| 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; |