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coagulation factor V; activated protein C cofactor; proaccelerin, labile factor; contains: coagulation factor V heavy chain; coagulation factor V light chain (F5)

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: secreted (putative) Expression: plasma Pathology: 1) factor V deficiency: a) very rare b) inheritance is autosomal recessive 2) defects in factor V may be associated with a) thrombophilia due to activated protein C resistance b) susceptibility to Budd-Chiari syndrome c) susceptibility to ischemic stroke d) factor V Quebec e) factor 5 Leiden

Interactions

molecular events

Related

coagulation cascade coagulation factor V autoantibody coagulation factor Va or accelerin factor V Leiden mutation (PT 20210) factor V Quebec

General

coagulation factor enzyme precursor (zymogen) glycoprotein PEST protein

Properties

SIZE: entity length = 2224 aa MW = 252 kD COMPARTMENT: plasma MOTIF: signal sequence {1-28} F5/8 type A 1 {30-329} MOTIF: Plastocyanin-like 1 {30-193} N-glycosylation site {N51} N-glycosylation site {N55} Ca+2-binding site SITE: 139-139 Ca+2-binding site SITE: 140-140 cysteine residue {C167} MODIFICATION: cysteine residue {C193} cysteine residue {C193} MODIFICATION: cysteine residue {C167} Plastocyanin-like 2 {203-329} N-glycosylation site {N239} cysteine residue {C248} MODIFICATION: cysteine residue {C329} N-glycosylation site {N297} cysteine residue {C329} MODIFICATION: cysteine residue {C248} proteolytic site {334-335} F5/8 type A 2 {348-684} MOTIF: Plastocyanin-like 3 {348-526} N-glycosylation site {N382} N-glycosylation site {N460} N-glycosylation site {N468} cysteine residue {C500} MODIFICATION: cysteine residue {C526} cysteine residue {C526} MODIFICATION: cysteine residue {C500} proteolytic site {534-535} Plastocyanin-like 4 {536-684} N-glycosylation site {N554} cysteine residue {C603} MODIFICATION: cysteine residue {C684} Thr phosphorylation site {T640} cysteine residue {C684} MODIFICATION: cysteine residue {C603} B {692-1573} MOTIF: proteolytic site {707-708} proteolytic site {737-738} N-glycosylation site {N741} N-glycosylation site {N752} N-glycosylation site {N760} N-glycosylation site {N776} N-glycosylation site {N782} N-glycosylation site {N821} domain {895-928} 1-1 {895-911} 1-2 {912-928} N-glycosylation site {N938} N-glycosylation site {N977} proteolytic site {1022-1023} proteolytic site {1046-1047} N-glycosylation site {N1074} N-glycosylation site {N1083} N-glycosylation site {N1103} N-glycosylation site {N1106} Ser phosphorylation site {S1150} domain {1185-1501} consensus repeat {1185-1501} (35) N-glycosylation site {N1499} N-glycosylation site {N1559} proteolytic site {1573-1574} F5/8 type A 3 {1578-1907} MOTIF: Plastocyanin-like 5 {1578-1751} N-glycosylation site {N1703} cysteine residue {C1725} MODIFICATION: cysteine residue {C1751} cysteine residue {C1751} MODIFICATION: cysteine residue {C1725} Plastocyanin-like 6 {1761-1907} copper [Cu]-binding site SITE: 1843-1843 MOTIF: histidine residue (3) copper [Cu]-binding site SITE: 1845-1845 MOTIF: histidine residue (3) coagulation factors 5/8 type C domain (FA58C) {1907-2061} MOTIF: cysteine residue {C1907} MODIFICATION: cysteine residue {C2061} N-glycosylation site {N2010} cysteine residue {C2061} MODIFICATION: cysteine residue {C1907} coagulation factors 5/8 type C domain (FA58C) {2066-2221} MOTIF: cysteine residue {C2066} MODIFICATION: cysteine residue {C2221} N-glycosylation site {N2209} cysteine residue {C2221} MODIFICATION: cysteine residue {C2066} PRECURSOR-FOR: coagulation factor Va MISC-INFO: STOKES_RADIUS 9.1-9.5 NM SEDIMENTATION_COEFFICIENT 9.19 S FRICTIONAL_RATIO 2.01 1/2life 12-15 HOURS CONCENTRATION 7 UG/ML

Database Correlations

OMIM correlations MORBIDMAP 612309 UniProt P12259 PFAM correlations Entrez Gene 2153 Kegg hsa:2153

References

  1. UniProt :accession P12259
  2. Wikipedia; Note: factor V entry http://en.wikipedia.org/wiki/factor_V
  3. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/F5
  4. SeattleSNPs http://pga.gs.washington.edu/data/f5/
  5. SHMPD; Singapore human mutation and polymorphism database http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F5
  6. Cotran et al Robbins Pathologic Basis of Disease, W.B. Saunders Co, Philadelphia, PA 1989 pg 696
  7. Wang KK et al Calmodulin-binding proteins as calpain substrates. Biochem J 262:693 1989 PMID: 2556106
  8. 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: 3125864