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UniProtKB/Swiss-Prot entry P00488


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F13A_HUMAN
Primary accession number P00488
Secondary accession numbers Q59HA7 Q8N6X2 Q96P24
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 125)
Name and origin of the protein
Protein name Coagulation factor XIII A chain [Precursor]
Synonyms Coagulation factor XIIIa
EC 2.3.2.13
Protein-glutamine gamma-glutamyltransferase A chain
Transglutaminase A chain
Gene name
Name: F13A1
Synonyms: F13A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2901091 [NCBI, ExPASy, EBI, Israel, Japan]
Ichinose A., Davie E.W.;
"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. 85:5829-5833(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00370a025; PubMed=3026437 [NCBI, ExPASy, EBI, Israel, Japan]
Ichinose A., Hendrickson L.E., Fujikawa K., Davie E.W.;
"Amino acid sequence of the a subunit of human factor XIII.";
Biochemistry 25:6900-6906(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2877457 [NCBI, ExPASy, EBI, Israel, Japan]
Grundmann U., Amann E., Zettlmeissl G., Kuepper H.A.;
"Characterization of cDNA coding for human factor XIIIa.";
Proc. Natl. Acad. Sci. U.S.A. 83:8024-8028(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-35; ILE-40; PHE-205; LEU-565; ILE-651 AND GLU-652.
Rieder M.J., Carrington D.P., Chung M.-W., Lee K.L., Poel C.L., Yi Q., Nickerson D.A.;
"SeattleSNPs. NHLBI HL66682 program for genomic applications, UW-FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu).";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-652.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-652.
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-731.
PubMed=2877456 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi N., Takahashi Y., Putnam F.W.;
"Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta.";
Proc. Natl. Acad. Sci. U.S.A. 83:8019-8023(1986).
[8]
PROTEIN SEQUENCE OF 2-44.
DOI=10.1021/bi00701a018; PubMed=4811064 [NCBI, ExPASy, EBI, Israel, Japan]
Takagi T., Doolittle R.F.;
"Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin.";
Biochemistry 13:750-756(1974).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=7913750 [NCBI, ExPASy, EBI, Israel, Japan]
Yee V.C., Pedersen L.C., Trong I.L., Bishop P.D., Stenkamp R.E., Teller D.C.;
"Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.";
Proc. Natl. Acad. Sci. U.S.A. 91:7296-7300(1994).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/0049-3848(95)00072-Y; PubMed=7660355 [NCBI, ExPASy, EBI, Israel, Japan]
Yee V.C., Pedersen L.C., Bishop P.D., Stenkamp R.E., Teller D.C.;
"Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII.";
Thromb. Res. 78:389-397(1995).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1016/S0014-5793(98)00098-2; PubMed=9515726 [NCBI, ExPASy, EBI, Israel, Japan]
Weiss M.S., Metzner H.J., Hilgenfeld R.;
"Two non-proline cis peptide bonds may be important for factor XIII function.";
FEBS Lett. 423:291-296(1998).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1074/jbc.274.8.4917; PubMed=9988734 [NCBI, ExPASy, EBI, Israel, Japan]
Fox B.A., Yee V.C., Pedersen L.C., le Trong I., Bishop P.D., Stenkamp R.E., Teller D.C.;
"Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography.";
J. Biol. Chem. 274:4917-4923(1999).
[14]
POLYMORPHISM.
DOI=10.1007/BF00202857; PubMed=7913909 [NCBI, ExPASy, EBI, Israel, Japan]
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. 94:129-135(1994).
[15]
VARIANT F13A DEFICIENCY HIS-682.
PubMed=1353995 [NCBI, ExPASy, EBI, Israel, Japan]
Board P., Coggan M., Miloszewski K.;
"Identification of a point mutation in factor XIII A subunit deficiency.";
Blood 80:937-941(1992).
[16]
CHARACTERIZATION OF VARIANT LEU-35.
PubMed=9763561 [NCBI, ExPASy, EBI, Israel, Japan]
Kangsadalampai S., Board P.G.;
"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 92:2766-2770(1998).
[17]
VARIANTS LEU-35; ILE-551; LEU-565; GLN-589; ILE-651 AND GLU-652.
DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan]
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions of human genes.";
Nat. Genet. 22:231-238(1999).
[18]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.;
Nat. Genet. 23:373-373(1999).
Comments
  • 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.
  • CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N5-alkylglutamine + NH3.
  • COFACTOR: Binds 1 calcium ion per subunit.
  • SUBUNIT: Tetramer of two A chains and two B chains.
  • SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.
  • PTM: The activation peptide is released by thrombin.
  • POLYMORPHISM: There are four main allelic forms of this protein; F13A*1A, F13A*1B, F13A*2A and F13A*2B. In addition two other intermediate forms (F13A*(2)A and F13A*(2)B) seem to exist. The sequence shown is that of F13A*(2)B.
  • DISEASE: Defects in F13A1 are the cause of F13A deficiency [MIM:134570]. F13A deficiency is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. In addition to the common presentation such as subcutaneous and intramuscular haematomas, severe bleeding such as intracranial hemorrhages may occur.
  • SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=F13A1";.
  • WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F13A1";.
  • WEB RESOURCE: Name=Wikipedia; Note=Factor XIII entry; URL="http://en.wikipedia.org/wiki/Factor_XIII";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M22001; AAA52415.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21987; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21988; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21989; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21990; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21991; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21992; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21993; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21995; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21996; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21997; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21998; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21999; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22000; AAA52415.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14539; AAA52489.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14354; AAA52488.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF418272; AAL12161.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB208852; BAD92089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027963; AAH27963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35583; EKHUX.
RefSeq NP_000120.2; -.
UniGene Hs.335513
3D structure databases
PDB
1EVU; X-ray; 2.01 A; A/B=3-732.[ExPASy / RCSB / EBI]
1EX0; X-ray; 2.00 A; A/B=3-732.[ExPASy / RCSB / EBI]
1F13; X-ray; 2.10 A; A/B=1-732.[ExPASy / RCSB / EBI]
1FIE; X-ray; 2.50 A; A/B=1-732.[ExPASy / RCSB / EBI]
1GGT; X-ray; 2.65 A; A/B=1-732.[ExPASy / RCSB / EBI]
1GGU; X-ray; 2.10 A; A/B=1-732.[ExPASy / RCSB / EBI]
1GGY; X-ray; 2.50 A; A/B=1-732.[ExPASy / RCSB / EBI]
1QRK; X-ray; 2.50 A; A/B=1-732.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EVU; -.
1EX0; -.
1F13; -.
1FIE; -.
1GGT; -.
1GGU; -.
1GGY; -.
1QRK; -.
ModBase P00488.
Protein-protein interaction databases
DIP DIP:377N; -.
PTM databases
PhosphoSite P00488; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
Polymorphism databases
SeattleSNPs F13A1.
2D gel databases
OGP P00488; -.
Organism-specific databases
HGNC HGNC:3531; F13A1.
GenAtlas F13A1.
HPA CAB002155; -.
HPA001804; -.
MIM 134570; gene+phenotype. [NCBI / EBI]
Orphanet 331; Factor XIII deficiency, congenital.
PharmGKB PA162; -.
GeneCards P00488.
Gene expression databases
ArrayExpress P00488; -.
CleanEx HS_F13A1; -.
GermOnline ENSG00000124491; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (traceable author statement from ProtInc).
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (traceable author statement from ProtInc).
GO:0007596; Biological process: blood coagulation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.
Pfam PF00927; Transglut_C; 2.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.
SMART SM00460; TGc; 1.
SMART graphical view of domain structure.
PROSITE PS00547; TRANSGLUTAMINASES; 1.
BLOCKS P00488.
Other
SWISS-3DIMAGE P00488.
Genome annotation databases
Ensembl ENSG00000124491; Homo sapiens. [Contig view]
GeneID 2162; -.
KEGG hsa:2162; -.
Phylogenomic databases
HOVERGEN P00488; -.
Other
DrugBank DB00130; L-Glutamine.
LinkHub P00488; -.
SOURCE F13A1; Homo sapiens.
ProtoNet P00488.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Acyltransferase; Blood coagulation; Calcium; Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein; Metal-binding; Polymorphism; Secreted; Transferase; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
PROPEP   2    38  37     Activation peptide. PRO_0000033646
CHAIN   39   732  694     Coagulation factor XIII A chain. PRO_0000033647
ACT_SITE   315   315         
ACT_SITE   374   374         
ACT_SITE   397   397         
METAL   437   437        Calcium. 
METAL   439   439        Calcium. 
METAL   486   486        Calcium. 
METAL   491   491        Calcium. 
SITE   38    39  2     Cleavage; by thrombin; to produce active factor XIII-A. 
MOD_RES   2     2        N-acetylserine. 
CARBOHYD   614   614        N-linked (GlcNAc...). 
VARIANT   35    35  1     V -> L (higher specific activity; dbSNP:rs5985 [NCBI]). VAR_013927 
VARIANT   40    40  1     V -> I. VAR_020910 
VARIANT   205   205  1     Y -> F. VAR_020911 
VARIANT   551   551  1     T -> I (in dbSNP:rs5984 [NCBI]). VAR_013928 
VARIANT   565   565  1     P -> L (in allele F13A*1A, allele F13A*2A and allele F13*(2)A; dbSNP:rs5982 [NCBI]). VAR_007471 
VARIANT   589   589  1     L -> Q (in dbSNP:rs5983 [NCBI]). VAR_013929 
VARIANT   651   651  1     V -> I (in allele F13A*2A and allele F13A*2B; dbSNP:rs5987 [NCBI]). VAR_007472 
VARIANT   652   652  1     Q -> E (in allele F13A*1A and allele F13A*1B; dbSNP:rs5988 [NCBI]). VAR_007473 
VARIANT   682   682  1     R -> H (in F13A deficiency). VAR_007474 
CONFLICT   36    36        Missing (in Ref. 8; AA sequence). 
CONFLICT   89    89        F -> L (in Ref. 3; AAA52488). 
CONFLICT   650   650        T -> I (in Ref. 6). 
STRAND   48    52  5      
HELIX   60    64  5      
STRAND   74    78  5      
STRAND   83    91  9      
TURN   95    97  3      
STRAND   100   105  6      
STRAND   107   109  3      
HELIX   112   114  3      
STRAND   116   120  5      
STRAND   122   125  4      
STRAND   132   139  8      
STRAND   142   148  7      
STRAND   156   166  11      
STRAND   169   172  4      
HELIX   177   179  3      
STRAND   181   184  4      
HELIX   199   205  7      
STRAND   210   217  8      
STRAND   220   227  8      
HELIX   235   245  11      
HELIX   250   252  3      
HELIX   256   267  12      
STRAND   274   278  5      
TURN   290   292  3      
HELIX   297   306  10      
STRAND   310   313  4      
HELIX   315   329  15      
STRAND   333   341  9      
STRAND   348   355  8      
TURN   363   365  3      
STRAND   371   381  11      
STRAND   392   403  12      
STRAND   406   414  9      
HELIX   415   420  6      
STRAND   425   428  4      
HELIX   429   437  9      
STRAND   439   445  7      
STRAND   451   457  7      
STRAND   464   468  5      
STRAND   470   473  4      
STRAND   475   477  3      
HELIX   479   482  4      
HELIX   489   500  12      
STRAND   519   525  7      
STRAND   534   542  9      
STRAND   544   546  3      
STRAND   548   559  12      
STRAND   565   578  14      
STRAND   580   590  11      
HELIX   592   594  3      
TURN   595   598  4      
STRAND   604   613  10      
TURN   614   616  3      
STRAND   619   627  9      
STRAND   634   639  6      
STRAND   647   654  8      
STRAND   657   659  3      
STRAND   661   669  9      
TURN   671   673  3      
STRAND   677   684  8