entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
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P00494 | HPRT_CRIGR | Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) | MATRSPSVVISDDEPGYDLDLFCIPNHYVEDLEKVFIPHGVIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKRYNLKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHICVISETGKAKYKA | Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity). |
P00497 | PUR1_BACSU | Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPATase) | MLAEIKGLNEECGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLITEVFQNGELSKVKGKGAIGHVRYATAGGGGYENVQPLLFRSQNNGSLALAHNGNLVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSMLKGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGATYLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNIDGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLIKNRYV... | Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:6794613}. |
P00502 | GSTA1_RAT | Glutathione S-transferase alpha-1 (EC 2.5.1.18) (13-hydroperoxyoctadecadienoate peroxidase) (EC 1.11.1.-) (Androst-5-ene-3,17-dione isomerase) (EC 5.3.3.-) (GST 1-1) (GST 1a-1a) (GST A1-1) (GST B) (Glutathione S-transferase Ya-1) (GST Ya1) (Ligandin) | MSGKPVLHYFNARGRMECIRWLLAAAGVEFDEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYTEGILDLTEMIMQLVICPPDQKEAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLLYVEEFDASLLTSFPLLKAFKSRISSLPNVKKFLQPGSQRKLPVDAKQIEEARKIFKF | Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (Probable). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also cataly... |
P00503 | AATC_PIG | Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A) | MAPPSVFAEVPQAQPVLVFKLIADFREDPDPRKVNLGVGAYRTDDCQPWVLPVVRKVEQRIANDSSLNHEYLPILGLAEFRTCASRLALGDDSPALQEKRVGGVQSLGGTGALRIGAEFLARWYNGTNNKDTPVYVSSPTWENHNGVFTTAGFKDIRSYRYWDTEKRGLDLQGFLSDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIASVMKRRFLFPFFDSAYQGFASGNLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVAKEPDSILRVLSQMEKIVRVTWSNPPAQGARIVARTLSDPELFHEW... | Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthe... |
P00504 | AATC_CHICK | Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A) | MAASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWK... | Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthe... |
P00505 | AATM_HUMAN | Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membran... | MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPP... | Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolis... |
P00506 | AATM_PIG | Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membran... | MALLHSGRVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRYVTVQTISGTGALRIGANFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLHSYRYYDPKTCGFDFTGALEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATLVKKNNLFAFFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPMYSNPP... | Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolis... |
P00507 | AATM_RAT | Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membran... | MALLHSGRVLSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPP... | Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolis... |
P00508 | AATM_CHICK | Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Transaminase A) | MALLQSRLLLSAPRRAAATARASSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKSYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIA... | Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolis... |
P00511 | PFKAM_RABIT | ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase) | MTHEEHHAARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEA... | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}. |
P00512 | PFKA_GEOSE | ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) | MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:8136379}. |
P00514 | KAP0_BOVIN | cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed] | MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPS... | Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. |
P00515 | KAP2_BOVIN | cAMP-dependent protein kinase type II-alpha regulatory subunit | MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQ... | Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity). |
P00516 | KGP1_BOVIN | cGMP-dependent protein kinase 1 (cGK 1) (cGK1) (EC 2.7.11.12) (cGMP-dependent protein kinase I) (cGKI) | MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDS... | Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contrib... |
P00517 | KAPCA_BOVIN | cAMP-dependent protein kinase catalytic subunit alpha (PKA C-alpha) (EC 2.7.11.11) | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK... | Phosphorylates a large number of substrates in the cytoplasm and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (By similarity). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds ... |
P00518 | PHKG1_RABIT | Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1, EC 2.7.11.26) | MTRDAALPGSHSTHGFYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQKRYTAEEALAHPFFQQYVVEEVRHFSPRGKFKVICLTVLASVRIYY... | Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3. |
P00519 | ABL1_HUMAN | Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150) | MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY... | Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyros... |
P00520 | ABL1_MOUSE | Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150) | MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY... | Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyros... |
P00522 | ABL_DROME | Tyrosine-protein kinase Abl (EC 2.7.10.2) (D-ash) (Protein abelson) | MGAQQGKDRGAHSGGGGSGAPVSCIGLSSSPVASVSPHCISSSSGVSSAPLGGGSTLRGSRIKSSSSGVASGSGSGGGGGGSGSGLSQRSGGHKDARCNPTVGLNIFTEHNEALLQSRPLPHIPAGSTAASLLADAAELQQHQQDSGGLGLQGSSLGGGHSSTTSVFESAHRWTSKENLLAPGPEEDDPQLFVALYDFQAGGENQLSLKKGEQVRILSYNKSGEWCEAHSDSGNVGWVPSNYVTPLNSLEKHSWYHGPISRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRISEDPDGKVFVTQEAKFN... | Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues may regulate cytoskeletal dynamics underlying a growth c... |
P00523 | SRC_CHICK | Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src) | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signalin... |
P00524 | SRC_RSVSA | Tyrosine-protein kinase transforming protein Src (EC 2.7.10.2) (pp60v-src) (p60-Src) (v-Src) | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWIETDLSFKKGERLQIVNNTEGNWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. Causes mitotic slippage in addition to cytokinesis failure in the host cell. Phosphorylates and attenuates the activity of host CD... |
P00528 | SRC64_DROME | Tyrosine-protein kinase Src64B (Dsrc64) (EC 2.7.10.2) | MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMS... | May play a role in the development of neural tissue and smooth muscle. |
P00533 | EGFR_HUMAN | Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1) | MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE... | Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers r... |
P00545 | KFMS_FSVMD | Tyrosine-protein kinase transforming protein fms (EC 2.7.10.1) | RMPSGPGHYGASAETPGPRPPLCPASSCCLPTEAMGPRALLVLLMATAWHAQGVPVIQPSGPELVVEPGTTVTLRCVGNGSVEWDGPISPHWNLDLDPPSSILTTNNATFQNTGTYHCTEPGNPRGGNATIHLYVKDPARPWKVLAQEVTVLEGQDALLPCLLTDPALEAGVSLVRVRGRPVLRQTNYSFSPWHGFTIHKAKFIENHVYQCSARVDGRTVTSMGIWLKVQKDISGPATLTLEPAELVRIQGEAAQIVCSASNIDVNFDVSLRHGDTKLTISQQSDFHDNRYQKVLTLNLDHVSFQDAGNYSCTATNAWGN... | Truncated version of the receptor for colony-stimulating factor 1 (CSF-1). |
P00546 | CDK1_YEAST | Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 1) | MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREISLLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQLCKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAPEVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIVYLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES | Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). Required to drive the G1-S transition. More than 200 substrates have been identified. Substrate specificity is in part regulated by the bound cyclin protein (By similarity). Phosphorylates YTA7 during S-phase... |
P00550 | PTM3C_ECOLI | PTS system mannitol-specific EIICBA component (EIICBA-Mtl) (EII-Mtl) [Includes: Mannitol permease IIC component (PTS system mannitol-specific EIIC component); Mannitol-specific phosphotransferase enzyme IIB component (EC 2.7.1.197) (PTS system mannitol-specific EIIB component); Mannitol-specific phosphotransferase enzy... | MSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLLPLLIGYTGGKLVGGERGGVVGAITTMGVIVGADMPMFLGSMIAGPLGGWCIKHFDRWVDGKIKSGFEMLVNNFSAGIIGMILAILAFLGIGPIVEALSKMLAAGVNFMVVHDMLPLASIFVEPAKILFLNNAINHGIFSPLGIQQSHELGKSIFFLIEANPGPGMGVLLAYMFFGRGSAKQSAGGAAIIHFLGGIHEIYFPYVLMNPRLILAVILGGMTGVFTLTILGGGLVSPASPGSILAVLAMTPKGAYFANIAGVC... | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in D-mannitol transport. Also able to use D-man... |
P00558 | PGK1_HUMAN | Phosphoglycerate kinase 1 (EC 2.7.2.3) (Cell migration-inducing gene 10 protein) (Primer recognition protein 2) (PRP 2) | MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPES... | Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm... |
P00568 | KAD1_HUMAN | Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.10) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) | MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor. Also catalyzes at a ... |
P00569 | KAD1_RABIT | Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.10) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) | MEEKLKKAKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKADTSKGFLIDGYPRQVQQGEEFERRIAQPTLLLYVDAGPETMQKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By s... |
P00570 | KAD1_BOVIN | Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.10) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) | MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVQQGEEFERRIAQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By s... |
P00571 | KAD1_PIG | Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.10) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) | MEEKLKKSKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVKQGEEFERKIGQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDDVFSQVCTHLDTLK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also... |
P00572 | KTHY_YEAST | Thymidylate kinase (EC 2.7.4.9) (dTMP kinase) | MMGRGKLILIEGLDRTGKTTQCNILYKKLQPNCKLLKFPERSTRIGGLINEYLTDDSFQLSDQAIHLLFSANRWEIVDKIKKDLLEGKNIVMDRYVYSGVAYSAAKGTNGMDLDWCLQPDVGLLKPDLTLFLSTQDVDNNAEKSGFGDERYETVKFQEKVKQTFMKLLDKEIRKGDESITIVDVTNKGIQEVEALIWQIVEPVLSTHIDHDKFSFF | Catalyzes the conversion of dTMP to dTDP. |
P00573 | RPOL_BPT7 | T7 RNA polymerase (DNA-directed RNA polymerase) (EC 2.7.7.6) | MNTINIAKNDFSDIELAAIPFNTLADHYGERLAREQLALEHESYEMGEARFRKMFERQLKAGEVADNAAAKPLITTLLPKMIARINDWFEEVKAKRGKRPTAFQFLQEIKPEAVAYITIKTTLACLTSADNTTVQAVASAIGRAIEDEARFGRIRDLEAKHFKKNVEEQLNKRVGHVYKKAFMQVVEADMLSKGLLGGEAWSSWHKEDSIHVGVRCIEMLIESTGMVSLHRQNAGVVGQDSETIELAPEYAEAIATRAGALAGISPMFQPCVVPPKPWTGITGGGYWANGRRPLALVRTHSKKALMRYEDVYMPEVYKAI... | Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA... |
P00579 | RPOD_ECOLI | RNA polymerase sigma factor RpoD (Sigma-70) | MEQNPQSQLKLLVTRGKEQGYLTYAEVNDHLPEDIVDSDQIEDIIQMINDMGIQVMEEAPDADDLMLAENTADEDAAEAAAQVLSSVESEIGRTTDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYDRVEAEEARLSDLITGFVDPNAEEDLAPTATHVGSELSQEDLDDDEDEDEEDGDDDSADDDNSIDPELAREKFAELRAQYVVTRDTIKAKGRSHATAQEEILKLSEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNETSDTWFNAAI... | Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Preferentially transcribes genes associated with fast growth, such as ribosomal operons, other protein-synthesis... |
P00581 | DPOL_BPT7 | DNA-directed DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gene product 5) (Gp5) | MIVSDIEANALLESVTKFHCGVIYDYSTAEYVSYRPSDFGAYLDALEAEVARGGLIVFHNGHKYDVPALTKLAKLQLNREFHLPRENCIDTLVLSRLIHSNLKDTDMGLLRSGKLPGKRFGSHALEAWGYRLGEMKGEYKDDFKRMLEEQGEEYVDGMEWWNFNEEMMDYNVQDVVVTKALLEKLLSDKHYFPPEIDFTDVGYTTFWSESLEAVDIEHRAAWLLAKQERNGFPFDTKAIEELYVELAARRSELLRKLTETFGSWYQPKGGTEMFCHPRTGKPLPKYPRIKTPKVGGIFKKPKNKAQREGREPCELDTREY... | Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This inter... |
P00582 | DPO1_ECOLI | DNA polymerase I (POL I) (EC 2.7.7.7) | MVQIPQNPLILVDGSSYLYRAYHAFPPLTNSAGEPTGAMYGVLNMLRSLIMQYKPTHAAVVFDAKGKTFRDELFEHYKSHRPPMPDDLRAQIEPLHAMVKAMGLPLLAVSGVEADDVIGTLAREAEKAGRPVLISTGDKDMAQLVTPNITLINTMTNTILGPEEVVNKYGVPPELIIDFLALMGDSSDNIPGVPGVGEKTAQALLQGLGGLDTLYAEPEKIAGLSFRGAKTMAAKLEQNKEVAYLSYQLATIKTDVELELTCEQLEVQQPAAEELLGLFKKYEFKRWTADVEAGKWLQAKGAKPAAKPQETSVADEAPEV... | In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. |
P00586 | THTR_BOVIN | Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese) | MVHQVLYRALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATCRKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETWVSQGKGGKA | Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur. |
P00588 | DTX_CORBE | Diphtheria toxin (DT) (NAD(+)--diphthamide ADP-ribosyltransferase) (EC 2.4.2.36) [Cleaved into: Diphtheria toxin fragment A; Diphtheria toxin fragment B] | MLVRGYVVSRKLFASILIGALLGIGAPPSAHAGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQV... | Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elongation fa... |
P00590 | CUTI1_FUSVN | Cutinase 1 (EC 3.1.1.74) (Cutin hydrolase 1) | MKFFALTTLLAATASALPTSNPAQELEARQLGRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGSA | Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4). |
P00591 | LIPP_PIG | Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3) | SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTN... | Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. |
P00592 | PA21B_PIG | Phospholipase A2, major isoenzyme (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B) | MKFLVLAVLLTVGAAQEGISSRALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDELDRCCETHDNCYRDAKNLDSCKFLVDNPYTESYSYSCSNTEITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDTKKYC | Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phospha... |
P00593 | PA21B_BOVIN | Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B) | MRLLVLAALLTVGAGQAGLNSRALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNNEITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC | Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phospha... |
P00594 | PA21B_HORSE | Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B) [Cleaved into: Phospholipase A2 isoform 2] | ENGISPRAVWQFRSMIQCTIPNSKPYLEFNDYGCYCGLGGSGTPVDELDACCQVHDNCYTQAKELSSCRFLVDNPYTESYKFSCSGTEVTCSDKNNACEAFICNCDRNAAICFSKAPYNPENKNLDSKRKCA | Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phospha... |
P00596 | PA2A1_NAJKA | Acidic phospholipase A2 CM-II (CM 2) (svPLA2) (EC 3.1.1.4) (Acidic phospholipase A2 1) (NnkPLA-I) (Phosphatidylcholine 2-acylhydrolase) | MNPAHLLILAAVCVSPLGAFSNRPMPLNLYQFKNMIQCTVPNRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISRCWPYFKTYSYECSQGTLTCKGDNDACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)=37 nM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neurona... |
P00597 | PA2A2_NAJKA | Acidic phospholipase A2 2 (svPLA2) (EC 3.1.1.4) (CM-III) (NnkPLA-II) (Phosphatidylcholine 2-acylhydrolase) | MNPAHLLILAAVCVSSLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00598 | PA2A1_NAJAT | Acidic phospholipase A2 1 (svPLA2) (EC 3.1.1.4) (Muscarinic protein) (MP) (Phosphatidylcholine 2-acylhydrolase) | MTPAHLLILAAVCVSPLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl... |
P00608 | PA2B_NOTSC | Basic phospholipase A2 notexin (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | NLVQFSYLIQCANHGKRPTWHYMDYGCYCGAGGSGTPVDELDRCCKIHDDCYDEAGKKGCFPKMSAYDYYCGENGPYCRNIKKKCLRFVCDCDVEAAFCFAKAPYNNANWNIDTKKRCQ | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect). Also has direct nephrotoxicity in experimental mice a single subcutaneous dose (1.38 ug/kg) prod... |
P00611 | PA2A1_LATSE | Acidic phospholipase A2 1 (svPLA2) (EC 3.1.1.4) (GL5-1) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 isozyme I) | MYPAHLLVLLAVCVSLLGATAIPPLPLNLVQFSNLIQCVNKGSRASYHYADYGCYCGAGGSGTPVDELDRCCKIHDDCYGEAEKMGCYPKWTLYTYDCSTEEPNCSTKTGCQGFVCACDLEAAKCFARSPYNNKNYNIDTSKRCK | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00614 | PA2TA_OXYSC | Basic phospholipase A2 taipoxin alpha chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | NLLQFGFMIRCANRRSRPVWHYMDYGCYCGKGGSGTPVDDLDRCCQVHDECYGEAVRRFGCAPYWTLYSWKCYGKAPTCNTKTRCQRFVCRCDAKAAECFARSPYQNSNWNINTKARCR | Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentra... |
P00615 | PA2HB_OXYSC | Neutral phospholipase A2 homolog taipoxin beta chain 1 (svPLA2 homolog) | MHPAHLLVLLAVCVSLLGASDIPPLPLNLVQFGKMIECAIRNRRPALDFMNYGCYCGKGGSGTPVDDLDRCCQVHDECYAEAEKHGCYPSLTTYTWECRQVGPYCNSKTQCEVFVCACDFAAAKCFAQEDYNPAHSNINTGERCK | Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentra... |
P00616 | PA2HG_OXYSC | Acidic phospholipase A2 homolog taipoxin gamma chain (svPLA2 homolog) | MHPAHLLVLLAVCVSLLGSSEIPQPSLDFEQFSNMIQCTIPCGESCLAYMDYGCYCGPGGSGTPIDDLDRCCKTHDECYAEAGKLSACKSVLSEPNNDTYSYECNEGQLTCNDDNDECKAFICNCDRTAVTCFAGAPYNDLNYNIGMIEHCK | Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentra... |
P00617 | PA2B1_BUNMU | Basic phospholipase A2 beta-bungarotoxin A1 chain (Beta-BuTX A1 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MNPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCGRIVCDCDRTAALCFGNSEYIEGHKNIDTARFCQ | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00618 | PA2B2_BUNMU | Basic phospholipase A2 beta-bungarotoxin A2 chain (Beta-BuTX A2 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MLIFLWCGAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALCFGNSEYIERHKNIDTKRHCR | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00619 | PA2A3_BUNMU | Acidic phospholipase A2 beta-bungarotoxin A3 chain (Beta-BuTX A3 chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MYPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYTNYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAANIRDCNPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGDSEYIEGHKNIDTARFCQ | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00624 | PA2A_CROAT | Acidic phospholipase A2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MRTLWIVAVLLLGVEGSLVQFETLIMKIAGRSGLLWYSAYGCYCGWGGHGLPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIICGGDDPCGTQICECDKAAAICFRDNIPSYDNKYWLFPPKNCREEPEPC | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00625 | PA2A1_OVOOK | Acidic phospholipase A2 DE-I (svPA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 Ook-E6) (Phospholipase A2 PLA2-01) | MRTLWIMAVLLLGVEGHLMQFETLIMKIAGRSGVWWYGSYGCYCGAGGQGRPQDPSDRCCFVHDCCYGKVTGCNTKDEFYTYSEENGAITCGGENPCLKEVCECDLAAAICFRDNLDTYNSKKYWMFPAKNCLEESEPC | Snake venom phospholipase A2 (PLA2) that inhibits the ADP- and collagen-induced human platelet aggregation (By similarity). Exhibits high hydrolytic activities and preferred the anionic micelles to the zwitterionic micelles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.... |
P00626 | PA2BA_VIPAA | Basic phospholipase A2 ammodytoxin A (AtxA) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) | MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDFLCKKESEKC | Snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transient inhibi... |
P00627 | PA2B6_BUNFA | Basic phospholipase A2 6 (svPLA2) (EC 3.1.1.4) (KBf VI) (KBf-6) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 isozyme VI) (Toxin VI) | AVCVSLLGAANIPPQSLNLYQFKNMIECAGTRTWLAYVKYGCYCGPGGTGTPLDELDRCCQTHDHCYDNAKKFGNCIPYLKTYVYTCNKPDITCTGAKGSCGRNVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Very weakly suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar n... |
P00628 | PA2BV_BUNFA | Basic phospholipase A2 KBf-VA (KBf Va) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Toxin V-2) | AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKSYEYTCNKPDLTCTDAKGSCARNVCDCDRAAAICFAAAPYNLANFGINKETHCQ | Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00629 | PA2B3_BUNFA | Basic phospholipase A2 Vb-2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Toxin V-3) | AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKTYEYTCNKPDITCTDAKGSCGRTVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ | Snake venom phospholipase A2 (PLA2) that has only a weak enzymatic activity. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00630 | PA2_APIME | Phospholipase A2 (bvPLA2) (EC 3.1.1.4) (Allergen Api m I) (Phosphatidylcholine 2-acylhydrolase) (allergen Api m 1) | MQVVLGSLFLLLLSTSHGWQIRDRIGDNELEERIIYPGTLWCGHGNKSSGPNELGRFKHTDACCRTHDMCPDVMSAGESKHGLTNTASHTRLSCDCDDKFYDCLKNSADTISSYFVGKMYFNLIDTKCYKLEHPVTGCGERTEGRCLHYTVDKSKPKVYQWFDLRKY | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
P00635 | PPA5_YEAST | Repressible acid phosphatase (EC 3.1.3.2) (P60) | MFKSVVYSILAASLANAGTIPLGKLADVDKIGTQKDIFPFLGGAGPYYSFPGDYGISRDLPEGCEMKQLQMVGRHGERYPTVSLAKTIKSTWYKLSNYTRQFNGSLSFLNDDYEFFIRDDDDLEMETTFANSDDVLNPYTGEMNAKRHARDFLAQYGYMVENQTSFAVFTSNSKRCHDTAQYFIDGLGDQFNITLQTVSEAESAGANTLSACNSCPAWDYDANDDIVNEYDTTYLDDIAKRLNKENKGLNLTSTDASTLFSWCAFEVNAKGYSDVCDIFTKDELVHYSYYQDLHTYYHEGPGYDIIKSVGSNLFNASVKL... | Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2. |
P00636 | F16P1_PIG | Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase) | MTDQAAFDTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILG... | Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Import... |
P00637 | F16P1_RABIT | Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase) | MADKAPFDTDISTMTRFVMEEGRKAGGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSTKDALQPGRNLVAAGYALYGSATMLVLAGGSGVNSFMLDPAIGEFILVDKNVKIKKKGNIYSLNEGYAKDFDPAVTEYIQKKKFPPDNSSPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPDGKLRLLYECNPMAFIMEKAGGMATTGKEAILDIVPTDIHQRAPVILG... | Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Import... |
P00639 | DNAS1_BOVIN | Deoxyribonuclease-1 (EC 3.1.21.1) (Deoxyribonuclease I) (DNase I) | MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT | Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs. Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin poly... |
P00642 | T2E1_ECOLX | Type II restriction enzyme EcoRI (R.EcoRI) (EC 3.1.21.4) (Endonuclease EcoRI) (Type-2 restriction enzyme EcoRI) | MSNKKQSNRLTEQHKLSQGVIGIFGDYAKAHDLAVGEVSKLVKKALSNEYPQLSFRYRDSIKKTEINEALKKIDPDLGGTLFVSNSSIKPDGGIVEVKDDYGEWRVVLVAEAKHQGKDIINIRNGLLVGKRGDQDLMAAGNAIERSHKNISEIANFMLSESHFPYVLFLEGSNFLTENISITRPDGRVVNLEYNSGILNRLDRLTAANYGMPINSNLCINKFVNHKDKSIMLQAASIYTQGDGREWDSKIMFEIMFDISTTSLRVLGRDLFEQLTSK | A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GAATTC-3' and cleaves after G-1. |
P00644 | NUC_STAAU | Thermonuclease (TNase) (EC 3.1.31.1) (Micrococcal nuclease) (Staphylococcal nuclease) [Cleaved into: Nuclease B; Nuclease A] | MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ | Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. |
P00655 | RNAS_ASPGI | Ribonuclease alpha-sarcin (EC 4.6.1.23) (rRNA endonuclease) | MVAIKNLVLVALTAVTALAVPSPLEARAVTWTCLNDQKNPKTNKYETKRLLYNQNKAESNSHHAPLSDGKTGSSYPHWFTNGYDGDGKLPKGRTPIKFGKSDCDRPPKHSKDGNGKTDHYLLEFPTFPDGHDYKFDSKKPKENPGPARVIYTYPNKVFCGIIAHTKENQGELKLCSH | Alpha-sarcin is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes (By similarity). Inhibits both the EFl (elongation factor 1)-dependent binding of aminoacyl-tRNA and the GTP-depend... |
P00657 | RNAS1_BUBBU | Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) | KETAAAKFQRQHMDSSTSSASSSNYCNQMMKSRNMTSDRCKPVNTFVHESLADVQAVCSQENVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHYDASV | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). |
P00659 | RNAS1_DAMKO | Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) | KESAAAKFZRZHMBSSTSSASSSBYCBZMMKSRNLTQDRCKPVBTFVHZSLABVZAVCSZKBVACKBGZTBCYZSYSTMSITBCRZTGSSKYPBCAYKTTQAKKHIIVACZGBPYVPVHFBASV | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). |
P00669 | RNS_BOVIN | Seminal ribonuclease (S-RNase) (Seminal RNase) (EC 4.6.1.18) (Ribonuclease BS-1) | MALKSLVVLPLLVLVLLLVRVQPSLGKESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV | This enzyme hydrolyzes both single- and double-stranded RNA. |
P00671 | RNAS1_PIG | Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) | KESPAKKFQRQHMDPDSSSSNSSNYCNLMMSRRNMTQGRCKPVNTFVHESLADVQAVCSQINVNCKNGQTNCYQSNSTMHITDCRQTGSSKYPNCAYKASQEQKHIIVACEGNPPVPVHFDASV | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). |
P00683 | RNAS1_MOUSE | Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) | MGLEKSLILFPLFFLLLGWVQPSLGRESAAQKFQRQHMDPDGSSINSPTYCNQMMKRRDMTNGSCKPVNTFVHEPLADVQAVCSQENVTCKNRKSNCYKSSSALHITDCHLKGNSKYPNCDYKTTQYQKHIIVACEGNPYVPVHFDATV | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). |
P00684 | RNS1B_RAT | Ribonuclease pancreatic beta-type (EC 4.6.1.18) (RL1) (RNase 1 gamma) (RNase A) | MGLEKSLFLFSLLVLVLGWVQPSLGGESRESSADKFKRQHMDTEGPSKSSPTYCNQMMKRQGMTKGSCKPVNTFVHEPLEDVQAICSQGQVTCKNGRNNCHKSSSTLRITDCRLKGSSKYPNCDYTTTDSQKHIIIACDGNPYVPVHFDASV | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). |
P00693 | AMY1_HORVU | Alpha-amylase type A isozyme (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (HvAMY1) (Low pI alpha-amylase) | MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAATFVDNHDTGSTQ... | Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin. |
P00697 | LYSC1_RAT | Lysozyme C-1 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) | MKALLVLGFLLLSASVQAKIYERCQFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSRYWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSGYIRNCGV | Lysozymes have primarily a bacteriolytic function those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. In the intestine they may also have a digestive function. |
P00698 | LYSC_CHICK | Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Allergen Gal d IV) (allergen Gal d 4) | MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL | Lysozymes have primarily a bacteriolytic function those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:22044478}. |
P00701 | LYSC_COTJA | Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) | MRSLLVLVLCFLPLAALGKVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNAWIRGCRL | Lysozymes have primarily a bacteriolytic function those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. |
P00702 | LYSC_PHACO | Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) | MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL | Lysozymes have primarily a bacteriolytic function those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. |
P00703 | LYSC_MELGA | Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) | MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL | Lysozymes have primarily a bacteriolytic function those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. |
P00709 | LALBA_HUMAN | Alpha-lactalbumin (Lactose synthase B protein) (Lysozyme-like protein 7) | MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose o... |
P00711 | LALBA_BOVIN | Alpha-lactalbumin (Lactose synthase B protein) (allergen Bos d 4) | MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose o... |
P00712 | LALBA_CAPHI | Alpha-lactalbumin (Lactose synthase B protein) | MMSFVSLLLVGILFHATQAEQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLCEKL | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose o... |
P00713 | LALBA_CAVPO | Alpha-lactalbumin (Lactose synthase B protein) | MMSFFPLLLVGILFPAVQAKQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose o... |
P00714 | LALBA_RAT | Alpha-lactalbumin (Lactose synthase B protein) | MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose o... |
P00720 | ENLYS_BPT4 | Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) | MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL | Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplas... |
P00727 | AMPL_BOVIN | Cytosol aminopeptidase (EC 3.4.11.1) (Cysteinylglycine-S-conjugate dipeptidase) (EC 3.4.13.23) (Leucine aminopeptidase 3) (LAP-3) (Leucyl aminopeptidase) (LAP) (Peptidase S) (Proline aminopeptidase) (EC 3.4.11.5) (Prolyl aminopeptidase) | MFLLPLPAAARVAVRHLSVKRLWAPGPAAADMTKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAA... | Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the prese... |
P00729 | CBPY_YEAST | Carboxypeptidase Y (CPD-Y) (cpY) (EC 3.4.16.5) (Carboxypeptidase YSCY) | MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSA... | Vacuolar serine-type carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. Also plays a role in breakdown of the autophagic body and th... |
P00730 | CBPA1_BOVIN | Carboxypeptidase A1 (EC 3.4.17.1) | MQGLLILSVLLGAALGKEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSRARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTT... | Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond. |
P00733 | CBPM_STRAL | Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14) (D-alanyl-D-alanine carboxypeptidase) (Metallo DD-peptidase) (Zn DD-peptidase) | MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI | This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to ... |
P00734 | THRB_HUMAN | Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] | MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEY... | Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. |
P00735 | THRB_BOVIN | Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] | MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSE... | Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). |
P00736 | C1R_HUMAN | Complement C1r subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r) [Cleaved into: Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain] | MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTI... | C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. |
P00738 | HPT_HUMAN | Haptoglobin (Zonulin) [Cleaved into: Haptoglobin alpha chain; Haptoglobin beta chain] | MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPE... | As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a ro... |
P00739 | HPTR_HUMAN | Haptoglobin-related protein | MSDLGAVISLLLWGRQLFALYSGNDVTDISDDRFPKPPEIANGYVEHLFRYQCKNYYRLRTEGDGVYTLNDKKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQVDIGLIKLKQKVLVNERVMPICLPSKNYAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGSTCPKWKAPKSPVGVQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDLEEDTWYAAGILSFD... | Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribut... |
P00740 | FA9_HUMAN | Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain] | MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLE... | Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. |
P00741 | FA9_BOVIN | Coagulation factor IX (EC 3.4.21.22) (Christmas factor) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain] | MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALL... | Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. |
P00742 | FA10_HUMAN | Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain] | MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYD... | Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. |
P00743 | FA10_BOVIN | Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain] | MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDF... | Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. |
P00745 | PROC_BOVIN | Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide] | XTSLLLFVTIWGISSTPAPPDSVFSSSQRAHQVLRIRKRANSFLEELRPGNVERECSEEVCEFEEAREIFQNTEDTMAFWSFYSDGDQCEDRPSGSPCDLPCCGRGKCIDGLGGFRCDCAEGWEGRFCLHEVRFSNCSAENGGCAHYCMEEEGRRHCSCAPGYRLEDDHQLCVSKVTFPCGRLGKRMEKKRKTLKRDTNQVDQKDQLDPRIVDGQEAGWGESPWQAVLLDSKKKLVCGAVLIHVSWVLTVAHCLDSRKKLIVRLGEYDMRRWESWEVDLDIKEVIIHPNYTKSTSDNDIALLRLAKPATLSQTIVPICLP... | Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. |
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