F13A_HUMAN
ID F13A_HUMAN Reviewed; 732 AA.
AC P00488; Q59HA7; Q8N6X2; Q96P24; Q9BX29;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 5.
DT 03-AUG-2022, entry version 242.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-651 AND GLN-652.
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], AND VARIANT GLN-652.
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 VARIANTS LEU-565 AND GLN-652.
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].
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].
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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 VARIANT ILE-650.
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 project:
RT 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 during
RT its activation by thrombin.";
RL Biochemistry 13:750-756(1974).
RN [10]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=4405643; DOI=10.1016/s0021-9258(19)44312-3;
RA Schwartz M.L., Pizzo S.V., Hill R.L., McKee P.A.;
RT "Human Factor XIII from plasma and platelets. Molecular weights, subunit
RT structures, proteolytic activation, and cross-linking of fibrinogen and
RT 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., Moore R.J.,
RA 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 cellular
RT 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 subunit B
RT 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 coagulation
RT 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., Stenkamp R.E.,
RA Teller D.C.;
RT "Identification of the calcium binding site and a novel ytterbium site in
RT 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 coagulation
RT factor XIII with description of the genesis of the 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 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 that the
RT 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 AND ILE-651.
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 of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [22]
RP ERRATUM OF PUBMED:10391209.
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 GLY-669.
RX PubMed=20179087; DOI=10.3324/haematol.2009.017210;
RA Ivaskevicius V., Biswas A., Bevans C., Schroeder V., Kohler H.P., Rott H.,
RA Halimeh S., Petrides P.E., Lenk H., Krause M., Miterski B., Harbrecht U.,
RA Oldenburg J.;
RT "Identification of eight novel coagulation factor XIII subunit A mutations:
RT 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 G273V
RT mutations in the F13A gene; diagnosis and classification according to the
RT 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 seven
RT families and identification of four novel mutations.";
RL Haemophilia 20:568-574(2014).
RN [27]
RP CHARACTERIZATION OF 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; HIS-612;
RP GLY-669; GLN-704 AND GLY-716, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27363989; DOI=10.1002/humu.23041;
RA Thomas A., Biswas A., Dodt J., Philippou H., Hethershaw E., Ensikat H.J.,
RA Ivaskevicius V., Oldenburg J.;
RT "Coagulation factor XIIIA subunit missense mutations affect structure and
RT 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 a
CC transglutaminase that catalyzes the formation of gamma-glutamyl-
CC epsilon-lysine cross-links between fibrin chains, thus stabilizing the
CC fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin,
CC to the alpha chains of fibrin. {ECO:0000269|PubMed:27363989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024, 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 -!- INTERACTION:
CC P00488; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-2565863, EBI-12015080;
CC P00488; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-2565863, EBI-1773949;
CC P00488; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-2565863, EBI-7247651;
CC P00488; Q99944: EGFL8; NbExp=3; IntAct=EBI-2565863, EBI-3924130;
CC P00488; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-2565863, EBI-10213520;
CC P00488; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-2565863, EBI-21567429;
CC P00488; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-2565863, EBI-11793142;
CC P00488; Q14005-2: IL16; NbExp=3; IntAct=EBI-2565863, EBI-17178971;
CC P00488; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-2565863, EBI-714379;
CC P00488; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-2565863, EBI-9088829;
CC P00488; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-2565863, EBI-9091052;
CC P00488; P19388: POLR2E; NbExp=3; IntAct=EBI-2565863, EBI-395189;
CC P00488; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-2565863, EBI-25835994;
CC P00488; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-2565863, EBI-25839575;
CC P00488; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-2565863, EBI-10182463;
CC P00488; O15273: TCAP; NbExp=3; IntAct=EBI-2565863, EBI-954089;
CC P00488; O60830: TIMM17B; NbExp=3; IntAct=EBI-2565863, EBI-2372529;
CC P00488; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-2565863, EBI-9089156;
CC P00488; O60636: TSPAN2; NbExp=3; IntAct=EBI-2565863, EBI-3914288;
CC P00488; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-2565863, EBI-12040603;
CC P00488; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-2565863, EBI-25830993;
CC P00488; Q7Z783; NbExp=3; IntAct=EBI-2565863, EBI-9088990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted {ECO:0000269|PubMed:4405643}.
CC Note=Secreted into the blood plasma. Cytoplasmic in most tissues, but
CC also secreted in the blood 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*1B. {ECO:0000269|PubMed:7913909}.
CC -!- DISEASE: Factor XIII subunit A deficiency (FA13AD) [MIM:613225]: An
CC autosomal recessive hematologic disorder characterized by a life-long
CC bleeding tendency, impaired wound healing and spontaneous abortion in
CC affected women. {ECO:0000269|PubMed:1353995,
CC ECO:0000269|PubMed:20179087, ECO:0000269|PubMed:24286209,
CC ECO:0000269|PubMed:24329762, ECO:0000269|PubMed:24889649,
CC ECO:0000269|PubMed:27363989}. Note=The disease is caused by variants
CC affecting the gene 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=Wikipedia; Note=Factor XIII entry;
CC URL="https://en.wikipedia.org/wiki/Factor_XIII";
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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 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 AlphaFoldDB; P00488; -.
DR SMR; P00488; -.
DR BioGRID; 108460; 13.
DR ComplexPortal; CPX-6231; Coagulation factor XIIIa complex.
DR DIP; DIP-377N; -.
DR IntAct; P00488; 33.
DR MINT; P00488; -.
DR STRING; 9606.ENSP00000264870; -.
DR BindingDB; P00488; -.
DR ChEMBL; CHEMBL4530; -.
DR DrugBank; DB13151; Anti-inhibitor coagulant complex.
DR DrugBank; DB11571; Human thrombin.
DR DrugBank; DB00130; L-Glutamine.
DR DrugBank; DB02340; N-Acetyl-Serine.
DR DrugBank; DB11311; Prothrombin.
DR DrugBank; DB11300; Thrombin.
DR DrugCentral; P00488; -.
DR GlyGen; P00488; 1 site.
DR iPTMnet; P00488; -.
DR PhosphoSitePlus; P00488; -.
DR BioMuta; F13A1; -.
DR DMDM; 119720; -.
DR OGP; P00488; -.
DR EPD; P00488; -.
DR jPOST; P00488; -.
DR MassIVE; P00488; -.
DR MaxQB; P00488; -.
DR PaxDb; P00488; -.
DR PeptideAtlas; P00488; -.
DR PRIDE; P00488; -.
DR ProteomicsDB; 51255; -.
DR TopDownProteomics; P00488; -.
DR Antibodypedia; 882; 1392 antibodies from 42 providers.
DR DNASU; 2162; -.
DR Ensembl; ENST00000264870.8; ENSP00000264870.3; ENSG00000124491.16.
DR GeneID; 2162; -.
DR KEGG; hsa:2162; -.
DR MANE-Select; ENST00000264870.8; ENSP00000264870.3; NM_000129.4; NP_000120.2.
DR UCSC; uc003mwv.4; human.
DR CTD; 2162; -.
DR DisGeNET; 2162; -.
DR GeneCards; F13A1; -.
DR HGNC; HGNC:3531; F13A1.
DR HPA; ENSG00000124491; Tissue enhanced (adipose tissue, placenta).
DR MalaCards; F13A1; -.
DR MIM; 134570; gene+phenotype.
DR MIM; 613225; phenotype.
DR neXtProt; NX_P00488; -.
DR OpenTargets; ENSG00000124491; -.
DR Orphanet; 331; Congenital factor XIII deficiency.
DR PharmGKB; PA162; -.
DR VEuPathDB; HostDB:ENSG00000124491; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; P00488; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; P00488; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; P00488; -.
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 Interleukin-13 signaling.
DR SignaLink; P00488; -.
DR BioGRID-ORCS; 2162; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; F13A1; human.
DR EvolutionaryTrace; P00488; -.
DR GeneWiki; Coagulation_factor_XIII,_A1_polypeptide; -.
DR GenomeRNAi; 2162; -.
DR Pharos; P00488; Tchem.
DR PRO; PR:P00488; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P00488; protein.
DR Bgee; ENSG00000124491; Expressed in monocyte and 183 other tissues.
DR ExpressionAtlas; P00488; baseline and differential.
DR Genevisible; P00488; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IC:ComplexPortal.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:1990234; C:transferase complex; IC:ComplexPortal.
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:ProtInc.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
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; IPR038765; Papain-like_cys_pep_sf.
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; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Blood coagulation; Calcium;
KW Cytoplasm; Direct protein sequencing; Disease variant; Glycoprotein;
KW Hemostasis; Metal-binding; Reference proteome; Secreted; Transferase;
KW Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:2877456,
FT ECO:0000305|PubMed:4811064"
FT PROPEP 2..38
FT /note="Activation peptide"
FT /id="PRO_0000033646"
FT CHAIN 39..732
FT /note="Coagulation factor XIII A chain"
FT /id="PRO_0000033647"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000269|PubMed:7913750"
FT ACT_SITE 374
FT /evidence="ECO:0000269|PubMed:7913750"
FT ACT_SITE 397
FT /evidence="ECO:0000269|PubMed:7913750"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9988734"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9988734"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9988734"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9988734"
FT SITE 38..39
FT /note="Cleavage; by thrombin; to produce active factor
FT XIII-A"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:2877456"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VARIANT 35
FT /note="V -> L (higher specific activity; dbSNP:rs5985)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:9763561"
FT /id="VAR_013927"
FT VARIANT 38
FT /note="R -> Q (in FA13AD; decreased intracellular protein
FT abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; no effect on fibrin alpha
FT chain and gamma chain cross-linking activity; decreased
FT clot fiber thickness; dbSNP:rs759324596)"
FT /evidence="ECO:0000269|PubMed:27363989"
FT /id="VAR_077619"
FT VARIANT 40
FT /note="V -> I (in dbSNP:rs3024472)"
FT /id="VAR_020910"
FT VARIANT 167
FT /note="P -> L (in FA13AD; mild; no effect on intracellular
FT protein abundance; no effect on protein-glutamine gamma-
FT glutamyltransferase activity; no effect on alpha-2-
FT antiplasmin to fibrin cross-linking activity; loss of
FT fibrin alpha chain cross-linking activity; decreased clot
FT fiber thickness; dbSNP:rs746272012)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074280"
FT VARIANT 168
FT /note="Y -> C (in FA13AD; decreased intracellular protein
FT abundance; decreased protein-glutamine gamma-
FT glutamyltransferase activity; no effect on alpha-2-
FT antiplasmin to fibrin cross-linking activity; loss of
FT fibrin alpha chain cross-linking activity; decreased clot
FT fiber thickness; dbSNP:rs779361778)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077620"
FT VARIANT 172
FT /note="R -> Q (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; decreased rate of fibrin
FT gamma chain cross-linking activity; decreased rate of
FT fibrin alpha chain cross-linking activity; decreased clot
FT fiber thickness; dbSNP:rs376147795)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074281"
FT VARIANT 205
FT /note="Y -> F (in dbSNP:rs3024477)"
FT /id="VAR_020911"
FT VARIANT 274
FT /note="G -> V (in FA13AD)"
FT /evidence="ECO:0000269|PubMed:24286209"
FT /id="VAR_074282"
FT VARIANT 290
FT /note="P -> R (in FA13AD; decreased intracellular protein
FT abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; loss of alpha-2-antiplasmin
FT to fibrin cross-linking activity; loss of fibrin gamma
FT chain cross-linking activity; decreased rate of fibrin
FT alpha chain cross-linking activity; decreased clot fiber
FT thickness)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077621"
FT VARIANT 343
FT /note="H -> Y (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; loss of fibrin gamma
FT chain cross-linking activity; decreased rate of fibrin
FT alpha chain cross-linking activity; decreased clot fiber
FT thickness)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074283"
FT VARIANT 347
FT /note="A -> D (in FA13AD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24329762"
FT /id="VAR_074284"
FT VARIANT 376
FT /note="W -> R (in FA13AD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24329762"
FT /id="VAR_074285"
FT VARIANT 414
FT /note="S -> L (in FA13AD; unknown pathological
FT significance; dbSNP:rs1396702202)"
FT /evidence="ECO:0000269|PubMed:24329762"
FT /id="VAR_074286"
FT VARIANT 416
FT /note="Q -> R (in FA13AD; mild; no effect on intracellular
FT protein abundance; no effect on protein-glutamine gamma-
FT glutamyltransferase activity; no effect on alpha-2-
FT antiplasmin to fibrin cross-linking activity; no effect on
FT fibrin alpha chain and gamma chain cross-linking activity;
FT decreased clot fiber thickness)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074287"
FT VARIANT 530
FT /note="L -> P (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; loss of fibrin gamma
FT chain cross-linking activity; decreased clot fiber
FT thickness)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074288"
FT VARIANT 541
FT /note="R -> Q (in FA13AD; decreased intracellular protein
FT abundance; no effect on protein-glutamine gamma-
FT glutamyltransferase activity; no effect on alpha-2-
FT antiplasmin to fibrin cross-linking activity; no effect on
FT fibrin alpha chain and gamma chain cross-linking activity;
FT decreased clot fiber thickness; dbSNP:rs367679357)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077622"
FT VARIANT 551
FT /note="T -> I (in dbSNP:rs5984)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013928"
FT VARIANT 565
FT /note="P -> L (in allele F13A*1A, allele F13A*2A and allele
FT F13*(2)A; dbSNP:rs5982)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:2901091, ECO:0000269|PubMed:7913909"
FT /id="VAR_007471"
FT VARIANT 589
FT /note="L -> Q (in dbSNP:rs5983)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013929"
FT VARIANT 593
FT /note="G -> S (in FA13AD; no effect on intracellular
FT protein abundance; increased protein-glutamine gamma-
FT glutamyltransferase activity; no effect on alpha-2-
FT antiplasmin to fibrin cross-linking activity; no effect on
FT fibrin alpha chain and gamma chain cross-linking activity;
FT decreased clot fiber thickness; dbSNP:rs138754417)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077623"
FT VARIANT 602
FT /note="Q -> K (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; loss of alpha-2-antiplasmin
FT to fibrin cross-linking activity; decreased rate of fibrin
FT gamma chain cross-linking activity; loss of fibrin alpha
FT chain cross-linking activity; decreased clot fiber
FT thickness; dbSNP:rs757172838)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074289"
FT VARIANT 612
FT /note="R -> H (in FA13AD; decreased intracellular protein
FT abundance; decreased protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; no effect on fibrin alpha
FT chain and gamma chain cross-linking activity; decreased
FT clot fiber thickness; dbSNP:rs369187276)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077624"
FT VARIANT 650
FT /note="T -> I (in dbSNP:rs17852475)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060545"
FT VARIANT 651
FT /note="V -> I (in allele F13A*2A and allele F13A*2B;
FT dbSNP:rs5987)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:3026437, ECO:0000269|PubMed:7913909"
FT /id="VAR_007472"
FT VARIANT 652
FT /note="E -> Q (in allele F13A*2A and allele F13A*2B;
FT dbSNP:rs5988)"
FT /evidence="ECO:0000269|PubMed:2877457,
FT ECO:0000269|PubMed:2901091, ECO:0000269|PubMed:3026437,
FT ECO:0000269|PubMed:7913909"
FT /id="VAR_007473"
FT VARIANT 669
FT /note="D -> G (in FA13AD; decreased intracellular protein
FT abundance; decreased protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; decreased rate of fibrin
FT alpha chain cross-linking activity; decreased clot fiber
FT thickness; dbSNP:rs375129902)"
FT /evidence="ECO:0000269|PubMed:20179087,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_077625"
FT VARIANT 682
FT /note="R -> H (in FA13AD; dbSNP:rs121913064)"
FT /evidence="ECO:0000269|PubMed:1353995"
FT /id="VAR_007474"
FT VARIANT 704
FT /note="R -> Q (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; decreased rate of fibrin
FT alpha chain cross-linking activity; decreased clot fiber
FT thickness; dbSNP:rs377484555)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074290"
FT VARIANT 716
FT /note="R -> G (in FA13AD; mild; decreased intracellular
FT protein abundance; loss of protein-glutamine gamma-
FT glutamyltransferase activity; decreased alpha-2-antiplasmin
FT to fibrin cross-linking activity; decreased rate of fibrin
FT gamma chain cross-linking activity; decreased rate of
FT fibrin alpha chain cross-linking activity; decreased clot
FT fiber thickness; dbSNP:rs778206273)"
FT /evidence="ECO:0000269|PubMed:24889649,
FT ECO:0000269|PubMed:27363989"
FT /id="VAR_074291"
FT CONFLICT 36
FT /note="Missing (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="F -> L (in Ref. 2; AAA52488)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1GGU"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 315..329
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 333..343
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 369..381
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1GGY"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:1EVU"
FT HELIX 415..419
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:1FIE"
FT STRAND 451..461
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1EX0"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 489..501
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 519..527
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 534..542
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 548..559
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:5MHO"
FT STRAND 565..578
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 580..590
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:4KTY"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 604..613
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 618..626
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 633..639
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 661..670
FT /evidence="ECO:0007829|PDB:4KTY"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 674..684
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 689..696
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 702..711
FT /evidence="ECO:0007829|PDB:4KTY"
FT STRAND 713..727
FT /evidence="ECO:0007829|PDB:4KTY"
SQ SEQUENCE 732 AA; 83268 MW; 4B6820414B09B0D4 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 VEFTNPLKET
LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG
ELDVQIQRRP SM
