| IED ID |
IndEnz0002006612 |
| Enzyme Type ID |
protease006612 |
| Protein Name |
Vitamin K-dependent protein Z
|
| Gene Name |
Proz |
| 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 |
MAGCILLLRGFILTLILHQVELSVFLPAPKANNVLRRWRRGSSYFLEEIFQGNLEKECYEEVCNYEEAREVFENDVITDEFWRQYGGGSPCVSQPCLNNGTCEDHIRSYSCTCSPGYEGKTCAMAKNECHLERTDGCQHFCHPGQSSYMCSCAKGYKLGKDQKSCGPSDKCACGALTSEHIRMTKSSQSQPSFPWQVRLTNSEGEDFCAGVLLQEDFVLTTAKCSLLHSNISVKANVDQRIRIKSTHVHMRYDEESGENDVSLLQLEEPLQCPSSGLPVCVPERDFAEHVLIPGTEGLLSGWMLNGTHLATTPMLLSVTQADGEECGQTLNVTVTTRTSCEKGSVVMGPWVEGSVVTREHKGTWFLTGILGSPPPPGQSQMLLLTAVPRYSMWFKQIMK |
| Enzyme Length |
399 |
| Uniprot Accession Number |
Q9CQW3 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids (By similarity). {ECO:0000250}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Disulfide bond (9); Domain (4); Glycosylation (4); Modified residue (12); Propeptide (1); Signal peptide (1) |
| Keywords |
Blood coagulation;Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydroxylation;Reference proteome;Repeat;Secreted;Serine protease homolog;Signal |
| Interact With |
|
| Induction |
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| Subcellular Location |
SUBCELLULAR LOCATION: Secreted. |
| Modified Residue |
MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 48; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 55; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 57; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 67; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 70; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 73; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 80; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00744, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 104; /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..22; /evidence=ECO:0000255 |
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
10829076;
11217851;
11372680;
12466851;
18344422;
21267068;
21677750;
23205927;
23963134;
25337252;
25474349;
30733279;
|
| Motif |
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| Gene Encoded By |
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| Mass |
44,304 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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