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 24-JAN-2024, entry version 250. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 15. 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 GlyCosmos; P00488; 1 site, No reported glycans. 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; 9606-ENSP00000264870; -. DR PeptideAtlas; P00488; -. DR ProteomicsDB; 51255; -. DR TopDownProteomics; P00488; -. DR Antibodypedia; 882; 1561 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 AGR; HGNC:3531; -. 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 OMA; EEVCQPW; -. DR OrthoDB; 5344745at2759; -. DR PhylomeDB; P00488; -. DR TreeFam; TF324278; -. DR BioCyc; MetaCyc:ENSG00000124491-MONOMER; -. 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; 12 hits in 1151 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 184 other cell types or tissues. DR ExpressionAtlas; P00488; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:1990234; C:transferase complex; NAS: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; Immunoglobulins; 3. DR Gene3D; 3.90.260.10; Transglutaminase-like; 1. 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; COAGULATION FACTOR XIII A CHAIN; 1. DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 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; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. DR Genevisible; P00488; HS. 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; no FT effect on fibrin alpha chain and gamma chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; no effect on FT alpha-2-antiplasmin to fibrin cross-linking activity; loss FT of fibrin alpha chain cross-linking activity; decreased FT clot 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 FT gamma-glutamyltransferase activity; no effect on FT alpha-2-antiplasmin to fibrin cross-linking activity; loss FT of fibrin alpha chain cross-linking activity; decreased FT clot 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; FT decreased rate of fibrin gamma chain cross-linking FT activity; decreased rate of fibrin alpha chain FT cross-linking activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; loss of FT alpha-2-antiplasmin to fibrin cross-linking activity; loss FT of fibrin gamma chain cross-linking activity; decreased FT rate of fibrin alpha chain cross-linking activity; FT decreased clot fiber 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; loss FT of fibrin gamma chain cross-linking activity; decreased FT rate of fibrin alpha chain cross-linking activity; FT decreased clot fiber 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24329762" FT /id="VAR_074284" FT VARIANT 376 FT /note="W -> R (in FA13AD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24329762" FT /id="VAR_074285" FT VARIANT 414 FT /note="S -> L (in FA13AD; uncertain significance; FT 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 FT gamma-glutamyltransferase activity; no effect on FT alpha-2-antiplasmin to fibrin cross-linking activity; no FT effect on fibrin alpha chain and gamma chain cross-linking FT activity; 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; loss FT of fibrin gamma chain cross-linking activity; decreased FT clot fiber 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 FT gamma-glutamyltransferase activity; no effect on FT alpha-2-antiplasmin to fibrin cross-linking activity; no FT effect on fibrin alpha chain and gamma chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; no effect on FT alpha-2-antiplasmin to fibrin cross-linking activity; no FT effect on fibrin alpha chain and gamma chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; loss of FT alpha-2-antiplasmin to fibrin cross-linking activity; FT decreased rate of fibrin gamma chain cross-linking FT activity; loss of fibrin alpha chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; no FT effect on fibrin alpha chain and gamma chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; FT decreased rate of fibrin alpha chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; FT decreased rate of fibrin alpha chain cross-linking FT activity; decreased clot fiber thickness; FT 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 FT gamma-glutamyltransferase activity; decreased FT alpha-2-antiplasmin to fibrin cross-linking activity; FT decreased rate of fibrin gamma chain cross-linking FT activity; decreased rate of fibrin alpha chain FT cross-linking activity; decreased clot fiber thickness; FT 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 //