Hmdb loader
Identification
HMDB Protein ID HMDBP00672
Secondary Accession Numbers
  • 5945
Name Coagulation factor XIII A chain
Synonyms
  1. Coagulation factor XIIIa
  2. Protein-glutamine gamma-glutamyltransferase A chain
  3. Transglutaminase A chain
Gene Name F13A1
Protein Type Unknown
Biological Properties
General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Specific 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.
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
  • Complement and coagulation cascades
  • 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
Protein glutamine + alkylamine → protein N(5)-alkylglutamine + Ammonia details
GO Classification
Biological Process
platelet activation
platelet degranulation
peptide cross-linking
Cellular Component
platelet alpha granule lumen
extracellular region
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring amino-acyl groups
protein-glutamine gamma-glutamyltransferase activity
Molecular Function
metal ion binding
protein-glutamine gamma-glutamyltransferase activity
Process
metabolic process
macromolecule metabolic process
post-translational protein modification
peptide cross-linking
macromolecule modification
protein modification process
Cellular Location
  1. Cytoplasm
  2. Secreted
Gene Properties
Chromosome Location 6
Locus 6p25.3-p24.3
SNPs F13A1
Gene Sequence
>2199 bp
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
Protein Properties
Number of Residues 732
Molecular Weight 83267.785
Theoretical pI 5.995
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Coagulation factor XIII A chain
MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDT
NKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPV
PIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETD
TYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCL
YVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDIL
LEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGN
VNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKH
GHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITD
TYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITF
RNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLL
EQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKET
LRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYG
ELDVQIQRRPSM
GenBank ID Protein 119395709
UniProtKB/Swiss-Prot ID P00488
UniProtKB/Swiss-Prot Entry Name F13A_HUMAN
PDB IDs
GenBank Gene ID NM_000129.3
GeneCard ID F13A1
GenAtlas ID F13A1
HGNC ID HGNC:3531
References
General References
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  3. 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. [PubMed:16335952 ]
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  5. 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. [PubMed:3026437 ]
  6. 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. [PubMed:2877457 ]
  7. 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. [PubMed:2901091 ]
  8. 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. [PubMed:2877456 ]
  9. 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. [PubMed:4811064 ]
  10. 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. [PubMed:7913750 ]
  11. 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. [PubMed:7660355 ]
  12. 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. [PubMed:9515726 ]
  13. 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. [PubMed:9988734 ]
  14. 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. [PubMed:7913909 ]
  15. 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. [PubMed:1353995 ]
  16. 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. [PubMed:9763561 ]