Detail Information for IndEnz0002001487
IED ID IndEnz0002001487
Enzyme Type ID protease001487
Protein Name 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
Gene Name Proc
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MWQFRVFLLLMSTWGISSIPAHPDPVFSSSEHAHQVLRVRRANSFLEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYFDGDQCSAPPLDHQCDSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQQELRFQDCRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRCKSTVNFPCGKLGRWIEKKRKILKRDTDLEDELEPDPRIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGLAQELTQAGQETVVTGWGYQSDRIKDGRRNRTFILTFIRIPLVARNECVEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHSYIGEKGVSLKSQKL
Enzyme Length 460
Uniprot Accession Number P33587
Absorption
Active Site ACT_SITE 253; /note=Charge relay system; ACT_SITE 299; /note=Charge relay system; ACT_SITE 401; /note=Charge relay system
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Degradation of blood coagulation factors Va and VIIIa.; EC=3.4.21.69;
DNA Binding
EC Number 3.4.21.69
Enzyme Function FUNCTION: 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. {ECO:0000250|UniProtKB:P04070}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (3); Disulfide bond (12); Domain (4); Glycosylation (3); Modified residue (11); Natural variant (2); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords Blood coagulation;Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Endoplasmic reticulum;Gamma-carboxyglutamic acid;Glycoprotein;Golgi apparatus;Hemostasis;Hydrolase;Hydroxylation;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}. Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04070}.
Modified Residue MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 48; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 55; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 57; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 67; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 70; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 76; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00745, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 112; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000250"
Post Translational Modification PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10691853; 10749569; 11154109; 11159184; 12466851; 12558604; 12579195; 12609841; 14645112; 14980205; 15466407; 15902301; 16014564; 16602821; 17047151; 17540840; 17872949; 18647222; 18799693; 19036061; 19188668; 19333141; 19350118; 19363121; 20348393; 20442369; 20858853; 21251201; 21267068; 21330465; 21420234; 22109555; 22167755; 22372856; 22447930; 23216621; 23267072; 23348224; 23550037; 24177324; 24753100; 26045607; 26069236; 26341257; 26457757; 27295971; 28302625; 28468828; 28687614; 28827518; 29343482; 30305662; 30865333; 8707309; 8798383; 9611252; 9616155; 9788960;
Motif
Gene Encoded By
Mass 51,818
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.69;