Coagulation factor XIII A chain

Details

Name
Coagulation factor XIII A chain
Kind
protein
Synonyms
  • 2.3.2.13
  • Coagulation factor XIIIa
  • F13A
  • Protein-glutamine gamma-glutamyltransferase A chain
  • Transglutaminase A chain
Gene Name
F13A1
UniProtKB Entry
P00488Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0055650|Coagulation factor XIII A chain
MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDT
NKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPV
PIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETD
TYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCL
YVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDIL
LEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGN
VNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKH
GHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITD
TYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITF
RNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLL
EQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVEFTNPLKET
LRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYG
ELDVQIQRRPSM
Number of residues
732
Molecular Weight
83267.785
Theoretical pI
5.95
GO Classification
Processes
blood coagulation, fibrin clot formation
Components
collagen-containing extracellular matrix / extracellular space / transferase complex
General Function
Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin
Specific Function
metal ion binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010128|Coagulation factor XIII A chain (F13A1)
ATGTCAGAAACTTCCAGGACCGCCTTTGGAGGCAGAAGAGCAGTTCCACCCAATAACTCT
AATGCAGCGGAAGATGACCTGCCCACAGTGGAGCTTCAGGGCGTGGTGCCCCGGGGCGTC
AACCTGCAAGAGTTTCTTAATGTCACGAGCGTTCACCTGTTCAAGGAGAGATGGGACACT
AACAAGGTGGACCACCACACTGACAAGTATGAAAACAACAAGCTGATTGTCCGCAGAGGG
CAGTCTTTCTATGTGCAGATTGACTTCAGTCGTCCATATGACCCCAGAAGGGATCTCTTC
AGGGTGGAATACGTCATTGGTCGCTACCCACAGGAGAACAAGGGAACCTACATCCCAGTG
CCTATAGTCTCAGAGTTACAAAGTGGAAAGTGGGGGGCCAAGATTGTCATGAGAGAGGAC
AGGTCTGTGCGGCTGTCCATCCAGTCTTCCCCCAAATGTATTGTGGGGAAATTCCGCATG
TATGTTGCTGTCTGGACTCCCTATGGCGTACTTCGAACCAGTCGAAACCCAGAAACAGAC
ACGTACATTCTCTTCAATCCTTGGTGTGAAGATGATGCTGTGTATCTGGACAATGAGAAA
GAAAGAGAAGAGTATGTCCTGAATGACATCGGGGTAATTTTTTATGGAGAGGTCAATGAC
ATCAAGACCAGAAGCTGGAGCTATGGTCAGTTTGAAGATGGCATCCTGGACACTTGCCTG
TATGTGATGGACAGAGCACAAATGGACCTCTCTGGAAGAGGGAATCCCATCAAAGTCAGC
CGTGTGGGGTCTGCAATGGTGAATGCCAAAGATGACGAAGGTGTCCTCGTTGGATCCTGG
GACAATATCTATGCCTATGGCGTCCCCCCATCGGCCTGGACTGGAAGCGTTGACATTCTA
TTGGAATACCGGAGCTCTGAGAATCCAGTCCGGTATGGCCAATGCTGGGTTTTTGCTGGT
GTCTTTAACACATTTTTACGATGCCTTGGAATACCAGCAAGAATTGTTACCAATTATTTC
TCTGCCCATGATAATGATGCCAATTTGCAAATGGACATCTTCCTGGAAGAAGATGGGAAC
GTGAATTCCAAACTCACCAAGGATTCAGTGTGGAACTACCACTGCTGGAATGAAGCATGG
ATGACAAGGCCTGACCTTCCTGTTGGATTTGGAGGCTGGCAAGCTGTGGACAGCACCCCC
CAGGAAAATAGCGATGGCATGTATCGGTGTGGCCCCGCCTCGGTTCAAGCCATCAAGCAC
GGCCATGTCTGCTTCCAATTTGATGCACCTTTTGTTTTTGCAGAGGTCAACAGCGACCTC
ATTTACATTACAGCTAAGAAAGATGGCACTCATGTGGTGGAAAATGTGGATGCCACCCAC
ATTGGGAAATTAATTGTGACCAAACAAATTGGAGGAGATGGCATGATGGATATTACTGAT
ACTTACAAATTCCAAGAAGGTCAAGAAGAAGAGAGATTGGCCCTAGAAACTGCCCTGATG
TACGGAGCTAAAAAGCCCCTCAACACAGAAGGTGTCATGAAATCAAGGTCCAACGTTGAC
ATGGACTTTGAAGTGGAAAATGCTGTGCTGGGAAAAGACTTCAAGCTCTCCATCACCTTC
CGGAACAACAGCCACAACCGTTACACCATCACAGCTTATCTCTCAGCCAACATCACCTTC
TACACCGGGGTCCCGAAGGCAGAATTCAAGAAGGAGACGTTCGACGTGACGCTGGAGCCC
TTGTCCTTCAAGAAAGAGGCGGTGCTGATCCAAGCCGGCGAGTACATGGGTCAGCTGCTG
GAACAAGCGTCCCTGCACTTCTTTGTCACAGCTCGCATCAATGAGACCAGGGATGTTCTG
GCCAAGCAAAAGTCCACCGTGCTAACCATCCCTGAGATCATCATCAAGGTCCGTGGCACT
CAGGTAGTTGGTTCTGACATGACTGTGACAGTTGAGTTTACCAATCCTTTAAAAGAAACC
CTGCGAAATGTCTGGGTACACCTGGATGGTCCTGGAGTAACAAGACCAATGAAGAAGATG
TTCCGTGAAATCCGGCCCAACTCCACCGTGCAGTGGGAAGAAGTGTGCCGGCCCTGGGTC
TCTGGGCATCGGAAGCTGATAGCCAGCATGAGCAGTGACTCCCTGAGACATGTGTATGGC
GAGCTGGACGTGCAGATTCAAAGACGACCTTCCATGTGA
Chromosome Location
6
Locus
6p25.1
External Identifiers
ResourceLink
UniProtKB IDP00488
UniProtKB Entry NameF13A_HUMAN
GenBank Protein ID182309
GenBank Gene IDM22001
GeneCard IDF13A1
GenAtlas IDF13A1
HGNC IDHGNC:3531
PDB ID(s)1EVU, 1EX0, 1F13, 1FIE, 1GGT, 1GGU, 1GGY, 1QRK, 4KTY, 5MHL, 5MHM, 5MHN, 5MHO
KEGG IDhsa:2162
NCBI Gene ID2162
General References
  1. Ichinose A, Hendrickson LE, Fujikawa K, Davie EW: Amino acid sequence of the a subunit of human factor XIII. Biochemistry. 1986 Nov 4;25(22):6900-6. [Article]
  2. Grundmann U, Amann E, Zettlmeissl G, Kupper HA: Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8024-8. [Article]
  3. Ichinose A, Davie EW: Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5829-33. [Article]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [Article]
  5. 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. [Article]
  6. Takahashi N, Takahashi Y, Putnam FW: Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8019-23. [Article]
  7. Takagi T, Doolittle RF: Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry. 1974 Feb 12;13(4):750-6. [Article]
  8. Schwartz ML, Pizzo SV, Hill RL, McKee PA: Human Factor XIII from plasma and platelets. Molecular weights, subunit structures, proteolytic activation, and cross-linking of fibrinogen and fibrin. J Biol Chem. 1973 Feb 25;248(4):1395-407. [Article]
  9. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [Article]
  10. Muszbek L, Bereczky Z, Bagoly Z, Komaromi I, Katona E: Factor XIII: a coagulation factor with multiple plasmatic and cellular functions. Physiol Rev. 2011 Jul;91(3):931-72. doi: 10.1152/physrev.00016.2010. [Article]
  11. Thomas A, Biswas A, Ivaskevicius V, Oldenburg J: Structural and functional influences of coagulation factor XIII subunit B heterozygous missense mutants. Mol Genet Genomic Med. 2015 Jul;3(4):258-71. doi: 10.1002/mgg3.138. Epub 2015 Apr 10. [Article]
  12. Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. [Article]
  13. Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC: Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res. 1995 Jun 1;78(5):389-97. [Article]
  14. Weiss MS, Metzner HJ, Hilgenfeld R: Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett. 1998 Feb 27;423(3):291-6. [Article]
  15. Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by x-ray crystallography. J Biol Chem. 1999 Feb 19;274(8):4917-23. [Article]
  16. Suzuki K, Iwata M, Ito S, Matsui K, Uchida A, Mizoi Y: Molecular basis for subtypic differences of the "a" subunit of coagulation factor XIII with description of the genesis of the subtypes. Hum Genet. 1994 Aug;94(2):129-35. [Article]
  17. Board P, Coggan M, Miloszewski K: Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. [Article]
  18. Kangsadalampai S, Board PG: The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity. Blood. 1998 Oct 15;92(8):2766-70. [Article]
  19. 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. [Article]
  20. Biswas A, Ivaskevicius V, Thomas A, Varvenne M, Brand B, Rott H, Haussels I, Ruehl H, Scholz U, Klamroth R, Oldenburg J: Eight novel F13A1 gene missense mutations in patients with mild FXIII deficiency: in silico analysis suggests changes in FXIII-A subunit structure/function. Ann Hematol. 2014 Oct;93(10):1665-76. doi: 10.1007/s00277-014-2102-4. Epub 2014 Jun 3. [Article]
  21. Souri M, Biswas A, Misawa M, Omura H, Ichinose A: Severe congenital factor XIII deficiency caused by novel W187X and G273V mutations in the F13A gene; diagnosis and classification according to the ISTH/SSC guidelines. Haemophilia. 2014 Mar;20(2):255-62. doi: 10.1111/hae.12298. Epub 2013 Nov 29. [Article]
  22. Borhany M, Handrkova H, Cairo A, Schroeder V, Fatima N, Naz A, Amanat S, Shamsi T, Peyvandi F, Kohler HP: Congenital factor XIII deficiency in Pakistan: characterization of seven families and identification of four novel mutations. Haemophilia. 2014 Jul;20(4):568-74. doi: 10.1111/hae.12340. Epub 2013 Dec 16. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
N-Acetyl-SerineexperimentalunknowntargetDetails
L-Glutamineapproved, investigational, nutraceuticalunknownenzymesubstrateDetails
ProthrombinapprovedyestargetagonistDetails
Anti-inhibitor coagulant complexapproved, investigationalyestargetagonistDetails
Human thrombinapprovedyestargetactivatorDetails
Thrombinapproved, investigationalyestargetactivatorDetails