Detail Information for IndEnz0002010270
IED ID IndEnz0002010270
Enzyme Type ID protease010270
Protein Name Vitamin K-dependent protein S
Gene Name PROS1 PROS
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 MRVLGGRCGALLACLLLVLPVSEANFLSKQQASQVLVRKRRANSLLEETKQGNLERECIEELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQCSPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPGSYHCSCKNGFVMLSNKKDCKDVDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKSCEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKSCEVVSVCLPLNLDTKYELLYLAEQFAGVVLYLKFRLPEISRFSAEFDFRTYDSEGVILYAESIDHSAWLLIALRGGKIEVQLKNEHTSKITTGGDVINNGLWNMVSVEELEHSISIKIAKEAVMDINKPGPLFKPENGLLETKVYFAGFPRKVESELIKPINPRLDGCIRSWNLMKQGASGIKEIIQEKQNKHCLVTVEKGSYYPGSGIAQFHIDYNNVSSAEGWHVNVTLNIRPSTGTGVMLALVSGNNTVPFAVSLVDSTSEKSQDILLSVENTVIYRIQALSLCSDQQSHLEFRVNRNNLELSTPLKIETISHEDLQRQLAVLDKAMKAKVATYLGGLPDVPFSATPVNAFYNGCMEVNINGVQLDLDEAISKHNDIRAHSCPSVWKKTKNS
Enzyme Length 676
Uniprot Accession Number P07225
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Disulfide bond (15); Domain (7); Erroneous gene model prediction (1); Glycosylation (3); Helix (1); Modified residue (12); Mutagenesis (2); Natural variant (99); Propeptide (1); Region (1); Sequence conflict (2); Signal peptide (1); Site (1); Turn (1)
Keywords 3D-structure;Blood coagulation;Calcium;Cleavage on pair of basic residues;Disease variant;Disulfide bond;EGF-like domain;Fibrinolysis;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydroxylation;Reference proteome;Repeat;Secreted;Signal;Thrombophilia;Zymogen
Interact With Q5SUL5; Q92993; Q8TAP4-4; Q96CV9; P62937-2; P17252; Q15047-2; P61981
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 48; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 55; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 57; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 67; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 70; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 73; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 77; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2820795"; MOD_RES 136; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000250"
Post Translational Modification 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..24
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 1Z6C;
Mapped Pubmed ID 10026158; 10068650; 10917896; 11252894; 11467946; 11513608; 11686322; 11843280; 11848449; 12193728; 12193972; 12413608; 12447359; 12490286; 12871408; 12907438; 14515184; 14652633; 15096498; 15175796; 15292065; 15456488; 15670064; 15893367; 16100035; 16105054; 16229836; 16363235; 16461766; 16488980; 16493484; 16607073; 16672217; 16720551; 16737840; 16840717; 16868938; 16885060; 16935856; 16961607; 16961608; 16969634; 17064312; 17157360; 17393035; 17442946; 17597997; 17849042; 17890957; 17938802; 17958742; 18045239; 18250462; 18278202; 18419747; 18424440; 18433462; 18435454; 18485091; 18680534; 18768782; 18779332; 18784085; 18824642; 18841302; 18922854; 18945960; 18954896; 19004141; 19128822; 19244162; 19404554; 19437370; 19466456; 19492164; 19630792; 19744001; 19815836; 19874463; 19878975; 19924026; 20002538; 20022358; 20088940; 20200160; 20308596; 20348395; 20378562; 20398916; 20452482; 20492471; 20514628; 20539904; 20673868; 20693287; 20705334; 20711500; 20811787; 20880255; 20881312; 20926118; 2110473; 21172841; 21190511; 21486865; 21508412; 21569220; 21811774; 21979881; 21988832; 22104477; 22261441; 22273984; 22318644; 22371115; 22627591; 22627709; 22908226; 23065156; 23074276; 23238804; 23300094; 23370801; 23407778; 23473639; 23497733; 23580615; 23640497; 23721692; 23789915; 23813890; 23892573; 24014240; 24226152; 24233490; 24331211; 24740810; 24992033; 2538457; 25399514; 25716664; 25868595; 25879167; 25997409; 26186226; 26354831; 26358807; 26466767; 27172994; 27181595; 27207541; 27342144; 27345772; 27748013; 27840905; 27846449; 28118606; 28174134; 28211163; 28214760; 28284075; 28374852; 28607330; 29304470; 29321366; 29419409; 29455618; 29511111; 29748776; 29883906; 30630120; 30669159; 31364267; 31511453; 31743498; 32145080; 32276277; 32426810; 32653888; 32945517; 33402927; 33812436; 34001977; 34254783; 34533296; 6454142; 6457647; 7499257; 7579448; 8144529; 8467233; 8473289; 8530480;
Motif
Gene Encoded By
Mass 75,123
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda