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Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]

 FA10_HUMAN              Reviewed;         488 AA.
P00742; Q14340;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
25-OCT-2017, entry version 237.
RecName: Full=Coagulation factor X;
EC=3.4.21.6;
AltName: Full=Stuart factor;
AltName: Full=Stuart-Prower factor;
Contains:
RecName: Full=Factor X light chain;
Contains:
RecName: Full=Factor X heavy chain;
Contains:
RecName: Full=Activated factor Xa heavy chain;
Flags: Precursor;
Name=F10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1902434; DOI=10.1016/0378-1119(91)90141-W;
Messier T.L., Pittman D.D., Long G.L., Kaufman R.J., Church W.R.;
"Cloning and expression in COS-1 cells of a full-length cDNA encoding
human coagulation factor X.";
Gene 99:291-294(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3768336; DOI=10.1021/bi00366a018;
Leytus S.P., Foster D.C., Kurachi K., Davie E.W.;
"Gene for human factor X: a blood coagulation factor whose gene
organization is essentially identical with that of factor IX and
protein C.";
Biochemistry 25:5098-5102(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-152 AND ARG-192.
SeattleSNPs variation discovery resource;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-488.
PubMed=2582420; DOI=10.1073/pnas.82.11.3591;
Fung M.R., Hay C.W., McGillivray R.T.A.;
"Characterization of an almost full-length cDNA coding for human blood
coagulation factor X.";
Proc. Natl. Acad. Sci. U.S.A. 82:3591-3595(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-488.
TISSUE=Liver;
PubMed=3011603; DOI=10.1016/0378-1119(86)90112-5;
Kaul R.K., Hildebrand B., Roberts S., Jagadeeswaran P.;
"Isolation and characterization of human blood-coagulation factor X
cDNA.";
Gene 41:311-314(1986).
[7]
PROTEIN SEQUENCE OF 41-179, HYDROXYLATION AT ASP-103, AND
GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59;
GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-79.
PubMed=6871167; DOI=10.1021/bi00281a016;
McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N.,
Kwa E.Y., Weinstein B.;
"Complete amino acid sequence of the light chain of human blood
coagulation factor X: evidence for identification of residue 63 as
beta-hydroxyaspartic acid.";
Biochemistry 22:2875-2884(1983).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 115-488, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=6587384; DOI=10.1073/pnas.81.12.3699;
Leytus S.P., Chung D.W., Kisiel W., Kurachi K., Davie E.W.;
"Characterization of a cDNA coding for human factor X.";
Proc. Natl. Acad. Sci. U.S.A. 81:3699-3702(1984).
[9]
PROTEIN SEQUENCE OF 183-234, AND GLYCOSYLATION AT THR-199; THR-211;
ASN-221 AND ASN-231.
PubMed=8243461; DOI=10.1111/j.1432-1033.1993.tb18361.x;
Inoue K., Morita T.;
"Identification of O-linked oligosaccharide chains in the activation
peptides of blood coagulation factor X. The role of the carbohydrate
moieties in the activation of factor X.";
Eur. J. Biochem. 218:153-163(1993).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
PubMed=2612918; DOI=10.1016/0378-1119(89)90529-5;
Jagadeeswaran P., Reddy S.V., Rao K.J., Hamsabhushanam K., Lyman G.;
"Cloning and characterization of the 5' end (exon 1) of the gene
encoding human factor X.";
Gene 84:517-519(1989).
[11]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=6323392;
Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
"Mechanism of inhibition of activated protein C by protein C
inhibitor.";
J. Biochem. 95:187-195(1984).
[12]
ENZYME REGULATION.
PubMed=20427285; DOI=10.1074/jbc.M110.112748;
Huang X., Dementiev A., Olson S.T., Gettins P.G.;
"Basis for the specificity and activation of the serpin protein Z-
dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-
associated factor Xa.";
J. Biol. Chem. 285:20399-20409(2010).
[13]
GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278.
PubMed=8355279; DOI=10.1006/jmbi.1993.1441;
Padmanabhan K., Padmanabhan K.P., Tulinsky A., Park C.H., Bode W.,
Huber R., Blankenship D.T., Cardin A.D., Kisiel W.;
"Structure of human des(1-45) factor Xa at 2.2-A resolution.";
J. Mol. Biol. 232:947-966(1993).
[15]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278.
PubMed=9618463; DOI=10.1073/pnas.95.12.6630;
Kamata K., Kawamoto H., Honma T., Iwama T., Kim S.H.;
"Structural basis for chemical inhibition of human blood coagulation
factor Xa.";
Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998).
[16]
X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 127-467.
PubMed=17227710; DOI=10.1016/j.bmc.2006.12.019;
Kochanny M.J., Adler M., Ewing J., Griedel B.D., Ho E.,
Karanjawala R., Lee W., Lentz D., Liang A.M., Morrissey M.M.,
Phillips G.B., Post J., Sacchi K.L., Sakata S.T., Subramanyam B.,
Vergona R., Walters J., White K.A., Whitlow M., Ye B., Zhao Z.,
Shaw K.J.;
"Substituted thiophene-anthranilamides as potent inhibitors of human
factor Xa.";
Bioorg. Med. Chem. 15:2127-2146(2007).
[17]
VARIANT FA10D CYS-366.
PubMed=2790181;
Reddy S.V., Zhou Z.Q., Rao K.J., Scott J.P., Watzke H., High K.A.,
Jagadeeswaran P.;
"Molecular characterization of human factor XSan Antonio.";
Blood 74:1486-1490(1989).
[18]
VARIANTS FA10D LYS-54 AND LYS-142, AND CHARACTERIZATION OF VARIANT
FA10D LYS-54.
PubMed=1973167;
Watzke H.H., Lechner K., Roberts H.R., Reddy S.V., Welsch D.J.,
Friedman P., Mahr G., Jagadeeswaran P., Monroe D.M., High K.A.;
"Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X
'Vorarlberg').";
J. Biol. Chem. 265:11982-11989(1990).
[19]
VARIANT FA10D SER-383.
PubMed=1985698;
James H.L., Girolami A., Fair D.S.;
"Molecular defect in coagulation factor XFriuli results from a
substitution of serine for proline at position 343.";
Blood 77:317-323(1991).
[20]
VARIANTS FA10D LYS-142 AND PRO-374.
PubMed=7669671; DOI=10.1111/j.1365-2141.1995.tb05214.x;
Marchetti G., Castaman G., Pinotti M., Lunghi B., Di Iasio M.G.,
Ruggieri M., Rodeghiero F., Bernardi F.;
"Molecular bases of CRM+ factor X deficiency: a frequent mutation
(Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in
the second EGF-like domain.";
Br. J. Haematol. 90:910-915(1995).
[21]
VARIANT FA10D PRO-374, AND CHARACTERIZATION OF VARIANT FA10D PRO-374.
PubMed=8529633; DOI=10.1111/j.1432-1033.1995.140_c.x;
Bezeaud A., Miyata T., Helley D., Zeng Y.Z., Kato H., Aillaud M.F.,
Juhan-Vague I., Guillin M.C.;
"Functional consequences of the Ser334-->Pro mutation in a human
factor X variant (factor XMarseille).";
Eur. J. Biochem. 234:140-147(1995).
[22]
VARIANT FA10D GLY-54.
PubMed=7860069; DOI=10.1007/BF00209404;
Kim D.J., Thompson A.R., James H.L.;
"Factor XKetchikan: a variant molecule in which Gly replaces a Gla
residue at position 14 in the light chain.";
Hum. Genet. 95:212-214(1995).
[23]
VARIANT FA10D ASN-322, AND CHARACTERIZATION OF VARIANT FA10D ASN-322.
PubMed=8845463;
Messier T.L., Wong C.Y., Bovill E.G., Long G.L., Church W.R.;
"Factor X Stockton: a mild bleeding diathesis associated with an
active site mutation in factor X.";
Blood Coagul. Fibrinolysis 7:5-14(1996).
[24]
VARIANT FA10D GLY-47.
PubMed=8910490; DOI=10.1074/jbc.271.45.28601;
Rudolph A.E., Mullane M.P., Porche-Sorbet R., Tsuda S., Miletich J.P.;
"Factor XSt. Louis II. Identification of a glycine substitution at
residue 7 and characterization of the recombinant protein.";
J. Biol. Chem. 271:28601-28606(1996).
[25]
VARIANT FA10D GLN-72.
PubMed=10468877; DOI=10.1046/j.1365-2141.1999.01614.x;
Zama T., Murata M., Watanabe R., Yokoyama K., Moriki T., Ambo H.,
Murakami H., Kikuchi M., Ikeda Y.;
"A family with hereditary factor X deficiency with a point mutation
Gla32 to Gln in the Gla domain (factor X Tokyo).";
Br. J. Haematol. 106:809-811(1999).
[26]
VARIANTS ILE-7 AND HIS-30.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[27]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[28]
VARIANTS FA10D LYS-54; TYR-149; TYR-151; ARG-289; LYS-304; TRP-327;
MET-338; LYS-350; MET-358; SER-363 AND ARG-404.
PubMed=10746568; DOI=10.1007/s004390051035;
Millar D.S., Elliston L., Deex P., Krawczak M., Wacey A.I.,
Reynaud J., Nieuwenhuis H.K., Bolton-Maggs P., Mannucci P.M.,
Reverter J.C., Cachia P., Pasi K.J., Layton D.M., Cooper D.N.;
"Molecular analysis of the genotype-phenotype relationship in factor X
deficiency.";
Hum. Genet. 106:249-257(2000).
[29]
CHARACTERIZATION OF VARIANT FA10D LYS-142.
PubMed=10739379;
Forberg E., Huhmann I., Jimenez-Boj E., Watzke H.H.;
"The impact of Glu102Lys on the factor X function in a patient with a
doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys).";
Thromb. Haemost. 83:234-238(2000).
[30]
VARIANT FA10D ASN-448.
PubMed=11248282; DOI=10.1016/S0049-3848(00)00406-0;
Simioni P., Vianello F., Kalafatis M., Barzon L., Ladogana S.,
Paolucci P., Carotenuto M., Dal Bello F., Palu G., Girolami A.;
"A dysfunctional factor X (factor X San Giovanni Rotondo) present at
homozygous and double heterozygous level: identification of a novel
microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the
factor X gene. A study of an Italian family.";
Thromb. Res. 101:219-230(2001).
[31]
VARIANTS FA10D PRO-374 AND ARG-420.
PubMed=11728527; DOI=10.1016/S0049-3848(01)00371-1;
Vianello F., Lombardi A.M., Boldrin C., Luni S., Girolami A.;
"A new factor X defect (factor X Padua 3): a compound heterozygous
between true deficiency (Gly(380)-->Arg) and an abnormality
(Ser(334)-->Pro).";
Thromb. Res. 104:257-264(2001).
[32]
VARIANT FA10D PHE-390.
PubMed=12945883; DOI=10.1097/00001721-200306000-00012;
Vianello F., Lombardi A.M., Bello F.D., Palu G., Zanon E.,
Girolami A.;
"A novel type I factor X variant (factor X Cys350Phe) due to loss of a
disulfide bond in the catalytic domain.";
Blood Coagul. Fibrinolysis 14:401-405(2003).
[33]
VARIANT FA10D ASP-421, AND CHARACTERIZATION OF VARIANT FA10D ASP-421.
PubMed=12574802;
Pinotti M., Camire R.M., Baroni M., Rajab A., Marchetti G.,
Bernardi F.;
"Impaired prothrombinase activity of factor X Gly381Asp results in
severe familial CRM+ FX deficiency.";
Thromb. Haemost. 89:243-248(2003).
[34]
VARIANT FA10D ALA-382, AND CHARACTERIZATION OF VARIANT FA10D ALA-382.
PubMed=15075089;
Pinotti M., Monti M., Baroni M., Marchetti G., Bernardi F.;
"Molecular characterization of factor X deficiency associated with
borderline plasma factor X level.";
Haematologica 89:501-502(2004).
[35]
VARIANT FA10D SER-406, AND CHARACTERIZATION OF VARIANT FA10D SER-406.
PubMed=15650540; DOI=10.1097/00001721-200501000-00002;
Isshiki I., Favier R., Moriki T., Uchida T., Ishihara H.,
Van Dreden P., Murata M., Ikeda Y.;
"Genetic analysis of hereditary factor X deficiency in a French
patient of Sri Lankan ancestry: in vitro expression study identified
Gly366Ser substitution as the molecular basis of the dysfunctional
factor X.";
Blood Coagul. Fibrinolysis 16:9-16(2005).
[36]
VARIANT FA10D LYS-91.
PubMed=17393015;
Al-Hilali A., Wulff K., Abdel-Razeq H., Saud K.A., Al-Gaili F.,
Herrmann F.H.;
"Analysis of the novel factor X gene mutation Glu51Lys in two families
with factor X-Riyadh anomaly.";
Thromb. Haemost. 97:542-545(2007).
[37]
VARIANT FA10D VAL-51.
PubMed=19135706; DOI=10.1016/j.thromres.2008.11.018;
Chafa O., Tagzirt M., Tapon-Bretaudiere J., Reghis A., Fischer A.M.,
LeBonniec B.F.;
"Characterization of a homozygous Gly11Val mutation in the Gla domain
of coagulation factor X.";
Thromb. Res. 124:144-148(2009).
[38]
VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421, AND
CHARACTERIZATION OF VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406
AND ASP-421.
PubMed=25313940; DOI=10.1021/bi500770p;
Abdel-Azeim S., Oliva R., Chermak E., De Cristofaro R., Cavallo L.;
"Molecular dynamics characterization of five pathogenic Factor X
mutants associated with decreased catalytic activity.";
Biochemistry 53:6992-7001(2014).
[39]
VARIANTS FA10D 176-THR--GLN-186 DEL AND ASP-262.
PubMed=26222694; DOI=10.1111/eci.12511;
Epcacan S., Menegatti M., Akbayram S., Cairo A., Peyvandi F.,
Oner A.F.;
"Frequency of the p.Gly262Asp mutation in congenital Factor X
deficiency.";
Eur. J. Clin. Invest. 45:1087-1091(2015).
-!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
converts prothrombin to thrombin in the presence of factor Va,
calcium and phospholipid during blood clotting.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then
Arg-|-Ile bonds in prothrombin to form thrombin.
-!- ENZYME REGULATION: Inhibited by SERPINA5 and SERPINA10.
{ECO:0000269|PubMed:20427285, ECO:0000269|PubMed:6323392}.
-!- SUBUNIT: The two chains are formed from a single-chain precursor
by the excision of two Arg residues and are held together by 1 or
more disulfide bonds. Forms a heterodimer with SERPINA5.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
{ECO:0000269|PubMed:6587384}.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
glutamate residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly
core 8 glycans. {ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:8243461}.
-!- PTM: The activation peptide is cleaved by factor IXa (in the
intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6871167}.
-!- DISEASE: Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic
disease with variable presentation. Affected individuals can
manifest prolonged nasal and mucosal hemorrhage, menorrhagia,
hematuria, and occasionally hemarthrosis. Some patients do not
have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877,
ECO:0000269|PubMed:10739379, ECO:0000269|PubMed:10746568,
ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527,
ECO:0000269|PubMed:12574802, ECO:0000269|PubMed:12945883,
ECO:0000269|PubMed:15075089, ECO:0000269|PubMed:15650540,
ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706,
ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698,
ECO:0000269|PubMed:25313940, ECO:0000269|PubMed:26222694,
ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671,
ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633,
ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor X entry;
URL="https://en.wikipedia.org/wiki/Factor_X";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f10/";
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EMBL; K03194; AAA52490.1; -; mRNA.
EMBL; M57285; AAA52421.1; -; mRNA.
EMBL; AF503510; AAM19347.1; -; Genomic_DNA.
EMBL; BC046125; AAH46125.1; -; mRNA.
EMBL; N00045; AAA52764.1; -; Genomic_DNA.
EMBL; L00390; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00391; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00392; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00393; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00394; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00395; AAA52764.1; JOINED; Genomic_DNA.
EMBL; L00396; AAA52764.1; JOINED; Genomic_DNA.
EMBL; M22613; AAA51984.1; -; mRNA.
EMBL; K01886; AAA52486.1; -; mRNA.
EMBL; M33297; AAA52636.1; -; Genomic_DNA.
CCDS; CCDS9530.1; -.
PIR; A24478; EXHU.
RefSeq; NP_000495.1; NM_000504.3.
RefSeq; NP_001299603.1; NM_001312674.1.
RefSeq; NP_001299604.1; NM_001312675.1.
UniGene; Hs.361463; -.
PDB; 1C5M; X-ray; 1.95 A; D=235-488, F=84-179.
PDB; 1EZQ; X-ray; 2.20 A; A=235-488, B=46-179.
PDB; 1F0R; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 1F0S; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 1FAX; X-ray; 3.00 A; A=235-488, L=84-179.
PDB; 1FJS; X-ray; 1.92 A; A=235-468, L=127-178.
PDB; 1FXY; X-ray; 2.15 A; A=235-344.
PDB; 1G2L; X-ray; 1.90 A; A=235-469, B=86-179.
PDB; 1G2M; X-ray; 3.02 A; A=235-469, B=86-179.
PDB; 1HCG; X-ray; 2.20 A; A=235-475, B=129-179.
PDB; 1IOE; X-ray; 2.90 A; A=235-469, L=84-179.
PDB; 1IQE; X-ray; 2.90 A; A=235-469, L=84-179.
PDB; 1IQF; X-ray; 3.20 A; A=235-469, L=84-179.
PDB; 1IQG; X-ray; 2.60 A; A=235-469, L=84-179.
PDB; 1IQH; X-ray; 3.00 A; A=235-469, L=84-179.
PDB; 1IQI; X-ray; 2.90 A; A=235-469, L=84-179.
PDB; 1IQJ; X-ray; 3.00 A; A=235-469, L=84-179.
PDB; 1IQK; X-ray; 3.20 A; A=235-469, L=84-179.
PDB; 1IQL; X-ray; 2.70 A; A=235-469, L=84-179.
PDB; 1IQM; X-ray; 2.60 A; A=235-469, L=84-179.
PDB; 1IQN; X-ray; 2.60 A; A=235-469, L=84-179.
PDB; 1KSN; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 1LPG; X-ray; 2.00 A; A=46-179, B=235-488.
PDB; 1LPK; X-ray; 2.20 A; A=46-179, B=235-488.
PDB; 1LPZ; X-ray; 2.40 A; A=46-179, B=235-488.
PDB; 1LQD; X-ray; 2.70 A; A=46-179, B=235-488.
PDB; 1MQ5; X-ray; 2.10 A; A=235-467, L=127-177.
PDB; 1MQ6; X-ray; 2.10 A; A=235-467, L=127-177.
PDB; 1MSX; Model; -; A=235-469.
PDB; 1NFU; X-ray; 2.05 A; A=235-488, B=46-240.
PDB; 1NFW; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 1NFX; X-ray; 2.15 A; A=235-488, B=46-179.
PDB; 1NFY; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 1NL8; Model; -; F=235-469, L=41-179.
PDB; 1P0S; X-ray; 2.80 A; H=235-488, L=41-178.
PDB; 1V3X; X-ray; 2.20 A; A=235-467, B=127-178.
PDB; 1WU1; X-ray; 2.30 A; A=235-467, B=85-179.
PDB; 1XKA; X-ray; 2.30 A; C=235-469, L=85-179.
PDB; 1XKB; X-ray; 2.40 A; A/B=85-179, C/D=235-469.
PDB; 1Z6E; X-ray; 1.80 A; A=235-468, L=127-178.
PDB; 2BMG; X-ray; 2.70 A; A=126-178, B=235-468.
PDB; 2BOH; X-ray; 2.20 A; A=46-179, B=235-488.
PDB; 2BOK; X-ray; 1.64 A; A=235-475, L=126-180.
PDB; 2BQ6; X-ray; 3.00 A; A=126-177, B=220-468.
PDB; 2BQ7; X-ray; 2.20 A; A=126-177, B=220-468.
PDB; 2BQW; X-ray; 2.95 A; A=126-177, B=220-468.
PDB; 2CJI; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 2D1J; X-ray; 2.20 A; A=235-467, B=125-178.
PDB; 2EI6; X-ray; 2.30 A; A=235-467, B=125-178.
PDB; 2EI7; X-ray; 2.30 A; A=235-467, B=125-178.
PDB; 2EI8; X-ray; 2.10 A; A=235-467, B=125-178.
PDB; 2FZZ; X-ray; 2.20 A; A=235-468, L=127-178.
PDB; 2G00; X-ray; 2.10 A; A=235-468, L=127-178.
PDB; 2GD4; X-ray; 3.30 A; A/L=126-182, B/H=235-475.
PDB; 2H9E; X-ray; 2.20 A; H=235-467, L=86-234.
PDB; 2J2U; X-ray; 1.90 A; A=235-488, B=46-179.
PDB; 2J34; X-ray; 2.01 A; A=235-488, B=46-179.
PDB; 2J38; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 2J4I; X-ray; 1.80 A; A=235-488, B=46-179.
PDB; 2J94; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 2J95; X-ray; 2.01 A; A=235-488, B=46-179.
PDB; 2JKH; X-ray; 1.25 A; A=235-475, L=126-180.
PDB; 2P16; X-ray; 2.30 A; A=235-468, L=127-178.
PDB; 2P3F; X-ray; 3.10 A; H=235-469, L=125-178.
PDB; 2P3T; X-ray; 1.92 A; A=127-178, B=235-467.
PDB; 2P3U; X-ray; 1.62 A; A=127-178, B=235-467.
PDB; 2P93; X-ray; 1.90 A; A=235-468, L=127-178.
PDB; 2P94; X-ray; 1.80 A; A=235-468, L=127-178.
PDB; 2P95; X-ray; 2.20 A; A=235-468, L=127-178.
PDB; 2PHB; X-ray; 2.30 A; A=235-468, B=128-178.
PDB; 2PR3; X-ray; 1.50 A; A=235-468, B=128-178.
PDB; 2Q1J; X-ray; 1.90 A; A=235-468, B=128-178.
PDB; 2RA0; X-ray; 2.30 A; A=235-468, L=128-178.
PDB; 2UWL; X-ray; 1.90 A; A=235-488, B=46-179.
PDB; 2UWO; X-ray; 1.75 A; A=235-488, B=46-179.
PDB; 2UWP; X-ray; 1.75 A; A=235-488, B=46-179.
PDB; 2VH0; X-ray; 1.70 A; A=235-488, B=46-179.
PDB; 2VH6; X-ray; 1.95 A; A=235-488, B=46-177.
PDB; 2VVC; X-ray; 1.95 A; A/B=235-475, K/L=126-180.
PDB; 2VVU; X-ray; 2.30 A; A=235-475, L=126-180.
PDB; 2VVV; X-ray; 1.73 A; A=235-475, L=126-180.
PDB; 2VWL; X-ray; 1.80 A; A=235-475, L=126-180.
PDB; 2VWM; X-ray; 1.96 A; A/B=235-475, K/L=126-180.
PDB; 2VWN; X-ray; 1.61 A; A=235-475, L=126-180.
PDB; 2VWO; X-ray; 1.60 A; A=235-475, L=126-180.
PDB; 2W26; X-ray; 2.08 A; A=235-468, B=129-177.
PDB; 2W3I; X-ray; 1.90 A; A=235-468, B=128-178.
PDB; 2W3K; X-ray; 2.05 A; A=235-468, B=128-178.
PDB; 2WYG; X-ray; 1.88 A; A=235-487, B=46-179.
PDB; 2WYJ; X-ray; 2.38 A; A=235-488, B=46-179.
PDB; 2XBV; X-ray; 1.66 A; A=235-475, L=126-180.
PDB; 2XBW; X-ray; 1.72 A; A=235-475, L=126-180.
PDB; 2XBX; X-ray; 1.85 A; A=235-475, L=126-180.
PDB; 2XBY; X-ray; 2.02 A; A=235-475, L=126-180.
PDB; 2XC0; X-ray; 2.05 A; A=235-475, L=126-180.
PDB; 2XC4; X-ray; 1.67 A; A=235-475, L=126-180.
PDB; 2XC5; X-ray; 1.70 A; A=235-475, L=126-180.
PDB; 2Y5F; X-ray; 1.29 A; A=235-468, L=127-180.
PDB; 2Y5G; X-ray; 1.29 A; A=235-468, L=127-180.
PDB; 2Y5H; X-ray; 1.33 A; A=235-468, L=127-180.
PDB; 2Y7X; X-ray; 1.90 A; A=235-488, B=46-179.
PDB; 2Y7Z; X-ray; 1.84 A; A=235-488, B=46-179.
PDB; 2Y80; X-ray; 1.90 A; A=235-488, B=46-179.
PDB; 2Y81; X-ray; 1.70 A; A=235-488, B=46-179.
PDB; 2Y82; X-ray; 2.20 A; A=235-488, B=46-179.
PDB; 3CEN; X-ray; 1.60 A; A=235-468, L=127-178.
PDB; 3CS7; X-ray; 2.20 A; A=235-468, L=127-178.
PDB; 3ENS; X-ray; 2.30 A; A/C=85-178, B/D=235-472.
PDB; 3FFG; X-ray; 1.54 A; A=235-468, L=127-178.
PDB; 3HPT; X-ray; 2.19 A; A/C=85-178, B/D=235-472.
PDB; 3IIT; X-ray; 1.80 A; A=235-467, B=125-178.
PDB; 3K9X; X-ray; 1.90 A; A/C=85-178, B/D=235-472.
PDB; 3KL6; X-ray; 1.45 A; A=235-475, B=126-179.
PDB; 3KQB; X-ray; 2.25 A; A=235-468, L=127-178.
PDB; 3KQC; X-ray; 2.20 A; A=235-468, L=127-178.
PDB; 3KQD; X-ray; 2.75 A; A=235-468, L=127-178.
PDB; 3KQE; X-ray; 2.35 A; A=235-468, L=127-178.
PDB; 3LIW; X-ray; 2.22 A; A=235-468, B=128-178.
PDB; 3M36; X-ray; 2.15 A; A=235-468, L=127-178.
PDB; 3M37; X-ray; 1.90 A; A=235-468, L=127-178.
PDB; 3Q3K; X-ray; 2.00 A; A=235-467, B=125-178.
PDB; 3SW2; X-ray; 2.42 A; A=85-178, B=235-472.
PDB; 3TK5; X-ray; 2.20 A; A=235-467, B=125-178.
PDB; 3TK6; X-ray; 1.80 A; A=235-467, B=125-178.
PDB; 4A7I; X-ray; 2.40 A; A=84-179, B=235-488.
PDB; 4BTI; X-ray; 2.30 A; A/E=84-179, B/F=235-488.
PDB; 4BTT; X-ray; 2.59 A; A/E=84-179, B/F=235-488.
PDB; 4BTU; X-ray; 2.37 A; A/E=84-179, B/F=235-488.
PDB; 4Y6D; X-ray; 1.55 A; A=235-488, B=46-179.
PDB; 4Y71; X-ray; 1.80 A; A=235-488, B=46-179.
PDB; 4Y76; X-ray; 2.00 A; A=235-488, B=46-179.
PDB; 4Y79; X-ray; 2.10 A; A=235-488, B=46-179.
PDB; 4Y7A; X-ray; 1.99 A; A=235-488, B=46-179.
PDB; 4Y7B; X-ray; 1.79 A; A=235-488, B=46-179.
PDB; 4ZH8; X-ray; 1.80 A; A=235-488, B=46-179.
PDB; 4ZHA; X-ray; 1.86 A; A=235-488, B=46-179.
PDB; 5JQY; X-ray; 1.99 A; B=86-124.
PDB; 5JTC; X-ray; 2.24 A; B=86-124.
PDB; 5JZ8; X-ray; 2.10 A; B=86-124.
PDB; 5JZU; X-ray; 2.50 A; B=86-111.
PDB; 5JZZ; X-ray; 2.29 A; B=102-119.
PDB; 5K0H; X-ray; 2.20 A; A=235-468, B=128-178.
PDBsum; 1C5M; -.
PDBsum; 1EZQ; -.
PDBsum; 1F0R; -.
PDBsum; 1F0S; -.
PDBsum; 1FAX; -.
PDBsum; 1FJS; -.
PDBsum; 1FXY; -.
PDBsum; 1G2L; -.
PDBsum; 1G2M; -.
PDBsum; 1HCG; -.
PDBsum; 1IOE; -.
PDBsum; 1IQE; -.
PDBsum; 1IQF; -.
PDBsum; 1IQG; -.
PDBsum; 1IQH; -.
PDBsum; 1IQI; -.
PDBsum; 1IQJ; -.
PDBsum; 1IQK; -.
PDBsum; 1IQL; -.
PDBsum; 1IQM; -.
PDBsum; 1IQN; -.
PDBsum; 1KSN; -.
PDBsum; 1LPG; -.
PDBsum; 1LPK; -.
PDBsum; 1LPZ; -.
PDBsum; 1LQD; -.
PDBsum; 1MQ5; -.
PDBsum; 1MQ6; -.
PDBsum; 1MSX; -.
PDBsum; 1NFU; -.
PDBsum; 1NFW; -.
PDBsum; 1NFX; -.
PDBsum; 1NFY; -.
PDBsum; 1NL8; -.
PDBsum; 1P0S; -.
PDBsum; 1V3X; -.
PDBsum; 1WU1; -.
PDBsum; 1XKA; -.
PDBsum; 1XKB; -.
PDBsum; 1Z6E; -.
PDBsum; 2BMG; -.
PDBsum; 2BOH; -.
PDBsum; 2BOK; -.
PDBsum; 2BQ6; -.
PDBsum; 2BQ7; -.
PDBsum; 2BQW; -.
PDBsum; 2CJI; -.
PDBsum; 2D1J; -.
PDBsum; 2EI6; -.
PDBsum; 2EI7; -.
PDBsum; 2EI8; -.
PDBsum; 2FZZ; -.
PDBsum; 2G00; -.
PDBsum; 2GD4; -.
PDBsum; 2H9E; -.
PDBsum; 2J2U; -.
PDBsum; 2J34; -.
PDBsum; 2J38; -.
PDBsum; 2J4I; -.
PDBsum; 2J94; -.
PDBsum; 2J95; -.
PDBsum; 2JKH; -.
PDBsum; 2P16; -.
PDBsum; 2P3F; -.
PDBsum; 2P3T; -.
PDBsum; 2P3U; -.
PDBsum; 2P93; -.
PDBsum; 2P94; -.
PDBsum; 2P95; -.
PDBsum; 2PHB; -.
PDBsum; 2PR3; -.
PDBsum; 2Q1J; -.
PDBsum; 2RA0; -.
PDBsum; 2UWL; -.
PDBsum; 2UWO; -.
PDBsum; 2UWP; -.
PDBsum; 2VH0; -.
PDBsum; 2VH6; -.
PDBsum; 2VVC; -.
PDBsum; 2VVU; -.
PDBsum; 2VVV; -.
PDBsum; 2VWL; -.
PDBsum; 2VWM; -.
PDBsum; 2VWN; -.
PDBsum; 2VWO; -.
PDBsum; 2W26; -.
PDBsum; 2W3I; -.
PDBsum; 2W3K; -.
PDBsum; 2WYG; -.
PDBsum; 2WYJ; -.
PDBsum; 2XBV; -.
PDBsum; 2XBW; -.
PDBsum; 2XBX; -.
PDBsum; 2XBY; -.
PDBsum; 2XC0; -.
PDBsum; 2XC4; -.
PDBsum; 2XC5; -.
PDBsum; 2Y5F; -.
PDBsum; 2Y5G; -.
PDBsum; 2Y5H; -.
PDBsum; 2Y7X; -.
PDBsum; 2Y7Z; -.
PDBsum; 2Y80; -.
PDBsum; 2Y81; -.
PDBsum; 2Y82; -.
PDBsum; 3CEN; -.
PDBsum; 3CS7; -.
PDBsum; 3ENS; -.
PDBsum; 3FFG; -.
PDBsum; 3HPT; -.
PDBsum; 3IIT; -.
PDBsum; 3K9X; -.
PDBsum; 3KL6; -.
PDBsum; 3KQB; -.
PDBsum; 3KQC; -.
PDBsum; 3KQD; -.
PDBsum; 3KQE; -.
PDBsum; 3LIW; -.
PDBsum; 3M36; -.
PDBsum; 3M37; -.
PDBsum; 3Q3K; -.
PDBsum; 3SW2; -.
PDBsum; 3TK5; -.
PDBsum; 3TK6; -.
PDBsum; 4A7I; -.
PDBsum; 4BTI; -.
PDBsum; 4BTT; -.
PDBsum; 4BTU; -.
PDBsum; 4Y6D; -.
PDBsum; 4Y71; -.
PDBsum; 4Y76; -.
PDBsum; 4Y79; -.
PDBsum; 4Y7A; -.
PDBsum; 4Y7B; -.
PDBsum; 4ZH8; -.
PDBsum; 4ZHA; -.
PDBsum; 5JQY; -.
PDBsum; 5JTC; -.
PDBsum; 5JZ8; -.
PDBsum; 5JZU; -.
PDBsum; 5JZZ; -.
PDBsum; 5K0H; -.
ProteinModelPortal; P00742; -.
SMR; P00742; -.
BioGrid; 108457; 9.
CORUM; P00742; -.
DIP; DIP-29896N; -.
ELM; P00742; -.
IntAct; P00742; 11.
MINT; MINT-276128; -.
STRING; 9606.ENSP00000364709; -.
BindingDB; P00742; -.
ChEMBL; CHEMBL244; -.
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.
DrugBank; DB08746; 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE.
DrugBank; DB07974; 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE.
DrugBank; DB07277; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE.
DrugBank; DB07278; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE.
DrugBank; DB08487; 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE.
DrugBank; DB08495; 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE.
DrugBank; DB04673; 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE.
DrugBank; DB08745; 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE.
DrugBank; DB08173; 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE.
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.
DrugBank; DB07843; 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE.
DrugBank; DB07847; 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE.
DrugBank; DB07844; 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB06605; Apixaban.
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB13150; Coagulation factor VII human.
DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DrugBank; DB09075; Edoxaban.
DrugBank; DB01225; Enoxaparin.
DrugBank; DB00569; Fondaparinux sodium.
DrugBank; DB03847; Gamma-Carboxy-Glutamic Acid.
DrugBank; DB01109; Heparin.
DrugBank; DB05713; LY-517717.
DrugBank; DB00170; Menadione.
DrugBank; DB07973; N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE.
DrugBank; DB07800; N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE.
DrugBank; DB06228; Rivaroxaban.
DrugBank; DB05362; SSR-126517E.
GuidetoPHARMACOLOGY; 2359; -.
MEROPS; S01.216; -.
iPTMnet; P00742; -.
PhosphoSitePlus; P00742; -.
UniCarbKB; P00742; -.
BioMuta; F10; -.
DMDM; 119761; -.
EPD; P00742; -.
PaxDb; P00742; -.
PeptideAtlas; P00742; -.
PRIDE; P00742; -.
Ensembl; ENST00000375559; ENSP00000364709; ENSG00000126218.
GeneID; 2159; -.
KEGG; hsa:2159; -.
CTD; 2159; -.
DisGeNET; 2159; -.
EuPathDB; HostDB:ENSG00000126218.11; -.
GeneCards; F10; -.
HGNC; HGNC:3528; F10.
MalaCards; F10; -.
MIM; 227600; phenotype.
MIM; 613872; gene.
neXtProt; NX_P00742; -.
OpenTargets; ENSG00000126218; -.
Orphanet; 328; Congenital factor X deficiency.
PharmGKB; PA27940; -.
eggNOG; ENOG410IGPV; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P00742; -.
KO; K01314; -.
OMA; NFLKWID; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00742; -.
TreeFam; TF327329; -.
BioCyc; MetaCyc:HS05000-MONOMER; -.
BRENDA; 3.4.21.6; 2681.
Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RK; P00742; -.
SIGNOR; P00742; -.
ChiTaRS; F10; human.
EvolutionaryTrace; P00742; -.
GeneWiki; Factor_X; -.
GenomeRNAi; 2159; -.
PMAP-CutDB; P00742; -.
PRO; PR:P00742; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000126218; -.
CleanEx; HS_F10; -.
ExpressionAtlas; P00742; baseline and differential.
Genevisible; P00742; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IC:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0006465; P:signal peptide processing; TAS:Reactome.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
Hydrolase; Hydroxylation; Polymorphism; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 31 {ECO:0000255}.
PROPEP 32 40 {ECO:0000269|PubMed:6871167}.
/FTId=PRO_0000027786.
CHAIN 41 488 Coagulation factor X.
/FTId=PRO_0000027787.
CHAIN 41 179 Factor X light chain.
/FTId=PRO_0000027788.
CHAIN 183 488 Factor X heavy chain.
/FTId=PRO_0000027789.
PROPEP 183 234 Activation peptide.
/FTId=PRO_0000027790.
CHAIN 235 488 Activated factor Xa heavy chain.
/FTId=PRO_0000027791.
DOMAIN 41 85 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 86 122 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 125 165 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 235 467 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 183 203 O-glycosylated at one site.
REGION 476 485 O-glycosylated at one site.
ACT_SITE 276 276 Charge relay system.
ACT_SITE 322 322 Charge relay system.
ACT_SITE 419 419 Charge relay system.
MOD_RES 46 46 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 47 47 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 54 54 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 56 56 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 59 59 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 60 60 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 65 65 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 66 66 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 69 69 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 72 72 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 79 79 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6871167}.
MOD_RES 103 103 (3R)-3-hydroxyaspartate.
{ECO:0000269|PubMed:6871167}.
CARBOHYD 199 199 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8243461}.
CARBOHYD 211 211 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8243461}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8243461}.
/FTId=CAR_000012.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8243461}.
/FTId=CAR_000013.
DISULFID 57 62 {ECO:0000250}.
DISULFID 90 101
DISULFID 95 110
DISULFID 112 121
DISULFID 129 140
DISULFID 136 149
DISULFID 151 164
DISULFID 172 342 Interchain (between light and heavy
chains).
DISULFID 241 246
DISULFID 261 277
DISULFID 390 404
DISULFID 415 443
VARIANT 7 7 L -> I (in dbSNP:rs5963).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014162.
VARIANT 30 30 Q -> H (in dbSNP:rs5961).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014163.
VARIANT 47 47 E -> G (in FA10D; St. Louis II; strongly
reduced activity; not activated by factor
VIIa and tissue factor;
dbSNP:rs121964943).
{ECO:0000269|PubMed:8910490}.
/FTId=VAR_065428.
VARIANT 51 51 G -> V (in FA10D; dbSNP:rs751782758).
{ECO:0000269|PubMed:19135706}.
/FTId=VAR_065429.
VARIANT 54 54 E -> G (in FA10D; Ketchikan;
dbSNP:rs121964944).
{ECO:0000269|PubMed:7860069}.
/FTId=VAR_065430.
VARIANT 54 54 E -> K (in FA10D; Vorarlberg; converts
prothrombin at a normal rate but shows
decreased affinity for calcium;
dbSNP:rs121964939).
{ECO:0000269|PubMed:10746568,
ECO:0000269|PubMed:1973167}.
/FTId=VAR_065431.
VARIANT 72 72 E -> Q (in FA10D; Tokyo;
dbSNP:rs121964945).
{ECO:0000269|PubMed:10468877}.
/FTId=VAR_065432.
VARIANT 91 91 E -> K (in FA10D; Riyadh).
{ECO:0000269|PubMed:17393015}.
/FTId=VAR_065433.
VARIANT 142 142 E -> K (in FA10D; uncertain pathological
significance; detected in patients
carrying K-54 or P-374; slightly reduced
activity; dbSNP:rs61753266).
{ECO:0000269|PubMed:10739379,
ECO:0000269|PubMed:1973167,
ECO:0000269|PubMed:7669671}.
/FTId=VAR_065434.
VARIANT 149 149 C -> Y (in FA10D).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065435.
VARIANT 151 151 C -> Y (in FA10D).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065436.
VARIANT 152 152 A -> T (in dbSNP:rs3211772).
{ECO:0000269|Ref.3}.
/FTId=VAR_020176.
VARIANT 176 186 Missing (in FA10D; unknown pathological
significance).
{ECO:0000269|PubMed:26222694}.
/FTId=VAR_075212.
VARIANT 192 192 G -> R (in dbSNP:rs3211783).
{ECO:0000269|Ref.3}.
/FTId=VAR_020177.
VARIANT 262 262 G -> D (in FA10D; unknown pathological
significance).
{ECO:0000269|PubMed:26222694}.
/FTId=VAR_075213.
VARIANT 289 289 G -> R (in FA10D; may affect splicing;
dbSNP:rs121964946).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065437.
VARIANT 304 304 E -> K (in FA10D; dbSNP:rs747292771).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065438.
VARIANT 322 322 D -> N (in FA10D; Stockton; 50% decrease
in specific activity; dbSNP:rs121964942).
{ECO:0000269|PubMed:25313940,
ECO:0000269|PubMed:8845463}.
/FTId=VAR_065439.
VARIANT 327 327 R -> W (in FA10D; dbSNP:rs770119164).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065440.
VARIANT 338 338 V -> M (in FA10D; dbSNP:rs121964947).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065441.
VARIANT 350 350 E -> K (in FA10D; dbSNP:rs372309538).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065442.
VARIANT 358 358 T -> M (in FA10D; Roma;
dbSNP:rs768222784).
{ECO:0000269|PubMed:10746568,
ECO:0000269|PubMed:25313940}.
/FTId=VAR_065443.
VARIANT 363 363 G -> S (in FA10D).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065444.
VARIANT 366 366 R -> C (in FA10D; San Antonio;
dbSNP:rs104894392).
{ECO:0000269|PubMed:2790181}.
/FTId=VAR_065445.
VARIANT 374 374 S -> P (in FA10D; Marseille; decreased
cleavage by factor IXa; normal catalytic
efficiency for prothrombin;
dbSNP:rs121964941).
{ECO:0000269|PubMed:11728527,
ECO:0000269|PubMed:7669671,
ECO:0000269|PubMed:8529633}.
/FTId=VAR_065446.
VARIANT 382 382 V -> A (in FA10D; partial loss of
activity). {ECO:0000269|PubMed:15075089,
ECO:0000269|PubMed:25313940}.
/FTId=VAR_072751.
VARIANT 383 383 P -> S (in FA10D; Friuli;
dbSNP:rs121964940).
{ECO:0000269|PubMed:1985698}.
/FTId=VAR_065447.
VARIANT 390 390 C -> F (in FA10D; Padua 4;
dbSNP:rs199778916).
{ECO:0000269|PubMed:12945883}.
/FTId=VAR_065448.
VARIANT 404 404 C -> R (in FA10D).
{ECO:0000269|PubMed:10746568}.
/FTId=VAR_065449.
VARIANT 406 406 G -> S (in FA10D; almost complete loss of
activity; dbSNP:rs376163818).
{ECO:0000269|PubMed:15650540,
ECO:0000269|PubMed:25313940}.
/FTId=VAR_065450.
VARIANT 420 420 G -> R (in FA10D; Padua 3;
dbSNP:rs750759634).
{ECO:0000269|PubMed:11728527}.
/FTId=VAR_065451.
VARIANT 421 421 G -> D (in FA10D; significant loss of
activity; dbSNP:rs758726161).
{ECO:0000269|PubMed:12574802,
ECO:0000269|PubMed:25313940}.
/FTId=VAR_072752.
VARIANT 448 448 K -> N (in FA10D; San Giovanni Rotondo).
{ECO:0000269|PubMed:11248282}.
/FTId=VAR_065452.
CONFLICT 285 288 KVRV -> E (in Ref. 6; AAA51984 and 8;
AAA52486). {ECO:0000305}.
CONFLICT 442 442 G -> S (in Ref. 5; AAA52490).
{ECO:0000305}.
HELIX 47 57 {ECO:0000244|PDB:1P0S}.
HELIX 64 71 {ECO:0000244|PDB:1P0S}.
HELIX 74 81 {ECO:0000244|PDB:1P0S}.
TURN 89 92 {ECO:0000244|PDB:1XKB}.
STRAND 96 98 {ECO:0000244|PDB:1XKA}.
STRAND 100 102 {ECO:0000244|PDB:3K9X}.
STRAND 105 107 {ECO:0000244|PDB:1XKB}.
STRAND 109 111 {ECO:0000244|PDB:3K9X}.
STRAND 116 118 {ECO:0000244|PDB:3K9X}.
STRAND 123 125 {ECO:0000244|PDB:3K9X}.
TURN 129 131 {ECO:0000244|PDB:2JKH}.
HELIX 132 135 {ECO:0000244|PDB:2JKH}.
STRAND 137 143 {ECO:0000244|PDB:2JKH}.
STRAND 146 150 {ECO:0000244|PDB:2JKH}.
STRAND 155 157 {ECO:0000244|PDB:2JKH}.
STRAND 164 170 {ECO:0000244|PDB:2JKH}.
STRAND 172 174 {ECO:0000244|PDB:1C5M}.
STRAND 236 240 {ECO:0000244|PDB:2JKH}.
TURN 243 245 {ECO:0000244|PDB:2VWO}.
STRAND 249 253 {ECO:0000244|PDB:2JKH}.
TURN 255 257 {ECO:0000244|PDB:1C5M}.
STRAND 259 265 {ECO:0000244|PDB:2JKH}.
STRAND 267 273 {ECO:0000244|PDB:2JKH}.
HELIX 275 279 {ECO:0000244|PDB:2JKH}.
STRAND 280 283 {ECO:0000244|PDB:2RA0}.
STRAND 285 289 {ECO:0000244|PDB:2JKH}.
STRAND 291 295 {ECO:0000244|PDB:2PR3}.
STRAND 301 303 {ECO:0000244|PDB:2JKH}.
STRAND 305 310 {ECO:0000244|PDB:2JKH}.
TURN 316 319 {ECO:0000244|PDB:2JKH}.
STRAND 324 330 {ECO:0000244|PDB:2JKH}.
HELIX 346 352 {ECO:0000244|PDB:2JKH}.
TURN 353 355 {ECO:0000244|PDB:2JKH}.
STRAND 356 364 {ECO:0000244|PDB:2JKH}.
STRAND 366 368 {ECO:0000244|PDB:2JKH}.
STRAND 372 376 {ECO:0000244|PDB:1C5M}.
STRAND 378 385 {ECO:0000244|PDB:2JKH}.
HELIX 387 393 {ECO:0000244|PDB:2JKH}.
STRAND 402 406 {ECO:0000244|PDB:2JKH}.
STRAND 408 411 {ECO:0000244|PDB:2JKH}.
TURN 416 420 {ECO:0000244|PDB:2JKH}.
STRAND 422 427 {ECO:0000244|PDB:2JKH}.
STRAND 430 439 {ECO:0000244|PDB:2JKH}.
STRAND 441 444 {ECO:0000244|PDB:2JKH}.
STRAND 450 454 {ECO:0000244|PDB:2JKH}.
HELIX 455 458 {ECO:0000244|PDB:2JKH}.
HELIX 459 465 {ECO:0000244|PDB:2JKH}.
STRAND 471 473 {ECO:0000244|PDB:1HCG}.
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


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