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coagulation factor X; Stuart factor; Stuart-Prower factor; contains: factor X light chain; factor X heavy chain; activated factor Xa heavy chain (F10)

Function: - precursor for coagulation factor Xa, a vitamin K- dependent serine protease that activates prothrombin to thrombin - vitamin K-dependent, enzymatic carboxylation of some Glu allows the modified protein to bind Ca+2 - the activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) - the iron & 2-oxoglutarate dependent 3-hydroxylation of Asp & Asn is (R) stereospecific within EGF domains - the two chains are formed from a single-chain precursor by the excision of two Arg & are held together by 1 or more disulfide bonds Structure: - N- & O-glycosylated - belongs to the peptidase S1 family - contains 2 EGF-like domains - contains 1 Gla (gamma-carboxy-glutamate) domain - contains 1 peptidase S1 domain Compartment: secreted Expression: plasma; synthesized in the liver Pathology: - defects in factor X are associated with factor X deficiency

Interactions

molecular events

Related

coagulation cascade coagulation factor Xa

Specific

Factor X Parenteral factor X variant

General

coagulation factor enzyme precursor (zymogen)

Properties

SIZE: entity length = 488 aa MW = 55 kD COMPARTMENT: plasma MOTIF: signal sequence {1-31} Gla {41-85} MOTIF: cysteine residue {C57} MODIFICATION: cysteine residue {C62} cysteine residue {C62} MODIFICATION: cysteine residue {C57} EGF domain {86-122} MOTIF: cysteine residue {C90} MODIFICATION: cysteine residue {C101} cysteine residue {C95} MODIFICATION: cysteine residue {C110} cysteine residue {C101} MODIFICATION: cysteine residue {C90} cysteine residue {C110} MODIFICATION: cysteine residue {C95} cysteine residue {C112} MODIFICATION: cysteine residue {C121} cysteine residue {C121} MODIFICATION: cysteine residue {C112} EGF domain {125-165} MOTIF: cysteine residue {C129} MODIFICATION: cysteine residue {C140} cysteine residue {C136} MODIFICATION: cysteine residue {C149} cysteine residue {C140} MODIFICATION: cysteine residue {C129} cysteine residue {C149} MODIFICATION: cysteine residue {C136} cysteine residue {C151} MODIFICATION: cysteine residue {C164} cysteine residue {C164} MODIFICATION: cysteine residue {C151} cysteine residue {C172} MODIFICATION: cysteine residue {C-INTERCHAIN} Thr glycosylation site {T199} Thr glycosylation site {T211} N-glycosylation site {N221} N-glycosylation site {N231} S1 domain {235-467} MOTIF: cysteine residue {C241} MODIFICATION: cysteine residue {C246} cysteine residue {C246} MODIFICATION: cysteine residue {C241} cysteine residue {C261} MODIFICATION: cysteine residue {C277} histidine residue {H276} cysteine residue {C277} MODIFICATION: cysteine residue {C261} aspartate residue {D322} cysteine residue {C390} MODIFICATION: cysteine residue {C404} cysteine residue {C404} MODIFICATION: cysteine residue {C390} cysteine residue {C415} MODIFICATION: cysteine residue {C443} serine residue {S419} cysteine residue {C443} MODIFICATION: cysteine residue {C415} PRECURSOR-FOR: coagulation factor Xa MISC-INFO: 1/2life 36 HOURS

Database Correlations

OMIM 227600 UniProt P00742 PFAM correlations Entrez Gene 2159 Kegg hsa:2159 ENZYME 3.4.21.6

References

  1. UniProt :accession P00742
  2. Wikipedia; Factor X entry http://en.wikipedia.org/wiki/factor_X
  3. SeattleSNPs http://pga.gs.washington.edu/data/f10/
  4. Baron M, Norman DG, Campbell ID. Protein modules. Trends Biochem Sci. 1991 Jan;16(1):13-7. Review. PMID: 2053133
  5. Suttie JW. Synthesis of vitamin K-dependent proteins. FASEB J. 1993 Mar;7(5):445-52. Review. PMID: 8462786
  6. Department of Veterans Affairs, VA National Formulary

Component-of

factor ix/factor vii/factor x/protein c/protein s/prothrombin/prothrombin complex concentrate prothrombin complex concentrate (Autoplex-T, Kcentra)