Detail Information for IndEnz0010001406
IED ID IndEnz0010001406
Enzyme Type ID esterase001406
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 (28); Chain (3); Compositional bias (1); Disulfide bond (20); Domain (6); Glycosylation (9); Helix (10); 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 (13)
Cross Reference PDB 4BDW; 4BDX; 4XDE; 4XE4; 6B74; 6B77; 6GT6; 6L63; 6QF7; 6SZW; 6X0S; 6X0T; 7FBP;
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; 34723512; 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;