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Identification
HMDB Protein ID HMDBP01730
Secondary Accession Numbers
  • 7074
Name Coagulation factor IX
Synonyms
  1. Christmas factor
  2. Coagulation factor IXa heavy chain
  3. Coagulation factor IXa light chain
  4. PTC
  5. Plasma thromboplastin component
Gene Name F9
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific Function Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa
Pathways
  • Acenocoumarol Action Pathway
  • Alteplase Action Pathway
  • Aminocaproic Acid Action Pathway
  • Anistreplase Action Pathway
  • Aprotinin Action Pathway
  • Ardeparin Action Pathway
  • Argatroban Action Pathway
  • Bivalirudin Action Pathway
  • Coagulation
  • Dicoumarol Action Pathway
  • Dicumarol Action Pathway
  • Enoxaparin Action Pathway
  • Fondaparinux Action Pathway
  • Heparin Action Pathway
  • Lepirudin Action Pathway
  • Phenindione Action Pathway
  • Phenprocoumon Action Pathway
  • Reteplase Action Pathway
  • Streptokinase Action Pathway
  • Tenecteplase Action Pathway
  • Tranexamic Acid Action Pathway
  • Urokinase Action Pathway
  • Warfarin Action Pathway
  • Ximelagatran Action Pathway
Reactions Not Available
GO Classification
Component
extracellular region
Function
endopeptidase activity
serine-type endopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
calcium ion binding
Process
blood coagulation
metabolic process
multicellular organismal process
macromolecule metabolic process
protein metabolic process
proteolysis
regulation of body fluid levels
hemostasis
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs F9
Gene Sequence
>1386 bp
ATGCAGCGCGTGAACATGATCATGGCAGAATCACCAGGCCTCATCACCATCTGCCTTTTA
GGATATCTACTCAGTGCTGAATGTACAGTTTTTCTTGATCATGAAAACGCCAACAAAATT
CTGAATCGGCCAAAGAGGTATAATTCAGGTAAATTGGAAGAGTTTGTTCAAGGGAACCTT
GAGAGAGAATGTATGGAAGAAAAGTGTAGTTTTGAAGAAGCACGAGAAGTTTTTGAAAAC
ACTGAAAGAACAACTGAATTTTGGAAGCAGTATGTTGATGGAGATCAGTGTGAGTCCAAT
CCATGTTTAAATGGCGGCAGTTGCAAGGATGACATTAATTCCTATGAATGTTGGTGTCCC
TTTGGATTTGAAGGAAAGAACTGTGAATTAGATGTAACATGTAACATTAAGAATGGCAGA
TGCGAGCAGTTTTGTAAAAATAGTGCTGATAACAAGGTGGTTTGCTCCTGTACTGAGGGA
TATCGACTTGCAGAAAACCAGAAGTCCTGTGAACCAGCAGTGCCATTTCCATGTGGAAGA
GTTTCTGTTTCACAAACTTCTAAGCTCACCCGTGCTGAGACTGTTTTTCCTGATGTGGAC
TATGTAAATTCTACTGAAGCTGAAACCATTTTGGATAACATCACTCAAAGCACCCAATCA
TTTAATGACTTCACTCGGGTTGTTGGTGGAGAAGATGCCAAACCAGGTCAATTCCCTTGG
CAGGTTGTTTTGAATGGTAAAGTTGATGCATTCTGTGGAGGCTCTATCGTTAATGAAAAA
TGGATTGTAACTGCTGCCCACTGTGTTGAAACTGGTGTTAAAATTACAGTTGTCGCAGGT
GAACATAATATTGAGGAGACAGAACATACAGAGCAAAAGCGAAATGTGATTCGAATTATT
CCTCACCACAACTACAATGCAGCTATTAATAAGTACAACCATGACATTGCCCTTCTGGAA
CTGGACGAACCCTTAGTGCTAAACAGCTACGTTACACCTATTTGCATTGCTGACAAGGAA
TACACGAACATCTTCCTCAAATTTGGATCTGGCTATGTAAGTGGCTGGGGAAGAGTCTTC
CACAAAGGGAGATCAGCTTTAGTTCTTCAGTACCTTAGAGTTCCACTTGTTGACCGAGCC
ACATGTCTTCGATCTACAAAGTTCACCATCTATAACAACATGTTCTGTGCTGGCTTCCAT
GAAGGAGGTAGAGATTCATGTCAAGGAGATAGTGGGGGACCCCATGTTACTGAAGTGGAA
GGGACCAGTTTCTTAACTGGAATTATTAGCTGGGGTGAAGAGTGTGCAATGAAAGGCAAA
TATGGAATATATACCAAGGTATCCCGGTATGTCAACTGGATTAAGGAAAAAACAAAGCTC
ACTTAA
Protein Properties
Number of Residues 461
Molecular Weight 51778.1
Theoretical pI 5.16
Pfam Domain Function
Signals
  • 1-28
Transmembrane Regions
  • None
Protein Sequence
>Coagulation factor IX
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNL
ERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCP
FGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGR
VSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPW
QVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRII
PHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVF
HKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVE
GTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
GenBank ID Protein 22385321
UniProtKB/Swiss-Prot ID P00740
UniProtKB/Swiss-Prot Entry Name FA9_HUMAN
PDB IDs
GenBank Gene ID AF536327
GeneCard ID F9
GenAtlas ID F9
HGNC ID HGNC:3551
References
General References
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  4. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed:10391209 ]
  5. Kurachi K, Davie EW: Isolation and characterization of a cDNA coding for human factor IX. Proc Natl Acad Sci U S A. 1982 Nov;79(21):6461-4. [PubMed:6959130 ]
  6. Jaye M, de la Salle H, Schamber F, Balland A, Kohli V, Findeli A, Tolstoshev P, Lecocq JP: Isolation of a human anti-haemophilic factor IX cDNA clone using a unique 52-base synthetic oligonucleotide probe deduced from the amino acid sequence of bovine factor IX. Nucleic Acids Res. 1983 Apr 25;11(8):2325-35. [PubMed:6687940 ]
  7. Anson DS, Choo KH, Rees DJ, Giannelli F, Gould K, Huddleston JA, Brownlee GG: The gene structure of human anti-haemophilic factor IX. EMBO J. 1984 May;3(5):1053-60. [PubMed:6329734 ]
  8. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry. 1985 Jul 2;24(14):3736-50. [PubMed:2994716 ]
  9. McGraw RA, Davis LM, Noyes CM, Lundblad RL, Roberts HR, Graham JB, Stafford DW: Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX. Proc Natl Acad Sci U S A. 1985 May;82(9):2847-51. [PubMed:3857619 ]
  10. de la Salle C, Charmantier JL, Ravanat C, Ohlmann P, Hartmann ML, Schuhler S, Bischoff R, Ebel C, Roecklin D, Balland A, et al.: The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by factor XIa. Nouv Rev Fr Hematol. 1993;35(5):473-80. [PubMed:8295821 ]
  11. Jagadeeswaran P, Lavelle DE, Kaul R, Mohandas T, Warren ST: Isolation and characterization of human factor IX cDNA: identification of Taq I polymorphism and regional assignment. Somat Cell Mol Genet. 1984 Sep;10(5):465-73. [PubMed:6089357 ]
  12. Suehiro K, Kawabata S, Miyata T, Takeya H, Takamatsu J, Ogata K, Kamiya T, Saito H, Niho Y, Iwanaga S: Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase. J Biol Chem. 1989 Dec 15;264(35):21257-65. [PubMed:2592373 ]
  13. Stoflet ES, Koeberl DD, Sarkar G, Sommer SS: Genomic amplification with transcript sequencing. Science. 1988 Jan 29;239(4839):491-4. [PubMed:3340835 ]
  14. de la Salle C, Charmantier JL, Baas MJ, Schwartz A, Wiesel ML, Grunebaum L, Cazenave JP: A deletion located in the 3' non translated part of the factor IX gene responsible for mild haemophilia B. Thromb Haemost. 1993 Aug 2;70(2):370-1. [PubMed:8236150 ]
  15. McMullen BA, Fujikawa K, Kisiel W: The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens. Biochem Biophys Res Commun. 1983 Aug 30;115(1):8-14. [PubMed:6688526 ]
  16. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [PubMed:659613 ]
  17. Morita T, Isaacs BS, Esmon CT, Johnson AE: Derivatives of blood coagulation factor IX contain a high affinity Ca2+-binding site that lacks gamma-carboxyglutamic acid. J Biol Chem. 1984 May 10;259(9):5698-704. [PubMed:6425296 ]
  18. Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T, Takao T, Shimonishi Y, Iwanaga S: Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J Biol Chem. 1989 Dec 5;264(34):20320-5. [PubMed:2511201 ]
  19. Iwanaga S, Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T: A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Adv Exp Med Biol. 1990;281:121-31. [PubMed:2129367 ]
  20. Nishimura H, Takao T, Hase S, Shimonishi Y, Iwanaga S: Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. J Biol Chem. 1992 Sep 5;267(25):17520-5. [PubMed:1517205 ]
  21. Agarwala KL, Kawabata S, Takao T, Murata H, Shimonishi Y, Nishimura H, Iwanaga S: Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169. Biochemistry. 1994 May 3;33(17):5167-71. [PubMed:8172892 ]
  22. Arruda VR, Hagstrom JN, Deitch J, Heiman-Patterson T, Camire RM, Chu K, Fields PA, Herzog RW, Couto LB, Larson PJ, High KA: Posttranslational modifications of recombinant myotube-synthesized human factor IX. Blood. 2001 Jan 1;97(1):130-8. [PubMed:11133752 ]
  23. Freedman SJ, Furie BC, Furie B, Baleja JD: Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem. 1995 Apr 7;270(14):7980-7. [PubMed:7713897 ]
  24. Freedman SJ, Furie BC, Furie B, Baleja JD: Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX. Biochemistry. 1995 Sep 26;34(38):12126-37. [PubMed:7547952 ]
  25. Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B: Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem. 1996 Jul 5;271(27):16227-36. [PubMed:8663165 ]
  26. Li L, Darden TA, Freedman SJ, Furie BC, Furie B, Baleja JD, Smith H, Hiskey RG, Pedersen LG: Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm. Biochemistry. 1997 Feb 25;36(8):2132-8. [PubMed:9047312 ]
  27. Huang LH, Cheng H, Pardi A, Tam JP, Sweeney WV: Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX. Biochemistry. 1991 Jul 30;30(30):7402-9. [PubMed:1854745 ]
  28. Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AG, Brownlee GG, Campbell ID: The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha. Protein Sci. 1992 Jan;1(1):81-90. [PubMed:1304885 ]
  29. Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stuart D: The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions. Cell. 1995 Jul 14;82(1):131-41. [PubMed:7606779 ]
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  32. Sommer SS: Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene. FASEB J. 1992 Jul;6(10):2767-74. [PubMed:1634040 ]
  33. Giannelli F, Green PM, High KA, Sommer S, Poon MC, Ludwig M, Schwaab R, Reitsma PH, Goossens M, Yoshioka A, et al.: Haemophilia B: database of point mutations and short additions and deletions--fourth edition, 1993. Nucleic Acids Res. 1993 Jul 1;21(13):3075-87. [PubMed:8392713 ]
  34. Noyes CM, Griffith MJ, Roberts HR, Lundblad RL: Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4200-2. [PubMed:6603618 ]
  35. Bentley AK, Rees DJ, Rizza C, Brownlee GG: Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4. Cell. 1986 May 9;45(3):343-8. [PubMed:3009023 ]
  36. Davis LM, McGraw RA, Ware JL, Roberts HR, Stafford DW: Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B. Blood. 1987 Jan;69(1):140-3. [PubMed:3790720 ]
  37. Ware J, Davis L, Frazier D, Bajaj SP, Stafford DW: Genetic defect responsible for the dysfunctional protein: factor IXLong Beach. Blood. 1988 Aug;72(2):820-2. [PubMed:3401602 ]
  38. Sugimoto M, Miyata T, Kawabata S, Yoshioka A, Fukui H, Takahashi H, Iwanaga S: Blood clotting factor IX Niigata: substitution of alanine-390 by valine in the catalytic domain. J Biochem. 1988 Dec;104(6):878-80. [PubMed:3243764 ]
  39. Monroe DM, McCord DM, Huang MN, High KA, Lundblad RL, Kasper CK, Roberts HR: Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo. Blood. 1989 May 1;73(6):1540-4. [PubMed:2713493 ]
  40. Attree O, Vidaud D, Vidaud M, Amselem S, Lavergne JM, Goossens M: Mutations in the catalytic domain of human coagulation factor IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior. Genomics. 1989 Apr;4(3):266-72. [PubMed:2714791 ]
  41. Koeberl DD, Bottema CD, Buerstedde JM, Sommer SS: Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG. Am J Hum Genet. 1989 Sep;45(3):448-57. [PubMed:2773937 ]
  42. Liddell MB, Peake IR, Taylor SA, Lillicrap DP, Giddings JC, Bloom AL: Factor IX Cardiff: a variant factor IX protein that shows abnormal activation is caused by an arginine to cysteine substitution at position 145. Br J Haematol. 1989 Aug;72(4):556-60. [PubMed:2775660 ]
  43. Sakai T, Yoshioka A, Yamamoto K, Niinomi K, Fujimura Y, Fukui H, Miyata T, Iwanaga S: Blood clotting factor IX Kashihara: amino acid substitution of valine-182 by phenylalanine. J Biochem. 1989 May;105(5):756-9. [PubMed:2753873 ]
  44. Ware J, Diuguid DL, Liebman HA, Rabiet MJ, Kasper CK, Furie BC, Furie B, Stafford DW: Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties. J Biol Chem. 1989 Jul 5;264(19):11401-6. [PubMed:2738071 ]
  45. Chen SH, Thompson AR, Zhang M, Scott CR: Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins. J Clin Invest. 1989 Jul;84(1):113-8. [PubMed:2472424 ]
  46. Wang NS, Zhang M, Thompson AR, Chen SH: Factor IX Chongqing: a new mutation in the calcium-binding domain of factor IX resulting in severe hemophilia B. Thromb Haemost. 1990 Feb 19;63(1):24-6. [PubMed:2339358 ]
  47. Taylor SA, Liddell MB, Peake IR, Bloom AL, Lillicrap DP: A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm. Br J Haematol. 1990 Jun;75(2):217-21. [PubMed:2372509 ]
  48. Bertina RM, van der Linden IK, Mannucci PM, Reinalda-Poot HH, Cupers R, Poort SR, Reitsma PH: Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. J Biol Chem. 1990 Jul 5;265(19):10876-83. [PubMed:2162822 ]
  49. Miyata T, Sakai T, Sugimoto M, Naka H, Yamamoto K, Yoshioka A, Fukui H, Mitsui K, Kamiya K, Umeyama H, et al.: Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities. Biochemistry. 1991 Nov 26;30(47):11286-91. [PubMed:1958666 ]
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