Detail Information for IndEnz0002006923
IED ID IndEnz0002006923
Enzyme Type ID protease006923
Protein Name 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
Gene Name F10
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 MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
Enzyme Length 488
Uniprot Accession Number P00742
Absorption
Active Site ACT_SITE 276; /note=Charge relay system; ACT_SITE 322; /note=Charge relay system; ACT_SITE 419; /note=Charge relay system
Activity Regulation ACTIVITY REGULATION: Inhibited by SERPINA5 and SERPINA10. {ECO:0000269|PubMed:20427285, ECO:0000269|PubMed:6323392}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
DNA Binding
EC Number 3.4.21.6
Enzyme Function FUNCTION: 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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (32); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (4); Helix (9); Modified residue (12); Natural variant (33); Propeptide (2); Region (2); Sequence conflict (3); Signal peptide (1); Turn (7)
Keywords 3D-structure;Blood coagulation;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disease variant;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen
Interact With P0DPK4; Q9UK55; Q9UHD9
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 56; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6871167"; MOD_RES 103; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000269|PubMed:6871167"
Post Translational Modification PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8243461}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (PubMed:8920993). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity). {ECO:0000250|UniProtKB:P00743, ECO:0000269|PubMed:8920993}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6871167}.
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000255
Structure 3D X-ray crystallography (153)
Cross Reference PDB 1C5M; 1EZQ; 1F0R; 1F0S; 1FAX; 1FJS; 1FXY; 1G2L; 1G2M; 1HCG; 1IOE; 1IQE; 1IQF; 1IQG; 1IQH; 1IQI; 1IQJ; 1IQK; 1IQL; 1IQM; 1IQN; 1KSN; 1LPG; 1LPK; 1LPZ; 1LQD; 1MQ5; 1MQ6; 1NFU; 1NFW; 1NFX; 1NFY; 1P0S; 1V3X; 1WU1; 1XKA; 1XKB; 1Z6E; 2BMG; 2BOH; 2BOK; 2BQ6; 2BQ7; 2BQW; 2CJI; 2D1J; 2EI6; 2EI7; 2EI8; 2FZZ; 2G00; 2GD4; 2H9E; 2J2U; 2J34; 2J38; 2J4I; 2J94; 2J95; 2JKH; 2P16; 2P3F; 2P3T; 2P3U; 2P93; 2P94; 2P95; 2PHB; 2PR3; 2Q1J; 2RA0; 2UWL; 2UWO; 2UWP; 2VH0; 2VH6; 2VVC; 2VVU; 2VVV; 2VWL; 2VWM; 2VWN; 2VWO; 2W26; 2W3I; 2W3K; 2WYG; 2WYJ; 2XBV; 2XBW; 2XBX; 2XBY; 2XC0; 2XC4; 2XC5; 2Y5F; 2Y5G; 2Y5H; 2Y7X; 2Y7Z; 2Y80; 2Y81; 2Y82; 3CEN; 3CS7; 3ENS; 3FFG; 3HPT; 3IIT; 3K9X; 3KL6; 3KQB; 3KQC; 3KQD; 3KQE; 3LIW; 3M36; 3M37; 3Q3K; 3SW2; 3TK5; 3TK6; 4A7I; 4BTI; 4BTT; 4BTU; 4Y6D; 4Y71; 4Y76; 4Y79; 4Y7A; 4Y7B; 4ZH8; 4ZHA; 5JQY; 5JTC; 5JZ8; 5JZU; 5K0H; 5VOE; 5VOF; 6Q9F; 6Q9I; 6RK9; 6YYW; 6YYX; 6YYY; 6Z6Q; 6Z6R; 7AHU; 7BMI; 7BMJ; 7E6J;
Mapped Pubmed ID 10068650; 10468875; 10779411; 10917896; 10966741; 11027132; 11252894; 11342132; 11513608; 11854268; 11864704; 11867437; 11914651; 11983337; 12011050; 12036878; 12039587; 12056907; 12061878; 12091341; 12123809; 12163491; 12220193; 12370181; 12379114; 12437104; 12501180; 12524437; 12529356; 12593649; 12805370; 12834348; 12941034; 1346975; 14532267; 14575696; 14579355; 14629468; 14640539; 14739327; 14750502; 14963035; 14979399; 14982929; 15009463; 15069066; 15326167; 15328360; 15347660; 15456260; 15494418; 15550696; 15567463; 15634274; 15641797; 15771420; 15857135; 15882255; 15892863; 15897196; 15911309; 15924438; 15952226; 15999990; 16042383; 16079143; 16105945; 16161994; 16169070; 16207719; 16212554; 16359518; 16517611; 16529937; 16580898; 16619025; 16697194; 16730984; 16839353; 16848746; 16894464; 16935856; 16940049; 16963264; 16982190; 16982192; 17020886; 17118432; 17173931; 17338508; 17343367; 17391309; 17403098; 17420122; 17469850; 17536795; 17553804; 17555959; 17581239; 17588602; 17588746; 17635109; 17646160; 17683371; 17726015; 17903294; 17914785; 17973648; 18000611; 18031796; 18053714; 18054228; 18062812; 18159923; 18174463; 18178242; 18198180; 18245654; 18267072; 18278195; 18296445; 18388497; 18391209; 18403394; 18419747; 18424044; 18502757; 18506702; 18550370; 18591887; 18612547; 18680100; 18765660; 18768472; 18784085; 18929857; 18974842; 18991406; 18998662; 19101972; 19108874; 19158249; 19172319; 19188667; 19190817; 19200624; 19231206; 19244162; 19250659; 19297154; 19350128; 19350129; 19404516; 19429866; 19541481; 19581306; 1958666; 19652365; 19691479; 19724895; 19843455; 19846852; 19851296; 19858193; 19895674; 19896847; 19900814; 19913121; 19931652; 20006499; 20062915; 20062929; 20088935; 20088937; 20100660; 20135059; 20140262; 20156644; 20198315; 20347121; 20355714; 20451919; 20454680; 20534818; 20589316; 20589317; 20628086; 20634491; 20650636; 20664909; 20694273; 20722419; 20730886; 20806114; 20806117; 20864578; 20886185; 20946166; 20949078; 20978714; 2105717; 21071689; 2110473; 21156843; 21252089; 21345673; 21349710; 21349711; 21596747; 21621824; 21637339; 21651559; 21673107; 21682820; 21778227; 21811937; 21840043; 21849463; 21871560; 21885613; 21947241; 22008904; 22041058; 22126652; 22160665; 22162109; 22190348; 22244010; 22409427; 22411993; 22424030; 2248955; 22627666; 2271516; 22796577; 22905983; 22931370; 22989889; 23019612; 2303434; 23214401; 23294934; 23416531; 23585459; 23658376; 23664564; 23677006; 23683607; 23754290; 23872307; 24041930; 24068708; 24117177; 24124146; 24158387; 24175584; 24226152; 24275667; 24449213; 24467409; 24554904; 24777000; 24821807; 25007770; 25064371; 25153592; 25163770; 25179519; 25399323; 25407022; 25572019; 25688138; 25743687; 25803519; 25855704; 26012870; 26023895; 26058941; 26083275; 26120939; 26175037; 26540129; 26607136; 26708756; 27031279; 27089317; 27264807; 27421960; 27774643; 27789475; 28213380; 28283478; 28692575; 28694557; 28717005; 28729433; 28801460; 28935233; 28983056; 29321328; 29452445; 29614522; 29863725; 30507709; 3052293; 31659163; 31699787; 31877279; 32029851; 32457455; 32599596; 32748957; 3275472; 32762584; 32859749; 33887099; 34077951; 34351069; 34995294; 3527261; 3965513; 6980899; 7803238; 8473289; 8530480; 8578528; 8639673; 8939944; 921929; 9427707; 9689066; 9707558;
Motif
Gene Encoded By
Mass 54,732
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.6;