ID FA10_HUMAN Reviewed; 488 AA. AC P00742; Q14340; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 27-MAR-2024, entry version 279. DE RecName: Full=Coagulation factor X; DE EC=3.4.21.6; DE AltName: Full=Stuart factor; DE AltName: Full=Stuart-Prower factor; DE Contains: DE RecName: Full=Factor X light chain; DE Contains: DE RecName: Full=Factor X heavy chain; DE Contains: DE RecName: Full=Activated factor Xa heavy chain; DE Flags: Precursor; GN Name=F10; 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]. RX PubMed=1902434; DOI=10.1016/0378-1119(91)90141-w; RA Messier T.L., Pittman D.D., Long G.L., Kaufman R.J., Church W.R.; RT "Cloning and expression in COS-1 cells of a full-length cDNA encoding human RT coagulation factor X."; RL Gene 99:291-294(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3768336; DOI=10.1021/bi00366a018; RA Leytus S.P., Foster D.C., Kurachi K., Davie E.W.; RT "Gene for human factor X: a blood coagulation factor whose gene RT organization is essentially identical with that of factor IX and protein RT C."; RL Biochemistry 25:5098-5102(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-152 AND ARG-192. RG SeattleSNPs variation discovery resource; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-488. RX PubMed=2582420; DOI=10.1073/pnas.82.11.3591; RA Fung M.R., Hay C.W., McGillivray R.T.A.; RT "Characterization of an almost full-length cDNA coding for human blood RT coagulation factor X."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3591-3595(1985). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-488. RC TISSUE=Liver; RX PubMed=3011603; DOI=10.1016/0378-1119(86)90112-5; RA Kaul R.K., Hildebrand B., Roberts S., Jagadeeswaran P.; RT "Isolation and characterization of human blood-coagulation factor X cDNA."; RL Gene 41:311-314(1986). RN [7] RP PROTEIN SEQUENCE OF 41-179, HYDROXYLATION AT ASP-103, AND RP GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; RP GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-79. RX PubMed=6871167; DOI=10.1021/bi00281a016; RA McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N., Kwa E.Y., RA Weinstein B.; RT "Complete amino acid sequence of the light chain of human blood coagulation RT factor X: evidence for identification of residue 63 as beta-hydroxyaspartic RT acid."; RL Biochemistry 22:2875-2884(1983). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-488, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=6587384; DOI=10.1073/pnas.81.12.3699; RA Leytus S.P., Chung D.W., Kisiel W., Kurachi K., Davie E.W.; RT "Characterization of a cDNA coding for human factor X."; RL Proc. Natl. Acad. Sci. U.S.A. 81:3699-3702(1984). RN [9] RP PROTEIN SEQUENCE OF 183-234, AND GLYCOSYLATION AT THR-199; THR-211; ASN-221 RP AND ASN-231. RX PubMed=8243461; DOI=10.1111/j.1432-1033.1993.tb18361.x; RA Inoue K., Morita T.; RT "Identification of O-linked oligosaccharide chains in the activation RT peptides of blood coagulation factor X. The role of the carbohydrate RT moieties in the activation of factor X."; RL Eur. J. Biochem. 218:153-163(1993). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. RX PubMed=2612918; DOI=10.1016/0378-1119(89)90529-5; RA Jagadeeswaran P., Reddy S.V., Rao K.J., Hamsabhushanam K., Lyman G.; RT "Cloning and characterization of the 5' end (exon 1) of the gene encoding RT human factor X."; RL Gene 84:517-519(1989). RN [11] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583; RA Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.; RT "Mechanism of inhibition of activated protein C by protein C inhibitor."; RL J. Biochem. 95:187-195(1984). RN [12] RP PROTEOLYTIC CLEAVAGE. RX PubMed=8920993; DOI=10.1042/bj3190873; RA Plescia J., Altieri D.C.; RT "Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G RT defines an alternative pathway of leucocyte initiation of coagulation."; RL Biochem. J. 319:873-879(1996). RN [13] RP ACTIVITY REGULATION. RX PubMed=20427285; DOI=10.1074/jbc.m110.112748; RA Huang X., Dementiev A., Olson S.T., Gettins P.G.; RT "Basis for the specificity and activation of the serpin protein Z-dependent RT proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor RT Xa."; RL J. Biol. Chem. 285:20399-20409(2010). RN [14] RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278. RX PubMed=8355279; DOI=10.1006/jmbi.1993.1441; RA Padmanabhan K., Padmanabhan K.P., Tulinsky A., Park C.H., Bode W., RA Huber R., Blankenship D.T., Cardin A.D., Kisiel W.; RT "Structure of human des(1-45) factor Xa at 2.2-A resolution."; RL J. Mol. Biol. 232:947-966(1993). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278. RX PubMed=9618463; DOI=10.1073/pnas.95.12.6630; RA Kamata K., Kawamoto H., Honma T., Iwama T., Kim S.H.; RT "Structural basis for chemical inhibition of human blood coagulation factor RT Xa."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 127-467. RX PubMed=17227710; DOI=10.1016/j.bmc.2006.12.019; RA Kochanny M.J., Adler M., Ewing J., Griedel B.D., Ho E., Karanjawala R., RA Lee W., Lentz D., Liang A.M., Morrissey M.M., Phillips G.B., Post J., RA Sacchi K.L., Sakata S.T., Subramanyam B., Vergona R., Walters J., RA White K.A., Whitlow M., Ye B., Zhao Z., Shaw K.J.; RT "Substituted thiophene-anthranilamides as potent inhibitors of human factor RT Xa."; RL Bioorg. Med. Chem. 15:2127-2146(2007). RN [18] RP VARIANT FA10D CYS-366. RX PubMed=2790181; RA Reddy S.V., Zhou Z.Q., Rao K.J., Scott J.P., Watzke H., High K.A., RA Jagadeeswaran P.; RT "Molecular characterization of human factor XSan Antonio."; RL Blood 74:1486-1490(1989). RN [19] RP VARIANTS FA10D LYS-54 AND LYS-142, AND CHARACTERIZATION OF VARIANT FA10D RP LYS-54. RX PubMed=1973167; DOI=10.1016/s0021-9258(19)38497-2; RA Watzke H.H., Lechner K., Roberts H.R., Reddy S.V., Welsch D.J., RA Friedman P., Mahr G., Jagadeeswaran P., Monroe D.M., High K.A.; RT "Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X RT 'Vorarlberg')."; RL J. Biol. Chem. 265:11982-11989(1990). RN [20] RP VARIANT FA10D SER-383. RX PubMed=1985698; RA James H.L., Girolami A., Fair D.S.; RT "Molecular defect in coagulation factor XFriuli results from a substitution RT of serine for proline at position 343."; RL Blood 77:317-323(1991). RN [21] RP VARIANTS FA10D LYS-142 AND PRO-374. RX PubMed=7669671; DOI=10.1111/j.1365-2141.1995.tb05214.x; RA Marchetti G., Castaman G., Pinotti M., Lunghi B., Di Iasio M.G., RA Ruggieri M., Rodeghiero F., Bernardi F.; RT "Molecular bases of CRM+ factor X deficiency: a frequent mutation RT (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the RT second EGF-like domain."; RL Br. J. Haematol. 90:910-915(1995). RN [22] RP VARIANT FA10D PRO-374, AND CHARACTERIZATION OF VARIANT FA10D PRO-374. RX PubMed=8529633; DOI=10.1111/j.1432-1033.1995.140_c.x; RA Bezeaud A., Miyata T., Helley D., Zeng Y.Z., Kato H., Aillaud M.F., RA Juhan-Vague I., Guillin M.C.; RT "Functional consequences of the Ser334-->Pro mutation in a human factor X RT variant (factor XMarseille)."; RL Eur. J. Biochem. 234:140-147(1995). RN [23] RP VARIANT FA10D GLY-54. RX PubMed=7860069; DOI=10.1007/bf00209404; RA Kim D.J., Thompson A.R., James H.L.; RT "Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue RT at position 14 in the light chain."; RL Hum. Genet. 95:212-214(1995). RN [24] RP VARIANT FA10D ASN-322, AND CHARACTERIZATION OF VARIANT FA10D ASN-322. RX PubMed=8845463; RA Messier T.L., Wong C.Y., Bovill E.G., Long G.L., Church W.R.; RT "Factor X Stockton: a mild bleeding diathesis associated with an active RT site mutation in factor X."; RL Blood Coagul. Fibrinolysis 7:5-14(1996). RN [25] RP VARIANT FA10D GLY-47. RX PubMed=8910490; DOI=10.1074/jbc.271.45.28601; RA Rudolph A.E., Mullane M.P., Porche-Sorbet R., Tsuda S., Miletich J.P.; RT "Factor XSt. Louis II. Identification of a glycine substitution at residue RT 7 and characterization of the recombinant protein."; RL J. Biol. Chem. 271:28601-28606(1996). RN [26] RP VARIANT FA10D GLN-72. RX PubMed=10468877; DOI=10.1046/j.1365-2141.1999.01614.x; RA Zama T., Murata M., Watanabe R., Yokoyama K., Moriki T., Ambo H., RA Murakami H., Kikuchi M., Ikeda Y.; RT "A family with hereditary factor X deficiency with a point mutation Gla32 RT to Gln in the Gla domain (factor X Tokyo)."; RL Br. J. Haematol. 106:809-811(1999). RN [27] RP VARIANTS ILE-7 AND HIS-30. 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 [28] 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 [29] RP VARIANTS FA10D LYS-54; TYR-149; TYR-151; ARG-289; LYS-304; TRP-327; RP MET-338; LYS-350; MET-358; SER-363 AND ARG-404. RX PubMed=10746568; DOI=10.1007/s004390051035; RA Millar D.S., Elliston L., Deex P., Krawczak M., Wacey A.I., Reynaud J., RA Nieuwenhuis H.K., Bolton-Maggs P., Mannucci P.M., Reverter J.C., Cachia P., RA Pasi K.J., Layton D.M., Cooper D.N.; RT "Molecular analysis of the genotype-phenotype relationship in factor X RT deficiency."; RL Hum. Genet. 106:249-257(2000). RN [30] RP CHARACTERIZATION OF VARIANT FA10D LYS-142. RX PubMed=10739379; RA Forberg E., Huhmann I., Jimenez-Boj E., Watzke H.H.; RT "The impact of Glu102Lys on the factor X function in a patient with a RT doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys)."; RL Thromb. Haemost. 83:234-238(2000). RN [31] RP VARIANT FA10D ASN-448. RX PubMed=11248282; DOI=10.1016/s0049-3848(00)00406-0; RA Simioni P., Vianello F., Kalafatis M., Barzon L., Ladogana S., Paolucci P., RA Carotenuto M., Dal Bello F., Palu G., Girolami A.; RT "A dysfunctional factor X (factor X San Giovanni Rotondo) present at RT homozygous and double heterozygous level: identification of a novel RT microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the RT factor X gene. A study of an Italian family."; RL Thromb. Res. 101:219-230(2001). RN [32] RP VARIANTS FA10D PRO-374 AND ARG-420. RX PubMed=11728527; DOI=10.1016/s0049-3848(01)00371-1; RA Vianello F., Lombardi A.M., Boldrin C., Luni S., Girolami A.; RT "A new factor X defect (factor X Padua 3): a compound heterozygous between RT true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro)."; RL Thromb. Res. 104:257-264(2001). RN [33] RP VARIANT FA10D PHE-390. RX PubMed=12945883; DOI=10.1097/00001721-200306000-00012; RA Vianello F., Lombardi A.M., Bello F.D., Palu G., Zanon E., Girolami A.; RT "A novel type I factor X variant (factor X Cys350Phe) due to loss of a RT disulfide bond in the catalytic domain."; RL Blood Coagul. Fibrinolysis 14:401-405(2003). RN [34] RP VARIANT FA10D ASP-421, AND CHARACTERIZATION OF VARIANT FA10D ASP-421. RX PubMed=12574802; RA Pinotti M., Camire R.M., Baroni M., Rajab A., Marchetti G., Bernardi F.; RT "Impaired prothrombinase activity of factor X Gly381Asp results in severe RT familial CRM+ FX deficiency."; RL Thromb. Haemost. 89:243-248(2003). RN [35] RP VARIANT FA10D ALA-382, AND CHARACTERIZATION OF VARIANT FA10D ALA-382. RX PubMed=15075089; RA Pinotti M., Monti M., Baroni M., Marchetti G., Bernardi F.; RT "Molecular characterization of factor X deficiency associated with RT borderline plasma factor X level."; RL Haematologica 89:501-502(2004). RN [36] RP VARIANT FA10D SER-406, AND CHARACTERIZATION OF VARIANT FA10D SER-406. RX PubMed=15650540; DOI=10.1097/00001721-200501000-00002; RA Isshiki I., Favier R., Moriki T., Uchida T., Ishihara H., Van Dreden P., RA Murata M., Ikeda Y.; RT "Genetic analysis of hereditary factor X deficiency in a French patient of RT Sri Lankan ancestry: in vitro expression study identified Gly366Ser RT substitution as the molecular basis of the dysfunctional factor X."; RL Blood Coagul. Fibrinolysis 16:9-16(2005). RN [37] RP VARIANT FA10D LYS-91. RX PubMed=17393015; DOI=10.1160/th06-09-0532; RA Al-Hilali A., Wulff K., Abdel-Razeq H., Saud K.A., Al-Gaili F., RA Herrmann F.H.; RT "Analysis of the novel factor X gene mutation Glu51Lys in two families with RT factor X-Riyadh anomaly."; RL Thromb. Haemost. 97:542-545(2007). RN [38] RP VARIANT FA10D VAL-51. RX PubMed=19135706; DOI=10.1016/j.thromres.2008.11.018; RA Chafa O., Tagzirt M., Tapon-Bretaudiere J., Reghis A., Fischer A.M., RA LeBonniec B.F.; RT "Characterization of a homozygous Gly11Val mutation in the Gla domain of RT coagulation factor X."; RL Thromb. Res. 124:144-148(2009). RN [39] RP VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421, AND RP CHARACTERIZATION OF VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND RP ASP-421. RX PubMed=25313940; DOI=10.1021/bi500770p; RA Abdel-Azeim S., Oliva R., Chermak E., De Cristofaro R., Cavallo L.; RT "Molecular dynamics characterization of five pathogenic Factor X mutants RT associated with decreased catalytic activity."; RL Biochemistry 53:6992-7001(2014). RN [40] RP VARIANTS FA10D 176-THR--GLN-186 DEL AND ASP-262. RX PubMed=26222694; DOI=10.1111/eci.12511; RA Epcacan S., Menegatti M., Akbayram S., Cairo A., Peyvandi F., Oner A.F.; RT "Frequency of the p.Gly262Asp mutation in congenital Factor X deficiency."; RL Eur. J. Clin. Invest. 45:1087-1091(2015). CC -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts CC prothrombin to thrombin in the presence of factor Va, calcium and CC phospholipid during blood clotting. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in CC prothrombin to form thrombin.; EC=3.4.21.6; CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5 and SERPINA10. CC {ECO:0000269|PubMed:20427285, ECO:0000269|PubMed:6323392}. CC -!- SUBUNIT: The two chains are formed from a single-chain precursor by the CC excision of two Arg residues and are held together by 1 or more CC disulfide bonds. Forms a heterodimer with SERPINA5. CC -!- INTERACTION: CC P00742; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-719750, EBI-22310682; CC P00742; Q9UK55: SERPINA10; NbExp=2; IntAct=EBI-719750, EBI-3941758; CC P00742; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-719750, EBI-947187; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver. CC {ECO:0000269|PubMed:6587384}. CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate CC residues allows the modified protein to bind calcium. CC -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core CC 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8243461}. CC -!- PTM: Proteolytically cleaved and activated by cathepsin CTSG CC (PubMed:8920993). The activation peptide is cleaved by factor IXa (in CC the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) CC (By similarity). {ECO:0000250|UniProtKB:P00743, CC ECO:0000269|PubMed:8920993}. CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate CC and asparagine is (R) stereospecific within EGF domains. CC {ECO:0000269|PubMed:6871167}. CC -!- DISEASE: Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic CC disease with variable presentation. Affected individuals can manifest CC prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and CC occasionally hemarthrosis. Some patients do not have clinical bleeding CC diathesis. {ECO:0000269|PubMed:10468877, ECO:0000269|PubMed:10739379, CC ECO:0000269|PubMed:10746568, ECO:0000269|PubMed:11248282, CC ECO:0000269|PubMed:11728527, ECO:0000269|PubMed:12574802, CC ECO:0000269|PubMed:12945883, ECO:0000269|PubMed:15075089, CC ECO:0000269|PubMed:15650540, ECO:0000269|PubMed:17393015, CC ECO:0000269|PubMed:19135706, ECO:0000269|PubMed:1973167, CC ECO:0000269|PubMed:1985698, ECO:0000269|PubMed:25313940, CC ECO:0000269|PubMed:26222694, ECO:0000269|PubMed:2790181, CC ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:7860069, CC ECO:0000269|PubMed:8529633, ECO:0000269|PubMed:8845463, CC ECO:0000269|PubMed:8910490}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor X entry; CC URL="https://en.wikipedia.org/wiki/Factor_X"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/f10/"; 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; K03194; AAA52490.1; -; mRNA. DR EMBL; M57285; AAA52421.1; -; mRNA. DR EMBL; AF503510; AAM19347.1; -; Genomic_DNA. DR EMBL; BC046125; AAH46125.1; -; mRNA. DR EMBL; N00045; AAA52764.1; -; Genomic_DNA. DR EMBL; L00390; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00391; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00392; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00393; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00394; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00395; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; L00396; AAA52764.1; JOINED; Genomic_DNA. DR EMBL; M22613; AAA51984.1; -; mRNA. DR EMBL; K01886; AAA52486.1; -; mRNA. DR EMBL; M33297; AAA52636.1; -; Genomic_DNA. DR CCDS; CCDS9530.1; -. DR PIR; A24478; EXHU. DR RefSeq; NP_000495.1; NM_000504.3. DR RefSeq; NP_001299603.1; NM_001312674.1. DR RefSeq; NP_001299604.1; NM_001312675.1. DR PDB; 1C5M; X-ray; 1.95 A; D=235-488, F=84-179. DR PDB; 1EZQ; X-ray; 2.20 A; A=235-488, B=46-179. DR PDB; 1F0R; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 1F0S; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 1FAX; X-ray; 3.00 A; A=235-488, L=84-179. DR PDB; 1FJS; X-ray; 1.92 A; A=235-468, L=127-178. DR PDB; 1FXY; X-ray; 2.15 A; A=235-344. DR PDB; 1G2L; X-ray; 1.90 A; A=235-469, B=86-179. DR PDB; 1G2M; X-ray; 3.02 A; A=235-469, B=86-179. DR PDB; 1HCG; X-ray; 2.20 A; A=235-475, B=129-179. DR PDB; 1IOE; X-ray; 2.90 A; A=235-469, L=84-179. DR PDB; 1IQE; X-ray; 2.90 A; A=235-469, L=84-179. DR PDB; 1IQF; X-ray; 3.20 A; A=235-469, L=84-179. DR PDB; 1IQG; X-ray; 2.60 A; A=235-469, L=84-179. DR PDB; 1IQH; X-ray; 3.00 A; A=235-469, L=84-179. DR PDB; 1IQI; X-ray; 2.90 A; A=235-469, L=84-179. DR PDB; 1IQJ; X-ray; 3.00 A; A=235-469, L=84-179. DR PDB; 1IQK; X-ray; 3.20 A; A=235-469, L=84-179. DR PDB; 1IQL; X-ray; 2.70 A; A=235-469, L=84-179. DR PDB; 1IQM; X-ray; 2.60 A; A=235-469, L=84-179. DR PDB; 1IQN; X-ray; 2.60 A; A=235-469, L=84-179. DR PDB; 1KSN; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 1LPG; X-ray; 2.00 A; A=46-179, B=235-488. DR PDB; 1LPK; X-ray; 2.20 A; A=46-179, B=235-488. DR PDB; 1LPZ; X-ray; 2.40 A; A=46-179, B=235-488. DR PDB; 1LQD; X-ray; 2.70 A; A=46-179, B=235-488. DR PDB; 1MQ5; X-ray; 2.10 A; A=235-467, L=127-177. DR PDB; 1MQ6; X-ray; 2.10 A; A=235-467, L=127-177. DR PDB; 1NFU; X-ray; 2.05 A; A=235-488, B=46-240. DR PDB; 1NFW; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 1NFX; X-ray; 2.15 A; A=235-488, B=46-179. DR PDB; 1NFY; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 1P0S; X-ray; 2.80 A; H=235-488, L=41-178. DR PDB; 1V3X; X-ray; 2.20 A; A=235-467, B=127-178. DR PDB; 1WU1; X-ray; 2.30 A; A=235-467, B=85-179. DR PDB; 1XKA; X-ray; 2.30 A; C=235-469, L=85-179. DR PDB; 1XKB; X-ray; 2.40 A; A/B=85-179, C/D=235-469. DR PDB; 1Z6E; X-ray; 1.80 A; A=235-468, L=127-178. DR PDB; 2BMG; X-ray; 2.70 A; A=126-178, B=235-468. DR PDB; 2BOH; X-ray; 2.20 A; A=46-179, B=235-488. DR PDB; 2BOK; X-ray; 1.64 A; A=235-475, L=126-180. DR PDB; 2BQ6; X-ray; 3.00 A; A=126-177, B=220-468. DR PDB; 2BQ7; X-ray; 2.20 A; A=126-177, B=220-468. DR PDB; 2BQW; X-ray; 2.95 A; A=126-177, B=220-468. DR PDB; 2CJI; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 2D1J; X-ray; 2.20 A; A=235-467, B=125-178. DR PDB; 2EI6; X-ray; 2.30 A; A=235-467, B=125-178. DR PDB; 2EI7; X-ray; 2.30 A; A=235-467, B=125-178. DR PDB; 2EI8; X-ray; 2.10 A; A=235-467, B=125-178. DR PDB; 2FZZ; X-ray; 2.20 A; A=235-468, L=127-178. DR PDB; 2G00; X-ray; 2.10 A; A=235-468, L=127-178. DR PDB; 2GD4; X-ray; 3.30 A; A/L=126-182, B/H=235-475. DR PDB; 2H9E; X-ray; 2.20 A; H=235-467, L=86-234. DR PDB; 2J2U; X-ray; 1.90 A; A=235-488, B=46-179. DR PDB; 2J34; X-ray; 2.01 A; A=235-488, B=46-179. DR PDB; 2J38; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 2J4I; X-ray; 1.80 A; A=235-488, B=46-179. DR PDB; 2J94; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 2J95; X-ray; 2.01 A; A=235-488, B=46-179. DR PDB; 2JKH; X-ray; 1.25 A; A=235-475, L=126-180. DR PDB; 2P16; X-ray; 2.30 A; A=235-468, L=127-178. DR PDB; 2P3F; X-ray; 3.10 A; H=235-469, L=125-178. DR PDB; 2P3T; X-ray; 1.92 A; A=127-178, B=235-467. DR PDB; 2P3U; X-ray; 1.62 A; A=127-178, B=235-467. DR PDB; 2P93; X-ray; 1.90 A; A=235-468, L=127-178. DR PDB; 2P94; X-ray; 1.80 A; A=235-468, L=127-178. DR PDB; 2P95; X-ray; 2.20 A; A=235-468, L=127-178. DR PDB; 2PHB; X-ray; 2.30 A; A=235-468, B=128-178. DR PDB; 2PR3; X-ray; 1.50 A; A=235-468, B=128-178. DR PDB; 2Q1J; X-ray; 1.90 A; A=235-468, B=128-178. DR PDB; 2RA0; X-ray; 2.30 A; A=235-468, L=128-178. DR PDB; 2UWL; X-ray; 1.90 A; A=235-488, B=46-179. DR PDB; 2UWO; X-ray; 1.75 A; A=235-488, B=46-179. DR PDB; 2UWP; X-ray; 1.75 A; A=235-488, B=46-179. DR PDB; 2VH0; X-ray; 1.70 A; A=235-488, B=46-179. DR PDB; 2VH6; X-ray; 1.95 A; A=235-488, B=46-177. DR PDB; 2VVC; X-ray; 1.95 A; A/B=235-475, K/L=126-180. DR PDB; 2VVU; X-ray; 2.30 A; A=235-475, L=126-180. DR PDB; 2VVV; X-ray; 1.73 A; A=235-475, L=126-180. DR PDB; 2VWL; X-ray; 1.80 A; A=235-475, L=126-180. DR PDB; 2VWM; X-ray; 1.96 A; A/B=235-475, K/L=126-180. DR PDB; 2VWN; X-ray; 1.61 A; A=235-475, L=126-180. DR PDB; 2VWO; X-ray; 1.60 A; A=235-475, L=126-180. DR PDB; 2W26; X-ray; 2.08 A; A=235-468, B=129-177. DR PDB; 2W3I; X-ray; 1.90 A; A=235-468, B=128-178. DR PDB; 2W3K; X-ray; 2.05 A; A=235-468, B=128-178. DR PDB; 2WYG; X-ray; 1.88 A; A=235-487, B=46-179. DR PDB; 2WYJ; X-ray; 2.38 A; A=235-488, B=46-179. DR PDB; 2XBV; X-ray; 1.66 A; A=235-475, L=126-180. DR PDB; 2XBW; X-ray; 1.72 A; A=235-475, L=126-180. DR PDB; 2XBX; X-ray; 1.85 A; A=235-475, L=126-180. DR PDB; 2XBY; X-ray; 2.02 A; A=235-475, L=126-180. DR PDB; 2XC0; X-ray; 2.05 A; A=235-475, L=126-180. DR PDB; 2XC4; X-ray; 1.67 A; A=235-475, L=126-180. DR PDB; 2XC5; X-ray; 1.70 A; A=235-475, L=126-180. DR PDB; 2Y5F; X-ray; 1.29 A; A=235-468, L=127-180. DR PDB; 2Y5G; X-ray; 1.29 A; A=235-468, L=127-180. DR PDB; 2Y5H; X-ray; 1.33 A; A=235-468, L=127-180. DR PDB; 2Y7X; X-ray; 1.90 A; A=235-488, B=46-179. DR PDB; 2Y7Z; X-ray; 1.84 A; A=235-488, B=46-179. DR PDB; 2Y80; X-ray; 1.90 A; A=235-488, B=46-179. DR PDB; 2Y81; X-ray; 1.70 A; A=235-488, B=46-179. DR PDB; 2Y82; X-ray; 2.20 A; A=235-488, B=46-179. DR PDB; 3CEN; X-ray; 1.60 A; A=235-468, L=127-178. DR PDB; 3CS7; X-ray; 2.20 A; A=235-468, L=127-178. DR PDB; 3ENS; X-ray; 2.30 A; A/C=85-178, B/D=235-472. DR PDB; 3FFG; X-ray; 1.54 A; A=235-468, L=127-178. DR PDB; 3HPT; X-ray; 2.19 A; A/C=85-178, B/D=235-472. DR PDB; 3IIT; X-ray; 1.80 A; A=235-467, B=125-178. DR PDB; 3K9X; X-ray; 1.90 A; A/C=85-178, B/D=235-472. DR PDB; 3KL6; X-ray; 1.45 A; A=235-475, B=126-179. DR PDB; 3KQB; X-ray; 2.25 A; A=235-468, L=127-178. DR PDB; 3KQC; X-ray; 2.20 A; A=235-468, L=127-178. DR PDB; 3KQD; X-ray; 2.75 A; A=235-468, L=127-178. DR PDB; 3KQE; X-ray; 2.35 A; A=235-468, L=127-178. DR PDB; 3LIW; X-ray; 2.22 A; A=235-468, B=128-178. DR PDB; 3M36; X-ray; 2.15 A; A=235-468, L=127-178. DR PDB; 3M37; X-ray; 1.90 A; A=235-468, L=127-178. DR PDB; 3Q3K; X-ray; 2.00 A; A=235-467, B=125-178. DR PDB; 3SW2; X-ray; 2.42 A; A=85-178, B=235-472. DR PDB; 3TK5; X-ray; 2.20 A; A=235-467, B=125-178. DR PDB; 3TK6; X-ray; 1.80 A; A=235-467, B=125-178. DR PDB; 4A7I; X-ray; 2.40 A; A=84-179, B=235-488. DR PDB; 4BTI; X-ray; 2.30 A; A/E=84-179, B/F=235-488. DR PDB; 4BTT; X-ray; 2.59 A; A/E=84-179, B/F=235-488. DR PDB; 4BTU; X-ray; 2.37 A; A/E=84-179, B/F=235-488. DR PDB; 4Y6D; X-ray; 1.55 A; A=235-488, B=46-179. DR PDB; 4Y71; X-ray; 1.80 A; A=235-488, B=46-179. DR PDB; 4Y76; X-ray; 2.00 A; A=235-488, B=46-179. DR PDB; 4Y79; X-ray; 2.10 A; A=235-488, B=46-179. DR PDB; 4Y7A; X-ray; 1.99 A; A=235-488, B=46-179. DR PDB; 4Y7B; X-ray; 1.79 A; A=235-488, B=46-179. DR PDB; 4ZH8; X-ray; 1.80 A; A=235-488, B=46-179. DR PDB; 4ZHA; X-ray; 1.86 A; A=235-488, B=46-179. DR PDB; 5JQY; X-ray; 1.99 A; B=86-124. DR PDB; 5JTC; X-ray; 2.24 A; B=86-124. DR PDB; 5JZ8; X-ray; 2.10 A; B=86-124. DR PDB; 5JZU; X-ray; 2.50 A; B=86-111. DR PDB; 5K0H; X-ray; 2.20 A; A=235-468, B=128-178. DR PDB; 5VOE; X-ray; 2.00 A; H=235-467, L=128-178. DR PDB; 5VOF; X-ray; 2.25 A; H=235-467, L=128-178. DR PDB; 6Q9F; X-ray; 1.63 A; B=86-124. DR PDB; 6Q9I; X-ray; 1.85 A; B=86-124. DR PDB; 6RK9; X-ray; 2.29 A; B=102-119. DR PDB; 6YYW; X-ray; 2.27 A; B=86-124. DR PDB; 6YYX; X-ray; 1.53 A; B=86-124. DR PDB; 6YYY; X-ray; 2.29 A; B=86-124. DR PDB; 6Z6Q; X-ray; 1.81 A; B=86-124. DR PDB; 6Z6R; X-ray; 2.13 A; B=86-124. DR PDB; 7AHU; X-ray; 2.60 A; C/E=235-475, D/F=126-182. DR PDB; 7BMI; X-ray; 1.66 A; B=86-124. DR PDB; 7BMJ; X-ray; 1.75 A; B=86-124. DR PDB; 7E6J; X-ray; 1.90 A; B=86-124. DR PDB; 7TPP; EM; 4.10 A; A=41-179, B=235-488. DR PDB; 7TPQ; EM; 5.30 A; A=41-179, B=235-488. DR PDB; 7YB8; X-ray; 1.98 A; B=86-124. DR PDB; 7YB9; X-ray; 1.54 A; B=86-124. DR PDB; 7YBB; X-ray; 1.68 A; B=86-124. DR PDB; 7YBC; X-ray; 1.84 A; B=86-124. DR PDB; 8EOK; EM; 3.53 A; C=235-488, L=46-179. DR PDBsum; 1C5M; -. DR PDBsum; 1EZQ; -. DR PDBsum; 1F0R; -. DR PDBsum; 1F0S; -. DR PDBsum; 1FAX; -. DR PDBsum; 1FJS; -. DR PDBsum; 1FXY; -. DR PDBsum; 1G2L; -. DR PDBsum; 1G2M; -. DR PDBsum; 1HCG; -. DR PDBsum; 1IOE; -. DR PDBsum; 1IQE; -. DR PDBsum; 1IQF; -. DR PDBsum; 1IQG; -. DR PDBsum; 1IQH; -. DR PDBsum; 1IQI; -. DR PDBsum; 1IQJ; -. DR PDBsum; 1IQK; -. DR PDBsum; 1IQL; -. DR PDBsum; 1IQM; -. DR PDBsum; 1IQN; -. DR PDBsum; 1KSN; -. DR PDBsum; 1LPG; -. DR PDBsum; 1LPK; -. DR PDBsum; 1LPZ; -. DR PDBsum; 1LQD; -. DR PDBsum; 1MQ5; -. DR PDBsum; 1MQ6; -. DR PDBsum; 1NFU; -. DR PDBsum; 1NFW; -. DR PDBsum; 1NFX; -. DR PDBsum; 1NFY; -. DR PDBsum; 1P0S; -. DR PDBsum; 1V3X; -. DR PDBsum; 1WU1; -. DR PDBsum; 1XKA; -. DR PDBsum; 1XKB; -. DR PDBsum; 1Z6E; -. DR PDBsum; 2BMG; -. DR PDBsum; 2BOH; -. DR PDBsum; 2BOK; -. DR PDBsum; 2BQ6; -. DR PDBsum; 2BQ7; -. DR PDBsum; 2BQW; -. DR PDBsum; 2CJI; -. DR PDBsum; 2D1J; -. DR PDBsum; 2EI6; -. DR PDBsum; 2EI7; -. DR PDBsum; 2EI8; -. DR PDBsum; 2FZZ; -. DR PDBsum; 2G00; -. DR PDBsum; 2GD4; -. DR PDBsum; 2H9E; -. DR PDBsum; 2J2U; -. DR PDBsum; 2J34; -. DR PDBsum; 2J38; -. DR PDBsum; 2J4I; -. DR PDBsum; 2J94; -. DR PDBsum; 2J95; -. DR PDBsum; 2JKH; -. DR PDBsum; 2P16; -. DR PDBsum; 2P3F; -. DR PDBsum; 2P3T; -. DR PDBsum; 2P3U; -. DR PDBsum; 2P93; -. DR PDBsum; 2P94; -. DR PDBsum; 2P95; -. DR PDBsum; 2PHB; -. DR PDBsum; 2PR3; -. DR PDBsum; 2Q1J; -. DR PDBsum; 2RA0; -. DR PDBsum; 2UWL; -. DR PDBsum; 2UWO; -. DR PDBsum; 2UWP; -. DR PDBsum; 2VH0; -. DR PDBsum; 2VH6; -. DR PDBsum; 2VVC; -. DR PDBsum; 2VVU; -. DR PDBsum; 2VVV; -. DR PDBsum; 2VWL; -. DR PDBsum; 2VWM; -. DR PDBsum; 2VWN; -. DR PDBsum; 2VWO; -. DR PDBsum; 2W26; -. DR PDBsum; 2W3I; -. DR PDBsum; 2W3K; -. DR PDBsum; 2WYG; -. DR PDBsum; 2WYJ; -. DR PDBsum; 2XBV; -. DR PDBsum; 2XBW; -. DR PDBsum; 2XBX; -. DR PDBsum; 2XBY; -. DR PDBsum; 2XC0; -. DR PDBsum; 2XC4; -. DR PDBsum; 2XC5; -. DR PDBsum; 2Y5F; -. DR PDBsum; 2Y5G; -. DR PDBsum; 2Y5H; -. DR PDBsum; 2Y7X; -. DR PDBsum; 2Y7Z; -. DR PDBsum; 2Y80; -. DR PDBsum; 2Y81; -. DR PDBsum; 2Y82; -. DR PDBsum; 3CEN; -. DR PDBsum; 3CS7; -. DR PDBsum; 3ENS; -. DR PDBsum; 3FFG; -. DR PDBsum; 3HPT; -. DR PDBsum; 3IIT; -. DR PDBsum; 3K9X; -. DR PDBsum; 3KL6; -. DR PDBsum; 3KQB; -. DR PDBsum; 3KQC; -. DR PDBsum; 3KQD; -. DR PDBsum; 3KQE; -. DR PDBsum; 3LIW; -. DR PDBsum; 3M36; -. DR PDBsum; 3M37; -. DR PDBsum; 3Q3K; -. DR PDBsum; 3SW2; -. DR PDBsum; 3TK5; -. DR PDBsum; 3TK6; -. DR PDBsum; 4A7I; -. DR PDBsum; 4BTI; -. DR PDBsum; 4BTT; -. DR PDBsum; 4BTU; -. DR PDBsum; 4Y6D; -. DR PDBsum; 4Y71; -. DR PDBsum; 4Y76; -. DR PDBsum; 4Y79; -. DR PDBsum; 4Y7A; -. DR PDBsum; 4Y7B; -. DR PDBsum; 4ZH8; -. DR PDBsum; 4ZHA; -. DR PDBsum; 5JQY; -. DR PDBsum; 5JTC; -. DR PDBsum; 5JZ8; -. DR PDBsum; 5JZU; -. DR PDBsum; 5K0H; -. DR PDBsum; 5VOE; -. DR PDBsum; 5VOF; -. DR PDBsum; 6Q9F; -. DR PDBsum; 6Q9I; -. DR PDBsum; 6RK9; -. DR PDBsum; 6YYW; -. DR PDBsum; 6YYX; -. DR PDBsum; 6YYY; -. DR PDBsum; 6Z6Q; -. DR PDBsum; 6Z6R; -. DR PDBsum; 7AHU; -. DR PDBsum; 7BMI; -. DR PDBsum; 7BMJ; -. DR PDBsum; 7E6J; -. DR PDBsum; 7TPP; -. DR PDBsum; 7TPQ; -. DR PDBsum; 7YB8; -. DR PDBsum; 7YB9; -. DR PDBsum; 7YBB; -. DR PDBsum; 7YBC; -. DR PDBsum; 8EOK; -. DR AlphaFoldDB; P00742; -. DR EMDB; EMD-26060; -. DR EMDB; EMD-26061; -. DR EMDB; EMD-28378; -. DR SMR; P00742; -. DR BioGRID; 108457; 44. DR ComplexPortal; CPX-6215; Coagulation factor Xa complex. DR CORUM; P00742; -. DR DIP; DIP-29896N; -. DR ELM; P00742; -. DR IntAct; P00742; 16. DR MINT; P00742; -. DR STRING; 9606.ENSP00000364709; -. DR BindingDB; P00742; -. DR ChEMBL; CHEMBL244; -. DR DrugBank; DB07211; (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE. DR DrugBank; DB08746; 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE. DR DrugBank; DB07974; 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE. DR DrugBank; DB07277; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE. DR DrugBank; DB07605; 2-({4-[(5-CHLORO-1H-INDOL-2-YL)SULFONYL]PIPERAZIN-1-YL}CARBONYL)THIENO[3,2-B]PYRIDINE 4-OXIDE. DR DrugBank; DB08487; 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE. DR DrugBank; DB08495; 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE. DR DrugBank; DB04673; 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE. DR DrugBank; DB08745; 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE. DR DrugBank; DB08488; 4-{[(E)-2-(5-CHLOROTHIEN-2-YL)VINYL]SULFONYL}-1-(1H-PYRROLO[3,2-C]PYRIDIN-2-YLMETHYL)PIPERAZIN-2-ONE. DR DrugBank; DB07804; 5-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1H-1,2,4-TRIAZOLE-3-SULFONAMIDE. DR DrugBank; DB08174; 5-CHLORO-N-((1R,2S)-2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO) CYCLOPENTYL)THIOPHENE-2-CARBOXAMIDE. DR DrugBank; DB08173; 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE. DR DrugBank; DB07872; 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide. DR DrugBank; DB07843; 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE. DR DrugBank; DB07848; 5-Chloro-N-{(3S)-1-[(2S)-1-(4-morpholinyl)-1-oxo-2-propanyl]-2-oxo-3-pyrrolidinyl}-1H-indole-2-sulfonamide. DR DrugBank; DB07875; 5-Chloro-thiophene-2-carboxylic acid ((3S,4S)-1-{[2-fluoro-4-(2-oxo-2H-pyridin-1-yl)-phenylcarbamoyl]-methyl}-4-hydroxy-pyrrolidin-3-yl)-amide. DR DrugBank; DB08143; 5-CHLORO-THIOPHENE-2-CARBOXYLIC ACID ((3S,4S)-4-FLUORO- 1-{[2-FLUORO-4-(2-OXO-2H-PYRIDIN-1-YL)-PHENYLCARBAMOYL]-METHYL}-PYRROLIDIN-3-YL)-AMIDE. DR DrugBank; DB07847; 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE. DR DrugBank; DB07844; 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE. DR DrugBank; DB13884; Albutrepenonacog alfa. DR DrugBank; DB13151; Anti-inhibitor coagulant complex. DR DrugBank; DB13192; Antihemophilic factor human. DR DrugBank; DB00025; Antihemophilic factor, human recombinant. DR DrugBank; DB11166; Antithrombin Alfa. DR DrugBank; DB06605; Apixaban. DR DrugBank; DB09258; Bemiparin. DR DrugBank; DB12364; Betrixaban. DR DrugBank; DB00100; Coagulation Factor IX (Recombinant). DR DrugBank; DB13152; Coagulation Factor IX Human. DR DrugBank; DB13150; Coagulation factor VII human. DR DrugBank; DB00036; Coagulation factor VIIa Recombinant Human. DR DrugBank; DB09075; Edoxaban. DR DrugBank; DB13923; Emicizumab. DR DrugBank; DB01225; Enoxaparin. DR DrugBank; DB06920; Eribaxaban. DR DrugBank; DB00569; Fondaparinux. DR DrugBank; DB03847; gamma-carboxy-L-glutamic acid. DR DrugBank; DB07278; GW-813893. DR DrugBank; DB01109; Heparin. DR DrugBank; DB06406; Idraparinux. DR DrugBank; DB09332; Kappadione. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB13998; Lonoctocog alfa. DR DrugBank; DB05713; LY-517717. DR DrugBank; DB13999; Moroctocog alfa. DR DrugBank; DB07630; N-((1R,2R)-2-(5-CHLORO-1H-INDOLE-2-CARBOXAMIDO)CYCLOHEXYL)-5-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO[5,4-C]PYRIDINE-2-CARBOXAMIDE. DR DrugBank; DB07629; N-((1R,2S)-2-(5-CHLORO-1H-INDOLE-2-CARBOXAMIDO)CYCLOHEXYL)-5-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO[5,4-C]PYRIDINE-2-CARBOXAMIDE. DR DrugBank; DB07973; N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE. DR DrugBank; DB07800; N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE. DR DrugBank; DB12598; Nafamostat. DR DrugBank; DB13933; Nonacog beta pegol. DR DrugBank; DB06635; Otamixaban. DR DrugBank; DB09141; Protamine sulfate. DR DrugBank; DB13149; Protein S human. DR DrugBank; DB11311; Prothrombin. DR DrugBank; DB06228; Rivaroxaban. DR DrugBank; DB06552; rNAPc2. DR DrugBank; DB05362; SSR-126517E. DR DrugBank; DB07261; THIENO[3,2-B]PYRIDINE-2-SULFONIC ACID [1-(1-AMINO-ISOQUINOLIN-7-YLMETHYL)-2-OXO-PYRROLDIN-3-YL]-AMIDE. DR DrugBank; DB08426; THIENO[3,2-B]PYRIDINE-2-SULFONIC ACID [2-OXO-1-(1H-PYRROLO[2,3-C]PYRIDIN-2-YLMETHYL)-PYRROLIDIN-3-YL]-AMIDE. DR DrugBank; DB09109; Turoctocog alfa. DR DrugBank; DB14738; Turoctocog alfa pegol. DR DrugCentral; P00742; -. DR GuidetoPHARMACOLOGY; 2359; -. DR MEROPS; S01.216; -. DR GlyConnect; 102; 16 N-Linked glycans (2 sites), 1 O-Linked glycan. DR GlyCosmos; P00742; 13 sites, 30 glycans. DR GlyGen; P00742; 14 sites, 26 N-linked glycans (2 sites), 6 O-linked glycans (11 sites). DR iPTMnet; P00742; -. DR PhosphoSitePlus; P00742; -. DR BioMuta; F10; -. DR DMDM; 119761; -. DR CPTAC; non-CPTAC-2649; -. DR jPOST; P00742; -. DR MassIVE; P00742; -. DR PaxDb; 9606-ENSP00000364709; -. DR PeptideAtlas; P00742; -. DR ProteomicsDB; 51275; -. DR Pumba; P00742; -. DR ABCD; P00742; 1 sequenced antibody. DR Antibodypedia; 11687; 761 antibodies from 35 providers. DR DNASU; 2159; -. DR Ensembl; ENST00000375559.8; ENSP00000364709.3; ENSG00000126218.12. DR GeneID; 2159; -. DR KEGG; hsa:2159; -. DR MANE-Select; ENST00000375559.8; ENSP00000364709.3; NM_000504.4; NP_000495.1. DR AGR; HGNC:3528; -. DR CTD; 2159; -. DR DisGeNET; 2159; -. DR GeneCards; F10; -. DR HGNC; HGNC:3528; F10. DR HPA; ENSG00000126218; Tissue enhanced (liver). DR MalaCards; F10; -. DR MIM; 227600; phenotype. DR MIM; 613872; gene. DR neXtProt; NX_P00742; -. DR OpenTargets; ENSG00000126218; -. DR Orphanet; 328; Congenital factor X deficiency. DR PharmGKB; PA27940; -. DR VEuPathDB; HostDB:ENSG00000126218; -. DR eggNOG; ENOG502QS4N; Eukaryota. DR GeneTree; ENSGT00940000157694; -. DR HOGENOM; CLU_006842_19_5_1; -. DR InParanoid; P00742; -. DR OMA; QKDWAEA; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P00742; -. DR TreeFam; TF327329; -. DR BioCyc; MetaCyc:HS05000-MONOMER; -. DR BRENDA; 3.4.21.6; 2681. DR PathwayCommons; P00742; -. DR Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors. DR Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus. DR Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins. DR Reactome; R-HSA-9672383; Defective factor IX causes thrombophilia. DR Reactome; R-HSA-9672396; Defective cofactor function of FVIIIa variant. DR Reactome; R-HSA-9673202; Defective F9 variant does not activate FX. DR SABIO-RK; P00742; -. DR SignaLink; P00742; -. DR SIGNOR; P00742; -. DR BioGRID-ORCS; 2159; 15 hits in 1160 CRISPR screens. DR ChiTaRS; F10; human. DR EvolutionaryTrace; P00742; -. DR GeneWiki; Factor_X; -. DR GenomeRNAi; 2159; -. DR Pharos; P00742; Tclin. DR PRO; PR:P00742; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P00742; Protein. DR Bgee; ENSG00000126218; Expressed in right lobe of liver and 111 other cell types or tissues. DR ExpressionAtlas; P00742; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IC:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL. DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc. DR GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL. DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR012224; Pept_S1A_FX. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24278; COAGULATION FACTOR; 1. DR PANTHER; PTHR24278:SF28; COAGULATION FACTOR X; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001143; Factor_X; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR SMART; SM00181; EGF; 2. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM00069; GLA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P00742; HS. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation; Calcium; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disease variant; Disulfide bond; EGF-like domain; KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; KW Hydroxylation; Protease; Reference proteome; Repeat; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT PROPEP 32..40 FT /evidence="ECO:0000269|PubMed:6871167" FT /id="PRO_0000027786" FT CHAIN 41..488 FT /note="Coagulation factor X" FT /id="PRO_0000027787" FT CHAIN 41..179 FT /note="Factor X light chain" FT /id="PRO_0000027788" FT CHAIN 183..488 FT /note="Factor X heavy chain" FT /id="PRO_0000027789" FT PROPEP 183..234 FT /note="Activation peptide" FT /id="PRO_0000027790" FT CHAIN 235..488 FT /note="Activated factor Xa heavy chain" FT /id="PRO_0000027791" FT DOMAIN 41..85 FT /note="Gla" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463" FT DOMAIN 86..122 FT /note="EGF-like 1; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 125..165 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 235..467 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 183..203 FT /note="O-glycosylated at one site" FT REGION 476..485 FT /note="O-glycosylated at one site" FT ACT_SITE 276 FT /note="Charge relay system" FT ACT_SITE 322 FT /note="Charge relay system" FT ACT_SITE 419 FT /note="Charge relay system" FT MOD_RES 46 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 47 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 54 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 56 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 59 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 60 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 65 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 66 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 69 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 72 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 79 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6871167" FT MOD_RES 103 FT /note="(3R)-3-hydroxyaspartate" FT /evidence="ECO:0000269|PubMed:6871167" FT CARBOHYD 199 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8243461" FT CARBOHYD 211 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8243461" FT CARBOHYD 221 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8243461" FT /id="CAR_000012" FT CARBOHYD 231 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8243461" FT /id="CAR_000013" FT DISULFID 57..62 FT /evidence="ECO:0000250" FT DISULFID 90..101 FT DISULFID 95..110 FT DISULFID 112..121 FT DISULFID 129..140 FT DISULFID 136..149 FT DISULFID 151..164 FT DISULFID 172..342 FT /note="Interchain (between light and heavy chains)" FT DISULFID 241..246 FT DISULFID 261..277 FT DISULFID 390..404 FT DISULFID 415..443 FT VARIANT 7 FT /note="L -> I (in dbSNP:rs5963)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014162" FT VARIANT 30 FT /note="Q -> H (in dbSNP:rs5961)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014163" FT VARIANT 47 FT /note="E -> G (in FA10D; St. Louis II; strongly reduced FT activity; not activated by factor VIIa and tissue factor; FT dbSNP:rs121964943)" FT /evidence="ECO:0000269|PubMed:8910490" FT /id="VAR_065428" FT VARIANT 51 FT /note="G -> V (in FA10D; dbSNP:rs751782758)" FT /evidence="ECO:0000269|PubMed:19135706" FT /id="VAR_065429" FT VARIANT 54 FT /note="E -> G (in FA10D; Ketchikan; dbSNP:rs121964944)" FT /evidence="ECO:0000269|PubMed:7860069" FT /id="VAR_065430" FT VARIANT 54 FT /note="E -> K (in FA10D; Vorarlberg; converts prothrombin FT at a normal rate but shows decreased affinity for calcium; FT dbSNP:rs121964939)" FT /evidence="ECO:0000269|PubMed:10746568, FT ECO:0000269|PubMed:1973167" FT /id="VAR_065431" FT VARIANT 72 FT /note="E -> Q (in FA10D; Tokyo; dbSNP:rs121964945)" FT /evidence="ECO:0000269|PubMed:10468877" FT /id="VAR_065432" FT VARIANT 91 FT /note="E -> K (in FA10D; Riyadh; dbSNP:rs1477329751)" FT /evidence="ECO:0000269|PubMed:17393015" FT /id="VAR_065433" FT VARIANT 142 FT /note="E -> K (in FA10D; uncertain significance; detected FT in patients carrying K-54 or P-374; slightly reduced FT activity; dbSNP:rs61753266)" FT /evidence="ECO:0000269|PubMed:10739379, FT ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:7669671" FT /id="VAR_065434" FT VARIANT 149 FT /note="C -> Y (in FA10D)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065435" FT VARIANT 151 FT /note="C -> Y (in FA10D)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065436" FT VARIANT 152 FT /note="A -> T (in dbSNP:rs3211772)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_020176" FT VARIANT 176..186 FT /note="Missing (in FA10D; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26222694" FT /id="VAR_075212" FT VARIANT 192 FT /note="G -> R (in dbSNP:rs3211783)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_020177" FT VARIANT 262 FT /note="G -> D (in FA10D; uncertain significance; FT dbSNP:rs1393705267)" FT /evidence="ECO:0000269|PubMed:26222694" FT /id="VAR_075213" FT VARIANT 289 FT /note="G -> R (in FA10D; may affect splicing; FT dbSNP:rs121964946)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065437" FT VARIANT 304 FT /note="E -> K (in FA10D; dbSNP:rs747292771)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065438" FT VARIANT 322 FT /note="D -> N (in FA10D; Stockton; 50% decrease in specific FT activity; dbSNP:rs121964942)" FT /evidence="ECO:0000269|PubMed:25313940, FT ECO:0000269|PubMed:8845463" FT /id="VAR_065439" FT VARIANT 327 FT /note="R -> W (in FA10D; dbSNP:rs770119164)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065440" FT VARIANT 338 FT /note="V -> M (in FA10D; dbSNP:rs121964947)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065441" FT VARIANT 350 FT /note="E -> K (in FA10D; dbSNP:rs372309538)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065442" FT VARIANT 358 FT /note="T -> M (in FA10D; Roma; dbSNP:rs768222784)" FT /evidence="ECO:0000269|PubMed:10746568, FT ECO:0000269|PubMed:25313940" FT /id="VAR_065443" FT VARIANT 363 FT /note="G -> S (in FA10D; dbSNP:rs1595099527)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065444" FT VARIANT 366 FT /note="R -> C (in FA10D; San Antonio; dbSNP:rs104894392)" FT /evidence="ECO:0000269|PubMed:2790181" FT /id="VAR_065445" FT VARIANT 374 FT /note="S -> P (in FA10D; Marseille; decreased cleavage by FT factor IXa; normal catalytic efficiency for prothrombin; FT dbSNP:rs121964941)" FT /evidence="ECO:0000269|PubMed:11728527, FT ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:8529633" FT /id="VAR_065446" FT VARIANT 382 FT /note="V -> A (in FA10D; partial loss of activity)" FT /evidence="ECO:0000269|PubMed:15075089, FT ECO:0000269|PubMed:25313940" FT /id="VAR_072751" FT VARIANT 383 FT /note="P -> S (in FA10D; Friuli; dbSNP:rs121964940)" FT /evidence="ECO:0000269|PubMed:1985698" FT /id="VAR_065447" FT VARIANT 390 FT /note="C -> F (in FA10D; Padua 4; dbSNP:rs199778916)" FT /evidence="ECO:0000269|PubMed:12945883" FT /id="VAR_065448" FT VARIANT 404 FT /note="C -> R (in FA10D; dbSNP:rs1595099645)" FT /evidence="ECO:0000269|PubMed:10746568" FT /id="VAR_065449" FT VARIANT 406 FT /note="G -> S (in FA10D; almost complete loss of activity; FT dbSNP:rs376163818)" FT /evidence="ECO:0000269|PubMed:15650540, FT ECO:0000269|PubMed:25313940" FT /id="VAR_065450" FT VARIANT 420 FT /note="G -> R (in FA10D; Padua 3; dbSNP:rs750759634)" FT /evidence="ECO:0000269|PubMed:11728527" FT /id="VAR_065451" FT VARIANT 421 FT /note="G -> D (in FA10D; significant loss of activity; FT dbSNP:rs758726161)" FT /evidence="ECO:0000269|PubMed:12574802, FT ECO:0000269|PubMed:25313940" FT /id="VAR_072752" FT VARIANT 448 FT /note="K -> N (in FA10D; San Giovanni Rotondo)" FT /evidence="ECO:0000269|PubMed:11248282" FT /id="VAR_065452" FT CONFLICT 285..288 FT /note="KVRV -> E (in Ref. 6; AAA51984 and 8; AAA52486)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="G -> S (in Ref. 5; AAA52490)" FT /evidence="ECO:0000305" FT HELIX 47..57 FT /evidence="ECO:0007829|PDB:1P0S" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:1P0S" FT HELIX 74..81 FT /evidence="ECO:0007829|PDB:1P0S" FT TURN 89..92 FT /evidence="ECO:0007829|PDB:1XKB" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1XKA" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:6YYX" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1XKB" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:3K9X" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:3K9X" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:3K9X" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 146..150 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1C5M" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:2JKH" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:2VWO" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:2JKH" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:1C5M" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 267..273 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 275..279 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:5VOF" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 291..295 FT /evidence="ECO:0007829|PDB:2PR3" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 305..310 FT /evidence="ECO:0007829|PDB:2JKH" FT TURN 316..319 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 324..330 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 346..352 FT /evidence="ECO:0007829|PDB:2JKH" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 356..364 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 372..376 FT /evidence="ECO:0007829|PDB:1C5M" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 387..393 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 408..411 FT /evidence="ECO:0007829|PDB:2JKH" FT TURN 416..420 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 430..439 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 441..444 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 450..454 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 455..458 FT /evidence="ECO:0007829|PDB:2JKH" FT HELIX 459..465 FT /evidence="ECO:0007829|PDB:2JKH" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:1HCG" SQ SEQUENCE 488 AA; 54732 MW; F81D5746AF4797AF CRC64; MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK //