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coagulation factor IX; Christmas factor; plasma thromboplastin component; PTC; contains: coagulation factor IXa light chain; coagulation factor IXa heavy chain (F9)

Function: - vitamin K-dependent coagulation factor - participates in the intrinsic pathway of blood coagulation by converting factor X to its active form (factor Xa) in the presence of Ca+2, phospholipids, & factor VIIIa - selective cleavage of Arg-|-Ile bond in factor X to form factor Xa - activated by factor XIa, which excises the activation peptide - the iron & 2-oxoglutarate dependent 3-hydroxylation of Asp & Asn is (R) stereospecific within EGF domains - heterodimer of a light chain & a heavy chain disulfide-linked Structure: - Ca+2 binds to the gamma-carboxyglutamic acid (Gla) residues &, with stronger affinity, to another site, beyond the Gla domain - 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: - synthesized primarily in the liver & secreted in plasma Pathology: - defects in F9 are the cause of recessive X-linked hemophilia B (Christmas disease) - mutations in position 43 (Oxford-3, San dimas) & 46 (Cambridge) prevent cleavage of the propeptide - mutation in position 93 (Alabama) probably fails to bind to cell membranes - mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide - defects in F9 are the cause of thrombophilia due to factor IX defect

Interactions

molecular events

Related

coagulation cascade coagulation factor IXa factor IX complex hemophilia B; factor IX deficiency ; Christmas disease

Specific

Factor Ix Parenteral factor IX variant recombinant factor IX Fc fusion protein (Aprolix)

General

coagulation factor enzyme precursor (zymogen) glycoprotein phosphoprotein

Properties

SIZE: entity length = 461 aa MW = 52 kD COMPARTMENT: plasma MOTIF: signal sequence {1-28} Gla {47-92} MOTIF: cysteine residue {C64} MODIFICATION: cysteine residue {C69} cysteine residue {C69} MODIFICATION: cysteine residue {C64} EGF domain {93-129} MOTIF: cysteine residue {C97} MODIFICATION: cysteine residue {C108} Ser glycosylation site {S99} cysteine residue {C102} MODIFICATION: cysteine residue {C117} Ser glycosylation site {S107} cysteine residue {C108} MODIFICATION: cysteine residue {C97} Ser phosphorylation site {S114} cysteine residue {C117} MODIFICATION: cysteine residue {C102} cysteine residue {C119} MODIFICATION: cysteine residue {C128} cysteine residue {C128} MODIFICATION: cysteine residue {C119} EGF domain {130-171} MOTIF: cysteine residue {C134} MODIFICATION: cysteine residue {C145} cysteine residue {C141} MODIFICATION: cysteine residue {C155} cysteine residue {C145} MODIFICATION: cysteine residue {C134} cysteine residue {C155} MODIFICATION: cysteine residue {C141} cysteine residue {C157} MODIFICATION: cysteine residue {C170} cysteine residue {C170} MODIFICATION: cysteine residue {C157} cysteine residue {C178} MODIFICATION: cysteine residue {C335} proteolytic site {191-192} N-glycosylation site {N203} Ser phosphorylation site {S204} Thr glycosylation site {T205} N-glycosylation site {N213} Thr glycosylation site {T215} proteolytic site {226-227} S1 domain {227-459} MOTIF: cysteine residue {C252} MODIFICATION: cysteine residue {C268} histidine residue {H267} cysteine residue {C268} MODIFICATION: cysteine residue {C252} aspartate residue {D315} cysteine residue {C335} MODIFICATION: cysteine residue {C178} cysteine residue {C382} MODIFICATION: cysteine residue {C396} cysteine residue {C396} MODIFICATION: cysteine residue {C382} cysteine residue {C407} MODIFICATION: cysteine residue {C435} serine residue {S411} cysteine residue {C435} MODIFICATION: cysteine residue {C407} PRECURSOR-FOR: coagulation factor IXa MISC-INFO: elimination route LIVER 1/2life 24 HOURS pregnancy-category C safety in lactation ?

Database Correlations

OMIM correlations MORBIDMAP 300746 UniProt P00740 PFAM correlations Entrez Gene 2158 Kegg hsa:2158 ENZYME 3.4.21.22

References

  1. UniProt :accession P00740
  2. Wikipedia; Factor IX entry http://en.wikipedia.org/wiki/factor_IX
  3. HAEMB; Note: hemophilia B mutation database http://www.kcl.ac.uk/ip/petergreen/haemBdatabase.html
  4. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/F9
  5. SeattleSNPs http://pga.gs.washington.edu/data/f9/
  6. Protein Spotlight; Note: the christmas factor - Issue 41 of December 2003 http://www.expasy.org/spotlight/back_issues/sptlt041.shtml
  7. Baron M, Norman DG, Campbell ID. Protein modules. Trends Biochem Sci. 1991 Jan;16(1):13-7. Review. PMID: 2053133
  8. Suttie JW. Synthesis of vitamin K-dependent proteins. FASEB J. 1993 Mar;7(5):445-52. Review. PMID: 8462786

Component-of

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