| IED ID |
IndEnz0002001424 |
| Enzyme Type ID |
protease001424 |
| Protein Name |
Vitamin K-dependent protein Z
|
| Gene Name |
PROZ |
| Organism |
Bos taurus (Bovine) |
| 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
Laurasiatheria
Artiodactyla
Ruminantia
Pecora
Bovidae
Bovinae
Bos (oxen
cattle)
Bos taurus (Bovine)
|
| Enzyme Sequence |
AGSYLLEELFEGHLEKECWEEICVYEEAREVFEDDETTDEFWRTYMGGSPCASQPCLNNGSCQDSIRGYACTCAPGYEGPNCAFAESECHPLRLDGCQHFCYPGPESYTCSCARGHKLGQDRRSCLPHDRCACGTLGPECCQRPQGSQQNLLPFPWQVKLTNSEGKDFCGGVLIQDNFVLTTATCSLLYANISVKTRSHFRLHVRGVHVHTRFEADTGHNDVALLDLARPVRCPDAGRPVCTADADFADSVLLPQPGVLGGWTLRGREMVPLRLRVTHVEPAECGRALNATVTTRTSCERGAAAGAARWVAGGAVVREHRGAWFLTGLLGAAPPEGPGPLLLIKVPRYALWLRQVTQQPSRASPRGDRGQGRDGEPVPGDRGGRWAPTALPPGPLV |
| Enzyme Length |
396 |
| Uniprot Accession Number |
P00744 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids (By similarity). Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. {ECO:0000250}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Disulfide bond (9); Domain (4); Glycosylation (5); Modified residue (14); Region (1) |
| Keywords |
Blood coagulation;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydroxylation;Reference proteome;Repeat;Secreted;Serine protease homolog |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Secreted. |
| Modified Residue |
MOD_RES 7; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 8; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 11; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 15; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 17; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 20; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 21; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 26; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 27; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 30; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 33; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 36; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 40; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3888670"; MOD_RES 64; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000269|PubMed:3888670" |
| Post Translational Modification |
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:3888670}. |
| Signal Peptide |
|
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
|
| Gene Encoded By |
|
| Mass |
43,113 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|