | 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... | 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 | MGSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRFDKLPGFGDSIEAQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIVFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDVFSSSANLSGISSAE... | 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 ... | 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 | MTPTGAGLKATIFCILTWVSLTAGDRVYIHPFHLLYYSKSTCAQLENPSVETLPEPTFEPVPIQAKTSPVDEKTLRDKLVLATEKLEAEDRQRAAQVAMIANFMGFRMYKMLSEARGVASGAVLSPPALFGTLVSFYLGSLDPTASQLQVLLGVPVKEGDCTSRLDGHKVLTALQAVQGLLVTQGGSSSQTPLLQSTVVGLFTAPGLRLKQPFVESLGPFTPAIFPRSLDLSTDPVLAAQKINRFVQAVTGWKMNLPLEGVSTDSTLFFNTYVHFQGKMRGFSQLTGLHEFWVDNSTSVSVPMLSGTGNFQHWSDAQNNF... | 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 learnin... | 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 ... | 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... | Rattus norvegicus (Rat) |
P01019 | ANGT_HUMAN | MAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNF... | 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];... | 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: I... | 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 vasoc... | 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-pote... | Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi) |
P01023 | A2MG_HUMAN | MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKL... | 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:0051... | 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:00... | 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... | Homo sapiens (Human) |
P01024 | CO3_HUMAN | MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLV... | 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 synaps... | 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]; sec... | 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 C... | 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... | Homo sapiens (Human) |
P01025 | CO3_PIG | MGSTSGPRLLLLLLTSLPLALGDPIYTIITPNVLRLESEEMVVLEAHEGQGDIRVSVTVHDFPAKRQVLSSETTTLNNANNYLSTVNIKIPASKEFKSEKGHKFVTVQALFGNVQVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVDHKLLPVGQTIVVTIETPEGIDIKRDSLSSHNQFGILALSWNIPELVNMGQWKIRAHYEDAPQQVFSAEFEVKEYVLPSFEVQVEPSEKFYYIDDPNGLTVNIIARFLYGESVDGTAFVIFGVQDGDQRISLSQSLTRVPIIDGTGEATLSQGVLLNGVHYSSVNDLVG... | 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 signal... | 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 C... | 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 simila... | Sus scrofa (Pig) |
P01026 | CO3_RAT | MGPTSGSQLLVLLLLLASSLLALGSPMYSIITPNVLRLESEETFILEAHDAQGDVPVTVTVQDFLKKQVLTSEKTVLTGATGHLNRVFIKIPASKEFNADKGHKYVTVVANFGATVVEKAVLVSFQSGYLFIQTDKTIYTPGSTVFYRIFTVDNNLLPVGKTVVIVIETPDGVPIKRDILSSHNQYGILPLSWNIPELVNMGQWKIRAFYEHAPKQTFSAEFEVKEYVLPSFEVLVEPTEKFYYIHGPKGLEVSITARFLYGKNVDGTAFVIFGVQDEDKKISLALSLTRVLIEDGSGEAVLSRKVLMDGVRPSSPEALV... | 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]; c... | 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 C... | 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:0000... | Rattus norvegicus (Rat) |
P01027 | CO3_MOUSE | MGPASGSQLLVLLLLLASSPLALGIPMYSIITPNVLRLESEETIVLEAHDAQGDIPVTVTVQDFLKRQVLTSEKTVLTGASGHLRSVSIKIPASKEFNSDKEGHKYVTVVANFGETVVEKAVMVSFQSGYLFIQTDKTIYTPGSTVLYRIFTVDNNLLPVGKTVVILIETPDGIPVKRDILSSNNQHGILPLSWNIPELVNMGQWKIRAFYEHAPKQIFSAEFEVKEYVLPSFEVRVEPTETFYYIDDPNGLEVSIIAKFLYGKNVDGTAFVIFGVQDGDKKISLAHSLTRVVIEDGVGDAVLTRKVLMEGVRPSNADAL... | 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 synaps... | 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 C... | 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... | Mus musculus (Mouse) |
P01029 | CO4B_MOUSE | MRLLWGLAWVFSFCASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPPGQEVKGSVFLRNPKGGSCSPKKDFKLSSGDDFVLLSLEVPLEDVRSCGLFDLRRAPHIQLVAQSPWLRNTAFKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDFLTITVENSHGLRVLKKEIFTSTSIFQDAFTIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKITPWKPYILMVPSNSDEIQLDIQARYIYGKPVQGVAYTRFALMDEQGKRTFLRGLETQAKLVEGRTHISISKDQFQAA... | 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 ... | 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 transacy... | Mus musculus (Mouse) |
P01031 | CO5_HUMAN | MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNN... | 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 organi... | 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 fr... | 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 acti... | 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... | 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 MMP1... | 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 peptidas... | 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 g... | 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, ... | 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 | MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFID... | 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 i... | 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 relea... | 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... | Homo sapiens (Human) |
P01044 | KNG1_BOVIN | MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVF... | 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... | Bos taurus (Bovine) |
P01045 | KNG2_BOVIN | MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDTVKKATVQVVGGLKYSIVFIA... | 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 bra... | Bos taurus (Bovine) |
P01048 | KNT1_RAT | MKLITILLLCSRLLPSLAQEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEF... | 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 ... | 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 e... | 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 mitochondr... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P01100 | FOS_HUMAN | MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATEL... | 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-myristat... | 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:00... | 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 pro... | 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 dephosphoryl... | 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... | Homo sapiens (Human) |
P01101 | FOS_MOUSE | MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAGMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTEL... | 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:007... | 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:000... | 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 pro... | 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 nucle... | 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 regulati... | Mus musculus (Mouse) |
P01106 | MYC_HUMAN | MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTH... | 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 ... | 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-bindin... | 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 phosphoryla... | 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 a... | Homo sapiens (Human) |
P01108 | MYC_MOUSE | MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTH... | 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:00... | 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 ... | 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 dimerizati... | 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. Phosphory... | 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 reprogrammi... | Mus musculus (Mouse) |
P01109 | MYC_CHICK | MASLRLAAGALEEPAAAAAMPLSASLPSKNYDYDYDSVQPYFYFEEEEENFYLAAQQRGSELQPPAPSEDIWKKFELLPTPPLSPSRRSSLAAASCFPSTADQLEMVTELLGGDMVNQSFICDPDDESFVKSIIIQDCMWSGFSAAAKLEKVVSEKLATYQASRREGGPAAASRPGPPPSGPPPPPAGPAASAGLYLHDLGAAAADCIDPSVVFPYPLSERAPRAAPPGANPAALLGVDTPPTTSSDSEEEQEEDEEIDVVTLAEANESESSTESSTEASEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKR... | 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 ... | 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 ... | 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:00002... | 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:... | 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]; fibr... | 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 ... | 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:000025... | 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:902015... | 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]; ... | 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... | 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... | 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... | 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... | 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 | MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSILDILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVVVGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNKTLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKTGLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQAAPGGNTSEASKSGSGGCCI... | 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 transd... | 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:2... | 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 ... | 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];... | 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 str... | 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 directl... | 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... | 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]; platel... | 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 ... | 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 ... | Homo sapiens (Human) |
P01129 | CDC10_SCHPO | MASANFIRQFELGNDSFSYQKRPEDEPSQPLSNRNINKLNDSSTLKDSSSRIFINSQVLRDGRPVELYAVECSGMKYMELSCGDNVALRRCPDSYFNISQILRLAGTSSSENAKELDDIIESGDYENVDSKHPQIDGVWVPYDRAISIAKRYGVYEILQPLISFNLDLFPKFSKQQQIESSSISKNLNTSSFNTRSPLRNHNFSNPSKSSKNGVHTINNMQSSPSPSSSFLLPLTQIDSQNVKRSNNYLSTSPPILEQRLKRHRIDVSDEDLHPSSQLNDNEASSLFPDTPRLNHSLSFVSLVSSLPPLDQNIMQDYHTS... | 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 pol... | 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. ... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P01130 | LDLR_HUMAN | MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLD... | 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 [... | 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 membr... | 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]; molec... | 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}. Lat... | 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 increas... | Homo sapiens (Human) |
P01131 | LDLR_BOVIN | MRLAGWGLRWAIALLIAVGEAAVEDNCGRNEFQCQDGKCISYKWVCDGTAECQDGSDESQETCKSVTCKMGDFSCGGRVNRCISGSWRCDGQVDCENGSDEEGCSPKTCSQDEFRCNDGKCIAPKFVCDLDLDCLDGSDEASCPMPTCGPANFQCNSSMCIPQLWACDGDPDCDDGSDEWPKHCGTPHPSGPLQDNNPCSALEFHCGSGECIHSSWHCDHDPDCKDKSDEENCAVATCRPDEFQCSDGTCIHGSRQCDREPDCKDLSDELGCVNVTLCEGPNKFKCQSGECISLDKVCNSVRDCRDWSDEPLKDCGTNEC... | 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 pr... | 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 par... | 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 ... | 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: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|UniP... | 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 increas... | Bos taurus (Bovine) |
P01132 | EGF_MOUSE | MPWGRRPTWLLLAFLLVFLKISILSVTAWQTGNCQPGPLERSERSGTCAGPAPFLVFSQGKSISRIDPDGTNHQQLVVDAGISADMDIHYKKERLYWVDVERQVLLRVFLNGTGLEKVCNVERKVSGLAIDWIDDEVLWVDQQNGVITVTDMTGKNSRVLLSSLKHPSNIAVDPIERLMFWSSEVTGSLHRAHLKGVDVKTLLETGGISVLTLDVLDKRLFWVQDSGEGSHAYIHSCDYEGGSVRLIRHQARHSLSSMAFFGDRIFYSVLKSKAIWIANKHTGKDTVRINLHPSFVTPGKLMVVHPRAQPRTEDAAKDPD... | 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 ... | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; guanyl-nucleotide exchange factor activity [GO:0005085]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; Wnt receptor activ... | PF00008;PF07645;PF14670;PF00058; | 2.10.25.10;2.120.10.30; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By simil... | Mus musculus (Mouse) |
P01133 | EGF_HUMAN | MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKL... | 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 signa... | 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] | 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 activ... | PF00008;PF07645;PF14670;PF00058; | 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}. | 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 indu... | Homo sapiens (Human) |
P01134 | TGFA_RAT | 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:0... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | 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. | Rattus norvegicus (Rat) |
P01135 | TGFA_HUMAN | 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]... | 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 ... | 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. | Homo sapiens (Human) |
P01136 | VGF_VACCW | 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] | extracellular space [GO:0005615]; host cell membrane [GO:0033644]; membrane [GO:0016020] | 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 ... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P01137 | TGFB1_HUMAN | MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | 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:0060... | 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]... | 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:... | 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... | 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: [Lat... | 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]; ... | 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 ... | 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]; negat... | 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)... | 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 ap... | 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:0007... | 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:000026... | 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 secr... | 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]... | 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:... | 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}.; S... | 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, PubMe... | 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:00... | 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 th... | 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: [Kali... | 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 PRKG... | 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. A... | 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 pre... | 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... | 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... | 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 vasopre... | 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:18... | 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 fe... | 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 va... | 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];... | 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 ... | 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... | 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];... | 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 ... | 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 ... | 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];... | 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 ... | 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 ... | 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 ... | 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 ... | 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:007... | 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 [... | 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... | 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... | 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 perce... | 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 cl... | 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 ... | 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 ... | 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 ... | 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]; orga... | 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 sig... | Homo sapiens (Human) |
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