coagulation factor V; activated protein C cofactor; proaccelerin, labile factor; contains: coagulation factor V heavy chain; coagulation factor V light chain (F5)
Jump to navigation
Jump to search
Function
- central regulator of hemostasis
- cofactor for the prothrombinase activity of factor Xa that results in activation of prothrombin to thrombin
- thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus & a light chain at the C-terminus)
- sulfation is required for efficient thrombin cleavage & activation & for full procoagulant activity
- activated protein C inactivates factor V & factor Va by proteolytic degradation
- phosphorylation sites are present in the extracellular medium
Structure
- domain B contains 35 x 9 AA tandem repeats, & 2 x 17 AA repeats
- belongs to the multicopper oxidase family
- contains domain homologous with ceruloplasmin
- contains 3 F5/8 type A domains
- contains 2 F5/8 type C domains
- contains 6 plastocyanin-like domains
Compartment
Expression
Pathology
- factor V deficiency:
- very rare
- inheritance is autosomal recessive
- defects in factor V may be associated with
- thrombophilia due to activated protein C resistance
- susceptibility to Budd-Chiari syndrome
- susceptibility to ischemic stroke
- factor V Quebec
- factor 5 Leiden
More general terms
Additional terms
- coagulation cascade
- coagulation factor V autoantibody
- coagulation factor Va or accelerin
- factor V Leiden mutation (PT 20210)
- factor V Quebec
References
- ↑ UniProt http://www.uniprot.org/uniprot/P12259.html
- ↑ Wikipedia; Note: factor V entry http://en.wikipedia.org/wiki/factor_V
- ↑ GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/F5
- ↑ SeattleSNPs http://pga.gs.washington.edu/data/f5/
- ↑ SHMPD; Singapore human mutation and polymorphism database http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F5
- ↑ Cotran et al Robbins Pathologic Basis of Disease, W.B. Saunders Co, Philadelphia, PA 1989 pg 696
- ↑ Wang KK et al Calmodulin-binding proteins as calpain substrates. Biochem J 262:693 1989 PMID: https://www.ncbi.nlm.nih.gov/pubmed/2556106
- ↑ Kane WH, Davie EW. Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood. 1988 Mar;71(3):539-55. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/3125864
Database
- Entrez gene: http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=2153
- Kegg: http://www.genome.jp/dbget-bin/www_bget?hsa:2153
- OMIM: https://mirror.omim.org/entry/188055
- OMIM: https://mirror.omim.org/entry/227400
- OMIM: https://mirror.omim.org/entry/600880
- OMIM: https://mirror.omim.org/entry/601367
- OMIM: https://mirror.omim.org/entry/612309
- UniProt: http://www.uniprot.org/uniprot/P12259.html