FA10_HUMAN
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 03-AUG-2022, entry version 270.
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/";
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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 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 AlphaFoldDB; P00742; -.
DR SMR; P00742; -.
DR BioGRID; 108457; 43.
DR ComplexPortal; CPX-6215; Coagulation factor Xa complex.
DR CORUM; P00742; -.
DR DIP; DIP-29896N; -.
DR ELM; P00742; -.
DR IntAct; P00742; 15.
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 GlyGen; P00742; 14 sites, 26 N-linked glycans (2 sites), 4 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; P00742; -.
DR PeptideAtlas; P00742; -.
DR PRIDE; P00742; -.
DR ProteomicsDB; 51275; -.
DR ABCD; P00742; 1 sequenced antibody.
DR Antibodypedia; 11687; 688 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 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; HCLHQAK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00742; -.
DR TreeFam; TF327329; -.
DR BioCyc; MetaCyc:HS05000-MON; -.
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; 14 hits in 1076 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 109 other tissues.
DR ExpressionAtlas; P00742; baseline and differential.
DR Genevisible; P00742; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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:0031233; C:intrinsic component of external side of plasma membrane; IC:BHF-UCL.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
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; IBA:GO_Central.
DR GO; GO:0072377; P:blood coagulation, common pathway; IC:ComplexPortal.
DR GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0031638; P:zymogen activation; IDA:ComplexPortal.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
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 Pfam; PF00008; EGF; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 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.
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 pathological
FT significance; detected in patients carrying K-54 or P-374;
FT slightly reduced 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; unknown pathological
FT 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; unknown pathological 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
