| IED ID | IndEnz0002005424 |
| Enzyme Type ID | protease005424 |
| Protein Name |
Coagulation factor XII EC 3.4.21.38 Hageman factor HAF Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain Beta-factor XIIa part 2 |
| Gene Name | F12 |
| 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 | MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS |
| Enzyme Length | 615 |
| Uniprot Accession Number | P00748 |
| Absorption | |
| Active Site | ACT_SITE 412; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 461; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 563; /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. {ECO:0000269|PubMed:21304106}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Chain (3); Compositional bias (1); Disulfide bond (20); Domain (6); Glycosylation (9); Helix (7); Natural variant (17); Region (1); Sequence conflict (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Blood coagulation;Direct protein sequencing;Disease variant;Disulfide bond;EGF-like domain;Fibrinolysis;Glycoprotein;Hemostasis;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | P05067; Q07021; P13473-2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Factor XII is activated by kallikrein in alpha-factor XIIa, which is further converted by trypsin into beta-factor XIIa. Alpha-factor XIIa is composed of an NH2-terminal heavy chain, called coagulation factor XIIa heavy chain, and a COOH-terminal light chain, called coagulation factor XIIa light chain, connected by a disulfide bond. Beta-factor XIIa is composed of 2 chains linked by a disulfide bond, an N-terminal nonapeptide, called beta-factor XIIa part 1, and coagulation factor XIIa light chain, also known in this context as beta-factor XIIa part 2.; PTM: O- and N-glycosylated. The O-linked polysaccharides were not identified, but are probably the mucin type linked to GalNAc. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1544894, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3886654}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:3886654 |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 4BDW; 4BDX; 4XDE; 4XE4; 6B74; 6B77; 6GT6; 6L63; 6QF7; 6SZW; 6X0S; 6X0T; |
| Mapped Pubmed ID | 1066663; 10781579; 10870808; 11204562; 11248286; 11792853; 11805911; 11821096; 11843842; 11986212; 12052484; 12208481; 12492481; 12773530; 12876626; 1451784; 14597972; 14691562; 15000805; 15116249; 15232129; 15257949; 15306750; 15567455; 15748262; 15749685; 16015420; 16157382; 16167952; 16170239; 16411408; 16493494; 17139385; 17143557; 17408404; 17605651; 17825897; 17982641; 18021303; 18024408; 18180442; 18278180; 18327401; 18441012; 18710647; 18725990; 18765660; 18793325; 18832903; 18974842; 19127083; 19178407; 19178938; 19204433; 19372376; 19420105; 19422815; 19448530; 19474702; 19477491; 19578796; 19625260; 19646235; 19647418; 19698288; 19786295; 19809305; 19878657; 19913121; 19933701; 19933990; 1998667; 20022356; 20142324; 20143645; 20228268; 2026621; 20303064; 20386432; 20452482; 20532885; 20589311; 20673868; 20729721; 20814302; 21071604; 21071930; 21192253; 21264442; 21297451; 21631522; 21828145; 21849258; 22500857; 22905925; 22920075; 2296585; 22993391; 2365061; 23659638; 23692437; 23849223; 23874198; 23896408; 24388213; 24509324; 24552232; 24691729; 24733030; 24855058; 24977287; 25113305; 25134986; 25241761; 25489738; 25589788; 25604127; 25609114; 2563376; 25744496; 25775543; 2578463; 25790805; 25800206; 25816745; 25879167; 26037346; 26105808; 26153047; 26153520; 26193639; 26248961; 26392288; 26613657; 26706311; 26709783; 26969407; 27003566; 27130860; 27188843; 27282310; 27694320; 27788882; 27933406; 28069606; 28346966; 28433996; 28514863; 28661939; 28743596; 28816340; 29075790; 29419864; 29519898; 29587641; 29885370; 29920929; 29994896; 29994899; 30354195; 30394658; 30512149; 30591525; 30929639; 31124034; 31181367; 31205020; 31279063; 31334892; 31771982; 31924766; 31940673; 31984663; 32335876; 32559765; 32839601; 33036649; 33412399; 3521732; 3756141; 4703226; 588558; 7391081; 7814636; 8529136; 8641707; 8710908; 874082; 8798678; 893417; 9920838; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,792 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.38; |