Detail Information for IndEnz0002005427
IED ID IndEnz0002005427
Enzyme Type ID protease005427
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 Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MTALLFLGSLLMSLDLTLSAPPWKSKEFKDGAGDPSVVLTVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYCLEPKKVKDHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQREKCFESQLLKFFHENEIWFRTGPGGVARCQCKGPQAVCKLLTSQVCRVNPCLNGGTCLLVEDHRLCHCPAGYAGPFCDLDLKATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDNDTRPWCYVWSGDRLSWDYCDLEQCQMPTLTSPVSPESHDMLKPRPPILQSSPRDSTRNQNVVSRTSTVVCGQRFRKRLSSLRRVVGGLVALPGSHPYIAALYWGDSFCAGSLIDPCWVLTAAHCLQKRPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLHEGFSSKTYQHDLALLRLRGRKNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLDRCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQEHTAF
Enzyme Length 595
Uniprot Accession Number D3ZTE0
Absorption
Active Site ACT_SITE 393; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 442; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 543; /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); Disulfide bond (20); Domain (6); Erroneous gene model prediction (1); Glycosylation (6); Region (1); Sequence conflict (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 {ECO:0000250}.
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 10048754; 11092686; 16046705; 2324612;
Motif
Gene Encoded By
Mass 65,844
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.38;