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coagulation factor VII; proconvertin; serum prothrombin conversion accelerator; SPCA; Eptacog alfa; contains: factor VII light chain; factor VII heavy chain (F7)

Function: - initiates the extrinsic pathway of blood coagulation - serine protease that circulates in the blood in a zymogen form - factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis - in the presence of tissue factor & Ca+2, factor VIIa then converts factor X to factor Xa by limited proteolysis - factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor & Ca+2 - selective cleavage of Arg-|-Ile bond in factor X to form factor Xa - vitamin K-dependent, enzymatic carboxylation of some Glu allows the modified protein to bind Ca+2 - the iron & 2-oxoglutarate dependent 3-hydroxylation of Asp & Asn is (R) stereospecific within EGF domains - heterodimer of a light chain & a heavy chain linked by a disulfide bond Structure: - 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 Alternative splicing: named isoforms=2; A,B Expression: plasma Pathology: - defects in F7 are the cause of factor VII deficiency Pharmacokinetics: - 1/2life of 6 hours, shortest of coagulation factors [8]

Interactions

molecular events

Related

coagulation cascade coagulation factor VIIa F7 gene mutation

Specific

recominant factor VII parenteral

General

coagulation factor enzyme precursor (zymogen) serine protease

Properties

SIZE: entity length = 466 aa MW = 52 kD COMPARTMENT: plasma MOTIF: signal sequence {1-20} Gla {61-105} MOTIF: cysteine residue {C77} MODIFICATION: cysteine residue {C82} cysteine residue {C82} MODIFICATION: cysteine residue {C77} EGF domain {106-142} MOTIF: cysteine residue {C110} MODIFICATION: cysteine residue {C121} Ser glycosylation site {S112} cysteine residue {C115} MODIFICATION: cysteine residue {C130} Ser glycosylation site {S120} cysteine residue {C121} MODIFICATION: cysteine residue {C110} cysteine residue {C130} MODIFICATION: cysteine residue {C115} cysteine residue {C132} MODIFICATION: cysteine residue {C141} cysteine residue {C141} MODIFICATION: cysteine residue {C132} EGF domain {147-188} MOTIF: cysteine residue {C151} MODIFICATION: cysteine residue {C162} cysteine residue {C158} MODIFICATION: cysteine residue {C172} cysteine residue {C162} MODIFICATION: cysteine residue {C151} cysteine residue {C172} MODIFICATION: cysteine residue {C158} cysteine residue {C174} MODIFICATION: cysteine residue {C187} cysteine residue {C187} MODIFICATION: cysteine residue {C174} cysteine residue {C195} MODIFICATION: cysteine residue {C322} N-glycosylation site {N205} proteolytic site {212-213} S1 domain {213-452} MOTIF: cysteine residue {C219} MODIFICATION: cysteine residue {C224} cysteine residue {C224} MODIFICATION: cysteine residue {C219} cysteine residue {C238} MODIFICATION: cysteine residue {C254} histidine residue {H253} cysteine residue {C254} MODIFICATION: cysteine residue {C238} aspartate residue {D302} cysteine residue {C322} MODIFICATION: cysteine residue {C195} cysteine residue {C370} MODIFICATION: cysteine residue {C389} N-glycosylation site {N382} cysteine residue {C389} MODIFICATION: cysteine residue {C370} binding site SITE: 398-398 FOR-BINDING-OF: Substrate cysteine residue {C400} MODIFICATION: cysteine residue {C428} serine residue {S404} cysteine residue {C428} MODIFICATION: cysteine residue {C400} PRECURSOR-FOR: coagulation factor VIIa MISC-INFO: 1/2life 6 HOURS

Database Correlations

OMIM 227500 UniProt P08709 PFAM correlations Entrez Gene 2155 Kegg hsa:2155 ENZYME 3.4.21.21

References

  1. UniProt :accession P08709
  2. Wikipedia; Factor VII entry http://en.wikipedia.org/wiki/factor_VII
  3. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/F7
  4. SeattleSNPs http://pga.gs.washington.edu/data/f7/
  5. SHMPD; Singapore human mutation and polymorphism database http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F7
  6. Baron M, Norman DG, Campbell ID. Protein modules. Trends Biochem Sci. 1991 Jan;16(1):13-7. Review. PMID: 2053133
  7. Suttie JW. Synthesis of vitamin K-dependent proteins. FASEB J. 1993 Mar;7(5):445-52. Review. PMID: 8462786
  8. Medical Knowledge Self Assessment Program (MKSAP) 17, American College of Physicians, Philadelphia 2015

Component-of

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