GenomeNet

Database: UniProt/SWISS-PROT
Entry: F13A_HUMAN
LinkDB: F13A_HUMAN
Original site: F13A_HUMAN 
ID   F13A_HUMAN              Reviewed;         732 AA.
AC   P00488; Q59HA7; Q8N6X2; Q96P24; Q9BX29;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   28-MAR-2018, entry version 217.
DE   RecName: Full=Coagulation factor XIII A chain;
DE            Short=Coagulation factor XIIIa;
DE            EC=2.3.2.13 {ECO:0000269|PubMed:27363989};
DE   AltName: Full=Protein-glutamine gamma-glutamyltransferase A chain;
DE   AltName: Full=Transglutaminase A chain;
DE   Flags: Precursor;
GN   Name=F13A1; Synonyms=F13A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-651.
RX   PubMed=3026437; DOI=10.1021/bi00370a025;
RA   Ichinose A., Hendrickson L.E., Fujikawa K., Davie E.W.;
RT   "Amino acid sequence of the a subunit of human factor XIII.";
RL   Biochemistry 25:6900-6906(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2877457; DOI=10.1073/pnas.83.21.8024;
RA   Grundmann U., Amann E., Zettlmeissl G., Kuepper H.A.;
RT   "Characterization of cDNA coding for human factor XIIIa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8024-8028(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-565.
RX   PubMed=2901091; DOI=10.1073/pnas.85.16.5829;
RA   Ichinose A., Davie E.W.;
RT   "Characterization of the gene for the a subunit of human factor XIII
RT   (plasma transglutaminase), a blood coagulation factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5829-5833(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-652.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-35; ILE-40;
RP   PHE-205; LEU-565; ILE-651 AND GLU-652.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-652.
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-650 AND
RP   GLU-652.
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-731, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT SER-2.
RX   PubMed=2877456; DOI=10.1073/pnas.83.21.8019;
RA   Takahashi N., Takahashi Y., Putnam F.W.;
RT   "Primary structure of blood coagulation factor XIIIa (fibrinoligase,
RT   transglutaminase) from human placenta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8019-8023(1986).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-44.
RX   PubMed=4811064; DOI=10.1021/bi00701a018;
RA   Takagi T., Doolittle R.F.;
RT   "Amino acid sequence studies on factor XIII and the peptide released
RT   during its activation by thrombin.";
RL   Biochemistry 13:750-756(1974).
RN   [10]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=4405643;
RA   Schwartz M.L., Pizzo S.V., Hill R.L., McKee P.A.;
RT   "Human Factor XIII from plasma and platelets. Molecular weights,
RT   subunit structures, proteolytic activation, and cross-linking of
RT   fibrinogen and fibrin.";
RL   J. Biol. Chem. 248:1395-1407(1973).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [12]
RP   REVIEW.
RX   PubMed=21742792; DOI=10.1152/physrev.00016.2010;
RA   Muszbek L., Bereczky Z., Bagoly Z., Komaromi I., Katona E.;
RT   "Factor XIII: a coagulation factor with multiple plasmatic and
RT   cellular functions.";
RL   Physiol. Rev. 91:931-972(2011).
RN   [13]
RP   INTERACTION WITH F13B.
RX   PubMed=26247044; DOI=10.1002/mgg3.138;
RA   Thomas A., Biswas A., Ivaskevicius V., Oldenburg J.;
RT   "Structural and functional influences of coagulation factor XIII
RT   subunit B heterozygous missense mutants.";
RL   Mol. Genet. Genomic Med. 3:258-271(2015).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=7913750; DOI=10.1073/pnas.91.15.7296;
RA   Yee V.C., Pedersen L.C., Trong I.L., Bishop P.D., Stenkamp R.E.,
RA   Teller D.C.;
RT   "Three-dimensional structure of a transglutaminase: human blood
RT   coagulation factor XIII.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7296-7300(1994).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), CALCIUM-BINDING, AND COFACTOR.
RX   PubMed=7660355; DOI=10.1016/0049-3848(95)00072-Y;
RA   Yee V.C., Pedersen L.C., Bishop P.D., Stenkamp R.E., Teller D.C.;
RT   "Structural evidence that the activation peptide is not released upon
RT   thrombin cleavage of factor XIII.";
RL   Thromb. Res. 78:389-397(1995).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=9515726; DOI=10.1016/S0014-5793(98)00098-2;
RA   Weiss M.S., Metzner H.J., Hilgenfeld R.;
RT   "Two non-proline cis peptide bonds may be important for factor XIII
RT   function.";
RL   FEBS Lett. 423:291-296(1998).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=9988734; DOI=10.1074/jbc.274.8.4917;
RA   Fox B.A., Yee V.C., Pedersen L.C., le Trong I., Bishop P.D.,
RA   Stenkamp R.E., Teller D.C.;
RT   "Identification of the calcium binding site and a novel ytterbium site
RT   in blood coagulation factor XIII by X-ray crystallography.";
RL   J. Biol. Chem. 274:4917-4923(1999).
RN   [18]
RP   POLYMORPHISM.
RX   PubMed=7913909; DOI=10.1007/BF00202857;
RA   Suzuki K., Iwata M., Ito S., Matsui K., Uchida A., Mizoi Y.;
RT   "Molecular basis for subtypic differences of the 'a' subunit of
RT   coagulation factor XIII with description of the genesis of the
RT   subtypes.";
RL   Hum. Genet. 94:129-135(1994).
RN   [19]
RP   VARIANT FA13AD HIS-682, AND INVOLVEMENT IN FA13AD.
RX   PubMed=1353995;
RA   Board P., Coggan M., Miloszewski K.;
RT   "Identification of a point mutation in factor XIII A subunit
RT   deficiency.";
RL   Blood 80:937-941(1992).
RN   [20]
RP   CHARACTERIZATION OF VARIANT LEU-35.
RX   PubMed=9763561;
RA   Kangsadalampai S., Board P.G.;
RT   "The Val34Leu polymorphism in the A subunit of coagulation factor XIII
RT   contributes to the large normal range in activity and demonstrates
RT   that the activation peptide plays a role in catalytic activity.";
RL   Blood 92:2766-2770(1998).
RN   [21]
RP   VARIANTS LEU-35; ILE-551; LEU-565; GLN-589; ILE-651 AND GLU-652.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [22]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [23]
RP   VARIANTS FA13AD CYS-168; ARG-290; GLN-541; SER-593; HIS-612 AND
RP   GLY-669.
RX   PubMed=20179087; DOI=10.3324/haematol.2009.017210;
RA   Ivaskevicius V., Biswas A., Bevans C., Schroeder V., Kohler H.P.,
RA   Rott H., Halimeh S., Petrides P.E., Lenk H., Krause M., Miterski B.,
RA   Harbrecht U., Oldenburg J.;
RT   "Identification of eight novel coagulation factor XIII subunit A
RT   mutations: implied consequences for structure and function.";
RL   Haematologica 95:956-962(2010).
RN   [24]
RP   VARIANTS FA13AD LEU-167; GLN-172; TYR-343; ARG-416; PRO-530; LYS-602;
RP   GLN-704 AND GLY-716.
RX   PubMed=24889649; DOI=10.1007/s00277-014-2102-4;
RA   Biswas A., Ivaskevicius V., Thomas A., Varvenne M., Brand B., Rott H.,
RA   Haussels I., Ruehl H., Scholz U., Klamroth R., Oldenburg J.;
RT   "Eight novel F13A1 gene missense mutations in patients with mild FXIII
RT   deficiency: in silico analysis suggests changes in FXIII-A subunit
RT   structure/function.";
RL   Ann. Hematol. 93:1665-1676(2014).
RN   [25]
RP   VARIANT FA13AD VAL-274.
RX   PubMed=24286209; DOI=10.1111/hae.12298;
RA   Souri M., Biswas A., Misawa M., Omura H., Ichinose A.;
RT   "Severe congenital factor XIII deficiency caused by novel W187X and
RT   G273V mutations in the F13A gene; diagnosis and classification
RT   according to the ISTH/SSC guidelines.";
RL   Haemophilia 20:255-262(2014).
RN   [26]
RP   VARIANTS FA13AD ASP-347; ARG-376 AND LEU-414.
RX   PubMed=24329762; DOI=10.1111/hae.12340;
RA   Borhany M., Handrkova H., Cairo A., Schroeder V., Fatima N., Naz A.,
RA   Amanat S., Shamsi T., Peyvandi F., Kohler H.P.;
RT   "Congenital factor XIII deficiency in Pakistan: characterization of
RT   seven families and identification of four novel mutations.";
RL   Haemophilia 20:568-574(2014).
RN   [27]
RP   CHARACTERIZATION VARIANTS FA13AD GLN-38; LEU-167; CYS-168; GLN-172;
RP   ARG-290; TYR-343; ARG-416; PRO-530; GLN-541; SER-593; LYS-602;
RP   HIS-612; GLY-669; GLN-704 AND GLY-716, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=27363989; DOI=10.1002/humu.23041;
RA   Thomas A., Biswas A., Dodt J., Philippou H., Hethershaw E.,
RA   Ensikat H.J., Ivaskevicius V., Oldenburg J.;
RT   "Coagulation factor XIIIA subunit missense mutations affect structure
RT   and function at the various steps of factor XIII action.";
RL   Hum. Mutat. 37:1030-1041(2016).
CC   -!- FUNCTION: Factor XIII is activated by thrombin and calcium ion to
CC       a transglutaminase that catalyzes the formation of gamma-glutamyl-
CC       epsilon-lysine cross-links between fibrin chains, thus stabilizing
CC       the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or
CC       fibronectin, to the alpha chains of fibrin.
CC       {ECO:0000269|PubMed:27363989}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {ECO:0000255|PROSITE-ProRule:PRU10024,
CC       ECO:0000269|PubMed:27363989}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:9988734};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:9988734};
CC   -!- SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains.
CC       {ECO:0000269|PubMed:26247044, ECO:0000269|PubMed:4405643}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted
CC       {ECO:0000269|PubMed:4405643}. Note=Secreted into the blood plasma.
CC       Cytoplasmic in most tissues, but also secreted in the blood
CC       plasma.
CC   -!- PTM: The activation peptide is released by thrombin.
CC   -!- POLYMORPHISM: There are four main allelic forms of this protein;
CC       F13A*1A, F13A*1B, F13A*2A and F13A*2B. In addition two other
CC       intermediate forms (F13A*(2)A and F13A*(2)B) seem to exist. The
CC       sequence shown is that of F13A*(2)B. {ECO:0000305}.
CC   -!- DISEASE: Factor XIII subunit A deficiency (FA13AD) [MIM:613225]:
CC       An autosomal recessive hematologic disorder characterized by a
CC       life-long bleeding tendency, impaired wound healing and
CC       spontaneous abortion in affected women.
CC       {ECO:0000269|PubMed:1353995, ECO:0000269|PubMed:20179087,
CC       ECO:0000269|PubMed:24286209, ECO:0000269|PubMed:24329762,
CC       ECO:0000269|PubMed:24889649, ECO:0000269|PubMed:27363989}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA52489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD92089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/f13a1/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F13A1";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Factor XIII entry;
CC       URL="https://en.wikipedia.org/wiki/Factor_XIII";
DR   EMBL; M14539; AAA52489.1; ALT_INIT; mRNA.
DR   EMBL; M14354; AAA52488.1; -; mRNA.
DR   EMBL; M22001; AAA52415.1; -; Genomic_DNA.
DR   EMBL; M21987; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21988; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21989; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21990; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21991; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21992; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21993; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21995; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21996; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21997; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21998; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M21999; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; M22000; AAA52415.1; JOINED; Genomic_DNA.
DR   EMBL; AB208852; BAD92089.1; ALT_INIT; mRNA.
DR   EMBL; AF418272; AAL12161.1; -; Genomic_DNA.
DR   EMBL; AL157775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027963; AAH27963.1; -; mRNA.
DR   CCDS; CCDS4496.1; -.
DR   PIR; A35583; EKHUX.
DR   RefSeq; NP_000120.2; NM_000129.3.
DR   UniGene; Hs.335513; -.
DR   PDB; 1EVU; X-ray; 2.01 A; A/B=2-732.
DR   PDB; 1EX0; X-ray; 2.00 A; A/B=2-732.
DR   PDB; 1F13; X-ray; 2.10 A; A/B=2-732.
DR   PDB; 1FIE; X-ray; 2.50 A; A/B=2-732.
DR   PDB; 1GGT; X-ray; 2.65 A; A/B=2-732.
DR   PDB; 1GGU; X-ray; 2.10 A; A/B=2-732.
DR   PDB; 1GGY; X-ray; 2.50 A; A/B=2-732.
DR   PDB; 1QRK; X-ray; 2.50 A; A/B=2-732.
DR   PDB; 4KTY; X-ray; 1.98 A; A/B=2-732.
DR   PDB; 5MHL; X-ray; 2.40 A; A/B=2-732.
DR   PDB; 5MHM; X-ray; 2.12 A; A/B=2-732.
DR   PDB; 5MHN; X-ray; 2.48 A; A/B=2-732.
DR   PDB; 5MHO; X-ray; 2.92 A; A/B=2-732.
DR   PDBsum; 1EVU; -.
DR   PDBsum; 1EX0; -.
DR   PDBsum; 1F13; -.
DR   PDBsum; 1FIE; -.
DR   PDBsum; 1GGT; -.
DR   PDBsum; 1GGU; -.
DR   PDBsum; 1GGY; -.
DR   PDBsum; 1QRK; -.
DR   PDBsum; 4KTY; -.
DR   PDBsum; 5MHL; -.
DR   PDBsum; 5MHM; -.
DR   PDBsum; 5MHN; -.
DR   PDBsum; 5MHO; -.
DR   ProteinModelPortal; P00488; -.
DR   SMR; P00488; -.
DR   BioGrid; 108460; 11.
DR   DIP; DIP-377N; -.
DR   IntAct; P00488; 9.
DR   MINT; P00488; -.
DR   STRING; 9606.ENSP00000264870; -.
DR   BindingDB; P00488; -.
DR   ChEMBL; CHEMBL4530; -.
DR   DrugBank; DB00130; L-Glutamine.
DR   DrugBank; DB02340; N-Acetyl-Serine.
DR   iPTMnet; P00488; -.
DR   PhosphoSitePlus; P00488; -.
DR   BioMuta; F13A1; -.
DR   DMDM; 119720; -.
DR   OGP; P00488; -.
DR   EPD; P00488; -.
DR   MaxQB; P00488; -.
DR   PaxDb; P00488; -.
DR   PeptideAtlas; P00488; -.
DR   PRIDE; P00488; -.
DR   TopDownProteomics; P00488; -.
DR   DNASU; 2162; -.
DR   Ensembl; ENST00000264870; ENSP00000264870; ENSG00000124491.
DR   GeneID; 2162; -.
DR   KEGG; hsa:2162; -.
DR   UCSC; uc003mwv.4; human.
DR   CTD; 2162; -.
DR   DisGeNET; 2162; -.
DR   EuPathDB; HostDB:ENSG00000124491.15; -.
DR   GeneCards; F13A1; -.
DR   HGNC; HGNC:3531; F13A1.
DR   HPA; CAB002155; -.
DR   HPA; HPA001804; -.
DR   MalaCards; F13A1; -.
DR   MIM; 134570; gene+phenotype.
DR   MIM; 613225; phenotype.
DR   neXtProt; NX_P00488; -.
DR   Orphanet; 331; Congenital factor XIII deficiency.
DR   PharmGKB; PA162; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; P00488; -.
DR   KO; K03917; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; P00488; -.
DR   TreeFam; TF324278; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
DR   ChiTaRS; F13A1; human.
DR   EvolutionaryTrace; P00488; -.
DR   GeneWiki; Coagulation_factor_XIII,_A1_polypeptide; -.
DR   GenomeRNAi; 2162; -.
DR   PMAP-CutDB; P00488; -.
DR   PRO; PR:P00488; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000124491; -.
DR   CleanEx; HS_F13A1; -.
DR   ExpressionAtlas; P00488; baseline and differential.
DR   Genevisible; P00488; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.90.260.10; -; 1.
DR   InterPro; IPR034810; Factor_XIII_A.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF42; PTHR11590:SF42; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF49309; SSF49309; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Blood coagulation;
KW   Calcium; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Disease mutation; Glycoprotein; Hemostasis; Metal-binding;
KW   Polymorphism; Reference proteome; Secreted; Transferase; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000305|PubMed:2877456,
FT                                ECO:0000305|PubMed:4811064}.
FT   PROPEP        2     38       Activation peptide.
FT                                /FTId=PRO_0000033646.
FT   CHAIN        39    732       Coagulation factor XIII A chain.
FT                                /FTId=PRO_0000033647.
FT   ACT_SITE    315    315       {ECO:0000269|PubMed:7913750}.
FT   ACT_SITE    374    374       {ECO:0000269|PubMed:7913750}.
FT   ACT_SITE    397    397       {ECO:0000269|PubMed:7913750}.
FT   METAL       437    437       Calcium. {ECO:0000269|PubMed:9988734}.
FT   METAL       439    439       Calcium. {ECO:0000269|PubMed:9988734}.
FT   METAL       486    486       Calcium. {ECO:0000269|PubMed:9988734}.
FT   METAL       491    491       Calcium. {ECO:0000269|PubMed:9988734}.
FT   SITE         38     39       Cleavage; by thrombin; to produce active
FT                                factor XIII-A.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000305|PubMed:2877456}.
FT   CARBOHYD    614    614       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952}.
FT   VARIANT      35     35       V -> L (higher specific activity;
FT                                dbSNP:rs5985).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:9763561,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_013927.
FT   VARIANT      38     38       R -> Q (in FA13AD; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; no effect on fibrin
FT                                alpha chain and gamma chain cross-linking
FT                                activity; decreased clot fiber thickness;
FT                                dbSNP:rs759324596).
FT                                {ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077619.
FT   VARIANT      40     40       V -> I. {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_020910.
FT   VARIANT     167    167       P -> L (in FA13AD; mild; no effect on
FT                                intracellular protein abundance; no
FT                                effect on protein-glutamine gamma-
FT                                glutamyltransferase activity; no effect
FT                                on alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; loss of fibrin alpha
FT                                chain cross-linking activity; decreased
FT                                clot fiber thickness).
FT                                {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074280.
FT   VARIANT     168    168       Y -> C (in FA13AD; decreased
FT                                intracellular protein abundance;
FT                                decreased protein-glutamine gamma-
FT                                glutamyltransferase activity; no effect
FT                                on alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; loss of fibrin alpha
FT                                chain cross-linking activity; decreased
FT                                clot fiber thickness).
FT                                {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077620.
FT   VARIANT     172    172       R -> Q (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; decreased rate of
FT                                fibrin gamma chain cross-linking
FT                                activity; decreased rate of fibrin alpha
FT                                chain cross-linking activity; decreased
FT                                clot fiber thickness).
FT                                {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074281.
FT   VARIANT     205    205       Y -> F (in dbSNP:rs3024477).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_020911.
FT   VARIANT     274    274       G -> V (in FA13AD).
FT                                {ECO:0000269|PubMed:24286209}.
FT                                /FTId=VAR_074282.
FT   VARIANT     290    290       P -> R (in FA13AD; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; loss of
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; loss of fibrin gamma
FT                                chain cross-linking activity; decreased
FT                                rate of fibrin alpha chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077621.
FT   VARIANT     343    343       H -> Y (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; loss of fibrin gamma
FT                                chain cross-linking activity; decreased
FT                                rate of fibrin alpha chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074283.
FT   VARIANT     347    347       A -> D (in FA13AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:24329762}.
FT                                /FTId=VAR_074284.
FT   VARIANT     376    376       W -> R (in FA13AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:24329762}.
FT                                /FTId=VAR_074285.
FT   VARIANT     414    414       S -> L (in FA13AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:24329762}.
FT                                /FTId=VAR_074286.
FT   VARIANT     416    416       Q -> R (in FA13AD; mild; no effect on
FT                                intracellular protein abundance; no
FT                                effect on protein-glutamine gamma-
FT                                glutamyltransferase activity; no effect
FT                                on alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; no effect on fibrin
FT                                alpha chain and gamma chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074287.
FT   VARIANT     530    530       L -> P (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; loss of fibrin gamma
FT                                chain cross-linking activity; decreased
FT                                clot fiber thickness).
FT                                {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074288.
FT   VARIANT     541    541       R -> Q (in FA13AD; decreased
FT                                intracellular protein abundance; no
FT                                effect on protein-glutamine gamma-
FT                                glutamyltransferase activity; no effect
FT                                on alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; no effect on fibrin
FT                                alpha chain and gamma chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077622.
FT   VARIANT     551    551       T -> I (in dbSNP:rs5984).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013928.
FT   VARIANT     565    565       P -> L (in allele F13A*1A, allele F13A*2A
FT                                and allele F13*(2)A; dbSNP:rs5982).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:2901091,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_007471.
FT   VARIANT     589    589       L -> Q (in dbSNP:rs5983).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013929.
FT   VARIANT     593    593       G -> S (in FA13AD; no effect on
FT                                intracellular protein abundance;
FT                                increased protein-glutamine gamma-
FT                                glutamyltransferase activity; no effect
FT                                on alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; no effect on fibrin
FT                                alpha chain and gamma chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077623.
FT   VARIANT     602    602       Q -> K (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; loss of
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; decreased rate of
FT                                fibrin gamma chain cross-linking
FT                                activity; loss of fibrin alpha chain
FT                                cross-linking activity; decreased clot
FT                                fiber thickness).
FT                                {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074289.
FT   VARIANT     612    612       R -> H (in FA13AD; decreased
FT                                intracellular protein abundance;
FT                                decreased protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; no effect on fibrin
FT                                alpha chain and gamma chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077624.
FT   VARIANT     650    650       T -> I (in dbSNP:rs17852475).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_060545.
FT   VARIANT     651    651       V -> I (in allele F13A*2A and allele
FT                                F13A*2B; dbSNP:rs5987).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:3026437,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_007472.
FT   VARIANT     652    652       Q -> E (in allele F13A*1A and allele
FT                                F13A*1B; dbSNP:rs5988).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:14574404,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
FT                                /FTId=VAR_007473.
FT   VARIANT     669    669       D -> G (in FA13AD; decreased
FT                                intracellular protein abundance;
FT                                decreased protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; decreased rate of
FT                                fibrin alpha chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:20179087,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_077625.
FT   VARIANT     682    682       R -> H (in FA13AD).
FT                                {ECO:0000269|PubMed:1353995}.
FT                                /FTId=VAR_007474.
FT   VARIANT     704    704       R -> Q (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; decreased rate of
FT                                fibrin alpha chain cross-linking
FT                                activity; decreased clot fiber
FT                                thickness). {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074290.
FT   VARIANT     716    716       R -> G (in FA13AD; mild; decreased
FT                                intracellular protein abundance; loss of
FT                                protein-glutamine gamma-
FT                                glutamyltransferase activity; decreased
FT                                alpha-2-antiplasmin to fibrin cross-
FT                                linking activity; decreased rate of
FT                                fibrin gamma chain cross-linking
FT                                activity; decreased rate of fibrin alpha
FT                                chain cross-linking activity; decreased
FT                                clot fiber thickness).
FT                                {ECO:0000269|PubMed:24889649,
FT                                ECO:0000269|PubMed:27363989}.
FT                                /FTId=VAR_074291.
FT   CONFLICT     36     36       Missing (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       F -> L (in Ref. 1; AAA52488).
FT                                {ECO:0000305}.
FT   STRAND       29     32       {ECO:0000244|PDB:4KTY}.
FT   HELIX        42     44       {ECO:0000244|PDB:4KTY}.
FT   STRAND       48     52       {ECO:0000244|PDB:4KTY}.
FT   HELIX        60     64       {ECO:0000244|PDB:4KTY}.
FT   STRAND       68     71       {ECO:0000244|PDB:1GGU}.
FT   STRAND       74     78       {ECO:0000244|PDB:4KTY}.
FT   STRAND       81     91       {ECO:0000244|PDB:4KTY}.
FT   TURN         95     97       {ECO:0000244|PDB:4KTY}.
FT   STRAND      100    105       {ECO:0000244|PDB:4KTY}.
FT   STRAND      107    109       {ECO:0000244|PDB:4KTY}.
FT   HELIX       112    114       {ECO:0000244|PDB:4KTY}.
FT   STRAND      116    125       {ECO:0000244|PDB:4KTY}.
FT   STRAND      132    139       {ECO:0000244|PDB:4KTY}.
FT   STRAND      142    148       {ECO:0000244|PDB:4KTY}.
FT   STRAND      156    166       {ECO:0000244|PDB:4KTY}.
FT   STRAND      169    172       {ECO:0000244|PDB:4KTY}.
FT   HELIX       177    179       {ECO:0000244|PDB:4KTY}.
FT   STRAND      181    184       {ECO:0000244|PDB:4KTY}.
FT   HELIX       199    205       {ECO:0000244|PDB:4KTY}.
FT   STRAND      210    217       {ECO:0000244|PDB:4KTY}.
FT   STRAND      220    227       {ECO:0000244|PDB:4KTY}.
FT   HELIX       235    245       {ECO:0000244|PDB:4KTY}.
FT   HELIX       250    252       {ECO:0000244|PDB:4KTY}.
FT   HELIX       256    266       {ECO:0000244|PDB:4KTY}.
FT   TURN        270    272       {ECO:0000244|PDB:4KTY}.
FT   STRAND      275    278       {ECO:0000244|PDB:4KTY}.
FT   HELIX       290    292       {ECO:0000244|PDB:4KTY}.
FT   HELIX       297    306       {ECO:0000244|PDB:4KTY}.
FT   STRAND      310    313       {ECO:0000244|PDB:4KTY}.
FT   HELIX       315    329       {ECO:0000244|PDB:4KTY}.
FT   STRAND      333    343       {ECO:0000244|PDB:4KTY}.
FT   STRAND      345    355       {ECO:0000244|PDB:4KTY}.
FT   STRAND      359    361       {ECO:0000244|PDB:4KTY}.
FT   TURN        363    365       {ECO:0000244|PDB:4KTY}.
FT   STRAND      369    381       {ECO:0000244|PDB:4KTY}.
FT   STRAND      384    386       {ECO:0000244|PDB:1GGY}.
FT   STRAND      392    396       {ECO:0000244|PDB:4KTY}.
FT   STRAND      402    404       {ECO:0000244|PDB:4KTY}.
FT   STRAND      406    414       {ECO:0000244|PDB:1EVU}.
FT   HELIX       415    419       {ECO:0000244|PDB:4KTY}.
FT   STRAND      425    428       {ECO:0000244|PDB:4KTY}.
FT   HELIX       429    437       {ECO:0000244|PDB:4KTY}.
FT   STRAND      439    445       {ECO:0000244|PDB:4KTY}.
FT   TURN        447    449       {ECO:0000244|PDB:1FIE}.
FT   STRAND      451    461       {ECO:0000244|PDB:4KTY}.
FT   STRAND      464    468       {ECO:0000244|PDB:4KTY}.
FT   STRAND      470    473       {ECO:0000244|PDB:1EX0}.
FT   STRAND      475    477       {ECO:0000244|PDB:4KTY}.
FT   HELIX       479    482       {ECO:0000244|PDB:4KTY}.
FT   HELIX       489    501       {ECO:0000244|PDB:4KTY}.
FT   STRAND      519    527       {ECO:0000244|PDB:4KTY}.
FT   STRAND      534    542       {ECO:0000244|PDB:4KTY}.
FT   STRAND      544    546       {ECO:0000244|PDB:4KTY}.
FT   STRAND      548    559       {ECO:0000244|PDB:4KTY}.
FT   STRAND      561    563       {ECO:0000244|PDB:5MHO}.
FT   STRAND      565    578       {ECO:0000244|PDB:4KTY}.
FT   STRAND      580    590       {ECO:0000244|PDB:4KTY}.
FT   HELIX       592    595       {ECO:0000244|PDB:4KTY}.
FT   HELIX       596    598       {ECO:0000244|PDB:4KTY}.
FT   STRAND      604    613       {ECO:0000244|PDB:4KTY}.
FT   TURN        614    617       {ECO:0000244|PDB:4KTY}.
FT   STRAND      618    626       {ECO:0000244|PDB:4KTY}.
FT   STRAND      633    639       {ECO:0000244|PDB:4KTY}.
FT   STRAND      647    654       {ECO:0000244|PDB:4KTY}.
FT   STRAND      657    659       {ECO:0000244|PDB:4KTY}.
FT   STRAND      661    670       {ECO:0000244|PDB:4KTY}.
FT   TURN        671    673       {ECO:0000244|PDB:4KTY}.
FT   STRAND      674    684       {ECO:0000244|PDB:4KTY}.
FT   STRAND      689    696       {ECO:0000244|PDB:4KTY}.
FT   STRAND      702    711       {ECO:0000244|PDB:4KTY}.
FT   STRAND      713    727       {ECO:0000244|PDB:4KTY}.
SQ   SEQUENCE   732 AA;  83267 MW;  51A83A9B8B1370D4 CRC64;
     MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS VHLFKERWDT
     NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF RVEYVIGRYP QENKGTYIPV
     PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD
     TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL
     YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL
     LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN
     VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH
     GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD
     TYKFQEGQEE ERLALETALM YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF
     RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL
     EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VQFTNPLKET
     LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG
     ELDVQIQRRP SM
//
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