Detail Information for IndEnz0002003019
IED ID IndEnz0002003019
Enzyme Type ID protease003019
Protein Name Coagulation factor V
Activated protein C cofactor
Proaccelerin, labile factor

Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain
Gene Name F5
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MFPGCPRLWVLVVLGTSWVGWGSQGTEAAQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFDKQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNCPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSDVDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDDDEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIRSFRNSSLNQEEEEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGSPLRHLIGKNSVLNSSTAEHSSPYSEDPIEDPLQPDVTGIRLLSLGAGEFKSQEHAKHKGPKVERDQAAKHRFSWMKLLAHKVGRHLSQDTGSPSGMRPWEDLPSQDTGSPSRMRPWKDPPSDLLLLKQSNSSKILVGRWHLASEKGSYEIIQDTDEDTAVNNWLISPQNASRAWGESTPLANKPGKQSGHPKFPRVRHKSLQVRQDGGKSRLKKSQFLIKTRKKKKEKHTHHAPLSPRTFHPLRSEAYNTFSERRLKHSLVLHKSNETSLPTDLNQTLPSMDFGWIASLPDHNQNSSNDTGQASCPPGLYQTVPPEEHYQTFPIQDPDQMHSTSDPSHRSSSPELSEMLEYDRSHKSFPTDISQMSPSSEHEVWQTVISPDLSQVTLSPELSQTNLSPDLSHTTLSPELIQRNLSPALGQMPISPDLSHTTLSPDLSHTTLSLDLSQTNLSPELSQTNLSPALGQMPLSPDLSHTTLSLDFSQTNLSPELSHMTLSPELSQTNLSPALGQMPISPDLSHTTLSLDFSQTNLSPELSQTNLSPALGQMPLSPDPSHTTLSLDLSQTNLSPELSQTNLSPDLSEMPLFADLSQIPLTPDLDQMTLSPDLGETDLSPNFGQMSLSPDLSQVTLSPDISDTTLLPDLSQISPPPDLDQIFYPSESSQSLLLQEFNESFPYPDLGQMPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPKEEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPMDMREFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRDCRMPMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAWSVEKLAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFKGNSTRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCSTPLGMENGKIENKQITASSFKKSWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSEMYVKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGCDIY
Enzyme Length 2224
Uniprot Accession Number P12259
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:2844223, ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:9556620}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (11); Chain (3); Compositional bias (2); Disulfide bond (7); Domain (11); Erroneous gene model prediction (1); Glycosylation (26); Helix (2); Metal binding (4); Modified residue (9); Natural variant (35); Propeptide (1); Region (9); Repeat (37); Sequence conflict (5); Signal peptide (1); Site (7); Turn (2)
Keywords 3D-structure;Blood coagulation;Calcium;Copper;Disease variant;Disulfide bond;Glycoprotein;Hemostasis;Metal-binding;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Sulfation;Thrombophilia;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue MOD_RES 640; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19690332; MOD_RES 693; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 724; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 726; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 859; /note=Phosphoserine; by FAM20C; /evidence=ECO:0000269|PubMed:26091039; MOD_RES 1522; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1538; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1543; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1593; /note=Sulfotyrosine; /evidence=ECO:0000255
Post Translational Modification PTM: Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).; PTM: Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. {ECO:0000269|PubMed:2168225, ECO:0000269|PubMed:7989361, ECO:0000269|PubMed:8204629}.; PTM: Activated protein C inactivates factor V and factor Va by proteolytic degradation. {ECO:0000269|PubMed:7989361}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
Signal Peptide SIGNAL 1..28
Structure 3D Electron microscopy (3); X-ray crystallography (6)
Cross Reference PDB 1CZS; 1CZT; 1CZV; 3P6Z; 3P70; 3S9C; 7KVE; 7KVF; 7KXY;
Mapped Pubmed ID 10383194; 10679020; 10747087; 10825291; 10903204; 10982397; 10993493; 11014961; 11022077; 11035026; 11056246; 11057877; 11057878; 11071624; 11084577; 11085290; 11091190; 11093465; 11095555; 11108898; 11108900; 11114134; 11115343; 11122096; 11122102; 11122103; 11127850; 11127862; 11128675; 11146461; 11151062; 11156651; 11183183; 11187029; 11197244; 11229520; 11242801; 11246546; 11259157; 11260012; 11279932; 11285137; 11305729; 11306556; 11307836; 11311153; 11315119; 11320983; 11321143; 11323021; 11331645; 11334615; 11341494; 11341749; 11346337; 11372667; 11372668; 11374681; 11385320; 11397354; 11406725; 11426488; 11434083; 11435632; 11454529; 11460958; 11471205; 11472046; 11502996; 11506076; 11522037; 11522740; 11523408; 11529632; 11529695; 11532625; 11568114; 11578716; 11583312; 11595479; 11595480; 11596779; 11683190; 11684865; 11685046; 11694407; 11697722; 11718065; 11726323; 11734663; 11734673; 11738073; 11738388; 11739968; 11741359; 11748101; 11761087; 11776127; 11776341; 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Motif
Gene Encoded By
Mass 251,703
Kinetics
Metal Binding METAL 139; /note=Calcium; /evidence=ECO:0000250; METAL 140; /note=Calcium; /evidence=ECO:0000250; METAL 1843; /note=Copper; /evidence=ECO:0000250; METAL 1845; /note=Copper; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda