IED ID | IndEnz0002005426 |
Enzyme Type ID | protease005426 |
Protein Name |
Coagulation factor XII EC 3.4.21.38 Hageman factor HAF Cleaved into: Coagulation factor XIIa heavy chain; Coagulation factor XIIa light chain |
Gene Name | F12 |
Organism | Sus scrofa (Pig) |
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 Suina Suidae (pigs) Sus Sus scrofa (Pig) |
Enzyme Sequence | MRALLLLGILLVSLESALLIPPWKDPRKHKVMASEHTVVLTVTGEPCHFPFQYYRQLYYKCIQRGQRGPRPWCATTPNFEKDQRWAYCLEPMKVKDHCNKGNPCQKGGTCVNMPNGPHCICPDHFTGKHCQKEKCFEPQFLQFFQENEIWHRFEPAGVSKCQCKGPKAQCKPVASQVCSTNPCLNGGSCLQTEGHRLCRCPTGYAGRLCDVDLKERCYSDRGLSYRGMAQTTLSGAPCQPWASEATYWNMTAEQALNWGLGDHAFCRNPDNDTRPWCFVWRGDQLSWQYCRLARCQAPIGEAPPILTPTQSPSEHQDSPLLSREPQPTTQTPSQNLTSAWCAPPEQRGPLPSAGLVGCGQRLRKRLSSLNRIVGGLVALPGAHPYIAALYWGQNFCAGSLIAPCWVLTAAHCLQNRPAPEELTVVLGQDRHNQSCEQCQTLAVRSYRLHESYSPKTYQHDLALVRLKETADGCCAHPSPFVQPVCLPRSVASSAEPEGALCEVAGWGHQFEGAEEYSSFLQEAQVPLISPERCSAADVHGAAFTPGMLCAGFLEGGTDACQGDSGGPLVCEDETAERQLVLRGIVSWGSGCGDRLKPGVYTDVANYLAWIQEHTTS |
Enzyme Length | 616 |
Uniprot Accession Number | O97507 |
Absorption | |
Active Site | ACT_SITE 411; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 460; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 564; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.; EC=3.4.21.38; |
DNA Binding | |
EC Number | 3.4.21.38 |
Enzyme Function | FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (2); Compositional bias (1); Disulfide bond (20); Domain (6); Glycosylation (5); Region (1); Signal peptide (1) |
Keywords | Blood coagulation;Disulfide bond;EGF-like domain;Fibrinolysis;Glycoprotein;Hemostasis;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: O- and N-glycosylated. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 68,012 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |