coagulation factor XII selections

coagulation factor XII; Hageman factor; HAF; contains: coagulation factor XIIa heavy chain; beta-factor XIIa part 1; beta-factor XIIa part 2; coagulation factor XIIa light chain (F12)

Function: - factor XII is a serum glycoprotein that participates in initiation of blood coagulation, fibrinolysis, & the generation of bradykinin & angiotensin - prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa & then trypsin cleaves it to beta-factor XIIa - alpha-factor XIIa activates factor XI to factor XIa - selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa & factor XI to form factor XIa - factor XII is activated by kallikrein in alpha-factor XIIa, which is then further converted by trypsin into beta-factor XIIa - alpha-factor XIIa is composed of the NH2-terminal heavy chain (coagulation factor XIIa heavy chain) & the COOH-terminal light chain (coagulation factor XIIa light chain), connected by a disulfide bond - beta-factor XIIa is composed of 2 chains linked by a disulfide bond, a light chain (beta-factor XIIa part 2), corresponding to the COOH-terminal light chain (coagulation factor XIIa light chain) & a nonapeptide (beta-factor XIIa part 1) Structure: - O- & N-glycosylated - O-linked polysaccharides are probably the mucin type linked to galNAc - belongs to the peptidase S1 family - contains 2 EGF-like domains - contains 1 fibronectin type-I domain - contains 1 fibronectin type-II domain - contains 1 kringle domain - contains 1 peptidase S1 domain Compartment: secreted Pathology: - defects in F12 are the cause of factor XII deficiency - defects in F12 are the cause of hereditary angioedema type 3

Interactions

molecular events

General

coagulation factor enzyme precursor (zymogen)

Properties

SIZE: entity length = 615 aa MW = 68 kD COMPARTMENT: plasma MOTIF: signal sequence {1-19} fibronectin type II domain or F2 module SITE: 42-90 FOR-BINDING-OF: collagen MOTIF: cysteine residue {*1} MODIFICATION: cysteine residue {*3} cysteine residue {*2} MODIFICATION: cysteine residue {*4} cysteine residue {*3} MODIFICATION: cysteine residue {*1} cysteine residue {*4} MODIFICATION: cysteine residue {*2} cysteine residue {C47} MODIFICATION: cysteine residue {C73} cysteine residue {C61} MODIFICATION: cysteine residue {C88} cysteine residue {C73} MODIFICATION: cysteine residue {C47} cysteine residue {C88} MODIFICATION: cysteine residue {C61} EGF domain {94-131} MOTIF: cysteine residue {C98} MODIFICATION: cysteine residue {C110} cysteine residue {C104} MODIFICATION: cysteine residue {C119} Thr glycosylation site {T109} cysteine residue {C110} MODIFICATION: cysteine residue {C98} cysteine residue {C119} MODIFICATION: cysteine residue {C104} cysteine residue {C121} MODIFICATION: cysteine residue {C130} cysteine residue {C130} MODIFICATION: cysteine residue {C121} fibronectin type I domain or F1 module {133-173} MOTIF: cysteine residue {C135} MODIFICATION: cysteine residue {C163} cysteine residue {C161} MODIFICATION: cysteine residue {C170} cysteine residue {C163} MODIFICATION: cysteine residue {C135} cysteine residue {C170} MODIFICATION: cysteine residue {C161} EGF domain {174-210} MOTIF: cysteine residue {C178} MODIFICATION: cysteine residue {C189} cysteine residue {C183} MODIFICATION: cysteine residue {C198} cysteine residue {C189} MODIFICATION: cysteine residue {C178} cysteine residue {C198} MODIFICATION: cysteine residue {C183} cysteine residue {C200} MODIFICATION: cysteine residue {C209} cysteine residue {C209} MODIFICATION: cysteine residue {C200} Kringle {217-295} MOTIF: cysteine residue {C217} MODIFICATION: cysteine residue {C295} cysteine residue {C238} MODIFICATION: cysteine residue {C277} N-glycosylation site {N249} cysteine residue {C266} MODIFICATION: cysteine residue {C290} cysteine residue {C277} MODIFICATION: cysteine residue {C238} cysteine residue {C290} MODIFICATION: cysteine residue {C266} cysteine residue {C295} MODIFICATION: cysteine residue {C217} proline-rich region SITE: 296-349 MOTIF: proline residue (SEVERAL) Thr glycosylation site {T299} Thr glycosylation site {T305} Ser glycosylation site {S308} Thr glycosylation site {T328} Thr glycosylation site {T329} Thr glycosylation site {T337} cysteine residue {C359} MODIFICATION: cysteine residue {C486} S1 domain {373-614} MOTIF: cysteine residue {C397} MODIFICATION: cysteine residue {C413} cysteine residue {C405} MODIFICATION: cysteine residue {C475} histidine residue {H412} cysteine residue {C413} MODIFICATION: cysteine residue {C397} N-glycosylation site {N433} cysteine residue {C436} MODIFICATION: cysteine residue {C439} cysteine residue {C439} MODIFICATION: cysteine residue {C436} aspartate residue {D461} cysteine residue {C475} MODIFICATION: cysteine residue {C405} cysteine residue {C486} MODIFICATION: cysteine residue {C359} cysteine residue {C500} MODIFICATION: cysteine residue {C569} cysteine residue {C532} MODIFICATION: cysteine residue {C548} cysteine residue {C548} MODIFICATION: cysteine residue {C532} cysteine residue {C559} MODIFICATION: cysteine residue {C590} serine residue {S563} cysteine residue {C569} MODIFICATION: cysteine residue {C500} cysteine residue {C590} MODIFICATION: cysteine residue {C559} PRECURSOR-FOR: coagulation factor XIIa

Database Correlations

OMIM correlations MORBIDMAP 610619 UniProt P00748 PFAM correlations Entrez Gene 2161 Kegg hsa:2161 ENZYME 3.4.21.38

References

UniProt :accession P00748
Wikipedia; Note: factor XII entry http://en.wikipedia.org/wiki/factor_XII
F12base; Note: F12 mutation db http://bioinf.uta.fi/F12base/
SeattleSNPs http://pga.gs.washington.edu/data/f12/

Component-of

molecular complex

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