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Database: UniProt
Entry: P00742
LinkDB: P00742
Original site: P00742 
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   13-FEB-2019, entry version 251.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   human 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
RT   protein 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
RT   project: 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
RT   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;
RP   GLU-60; 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.,
RA   Kwa E.Y., Weinstein B.;
RT   "Complete amino acid sequence of the light chain of human blood
RT   coagulation factor X: evidence for identification of residue 63 as
RT   beta-hydroxyaspartic 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;
RP   ASN-221 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
RT   encoding human factor X.";
RL   Gene 84:517-519(1989).
RN   [11]
RP   ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX   PubMed=6323392;
RA   Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
RT   "Mechanism of inhibition of activated protein C by protein C
RT   inhibitor.";
RL   J. Biochem. 95:187-195(1984).
RN   [12]
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-
RT   dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-
RT   associated factor Xa.";
RL   J. Biol. Chem. 285:20399-20409(2010).
RN   [13]
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
RT   N-and O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [14]
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   [15]
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
RT   factor Xa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998).
RN   [16]
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.,
RA   Karanjawala R., Lee W., Lentz D., Liang A.M., Morrissey M.M.,
RA   Phillips G.B., Post J., Sacchi K.L., Sakata S.T., Subramanyam B.,
RA   Vergona R., Walters J., White K.A., Whitlow M., Ye B., Zhao Z.,
RA   Shaw K.J.;
RT   "Substituted thiophene-anthranilamides as potent inhibitors of human
RT   factor Xa.";
RL   Bioorg. Med. Chem. 15:2127-2146(2007).
RN   [17]
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   [18]
RP   VARIANTS FA10D LYS-54 AND LYS-142, AND CHARACTERIZATION OF VARIANT
RP   FA10D LYS-54.
RX   PubMed=1973167;
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   [19]
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
RT   substitution of serine for proline at position 343.";
RL   Blood 77:317-323(1991).
RN   [20]
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
RT   the second EGF-like domain.";
RL   Br. J. Haematol. 90:910-915(1995).
RN   [21]
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
RT   factor X variant (factor XMarseille).";
RL   Eur. J. Biochem. 234:140-147(1995).
RN   [22]
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
RT   residue at position 14 in the light chain.";
RL   Hum. Genet. 95:212-214(1995).
RN   [23]
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
RT   active site mutation in factor X.";
RL   Blood Coagul. Fibrinolysis 7:5-14(1996).
RN   [24]
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
RT   residue 7 and characterization of the recombinant protein.";
RL   J. Biol. Chem. 271:28601-28606(1996).
RN   [25]
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
RT   Gla32 to Gln in the Gla domain (factor X Tokyo).";
RL   Br. J. Haematol. 106:809-811(1999).
RN   [26]
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
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [27]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [28]
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.,
RA   Reynaud J., Nieuwenhuis H.K., Bolton-Maggs P., Mannucci P.M.,
RA   Reverter J.C., Cachia P., 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   [29]
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   [30]
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.,
RA   Paolucci P., 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   [31]
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
RT   between true deficiency (Gly(380)-->Arg) and an abnormality
RT   (Ser(334)-->Pro).";
RL   Thromb. Res. 104:257-264(2001).
RN   [32]
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.,
RA   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   [33]
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.,
RA   Bernardi F.;
RT   "Impaired prothrombinase activity of factor X Gly381Asp results in
RT   severe familial CRM+ FX deficiency.";
RL   Thromb. Haemost. 89:243-248(2003).
RN   [34]
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   [35]
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.,
RA   Van Dreden P., Murata M., Ikeda Y.;
RT   "Genetic analysis of hereditary factor X deficiency in a French
RT   patient of Sri Lankan ancestry: in vitro expression study identified
RT   Gly366Ser substitution as the molecular basis of the dysfunctional
RT   factor X.";
RL   Blood Coagul. Fibrinolysis 16:9-16(2005).
RN   [36]
RP   VARIANT FA10D LYS-91.
RX   PubMed=17393015;
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
RT   with factor X-Riyadh anomaly.";
RL   Thromb. Haemost. 97:542-545(2007).
RN   [37]
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
RT   of coagulation factor X.";
RL   Thromb. Res. 124:144-148(2009).
RN   [38]
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
RP   AND 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
RT   mutants associated with decreased catalytic activity.";
RL   Biochemistry 53:6992-7001(2014).
RN   [39]
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.,
RA   Oner A.F.;
RT   "Frequency of the p.Gly262Asp mutation in congenital Factor X
RT   deficiency.";
RL   Eur. J. Clin. Invest. 45:1087-1091(2015).
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds
CC         in 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
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds. Forms a heterodimer with SERPINA5.
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
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly
CC       core 8 glycans. {ECO:0000269|PubMed:22171320,
CC       ECO:0000269|PubMed:8243461}.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate 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
CC       manifest prolonged nasal and mucosal hemorrhage, menorrhagia,
CC       hematuria, and occasionally hemarthrosis. Some patients do not
CC       have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877,
CC       ECO:0000269|PubMed:10739379, ECO:0000269|PubMed:10746568,
CC       ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527,
CC       ECO:0000269|PubMed:12574802, ECO:0000269|PubMed:12945883,
CC       ECO:0000269|PubMed:15075089, ECO:0000269|PubMed:15650540,
CC       ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706,
CC       ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698,
CC       ECO:0000269|PubMed:25313940, ECO:0000269|PubMed:26222694,
CC       ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671,
CC       ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633,
CC       ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-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/";
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   UniGene; Hs.361463; -.
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; 1MSX; Model; -; A=235-469.
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; 1NL8; Model; -; F=235-469, L=41-179.
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; 5JZZ; X-ray; 2.29 A; B=102-119.
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   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; 1MSX; -.
DR   PDBsum; 1NFU; -.
DR   PDBsum; 1NFW; -.
DR   PDBsum; 1NFX; -.
DR   PDBsum; 1NFY; -.
DR   PDBsum; 1NL8; -.
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; 5JZZ; -.
DR   PDBsum; 5K0H; -.
DR   PDBsum; 5VOE; -.
DR   PDBsum; 5VOF; -.
DR   ProteinModelPortal; P00742; -.
DR   SMR; P00742; -.
DR   BioGrid; 108457; 9.
DR   CORUM; P00742; -.
DR   DIP; DIP-29896N; -.
DR   ELM; P00742; -.
DR   IntAct; P00742; 12.
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; DB07278; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE.
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; 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; 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; DB00025; Antihemophilic Factor (Recombinant).
DR   DrugBank; DB06605; Apixaban.
DR   DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DR   DrugBank; DB13150; Coagulation factor VII human.
DR   DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DR   DrugBank; DB09075; Edoxaban.
DR   DrugBank; DB01225; Enoxaparin.
DR   DrugBank; DB00569; Fondaparinux sodium.
DR   DrugBank; DB03847; Gamma-Carboxy-Glutamic Acid.
DR   DrugBank; DB01109; Heparin.
DR   DrugBank; DB05713; LY-517717.
DR   DrugBank; DB00170; Menadione.
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; DB06228; Rivaroxaban.
DR   DrugBank; DB05362; SSR-126517E.
DR   GuidetoPHARMACOLOGY; 2359; -.
DR   MEROPS; S01.216; -.
DR   GlyConnect; 102; -.
DR   iPTMnet; P00742; -.
DR   PhosphoSitePlus; P00742; -.
DR   UniCarbKB; P00742; -.
DR   BioMuta; F10; -.
DR   DMDM; 119761; -.
DR   jPOST; P00742; -.
DR   PaxDb; P00742; -.
DR   PeptideAtlas; P00742; -.
DR   PRIDE; P00742; -.
DR   ProteomicsDB; 51275; -.
DR   Ensembl; ENST00000375559; ENSP00000364709; ENSG00000126218.
DR   GeneID; 2159; -.
DR   KEGG; hsa:2159; -.
DR   CTD; 2159; -.
DR   DisGeNET; 2159; -.
DR   EuPathDB; HostDB:ENSG00000126218.11; -.
DR   GeneCards; F10; -.
DR   HGNC; HGNC:3528; F10.
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   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000157694; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P00742; -.
DR   KO; K01314; -.
DR   OMA; CAGYDAK; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; P00742; -.
DR   TreeFam; TF327329; -.
DR   BioCyc; MetaCyc:HS05000-MONOMER; -.
DR   BRENDA; 3.4.21.6; 2681.
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   SABIO-RK; P00742; -.
DR   SIGNOR; P00742; -.
DR   ChiTaRS; F10; human.
DR   EvolutionaryTrace; P00742; -.
DR   GeneWiki; Factor_X; -.
DR   GenomeRNAi; 2159; -.
DR   PMAP-CutDB; P00742; -.
DR   PRO; PR:P00742; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000126218; Expressed in 127 organ(s), highest expression level in right lobe of liver.
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: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; IBA:GO_Central.
DR   GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
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   CDD; cd00190; Tryp_SPc; 1.
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; IPR013032; EGF-like_CS.
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; 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; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW   Hydrolase; Hydroxylation; Polymorphism; Protease; Reference proteome;
KW   Repeat; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   PROPEP       32     40       {ECO:0000269|PubMed:6871167}.
FT                                /FTId=PRO_0000027786.
FT   CHAIN        41    488       Coagulation factor X.
FT                                /FTId=PRO_0000027787.
FT   CHAIN        41    179       Factor X light chain.
FT                                /FTId=PRO_0000027788.
FT   CHAIN       183    488       Factor X heavy chain.
FT                                /FTId=PRO_0000027789.
FT   PROPEP      183    234       Activation peptide.
FT                                /FTId=PRO_0000027790.
FT   CHAIN       235    488       Activated factor Xa heavy chain.
FT                                /FTId=PRO_0000027791.
FT   DOMAIN       41     85       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      125    165       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      235    467       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION      183    203       O-glycosylated at one site.
FT   REGION      476    485       O-glycosylated at one site.
FT   ACT_SITE    276    276       Charge relay system.
FT   ACT_SITE    322    322       Charge relay system.
FT   ACT_SITE    419    419       Charge relay system.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      72     72       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES      79     79       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:6871167}.
FT   MOD_RES     103    103       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000269|PubMed:6871167}.
FT   CARBOHYD    199    199       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:8243461}.
FT   CARBOHYD    211    211       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:8243461}.
FT   CARBOHYD    221    221       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:8243461}.
FT                                /FTId=CAR_000012.
FT   CARBOHYD    231    231       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:8243461}.
FT                                /FTId=CAR_000013.
FT   DISULFID     57     62       {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       Interchain (between light and heavy
FT                                chains).
FT   DISULFID    241    246
FT   DISULFID    261    277
FT   DISULFID    390    404
FT   DISULFID    415    443
FT   VARIANT       7      7       L -> I (in dbSNP:rs5963).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_014162.
FT   VARIANT      30     30       Q -> H (in dbSNP:rs5961).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_014163.
FT   VARIANT      47     47       E -> G (in FA10D; St. Louis II; strongly
FT                                reduced activity; not activated by factor
FT                                VIIa and tissue factor;
FT                                dbSNP:rs121964943).
FT                                {ECO:0000269|PubMed:8910490}.
FT                                /FTId=VAR_065428.
FT   VARIANT      51     51       G -> V (in FA10D; dbSNP:rs751782758).
FT                                {ECO:0000269|PubMed:19135706}.
FT                                /FTId=VAR_065429.
FT   VARIANT      54     54       E -> G (in FA10D; Ketchikan;
FT                                dbSNP:rs121964944).
FT                                {ECO:0000269|PubMed:7860069}.
FT                                /FTId=VAR_065430.
FT   VARIANT      54     54       E -> K (in FA10D; Vorarlberg; converts
FT                                prothrombin at a normal rate but shows
FT                                decreased affinity for calcium;
FT                                dbSNP:rs121964939).
FT                                {ECO:0000269|PubMed:10746568,
FT                                ECO:0000269|PubMed:1973167}.
FT                                /FTId=VAR_065431.
FT   VARIANT      72     72       E -> Q (in FA10D; Tokyo;
FT                                dbSNP:rs121964945).
FT                                {ECO:0000269|PubMed:10468877}.
FT                                /FTId=VAR_065432.
FT   VARIANT      91     91       E -> K (in FA10D; Riyadh;
FT                                dbSNP:rs1477329751).
FT                                {ECO:0000269|PubMed:17393015}.
FT                                /FTId=VAR_065433.
FT   VARIANT     142    142       E -> K (in FA10D; uncertain pathological
FT                                significance; detected in patients
FT                                carrying K-54 or P-374; slightly reduced
FT                                activity; dbSNP:rs61753266).
FT                                {ECO:0000269|PubMed:10739379,
FT                                ECO:0000269|PubMed:1973167,
FT                                ECO:0000269|PubMed:7669671}.
FT                                /FTId=VAR_065434.
FT   VARIANT     149    149       C -> Y (in FA10D).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065435.
FT   VARIANT     151    151       C -> Y (in FA10D).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065436.
FT   VARIANT     152    152       A -> T (in dbSNP:rs3211772).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_020176.
FT   VARIANT     176    186       Missing (in FA10D; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26222694}.
FT                                /FTId=VAR_075212.
FT   VARIANT     192    192       G -> R (in dbSNP:rs3211783).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_020177.
FT   VARIANT     262    262       G -> D (in FA10D; unknown pathological
FT                                significance; dbSNP:rs1393705267).
FT                                {ECO:0000269|PubMed:26222694}.
FT                                /FTId=VAR_075213.
FT   VARIANT     289    289       G -> R (in FA10D; may affect splicing;
FT                                dbSNP:rs121964946).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065437.
FT   VARIANT     304    304       E -> K (in FA10D; dbSNP:rs747292771).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065438.
FT   VARIANT     322    322       D -> N (in FA10D; Stockton; 50% decrease
FT                                in specific activity; dbSNP:rs121964942).
FT                                {ECO:0000269|PubMed:25313940,
FT                                ECO:0000269|PubMed:8845463}.
FT                                /FTId=VAR_065439.
FT   VARIANT     327    327       R -> W (in FA10D; dbSNP:rs770119164).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065440.
FT   VARIANT     338    338       V -> M (in FA10D; dbSNP:rs121964947).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065441.
FT   VARIANT     350    350       E -> K (in FA10D; dbSNP:rs372309538).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065442.
FT   VARIANT     358    358       T -> M (in FA10D; Roma;
FT                                dbSNP:rs768222784).
FT                                {ECO:0000269|PubMed:10746568,
FT                                ECO:0000269|PubMed:25313940}.
FT                                /FTId=VAR_065443.
FT   VARIANT     363    363       G -> S (in FA10D).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065444.
FT   VARIANT     366    366       R -> C (in FA10D; San Antonio;
FT                                dbSNP:rs104894392).
FT                                {ECO:0000269|PubMed:2790181}.
FT                                /FTId=VAR_065445.
FT   VARIANT     374    374       S -> P (in FA10D; Marseille; decreased
FT                                cleavage by factor IXa; normal catalytic
FT                                efficiency for prothrombin;
FT                                dbSNP:rs121964941).
FT                                {ECO:0000269|PubMed:11728527,
FT                                ECO:0000269|PubMed:7669671,
FT                                ECO:0000269|PubMed:8529633}.
FT                                /FTId=VAR_065446.
FT   VARIANT     382    382       V -> A (in FA10D; partial loss of
FT                                activity). {ECO:0000269|PubMed:15075089,
FT                                ECO:0000269|PubMed:25313940}.
FT                                /FTId=VAR_072751.
FT   VARIANT     383    383       P -> S (in FA10D; Friuli;
FT                                dbSNP:rs121964940).
FT                                {ECO:0000269|PubMed:1985698}.
FT                                /FTId=VAR_065447.
FT   VARIANT     390    390       C -> F (in FA10D; Padua 4;
FT                                dbSNP:rs199778916).
FT                                {ECO:0000269|PubMed:12945883}.
FT                                /FTId=VAR_065448.
FT   VARIANT     404    404       C -> R (in FA10D).
FT                                {ECO:0000269|PubMed:10746568}.
FT                                /FTId=VAR_065449.
FT   VARIANT     406    406       G -> S (in FA10D; almost complete loss of
FT                                activity; dbSNP:rs376163818).
FT                                {ECO:0000269|PubMed:15650540,
FT                                ECO:0000269|PubMed:25313940}.
FT                                /FTId=VAR_065450.
FT   VARIANT     420    420       G -> R (in FA10D; Padua 3;
FT                                dbSNP:rs750759634).
FT                                {ECO:0000269|PubMed:11728527}.
FT                                /FTId=VAR_065451.
FT   VARIANT     421    421       G -> D (in FA10D; significant loss of
FT                                activity; dbSNP:rs758726161).
FT                                {ECO:0000269|PubMed:12574802,
FT                                ECO:0000269|PubMed:25313940}.
FT                                /FTId=VAR_072752.
FT   VARIANT     448    448       K -> N (in FA10D; San Giovanni Rotondo).
FT                                {ECO:0000269|PubMed:11248282}.
FT                                /FTId=VAR_065452.
FT   CONFLICT    285    288       KVRV -> E (in Ref. 6; AAA51984 and 8;
FT                                AAA52486). {ECO:0000305}.
FT   CONFLICT    442    442       G -> S (in Ref. 5; AAA52490).
FT                                {ECO:0000305}.
FT   HELIX        47     57       {ECO:0000244|PDB:1P0S}.
FT   HELIX        64     71       {ECO:0000244|PDB:1P0S}.
FT   HELIX        74     81       {ECO:0000244|PDB:1P0S}.
FT   TURN         89     92       {ECO:0000244|PDB:1XKB}.
FT   STRAND       96     98       {ECO:0000244|PDB:1XKA}.
FT   STRAND      100    102       {ECO:0000244|PDB:3K9X}.
FT   STRAND      105    107       {ECO:0000244|PDB:1XKB}.
FT   STRAND      109    111       {ECO:0000244|PDB:3K9X}.
FT   STRAND      116    118       {ECO:0000244|PDB:3K9X}.
FT   STRAND      123    125       {ECO:0000244|PDB:3K9X}.
FT   TURN        129    131       {ECO:0000244|PDB:2JKH}.
FT   HELIX       132    135       {ECO:0000244|PDB:2JKH}.
FT   STRAND      137    143       {ECO:0000244|PDB:2JKH}.
FT   STRAND      146    150       {ECO:0000244|PDB:2JKH}.
FT   STRAND      155    157       {ECO:0000244|PDB:2JKH}.
FT   STRAND      164    170       {ECO:0000244|PDB:2JKH}.
FT   STRAND      172    174       {ECO:0000244|PDB:1C5M}.
FT   STRAND      236    240       {ECO:0000244|PDB:2JKH}.
FT   TURN        243    245       {ECO:0000244|PDB:2VWO}.
FT   STRAND      249    253       {ECO:0000244|PDB:2JKH}.
FT   TURN        255    257       {ECO:0000244|PDB:1C5M}.
FT   STRAND      259    265       {ECO:0000244|PDB:2JKH}.
FT   STRAND      267    273       {ECO:0000244|PDB:2JKH}.
FT   HELIX       275    279       {ECO:0000244|PDB:2JKH}.
FT   STRAND      281    283       {ECO:0000244|PDB:5VOF}.
FT   STRAND      285    289       {ECO:0000244|PDB:2JKH}.
FT   STRAND      291    295       {ECO:0000244|PDB:2PR3}.
FT   STRAND      301    303       {ECO:0000244|PDB:2JKH}.
FT   STRAND      305    310       {ECO:0000244|PDB:2JKH}.
FT   TURN        316    319       {ECO:0000244|PDB:2JKH}.
FT   STRAND      324    330       {ECO:0000244|PDB:2JKH}.
FT   HELIX       346    352       {ECO:0000244|PDB:2JKH}.
FT   TURN        353    355       {ECO:0000244|PDB:2JKH}.
FT   STRAND      356    364       {ECO:0000244|PDB:2JKH}.
FT   STRAND      366    368       {ECO:0000244|PDB:2JKH}.
FT   STRAND      372    376       {ECO:0000244|PDB:1C5M}.
FT   STRAND      378    385       {ECO:0000244|PDB:2JKH}.
FT   HELIX       387    393       {ECO:0000244|PDB:2JKH}.
FT   STRAND      402    406       {ECO:0000244|PDB:2JKH}.
FT   STRAND      408    411       {ECO:0000244|PDB:2JKH}.
FT   TURN        416    420       {ECO:0000244|PDB:2JKH}.
FT   STRAND      422    427       {ECO:0000244|PDB:2JKH}.
FT   STRAND      430    439       {ECO:0000244|PDB:2JKH}.
FT   STRAND      441    444       {ECO:0000244|PDB:2JKH}.
FT   STRAND      450    454       {ECO:0000244|PDB:2JKH}.
FT   HELIX       455    458       {ECO:0000244|PDB:2JKH}.
FT   HELIX       459    465       {ECO:0000244|PDB:2JKH}.
FT   STRAND      471    473       {ECO:0000244|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
//
DBGET integrated database retrieval system