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NameCoagulation factor X
Synonyms
  • 3.4.21.6
  • Stuart factor
  • Stuart-Prower factor
Gene NameF10
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010204|Coagulation factor X
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEE
TCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKN
CELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR
KRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQE
CKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGE
AVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGI
VSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSG
GPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPE
VITSSPLK
Number of residues488
Molecular Weight54731.255
Theoretical pI5.74
GO Classification
Functions
  • calcium ion binding
  • serine-type endopeptidase activity
  • phospholipid binding
Processes
  • blood coagulation, intrinsic pathway
  • blood coagulation, extrinsic pathway
  • blood coagulation
  • positive regulation of protein kinase B signaling
  • proteolysis
  • peptidyl-glutamic acid carboxylation
  • positive regulation of cell migration
  • cellular protein metabolic process
  • post-translational protein modification
Components
  • Golgi lumen
  • intrinsic component of external side of plasma membrane
  • extracellular region
  • plasma membrane
  • extracellular space
  • endoplasmic reticulum lumen
General FunctionSerine-type endopeptidase activity
Specific FunctionFactor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID182841
UniProtKB IDP00742
UniProtKB Entry NameFA10_HUMAN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0010205|Coagulation factor X (F10)
ATGGGGCGCCCACTGCACCTCGTCCTGCTCAGTGCCTCCCTGGCTGGCCTCCTGCTGCTC
GGGGAAAGTCTGTTCATCCGCAGGGAGCAGGCCAACAACATCCTGGCGAGGGTCACGAGG
GCCAATTCCTTTCTTGAAGAGATGAAGAAAGGACACCTCGAAAGAGAGTGCATGGAAGAG
ACCTGCTCATACGAAGAGGCCCGCGAGGTCTTTGAGGACAGCGACAAGACGAATGAATTC
TGGAATAAATACAAAGATGGCGACCAGTGTGAGACCAGTCCTTGCCAGAACCAGGGCAAA
TGTAAAGACGGCCTCGGGGAATACACCTGCACCTGTTTAGAAGGATTCGAAGGCAAAAAC
TGTGAATTATTCACACGGAAGCTCTGCAGCCTGGACAACGGGGACTGTGACCAGTTCTGC
CACGAGGAACAGAACTCTGTGGTGTGCTCCTGCGCCCGCGGGTACACCCTGGCTGACAAC
GGCAAGGCCTGCATTCCCACAGGGCCCTACCCCTGTGGGAAACAGACCCTGGAACGCAGG
AAGAGGTCAGTGGCCCAGGCCACCAGCAGCAGCGGGGAGGCCCCTGACAGCATCACATGG
AAGCCATATGATGCAGCCGACCTGGACCCCACCGAGAACCCCTTCGACCTGCTTGACTTC
AACCAGACGCAGCCTGAGAGGGGCGACAACAACCTCACCAGGATCGTGGGAGGCCAGGAA
TGCAAGGACGGGGAGTGTCCCTGGCAGGCCCTGCTCATCAATGAGGAAAACGAGGGTTTC
TGTGGTGGAACCATTCTGAGCGAGTTCTACATCCTAACGGCAGCCCACTGTCTCTACCAA
GCCAAGAGATTCAAGGTGAGGGTAGGGGACCGGAACACGGAGCAGGAGGAGGGCGGTGAG
GCGGTGCACGAGGTGGAGGTGGTCATCAAGCACAACCGGTTCACAAAGGAGACCTATGAC
TTCGACATCGCCGTGCTCCGGCTCAAGACCCCCATCACCTTCCGCATGAACGTGGCGCCT
GCCTGCCTCCCCGAGCGTGACTGGGCCGAGTCCACGCTGATGACGCAGAAGACGGGGATT
GTGAGCGGCTTCGGGCGCACCCACGAGAAGGGCCGGCAGTCCACCAGGCTCAAGATGCTG
GAGGTGCCCTACGTGGACCGCAACAGCTGCAAGCTGTCCAGCAGCTTCATCATCACCCAG
AACATGTTCTGTGCCGGCTACGACACCAAGCAGGAGGATGCCTGCCAGGGGGACAGCGGG
GGCCCGCACGTCACCCGCTTCAAGGACACCTACTTCGTGACAGGCATCGTCAGCTGGGGA
GAGGGCTGTGCCCGTAAGGGGAAGTACGGGATCTACACCAAGGTCACCGCCTTCCTCAAG
TGGATCGACAGGTCCATGAAAACCAGGGGCTTGCCCAAGGCCAAGAGCCATGCCCCGGAG
GTCATAACGTCCTCTCCATTAAAGTGA
GenBank Gene IDK03194
GeneCard IDNot Available
GenAtlas IDF10
HGNC IDHGNC:3528
Chromosome Location13
Locus13q34
References
  1. Messier TL, Pittman DD, Long GL, Kaufman RJ, Church WR: Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. Gene. 1991 Mar 15;99(2):291-4. 1902434
  2. Leytus SP, Foster DC, Kurachi K, Davie EW: Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry. 1986 Sep 9;25(18):5098-102. 3768336
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  4. Fung MR, Hay CW, MacGillivray RT: Characterization of an almost full-length cDNA coding for human blood coagulation factor X. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3591-5. 2582420
  5. Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P: Isolation and characterization of human blood-coagulation factor X cDNA. Gene. 1986;41(2-3):311-4. 3011603
  6. McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B: Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. Biochemistry. 1983 Jun 7;22(12):2875-84. 6871167
  7. Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW: Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3699-702. 6587384
  8. Inoue K, Morita T: Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. Eur J Biochem. 1993 Nov 15;218(1):153-63. 8243461
  9. Jagadeeswaran P, Reddy SV, Rao KJ, Hamsabhushanam K, Lyman G: Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X. Gene. 1989 Dec 14;84(2):517-9. 2612918
  10. Suzuki K, Nishioka J, Kusumoto H, Hashimoto S: Mechanism of inhibition of activated protein C by protein C inhibitor. J Biochem. 1984 Jan;95(1):187-95. 6323392
  11. Huang X, Dementiev A, Olson ST, Gettins PG: Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa. J Biol Chem. 2010 Jun 25;285(26):20399-409. doi: 10.1074/jbc.M110.112748. Epub 2010 Apr 28. 20427285
  12. Halim A, Nilsson J, Ruetschi U, Hesse C, Larson G: Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. Mol Cell Proteomics. 2012 Apr;11(4):M111.013649. doi: 10.1074/mcp.M111.013649. Epub 2011 Dec 14. 22171320
  13. Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W: Structure of human des(1-45) factor Xa at 2.2 A resolution. J Mol Biol. 1993 Aug 5;232(3):947-66. 8355279
  14. Kamata K, Kawamoto H, Honma T, Iwama T, Kim SH: Structural basis for chemical inhibition of human blood coagulation factor Xa. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6630-5. 9618463
  15. Kochanny MJ, Adler M, Ewing J, Griedel BD, Ho E, Karanjawala R, Lee W, Lentz D, Liang AM, Morrissey MM, Phillips GB, Post J, Sacchi KL, Sakata ST, Subramanyam B, Vergona R, Walters J, White KA, Whitlow M, Ye B, Zhao Z, Shaw KJ: Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa. Bioorg Med Chem. 2007 Mar 1;15(5):2127-46. Epub 2006 Dec 13. 17227710
  16. Reddy SV, Zhou ZQ, Rao KJ, Scott JP, Watzke H, High KA, Jagadeeswaran P: Molecular characterization of human factor XSan Antonio. Blood. 1989 Oct;74(5):1486-90. 2790181
  17. Watzke HH, Lechner K, Roberts HR, Reddy SV, Welsch DJ, Friedman P, Mahr G, Jagadeeswaran P, Monroe DM, High KA: Molecular defect (Gla+14----Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg"). J Biol Chem. 1990 Jul 15;265(20):11982-9. 1973167
  18. James HL, Girolami A, Fair DS: Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343. Blood. 1991 Jan 15;77(2):317-23. 1985698
  19. Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio MG, Ruggieri M, Rodeghiero F, Bernardi F: Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain. Br J Haematol. 1995 Aug;90(4):910-5. 7669671
  20. Bezeaud A, Miyata T, Helley D, Zeng YZ, Kato H, Aillaud MF, Juhan-Vague I, Guillin MC: Functional consequences of the Ser334-->Pro mutation in a human factor X variant (factor XMarseille). Eur J Biochem. 1995 Nov 15;234(1):140-7. 8529633
  21. Kim DJ, Thompson AR, James HL: Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain. Hum Genet. 1995 Feb;95(2):212-4. 7860069
  22. Messier TL, Wong CY, Bovill EG, Long GL, Church WR: Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X. Blood Coagul Fibrinolysis. 1996 Jan;7(1):5-14. 8845463
  23. Rudolph AE, Mullane MP, Porche-Sorbet R, Tsuda S, Miletich JP: Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. J Biol Chem. 1996 Nov 8;271(45):28601-6. 8910490
  24. Zama T, Murata M, Watanabe R, Yokoyama K, Moriki T, Ambo H, Murakami H, Kikuchi M, Ikeda Y: A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo). Br J Haematol. 1999 Sep;106(3):809-11. 10468877
  25. 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. 10391209
  26. Millar DS, Elliston L, Deex P, Krawczak M, Wacey AI, Reynaud J, Nieuwenhuis HK, Bolton-Maggs P, Mannucci PM, Reverter JC, Cachia P, Pasi KJ, Layton DM, Cooper DN: Molecular analysis of the genotype-phenotype relationship in factor X deficiency. Hum Genet. 2000 Feb;106(2):249-57. 10746568
  27. Forberg E, Huhmann I, Jimenez-Boj E, Watzke HH: The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). Thromb Haemost. 2000 Feb;83(2):234-8. 10739379
  28. Simioni P, Vianello F, Kalafatis M, Barzon L, Ladogana S, Paolucci P, Carotenuto M, Dal Bello F, Palu G, Girolami A: A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the factor X gene. A study of an Italian family. Thromb Res. 2001 Feb 15;101(4):219-30. 11248282
  29. Vianello F, Lombardi AM, Boldrin C, Luni S, Girolami A: A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro). Thromb Res. 2001 Nov 15;104(4):257-64. 11728527
  30. Vianello F, Lombardi AM, Bello FD, Palu G, Zanon E, Girolami A: A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain. Blood Coagul Fibrinolysis. 2003 Jun;14(4):401-5. 12945883
  31. Pinotti M, Camire RM, Baroni M, Rajab A, Marchetti G, Bernardi F: Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency. Thromb Haemost. 2003 Feb;89(2):243-8. 12574802
  32. Pinotti M, Monti M, Baroni M, Marchetti G, Bernardi F: Molecular characterization of factor X deficiency associated with borderline plasma factor X level. Haematologica. 2004 Apr;89(4):501-2. 15075089
  33. Isshiki I, Favier R, Moriki T, Uchida T, Ishihara H, Van Dreden P, Murata M, Ikeda Y: Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X. Blood Coagul Fibrinolysis. 2005 Jan;16(1):9-16. 15650540
  34. Al-Hilali A, Wulff K, Abdel-Razeq H, Saud KA, Al-Gaili F, Herrmann FH: Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly. Thromb Haemost. 2007 Apr;97(4):542-5. 17393015
  35. Chafa O, Tagzirt M, Tapon-Bretaudiere J, Reghis A, Fischer AM, LeBonniec BF: Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X. Thromb Res. 2009 May;124(1):144-8. doi: 10.1016/j.thromres.2008.11.018. Epub 2009 Jan 10. 19135706
  36. Abdel-Azeim S, Oliva R, Chermak E, De Cristofaro R, Cavallo L: Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity. Biochemistry. 2014 Nov 11;53(44):6992-7001. doi: 10.1021/bi500770p. Epub 2014 Oct 24. 25313940