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Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]

 FA7_HUMAN               Reviewed;         466 AA.
P08709; B0YJC8; Q14339; Q5JVF1; Q5JVF2; Q9UD52; Q9UD53; Q9UD54;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 241.
RecName: Full=Coagulation factor VII;
EC=3.4.21.21;
AltName: Full=Proconvertin;
AltName: Full=Serum prothrombin conversion accelerator;
Short=SPCA;
AltName: INN=Eptacog alfa;
Contains:
RecName: Full=Factor VII light chain;
Contains:
RecName: Full=Factor VII heavy chain;
Flags: Precursor;
Name=F7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Liver;
PubMed=3486420; DOI=10.1073/pnas.83.8.2412;
Hagen F.S., Gray C.L., O'Hara P.J., Grant F.J., Saari G.C.,
Woodbury R.G., Hart C.E., Insley M.Y., Kisiel W., Kurachi K.,
Davie E.W.;
"Characterization of a cDNA coding for human factor VII.";
Proc. Natl. Acad. Sci. U.S.A. 83:2412-2416(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3037537; DOI=10.1073/pnas.84.15.5158;
O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y.,
Hagen F.S., Murray M.J.;
"Nucleotide sequence of the gene coding for human factor VII, a
vitamin K-dependent protein participating in blood coagulation.";
Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-354 AND GLN-413.
PubMed=16292673; DOI=10.1007/s00439-005-0045-5;
Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J.,
Fontcuberta J., Calafell F.;
"Human F7 sequence is split into three deep clades that are related to
FVII plasma levels.";
Hum. Genet. 118:741-751(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Soria J.M., Almasy L., Souto J.C., Sabater M., Fontcuberta J.,
Blangero J.;
"Complete dissection of a human quantitative trait locus: allelic
architecture of F7 and factor VII levels.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Masroori N., Habibi Roudkenar M., Halabian R.;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-352; GLN-413 AND
LYS-445.
SeattleSNPs variation discovery resource;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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).
[10]
PROTEIN SEQUENCE OF 61-466, GAMMA-CARBOXYGLUTAMATION AT GLU-66;
GLU-67; GLU-74; GLU-76; GLU-79; GLU-80; GLU-85; GLU-86; GLU-89 AND
GLU-95, HYDROXYLATION AT ASP-123, AND GLYCOSYLATION AT ASN-205 AND
ASN-382.
PubMed=3264725; DOI=10.1021/bi00420a030;
Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T.,
Pedersen A.H., Hedner U.;
"Amino acid sequence and posttranslational modifications of human
factor VIIa from plasma and transfected baby hamster kidney cells.";
Biochemistry 27:7785-7793(1988).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS FA7D ILE-358;
GLN-364; PHE-370 AND ARG-402, AND VARIANT GLN-413.
PubMed=8043443; DOI=10.1111/j.1365-2141.1994.tb04793.x;
Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C.,
Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S.,
Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G.;
"Molecular defects in CRM+ factor VII deficiencies: modelling of
missense mutations in the catalytic domain of FVII.";
Br. J. Haematol. 86:610-618(1994).
[12]
STRUCTURE OF CARBOHYDRATE ON SER-112.
PubMed=2511201;
Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
Shimonishi Y., Iwanaga S.;
"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-
Glc) O-glycosidically linked to a serine residue in the first
epidermal growth factor-like domain of human factors VII and IX and
protein Z and bovine protein Z.";
J. Biol. Chem. 264:20320-20325(1989).
[13]
STRUCTURE OF CARBOHYDRATE ON SER-112.
PubMed=2129367;
Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
"A new trisaccharide sugar chain linked to a serine residue in the
first EGF-like domain of clotting factors VII and IX and protein Z.";
Adv. Exp. Med. Biol. 281:121-131(1990).
[14]
GLYCOSYLATION AT SER-112 AND SER-120.
PubMed=1904059;
Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M.,
Komiyama Y., Pedersen A.H., Kisiel W.;
"Human plasma and recombinant factor VII. Characterization of O-
glycosylations at serine residues 52 and 60 and effects of site-
directed mutagenesis of serine 52 to alanine.";
J. Biol. Chem. 266:11051-11057(1991).
[15]
GLYCOSYLATION AT SER-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9023546; DOI=10.1093/glycob/6.8.837;
Wang Y., Lee G.F., Kelley R.F., Spellman M.W.;
"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and
enzymatic addition of O-linked fucose to EGF domains.";
Glycobiology 6:837-842(1996).
[16]
GLYCOSYLATION AT ASN-205 AND ASN-382.
PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
Ruiz-Canada C., Kelleher D.J., Gilmore R.;
"Cotranslational and posttranslational N-glycosylation of polypeptides
by distinct mammalian OST isoforms.";
Cell 136:272-283(2009).
[17]
GLYCOSYLATION AT SER-112, AND MUTAGENESIS OF SER-112 AND SER-113.
PubMed=21949356; DOI=10.1073/pnas.1109696108;
Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A.,
Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A.,
Jafar-Nejad H., Haltiwanger R.S.;
"Rumi functions as both a protein O-glucosyltransferase and a protein
O-xylosyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
PubMed=8598903; DOI=10.1038/380041a0;
Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A.,
Konigsberg W.H., Nemreson Y., Kirchhofer D.;
"The crystal structure of the complex of blood coagulation factor VIIa
with soluble tissue factor.";
Nature 380:41-46(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
PubMed=9925787; DOI=10.1006/jmbi.1998.2452;
Zhang E., St Charles R., Tulinsky A.;
"Structure of extracellular tissue factor complexed with factor VIIa
inhibited with a BPTI mutant.";
J. Mol. Biol. 285:2089-2104(1999).
[20]
STRUCTURE BY NMR OF 105-145.
PubMed=9692950; DOI=10.1021/bi980522f;
Muranyi A., Finn B.E., Gippert G.P., Forsen S., Stenflo J.,
Drakenberg T.;
"Solution structure of the N-terminal EGF-like domain from human
factor VII.";
Biochemistry 37:10605-10615(1998).
[21]
VARIANT FA7D GLN-364.
PubMed=2070047;
O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J.,
Meade T.W., Tuddenham E.G.D.;
"Purification and characterization of factor VII 304-Gln: a variant
molecule with reduced activity isolated from a clinically unaffected
male.";
Blood 78:132-140(1991).
[22]
VARIANTS FA7D GLN-364 AND PHE-370.
PubMed=1634227; DOI=10.1007/BF00219173;
Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M.,
Rodorigo G., Casonato A., Girolami A., Bernardi F.;
"Detection of two missense mutations and characterization of a repeat
polymorphism in the factor VII gene (F7).";
Hum. Genet. 89:497-502(1992).
[23]
VARIANT FA7D TYR-238.
PubMed=8364544; DOI=10.1093/hmg/2.7.1055;
Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F.;
"A missense mutation (178Cys-->Tyr) and two neutral dimorphisms
(115His and 333Ser) in the human coagulation factor VII gene.";
Hum. Mol. Genet. 2:1055-1056(1993).
[24]
VARIANTS FA7D GLN-139; TRP-139; ARG-160; GLU-197 AND GLN-364.
PubMed=8242057; DOI=10.1093/hmg/2.9.1355;
Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N.,
von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H.,
Tuddenham E.G.D., McVey J.H.;
"Detection of missense mutations by single-strand conformational
polymorphism (SSCP) analysis in five dysfunctional variants of
coagulation factor VII.";
Hum. Mol. Genet. 2:1355-1359(1993).
[25]
VARIANTS FA7D GLN-139 AND GLN-212.
PubMed=8204879;
Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W.,
Roberts H.R., Blajchman M., Monroe D.M., High K.A.;
"Severe factor VII deficiency caused by mutations abolishing the
cleavage site for activation and altering binding to tissue factor.";
Blood 83:3524-3535(1994).
[26]
VARIANT SER-367.
PubMed=7860081; DOI=10.1159/000154235;
Dewald G., Noethen M.M., Ruther K.;
"A common Ser/Thr polymorphism in the perforin-homologous region of
human complement component C7.";
Hum. Hered. 44:301-304(1994).
[27]
VARIANT FA7D VAL-354.
PubMed=7981691; DOI=10.1093/hmg/3.7.1175;
Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B.,
Rodeghiero F., Marchetti G.;
"Topologically equivalent mutations causing dysfunctional coagulation
factors VII (294Ala-->Val) and X (334Ser-->Pro).";
Hum. Mol. Genet. 3:1175-1177(1994).
[28]
VARIANT FA7D HIS-307.
PubMed=7974346;
Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K.;
"Factor VII Mie: homozygous asymptomatic type I deficiency caused by
an amino acid substitution of His (CAC) for Arg(247) (CGC) in the
catalytic domain.";
Thromb. Haemost. 71:773-777(1994).
[29]
VARIANT FA7D MET-419.
PubMed=8652821;
Arbini A.A., Mannucci P.M., Bauer K.A.;
"A Thr359Met mutation in factor VII of a patient with a hereditary
deficiency causes defective secretion of the molecule.";
Blood 87:5085-5094(1996).
[30]
VARIANTS FA7D TRP-283; LYS-325; VAL-358; GLN-364 AND GLU-402, AND
VARIANT GLN-413.
PubMed=8844208;
DOI=10.1002/(SICI)1098-1004(1996)8:2<108::AID-HUMU2>3.0.CO;2-7;
Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G.,
Lunghi B., Rodeghiero F., Marchetti G.;
"Mutation pattern in clinically asymptomatic coagulation factor VII
deficiency.";
Hum. Mutat. 8:108-115(1996).
[31]
VARIANT FA7D SER-388, AND CHARACTERIZATION OF VARIANT FA7D SER-388.
PubMed=8940045; DOI=10.1074/jbc.271.48.30685;
Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C.,
Kisiel W.;
"Factor VII central. A novel mutation in the catalytic domain that
reduces tissue factor binding, impairs activation by factor Xa, and
abolishes amidolytic and coagulant activity.";
J. Biol. Chem. 271:30685-30691(1996).
[32]
VARIANT FA7D VAL-304.
PubMed=8883260;
Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N.,
Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R.,
Seligsohn U.;
"Ala244Val is a common, probably ancient mutation causing factor VII
deficiency in Moroccan and Iranian Jews.";
Thromb. Haemost. 76:283-291(1996).
[33]
VARIANT FA7D ASP-117, AND CHARACTERIZATION OF VARIANT FA7D ASP-117.
PubMed=9414278;
Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S.,
Yang D., Clarke B.J.;
"Factor VII deficiency caused by a structural variant N57D of the
first epidermal growth factor domain.";
Blood 91:142-148(1998).
[34]
VARIANT FA7D PRO-13.
PubMed=9576180; DOI=10.1046/j.1365-2141.1998.00666.x;
Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S.,
Sakuragawa N.;
"Factor VII Morioka (FVII L-26P): a homozygous missense mutation in
the signal sequence identified in a patient with factor VII
deficiency.";
Br. J. Haematol. 101:47-49(1998).
[35]
VARIANTS FA7D THR-194 AND VAL-304.
PubMed=9452082;
Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.;
"Two new missense mutations (P134T and A244V) in the coagulation
factor VII gene.";
Hum. Mutat. Suppl. 1:S189-S191(1998).
[36]
VARIANTS ASP-295 AND GLN-413.
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).
[37]
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).
[38]
VARIANT FA7D GLY-389.
PubMed=11091194; DOI=10.1046/j.1365-2141.2000.02332.x;
Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L.;
"Two novel factor VII gene mutations in a Chinese family with factor
VII deficiency.";
Br. J. Haematol. 111:143-145(2000).
[39]
VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139;
SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302;
THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370;
GLY-389; SER-391 AND GLU-435.
PubMed=11129332; DOI=10.1007/s004390000373;
Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D.,
Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A.,
Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R.,
Krawczak M., Cooper D.N.;
"Molecular analysis of the genotype-phenotype relationship in factor
VII deficiency.";
Hum. Genet. 107:327-342(2000).
[40]
VARIANTS FA7D LEU-64; PRO-120; CYS-128; LYS-154; SER-157; ARG-160;
ARG-195; GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304;
CYS-307; MET-312; LYS-325; PHE-341; VAL-354; ILE-358; ARG-363;
PHE-370; HIS-403 AND MET-419.
PubMed=10862079;
DOI=10.1002/1098-1004(200006)15:6<489::AID-HUMU1>3.0.CO;2-J;
Wulff K., Herrmann F.H.;
"Twenty two novel mutations of the factor VII gene in factor VII
deficiency.";
Hum. Mutat. 15:489-496(2000).
[41]
VARIANT GLN-413.
PubMed=10984565; DOI=10.1056/NEJM200009143431104;
Girelli D., Russo C., Ferraresi P., Olivieri O., Pinotti M., Friso S.,
Manzato F., Mazzucco A., Bernardi F., Corrocher R.;
"Polymorphisms in the factor VII gene and the risk of myocardial
infarction in patients with coronary artery disease.";
N. Engl. J. Med. 343:774-780(2000).
[42]
VARIANTS FA7D LYS-85 AND GLN-408.
PubMed=12472587; DOI=10.1046/j.1365-2141.2002.03933.x;
Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K.,
Arai M., Fukutake K.;
"Two double heterozygous mutations in the F7 gene show different
manifestations.";
Br. J. Haematol. 119:1052-1058(2002).
[43]
VARIANT FA7D CYS-414, AND CHARACTERIZATION OF VARIANT FA7D CYS-414.
PubMed=14717781; DOI=10.1046/j.1365-2141.2003.04778.x;
Takamiya O., Hino K.;
"A patient homozygous for a Gly354Cys mutation in factor VII that
results in severely impaired secretion of the molecule, but not
complete deficiency.";
Br. J. Haematol. 124:336-342(2004).
[44]
VARIANTS FA7D ARG-82; ARG-177; THR-198; GLN-212; PRO-251; ARG-323;
ARG-344; PHE-370; MET-384; GLU-398 AND ARG-408.
PubMed=19751712; DOI=10.1016/j.cca.2009.09.007;
Mota L., Shetty S., Idicula-Thomas S., Ghosh K.;
"Phenotypic and genotypic characterization of Factor VII deficiency
patients from Western India.";
Clin. Chim. Acta 409:106-111(2009).
[45]
VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88;
PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157;
ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194;
THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254;
TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298;
GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307;
MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343;
SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363;
GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387;
SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413;
MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND
PHE-437.
PubMed=18976247; DOI=10.1111/j.1365-2516.2008.01910.x;
Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J.,
Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N.,
Salazar-Sanchez L.;
"Factor VII deficiency: clinical manifestation of 717 subjects from
Europe and Latin America with mutations in the factor 7 gene.";
Haemophilia 15:267-280(2009).
[46]
VARIANT FA7D ARG-240.
PubMed=19432927; DOI=10.1111/j.1365-2516.2009.02004.x;
Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O.,
Kapelushnik J.;
"Familial factor VII deficiency with foetal and neonatal fatal
cerebral haemorrhage associated with homozygosis to Gly180Arg
mutation.";
Haemophilia 15:774-778(2009).
[47]
VARIANTS FA7D ARG-59 INS; VAL-314; SER-343 AND GLY-389.
PubMed=21206266; DOI=10.1097/MBC.0b013e328343641a;
Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J.;
"Recurrent mutations and genotype-phenotype correlations in hereditary
factor VII deficiency in Korea.";
Blood Coagul. Fibrinolysis 22:102-105(2011).
[48]
VARIANT FA7D PHE-250.
PubMed=21372693; DOI=10.1097/MBC.0b013e3283447388;
Jiang M., Wang Z., Yu Z., Bai X., Su J., Cao L., Zhang W., Ruan C.;
"A novel missense mutation close to the charge-stabilizing system in a
patient with congenital factor VII deficiency.";
Blood Coagul. Fibrinolysis 22:264-270(2011).
[49]
VARIANT FA7D GLY-344.
PubMed=26761581; DOI=10.1097/MBC.0000000000000499;
Hao X., Cheng X., Ye J., Wang Y., Yang L., Wang M., Jin Y.;
"Severe coagulation factor VII deficiency caused by a novel homozygous
mutation (p. Trp284Gly) in loop 140s.";
Blood Coagul. Fibrinolysis 27:461-463(2016).
-!- FUNCTION: Initiates the extrinsic pathway of blood coagulation.
Serine protease that circulates in the blood in a zymogen form.
Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
factor IXa, or thrombin by minor proteolysis. In the presence of
tissue factor and calcium ions, factor VIIa then converts factor X
to factor Xa by limited proteolysis. Factor VIIa will also convert
factor IX to factor IXa in the presence of tissue factor and
calcium.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
X to form factor Xa.
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
a disulfide bond. {ECO:0000269|PubMed:8598903,
ECO:0000269|PubMed:9925787}.
-!- INTERACTION:
P13726:F3; NbExp=7; IntAct=EBI-355972, EBI-1040727;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P08709-1; Sequence=Displayed;
Name=B;
IsoId=P08709-2; Sequence=VSP_005387;
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
glutamate residues allows the modified protein to bind calcium.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:3264725}.
-!- PTM: O- and N-glycosylated. N-glycosylation at Asn-205 occurs
cotranslationally and is mediated by STT3A-containing complexes,
while glycosylation at Asn-382 is post-translational and is
mediated STT3B-containing complexes before folding. O-fucosylated
by POFUT1 on a conserved serine or threonine residue found in the
consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and
C3 are the second and third conserved cysteines.
{ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:9023546}.
-!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-112 by
POGLUT1 in vitro.
-!- DISEASE: Factor VII deficiency (FA7D) [MIM:227500]: A hemorrhagic
disease with variable presentation. The clinical picture can be
very severe, with the early occurrence of intracerebral
hemorrhages or repeated hemarthroses, or, in contrast, moderate
with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or
hemorrhages provoked by a surgical intervention. Finally, numerous
subjects are completely asymptomatic despite very low factor VII
levels. {ECO:0000269|PubMed:10862079, ECO:0000269|PubMed:11091194,
ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:12472587,
ECO:0000269|PubMed:14717781, ECO:0000269|PubMed:1634227,
ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19432927,
ECO:0000269|PubMed:19751712, ECO:0000269|PubMed:2070047,
ECO:0000269|PubMed:21206266, ECO:0000269|PubMed:21372693,
ECO:0000269|PubMed:26761581, ECO:0000269|PubMed:7974346,
ECO:0000269|PubMed:7981691, ECO:0000269|PubMed:8043443,
ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8242057,
ECO:0000269|PubMed:8364544, ECO:0000269|PubMed:8652821,
ECO:0000269|PubMed:8844208, ECO:0000269|PubMed:8883260,
ECO:0000269|PubMed:8940045, ECO:0000269|PubMed:9414278,
ECO:0000269|PubMed:9452082, ECO:0000269|PubMed:9576180}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- PHARMACEUTICAL: Available under the names Niastase or Novoseven
(Novo Nordisk). Used for the treatment of bleeding episodes in
hemophilia A or B patients with antibodies to coagulation factors
VIII or IX.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor VII entry;
URL="https://en.wikipedia.org/wiki/Factor_VII";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f7/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F7";
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EMBL; M13232; AAA88040.1; -; mRNA.
EMBL; M13232; AAA88041.1; -; mRNA.
EMBL; J02933; AAA51983.1; -; Genomic_DNA.
EMBL; DQ142911; ABD17891.1; -; Genomic_DNA.
EMBL; AY212252; AAP33841.1; -; Genomic_DNA.
EMBL; EU557239; ACB87203.1; -; mRNA.
EMBL; AF466933; AAL66184.1; -; Genomic_DNA.
EMBL; EF445049; ACA06107.1; -; Genomic_DNA.
EMBL; EF445049; ACA06108.1; -; Genomic_DNA.
EMBL; AL137002; CAI41381.1; -; Genomic_DNA.
EMBL; AL137002; CAI41382.1; -; Genomic_DNA.
EMBL; BC130468; AAI30469.1; -; mRNA.
CCDS; CCDS9528.1; -. [P08709-1]
CCDS; CCDS9529.1; -. [P08709-2]
PIR; A28322; KFHU7.
RefSeq; NP_000122.1; NM_000131.4. [P08709-1]
RefSeq; NP_062562.1; NM_019616.3. [P08709-2]
UniGene; Hs.36989; -.
PDB; 1BF9; NMR; -; A=105-145.
PDB; 1CVW; X-ray; 2.28 A; H=213-466, L=150-204.
PDB; 1DAN; X-ray; 2.00 A; H=213-466, L=61-212.
PDB; 1DVA; X-ray; 3.00 A; H/I=213-466, L/M=102-202.
PDB; 1F7E; NMR; -; A=105-147.
PDB; 1F7M; NMR; -; A=105-147.
PDB; 1FAK; X-ray; 2.10 A; H=213-466, L=61-212.
PDB; 1FF7; NMR; -; A=105-147.
PDB; 1FFM; NMR; -; A=105-147.
PDB; 1J9C; X-ray; 2.90 A; H=213-466, L=108-202.
PDB; 1JBU; X-ray; 2.00 A; H=213-466, L=150-212.
PDB; 1KLI; X-ray; 1.69 A; H=213-466, L=144-212.
PDB; 1KLJ; X-ray; 2.44 A; H=213-466, L=144-212.
PDB; 1NL8; Model; -; H=213-466, M=61-202.
PDB; 1O5D; X-ray; 2.05 A; H=213-466, L=61-212.
PDB; 1QFK; X-ray; 2.80 A; H=213-466, L=109-212.
PDB; 1W0Y; X-ray; 2.50 A; H=213-466, L=61-202.
PDB; 1W2K; X-ray; 3.00 A; H=213-466, L=61-202.
PDB; 1W7X; X-ray; 1.80 A; H=213-466, L=150-204.
PDB; 1W8B; X-ray; 3.00 A; H=213-466, L=148-204.
PDB; 1WQV; X-ray; 2.50 A; H=213-466, L=61-212.
PDB; 1WSS; X-ray; 2.60 A; H=213-466, L=61-212.
PDB; 1WTG; X-ray; 2.20 A; H=213-466, L=61-212.
PDB; 1WUN; X-ray; 2.40 A; H=213-466, L=61-212.
PDB; 1WV7; X-ray; 2.70 A; H=213-466, L=61-212.
PDB; 1YGC; X-ray; 2.00 A; H=213-466, L=150-212.
PDB; 1Z6J; X-ray; 2.00 A; H=213-466, L=61-202.
PDB; 2A2Q; X-ray; 1.80 A; H=213-466, L=61-212.
PDB; 2AEI; X-ray; 2.52 A; H=213-466, L=61-212.
PDB; 2AER; X-ray; 1.87 A; H=213-466, L=61-202.
PDB; 2B7D; X-ray; 2.24 A; H=213-466, L=61-212.
PDB; 2B8O; X-ray; 2.80 A; H=213-466, L=61-202.
PDB; 2BZ6; X-ray; 1.60 A; H=213-466, L=150-202.
PDB; 2C4F; X-ray; 1.72 A; H=213-466, L=61-202.
PDB; 2EC9; X-ray; 2.00 A; H=213-466, L=61-202.
PDB; 2F9B; X-ray; 2.54 A; H=213-466, L=61-212.
PDB; 2FIR; X-ray; 2.00 A; H=213-466, L=61-202.
PDB; 2FLB; X-ray; 1.95 A; H=213-466, L=61-212.
PDB; 2FLR; X-ray; 2.35 A; H=213-466, L=61-212.
PDB; 2PUQ; X-ray; 2.05 A; H=213-466, L=109-202.
PDB; 2ZP0; X-ray; 2.70 A; H=213-466, L=61-212.
PDB; 2ZWL; X-ray; 2.20 A; H=213-466, L=61-212.
PDB; 2ZZU; X-ray; 2.50 A; H=213-466, L=61-212.
PDB; 3ELA; X-ray; 2.20 A; H=213-466, L=61-212.
PDB; 3TH2; X-ray; 1.72 A; H=213-466, L=61-202.
PDB; 3TH3; X-ray; 2.70 A; H=213-466, L=61-202.
PDB; 3TH4; X-ray; 1.80 A; H=213-466, L=61-202.
PDB; 4IBL; X-ray; 1.80 A; H=213-466, L=61-212.
PDB; 4ISH; X-ray; 1.82 A; H=213-466, L=150-204.
PDB; 4ISI; X-ray; 1.94 A; H=213-466, L=150-204.
PDB; 4JYU; X-ray; 1.80 A; H=213-466, L=150-204.
PDB; 4JYV; X-ray; 2.19 A; H=213-466, L=150-204.
PDB; 4JZD; X-ray; 2.20 A; H=213-466, L=150-204.
PDB; 4JZE; X-ray; 1.52 A; H=213-466, L=150-204.
PDB; 4JZF; X-ray; 1.84 A; H=213-466, L=150-204.
PDB; 4NA9; X-ray; 2.24 A; H=213-466, L=150-204.
PDB; 4NG9; X-ray; 2.20 A; H=213-466, L=150-204.
PDB; 4NGA; X-ray; 2.15 A; H=213-466, L=150-204.
PDB; 4X8S; X-ray; 2.10 A; H=213-466, L=150-204.
PDB; 4X8T; X-ray; 2.20 A; H=213-466, L=150-204.
PDB; 4X8U; X-ray; 2.10 A; H=213-466, L=150-204.
PDB; 4X8V; X-ray; 2.50 A; H=213-466, L=150-204.
PDB; 4YLQ; X-ray; 1.40 A; H=213-466, L=61-212.
PDB; 4YT6; X-ray; 2.07 A; H=213-466, L=148-204.
PDB; 4YT7; X-ray; 2.30 A; H=213-466, L=148-204.
PDB; 4Z6A; X-ray; 2.25 A; H=213-466, L=108-203.
PDB; 4ZMA; X-ray; 2.30 A; H=213-466, L=61-212.
PDB; 4ZXX; X-ray; 2.60 A; H=213-466, L=150-204.
PDB; 4ZXY; X-ray; 2.06 A; H=213-466, L=150-204.
PDB; 5I46; X-ray; 2.06 A; H=213-466, L=150-204.
PDB; 5L0S; X-ray; 1.45 A; B=105-145.
PDB; 5L2Y; X-ray; 1.82 A; H=213-466, L=150-204.
PDB; 5L2Z; X-ray; 1.79 A; H=213-466, L=147-204.
PDB; 5L30; X-ray; 1.73 A; H=213-466, L=147-204.
PDB; 5PA8; X-ray; 1.98 A; A=149-212, C=213-466.
PDB; 5PA9; X-ray; 1.55 A; A=149-212, C=213-466.
PDB; 5PAA; X-ray; 1.98 A; A=149-212, C=213-466.
PDB; 5PAB; X-ray; 1.99 A; H=213-466, L=149-212.
PDB; 5PAC; X-ray; 1.50 A; A=149-212, B=213-466.
PDB; 5PAE; X-ray; 1.45 A; A=149-212, B=213-466.
PDB; 5PAF; X-ray; 1.50 A; A=149-212, B=213-466.
PDB; 5PAG; X-ray; 1.36 A; A=149-212, B=213-466.
PDB; 5PAI; X-ray; 1.73 A; A=149-212, B=213-466.
PDB; 5PAJ; X-ray; 1.70 A; A=149-212, B=213-466.
PDB; 5PAK; X-ray; 1.56 A; A=149-212, C=213-466.
PDB; 5PAM; X-ray; 1.60 A; A=149-212, B=213-466.
PDB; 5PAN; X-ray; 1.62 A; A=149-212, B=213-466.
PDB; 5PAO; X-ray; 1.40 A; A=149-212, C=213-466.
PDB; 5PAQ; X-ray; 1.59 A; A=149-212, B=213-466.
PDB; 5PAR; X-ray; 2.10 A; A=149-212, C=213-466.
PDB; 5PAS; X-ray; 1.48 A; A=149-212, C=213-466.
PDB; 5PAT; X-ray; 1.60 A; A=149-212, B=213-466.
PDB; 5PAU; X-ray; 1.55 A; A=149-212, C=213-466.
PDB; 5PAV; X-ray; 1.40 A; A=149-212, C=213-466.
PDB; 5PAW; X-ray; 2.20 A; A=149-212, B=213-466.
PDB; 5PAX; X-ray; 1.36 A; A=149-212, C=213-466.
PDB; 5PAY; X-ray; 1.66 A; A=149-212, C=213-466.
PDB; 5PB0; X-ray; 1.98 A; A=149-212, B=213-466.
PDB; 5PB1; X-ray; 1.90 A; A=149-212, D=213-466.
PDB; 5PB2; X-ray; 1.45 A; A=149-212, C=213-466.
PDB; 5PB3; X-ray; 1.90 A; A=149-212, C=213-466.
PDB; 5PB4; X-ray; 2.43 A; A=149-212, C=213-466.
PDB; 5PB5; X-ray; 1.84 A; A=149-212, B=213-466.
PDB; 5PB6; X-ray; 1.90 A; A=149-212, C=213-466.
PDB; 5TQE; X-ray; 1.90 A; H=213-466, L=150-204.
PDB; 5TQF; X-ray; 1.85 A; H=213-466, L=150-204.
PDB; 5TQG; X-ray; 1.90 A; H=213-466, L=150-204.
PDB; 5U6J; X-ray; 2.30 A; H=213-466, L=150-204.
PDBsum; 1BF9; -.
PDBsum; 1CVW; -.
PDBsum; 1DAN; -.
PDBsum; 1DVA; -.
PDBsum; 1F7E; -.
PDBsum; 1F7M; -.
PDBsum; 1FAK; -.
PDBsum; 1FF7; -.
PDBsum; 1FFM; -.
PDBsum; 1J9C; -.
PDBsum; 1JBU; -.
PDBsum; 1KLI; -.
PDBsum; 1KLJ; -.
PDBsum; 1NL8; -.
PDBsum; 1O5D; -.
PDBsum; 1QFK; -.
PDBsum; 1W0Y; -.
PDBsum; 1W2K; -.
PDBsum; 1W7X; -.
PDBsum; 1W8B; -.
PDBsum; 1WQV; -.
PDBsum; 1WSS; -.
PDBsum; 1WTG; -.
PDBsum; 1WUN; -.
PDBsum; 1WV7; -.
PDBsum; 1YGC; -.
PDBsum; 1Z6J; -.
PDBsum; 2A2Q; -.
PDBsum; 2AEI; -.
PDBsum; 2AER; -.
PDBsum; 2B7D; -.
PDBsum; 2B8O; -.
PDBsum; 2BZ6; -.
PDBsum; 2C4F; -.
PDBsum; 2EC9; -.
PDBsum; 2F9B; -.
PDBsum; 2FIR; -.
PDBsum; 2FLB; -.
PDBsum; 2FLR; -.
PDBsum; 2PUQ; -.
PDBsum; 2ZP0; -.
PDBsum; 2ZWL; -.
PDBsum; 2ZZU; -.
PDBsum; 3ELA; -.
PDBsum; 3TH2; -.
PDBsum; 3TH3; -.
PDBsum; 3TH4; -.
PDBsum; 4IBL; -.
PDBsum; 4ISH; -.
PDBsum; 4ISI; -.
PDBsum; 4JYU; -.
PDBsum; 4JYV; -.
PDBsum; 4JZD; -.
PDBsum; 4JZE; -.
PDBsum; 4JZF; -.
PDBsum; 4NA9; -.
PDBsum; 4NG9; -.
PDBsum; 4NGA; -.
PDBsum; 4X8S; -.
PDBsum; 4X8T; -.
PDBsum; 4X8U; -.
PDBsum; 4X8V; -.
PDBsum; 4YLQ; -.
PDBsum; 4YT6; -.
PDBsum; 4YT7; -.
PDBsum; 4Z6A; -.
PDBsum; 4ZMA; -.
PDBsum; 4ZXX; -.
PDBsum; 4ZXY; -.
PDBsum; 5I46; -.
PDBsum; 5L0S; -.
PDBsum; 5L2Y; -.
PDBsum; 5L2Z; -.
PDBsum; 5L30; -.
PDBsum; 5PA8; -.
PDBsum; 5PA9; -.
PDBsum; 5PAA; -.
PDBsum; 5PAB; -.
PDBsum; 5PAC; -.
PDBsum; 5PAE; -.
PDBsum; 5PAF; -.
PDBsum; 5PAG; -.
PDBsum; 5PAI; -.
PDBsum; 5PAJ; -.
PDBsum; 5PAK; -.
PDBsum; 5PAM; -.
PDBsum; 5PAN; -.
PDBsum; 5PAO; -.
PDBsum; 5PAQ; -.
PDBsum; 5PAR; -.
PDBsum; 5PAS; -.
PDBsum; 5PAT; -.
PDBsum; 5PAU; -.
PDBsum; 5PAV; -.
PDBsum; 5PAW; -.
PDBsum; 5PAX; -.
PDBsum; 5PAY; -.
PDBsum; 5PB0; -.
PDBsum; 5PB1; -.
PDBsum; 5PB2; -.
PDBsum; 5PB3; -.
PDBsum; 5PB4; -.
PDBsum; 5PB5; -.
PDBsum; 5PB6; -.
PDBsum; 5TQE; -.
PDBsum; 5TQF; -.
PDBsum; 5TQG; -.
PDBsum; 5U6J; -.
ProteinModelPortal; P08709; -.
SMR; P08709; -.
BioGrid; 108453; 18.
CORUM; P08709; -.
DIP; DIP-6135N; -.
ELM; P08709; -.
IntAct; P08709; 10.
MINT; MINT-1155299; -.
STRING; 9606.ENSP00000364731; -.
BindingDB; P08709; -.
ChEMBL; CHEMBL3991; -.
DrugBank; DB04590; (2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID.
DrugBank; DB07207; 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DrugBank; DB04758; 2-[2-ETHANESULFONYLAMINO-3-(1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIM IDOYL-BENZYLAMIDE).
DrugBank; DB04606; 2-[2-ETHANESULFONYLAMINO-3-(5-PROPOXY-1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIMIDOYL-BENZYLAMIDE).
DrugBank; DB04593; 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID.
DrugBank; DB07376; 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID).
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DrugBank; DB00170; Menadione.
DrugBank; DB04767; N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID.
GuidetoPHARMACOLOGY; 2363; -.
MEROPS; S01.215; -.
iPTMnet; P08709; -.
PhosphoSitePlus; P08709; -.
UniCarbKB; P08709; -.
BioMuta; F7; -.
DMDM; 119766; -.
MaxQB; P08709; -.
PaxDb; P08709; -.
PeptideAtlas; P08709; -.
PRIDE; P08709; -.
Ensembl; ENST00000346342; ENSP00000329546; ENSG00000057593. [P08709-2]
Ensembl; ENST00000375581; ENSP00000364731; ENSG00000057593. [P08709-1]
GeneID; 2155; -.
KEGG; hsa:2155; -.
UCSC; uc001vsv.5; human. [P08709-1]
CTD; 2155; -.
DisGeNET; 2155; -.
EuPathDB; HostDB:ENSG00000057593.13; -.
GeneCards; F7; -.
HGNC; HGNC:3544; F7.
MalaCards; F7; -.
MIM; 227500; phenotype.
MIM; 613878; gene.
neXtProt; NX_P08709; -.
OpenTargets; ENSG00000057593; -.
Orphanet; 327; Congenital factor VII deficiency.
PharmGKB; PA160; -.
eggNOG; ENOG410IIMB; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOVERGEN; HBG013304; -.
InParanoid; P08709; -.
KO; K01320; -.
OMA; CEQYCSD; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P08709; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.21; 2681.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-140834; Extrinsic 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; P08709; -.
EvolutionaryTrace; P08709; -.
GeneWiki; Factor_VII; -.
GenomeRNAi; 2155; -.
PMAP-CutDB; P08709; -.
PRO; PR:P08709; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000057593; -.
CleanEx; HS_F7; -.
ExpressionAtlas; P08709; baseline and differential.
Genevisible; P08709; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:1905286; C:serine-type peptidase complex; IPI:BHF-UCL.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:BHF-UCL.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
GO; GO:0061476; P:response to anticoagulant; IEA:Ensembl.
GO; GO:1905217; P:response to astaxanthin; IEA:Ensembl.
GO; GO:0010037; P:response to carbon dioxide; IEA:Ensembl.
GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0033595; P:response to genistein; IEA:Ensembl.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:1904400; P:response to Thyroid stimulating hormone; IEA:Ensembl.
GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEA:Ensembl.
GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
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; IPR033190; F7.
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.
PANTHER; PTHR44064:SF1; PTHR44064:SF1; 1.
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; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
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; Alternative splicing; 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; Pharmaceutical; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 60 {ECO:0000269|PubMed:3264725}.
/FTId=PRO_0000027729.
CHAIN 61 212 Factor VII light chain.
/FTId=PRO_0000027730.
CHAIN 213 466 Factor VII heavy chain.
/FTId=PRO_0000027731.
DOMAIN 61 105 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 106 142 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 147 188 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 213 452 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 253 253 Charge relay system. {ECO:0000250}.
ACT_SITE 302 302 Charge relay system. {ECO:0000250}.
ACT_SITE 404 404 Charge relay system. {ECO:0000250}.
BINDING 398 398 Substrate. {ECO:0000250}.
SITE 113 113 Important for S-112 for O-xylosylation.
SITE 212 213 Cleavage; by factor Xa, factor XIIa,
factor IXa, or thrombin.
MOD_RES 66 66 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 67 67 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 74 74 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 76 76 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 79 79 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725}.
MOD_RES 80 80 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 85 85 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 86 86 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 89 89 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 95 95 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3264725,
ECO:0000269|PubMed:3486420}.
MOD_RES 123 123 (3R)-3-hydroxyaspartate.
{ECO:0000269|PubMed:3264725}.
CARBOHYD 112 112 O-linked (Glc...) serine.
{ECO:0000269|PubMed:1904059,
ECO:0000269|PubMed:21949356}.
/FTId=CAR_000007.
CARBOHYD 112 112 O-linked (Glc...) serine; alternate.
{ECO:0000269|PubMed:1904059,
ECO:0000269|PubMed:21949356}.
CARBOHYD 112 112 O-linked (Xyl...) serine; alternate.
{ECO:0000269|PubMed:1904059,
ECO:0000269|PubMed:21949356}.
CARBOHYD 120 120 O-linked (Fuc) serine.
{ECO:0000269|PubMed:1904059,
ECO:0000269|PubMed:9023546}.
/FTId=CAR_000180.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:3264725}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:3264725}.
DISULFID 77 82
DISULFID 110 121
DISULFID 115 130
DISULFID 132 141
DISULFID 151 162
DISULFID 158 172
DISULFID 174 187
DISULFID 195 322
DISULFID 219 224
DISULFID 238 254
DISULFID 370 389
DISULFID 400 428
VAR_SEQ 22 43 Missing (in isoform B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3486420}.
/FTId=VSP_005387.
VARIANT 13 13 L -> P (in FA7D; Morioka;
dbSNP:rs387906507).
{ECO:0000269|PubMed:9576180}.
/FTId=VAR_014391.
VARIANT 59 59 R -> RR (in FA7D).
{ECO:0000269|PubMed:21206266}.
/FTId=VAR_065369.
VARIANT 64 64 F -> L (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015135.
VARIANT 73 73 L -> Q (in FA7D; dbSNP:rs45572939).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014405.
VARIANT 79 79 E -> Q (in FA7D).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014406.
VARIANT 82 82 C -> F (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065370.
VARIANT 82 82 C -> R (in FA7D; dbSNP:rs745374448).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065371.
VARIANT 84 84 Missing (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065372.
VARIANT 85 85 E -> K (in FA7D; dbSNP:rs121964935).
{ECO:0000269|PubMed:12472587}.
/FTId=VAR_065373.
VARIANT 88 88 R -> G (in FA7D; dbSNP:rs776354144).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065374.
VARIANT 88 88 R -> P (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065375.
VARIANT 117 117 N -> D (in FA7D; exhibits no procoagulant
activity and is unable to bind tissue
factor; dbSNP:rs121964932).
{ECO:0000269|PubMed:9414278}.
/FTId=VAR_065376.
VARIANT 120 120 S -> P (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015136.
VARIANT 121 121 C -> F (in FA7D).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014407.
VARIANT 125 125 L -> P (in FA7D).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014408.
VARIANT 128 128 Y -> C (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014409.
VARIANT 138 138 G -> D (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065377.
VARIANT 139 139 R -> K (in FA7D).
/FTId=VAR_006497.
VARIANT 139 139 R -> Q (in FA7D; Charlotte;
dbSNP:rs150525536).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8204879,
ECO:0000269|PubMed:8242057}.
/FTId=VAR_006498.
VARIANT 139 139 R -> W (in FA7D; dbSNP:rs776796178).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:8242057}.
/FTId=VAR_006499.
VARIANT 151 151 C -> S (in FA7D).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014410.
VARIANT 154 154 E -> K (in FA7D; dbSNP:rs146795869).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015137.
VARIANT 156 156 G -> S (in FA7D; dbSNP:rs563972504).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065378.
VARIANT 157 157 G -> C (in FA7D).
/FTId=VAR_006501.
VARIANT 157 157 G -> S (in FA7D; dbSNP:rs763458490).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_006500.
VARIANT 157 157 G -> V (in FA7D; dbSNP:rs771335282).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014411.
VARIANT 160 160 Q -> R (in FA7D; dbSNP:rs200016360).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8242057}.
/FTId=VAR_006502.
VARIANT 171 171 S -> F (in FA7D; dbSNP:rs143855920).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065379.
VARIANT 177 177 G -> R (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065380.
VARIANT 181 181 L -> P (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065381.
VARIANT 183 183 D -> N (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065382.
VARIANT 186 186 S -> F (in FA7D; dbSNP:rs764971156).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065383.
VARIANT 189 189 P -> S (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065384.
VARIANT 194 194 P -> L (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065385.
VARIANT 194 194 P -> T (in FA7D; Malta-I).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:9452082}.
/FTId=VAR_006503.
VARIANT 195 195 C -> R (in FA7D; dbSNP:rs372577568).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014412.
VARIANT 197 197 K -> E (in FA7D).
{ECO:0000269|PubMed:8242057}.
/FTId=VAR_006504.
VARIANT 198 198 I -> T (in FA7D; dbSNP:rs762621913).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065386.
VARIANT 212 212 R -> Q (in FA7D; Charlotte;
dbSNP:rs868044209).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:19751712,
ECO:0000269|PubMed:8204879}.
/FTId=VAR_006505.
VARIANT 216 216 G -> D (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015138.
VARIANT 238 238 C -> Y (in FA7D; dbSNP:rs121964928).
{ECO:0000269|PubMed:8364544}.
/FTId=VAR_006506.
VARIANT 240 240 G -> R (in FA7D).
{ECO:0000269|PubMed:19432927}.
/FTId=VAR_065387.
VARIANT 241 241 T -> N (in FA7D).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014413.
VARIANT 250 250 S -> F (in FA7D).
{ECO:0000269|PubMed:21372693}.
/FTId=VAR_065388.
VARIANT 251 251 A -> P (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065389.
VARIANT 251 251 A -> T (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065390.
VARIANT 254 254 C -> R (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065391.
VARIANT 254 254 C -> Y (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015139.
VARIANT 264 264 L -> P (in FA7D; dbSNP:rs753266903).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065392.
VARIANT 266 266 A -> T (in FA7D; dbSNP:rs764807079).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015140.
VARIANT 272 272 D -> N (in FA7D; dbSNP:rs751028917).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065393.
VARIANT 277 277 D -> N (in FA7D; dbSNP:rs550074221).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065394.
VARIANT 283 283 R -> W (in FA7D; dbSNP:rs779589651).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8844208}.
/FTId=VAR_006507.
VARIANT 295 295 V -> D (in dbSNP:rs6045).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013936.
VARIANT 298 298 T -> I (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065395.
VARIANT 301 301 H -> Q (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065396.
VARIANT 302 302 D -> H (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014414.
VARIANT 302 302 D -> N (in FA7D; dbSNP:rs770328850).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014415.
VARIANT 304 304 A -> T (in FA7D; dbSNP:rs773627551).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014416.
VARIANT 304 304 A -> V (in FA7D; Malta-II;
dbSNP:rs121964931).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8883260,
ECO:0000269|PubMed:9452082}.
/FTId=VAR_006508.
VARIANT 307 307 R -> C (in FA7D; dbSNP:rs147680958).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014417.
VARIANT 307 307 R -> H (in FA7D; Mie; dbSNP:rs121964929).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:7974346}.
/FTId=VAR_006509.
VARIANT 312 312 V -> M (in FA7D; dbSNP:rs201991361).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015141.
VARIANT 314 314 L -> V (in FA7D).
{ECO:0000269|PubMed:21206266}.
/FTId=VAR_065397.
VARIANT 321 321 L -> F (in FA7D; dbSNP:rs778138366).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065398.
VARIANT 323 323 L -> R (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065399.
VARIANT 325 325 E -> K (in FA7D; dbSNP:rs749760143).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8844208}.
/FTId=VAR_006510.
VARIANT 326 326 R -> Q (in FA7D; dbSNP:rs146698837).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065400.
VARIANT 332 332 T -> M (in FA7D; dbSNP:rs200212201).
{ECO:0000269|PubMed:11129332}.
/FTId=VAR_014418.
VARIANT 337 337 R -> C (in FA7D; dbSNP:rs139372641).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065401.
VARIANT 341 341 V -> F (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015142.
VARIANT 343 343 G -> S (in FA7D).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:21206266}.
/FTId=VAR_065402.
VARIANT 344 344 W -> G (in FA7D).
{ECO:0000269|PubMed:26761581}.
/FTId=VAR_076570.
VARIANT 344 344 W -> R (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065403.
VARIANT 345 345 G -> S (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065404.
VARIANT 350 350 R -> C (in FA7D; dbSNP:rs747876824).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065405.
VARIANT 352 352 A -> T (in dbSNP:rs3093267).
{ECO:0000269|Ref.6}.
/FTId=VAR_013122.
VARIANT 354 354 A -> V (in FA7D; dbSNP:rs36209567).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:16292673,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:7981691}.
/FTId=VAR_006511.
VARIANT 358 358 M -> I (in FA7D; dbSNP:rs149283257).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8043443}.
/FTId=VAR_006512.
VARIANT 358 358 M -> V (in FA7D).
{ECO:0000269|PubMed:8844208}.
/FTId=VAR_006513.
VARIANT 360 360 L -> P (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065406.
VARIANT 363 363 P -> H (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065407.
VARIANT 363 363 P -> R (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015143.
VARIANT 364 364 R -> Q (in FA7D; Harrow/Padua;
dbSNP:rs121964926).
{ECO:0000269|PubMed:1634227,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:2070047,
ECO:0000269|PubMed:8043443,
ECO:0000269|PubMed:8242057,
ECO:0000269|PubMed:8844208}.
/FTId=VAR_006514.
VARIANT 364 364 R -> W (in FA7D; dbSNP:rs750980786).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065408.
VARIANT 367 367 T -> S (in dbSNP:rs747673406).
{ECO:0000269|PubMed:7860081}.
/FTId=VAR_018671.
VARIANT 370 370 C -> F (in FA7D; dbSNP:rs121964927).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:1634227,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:19751712,
ECO:0000269|PubMed:8043443}.
/FTId=VAR_006515.
VARIANT 375 375 R -> W (in FA7D; dbSNP:rs137919286).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065409.
VARIANT 384 384 T -> M (in FA7D; dbSNP:rs531225271).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:19751712}.
/FTId=VAR_065410.
VARIANT 387 387 M -> T (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065411.
VARIANT 387 387 M -> V (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065412.
VARIANT 388 388 F -> S (in FA7D; reduces tissue factor
binding; impairs activation by factor Xa;
abolishes amidolytic and coagulant
activities; dbSNP:rs121964938).
{ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8940045}.
/FTId=VAR_065413.
VARIANT 389 389 C -> G (in FA7D; dbSNP:rs121964934).
{ECO:0000269|PubMed:11091194,
ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:21206266}.
/FTId=VAR_014392.
VARIANT 391 391 G -> C (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065414.
VARIANT 391 391 G -> S (in FA7D; dbSNP:rs190485816).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014419.
VARIANT 398 398 D -> E (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065415.
VARIANT 401 401 K -> E (in FA7D; dbSNP:rs748979195).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065416.
VARIANT 402 402 G -> E (in FA7D).
{ECO:0000269|PubMed:8844208}.
/FTId=VAR_006517.
VARIANT 402 402 G -> R (in FA7D).
{ECO:0000269|PubMed:8043443}.
/FTId=VAR_006516.
VARIANT 403 403 D -> H (in FA7D).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_015144.
VARIANT 404 404 S -> N (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065417.
VARIANT 408 408 H -> Q (in FA7D; dbSNP:rs121964936).
{ECO:0000269|PubMed:12472587}.
/FTId=VAR_065418.
VARIANT 408 408 H -> R (in FA7D).
{ECO:0000269|PubMed:19751712}.
/FTId=VAR_065419.
VARIANT 413 413 R -> G (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065420.
VARIANT 413 413 R -> Q (may be associated with decreased
susceptibility to myocardial infarction;
dbSNP:rs6046).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10984565,
ECO:0000269|PubMed:16292673,
ECO:0000269|PubMed:8043443,
ECO:0000269|PubMed:8844208,
ECO:0000269|Ref.6}.
/FTId=VAR_006518.
VARIANT 414 414 G -> C (in FA7D; results in severely
impaired protein secretion;
dbSNP:rs121964937).
{ECO:0000269|PubMed:14717781}.
/FTId=VAR_065421.
VARIANT 419 419 T -> M (in FA7D; dbSNP:rs121964930).
{ECO:0000269|PubMed:10862079,
ECO:0000269|PubMed:18976247,
ECO:0000269|PubMed:8652821}.
/FTId=VAR_006519.
VARIANT 422 422 V -> F (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065422.
VARIANT 425 425 G -> A (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065423.
VARIANT 425 425 G -> C (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065424.
VARIANT 429 429 A -> T (in FA7D; dbSNP:rs755377592).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065425.
VARIANT 432 432 G -> D (in FA7D).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065426.
VARIANT 435 435 G -> E (in FA7D; dbSNP:rs756956471).
{ECO:0000269|PubMed:11129332,
ECO:0000269|PubMed:18976247}.
/FTId=VAR_014420.
VARIANT 437 437 Y -> F (in FA7D; dbSNP:rs758213652).
{ECO:0000269|PubMed:18976247}.
/FTId=VAR_065427.
VARIANT 445 445 E -> K (in dbSNP:rs3093248).
{ECO:0000269|Ref.6}.
/FTId=VAR_013123.
MUTAGEN 112 112 S->A: Complete loss of O-glycosylation
and O-xylosylation by POGLUT1.
{ECO:0000269|PubMed:21949356}.
MUTAGEN 113 113 S->A: No effect on O-glycosylation by
POGLUT1. Drastic decrease in O-
xylosylation.
{ECO:0000269|PubMed:21949356}.
HELIX 66 68 {ECO:0000244|PDB:4YLQ}.
HELIX 73 77 {ECO:0000244|PDB:4YLQ}.
HELIX 84 91 {ECO:0000244|PDB:4YLQ}.
HELIX 94 104 {ECO:0000244|PDB:4YLQ}.
TURN 109 112 {ECO:0000244|PDB:4YLQ}.
TURN 116 118 {ECO:0000244|PDB:1QFK}.
STRAND 120 124 {ECO:0000244|PDB:4YLQ}.
STRAND 127 131 {ECO:0000244|PDB:4YLQ}.
STRAND 136 138 {ECO:0000244|PDB:4YLQ}.
HELIX 145 147 {ECO:0000244|PDB:2C4F}.
STRAND 148 150 {ECO:0000244|PDB:1QFK}.
TURN 151 153 {ECO:0000244|PDB:4YLQ}.
HELIX 154 157 {ECO:0000244|PDB:4YLQ}.
STRAND 159 165 {ECO:0000244|PDB:4YLQ}.
STRAND 168 173 {ECO:0000244|PDB:4YLQ}.
STRAND 178 180 {ECO:0000244|PDB:4YLQ}.
STRAND 187 193 {ECO:0000244|PDB:4YLQ}.
TURN 199 201 {ECO:0000244|PDB:4YLQ}.
HELIX 220 222 {ECO:0000244|PDB:1JBU}.
STRAND 227 232 {ECO:0000244|PDB:4YLQ}.
STRAND 235 242 {ECO:0000244|PDB:4YLQ}.
STRAND 244 250 {ECO:0000244|PDB:4YLQ}.
HELIX 252 255 {ECO:0000244|PDB:4YLQ}.
HELIX 261 263 {ECO:0000244|PDB:4YLQ}.
STRAND 264 269 {ECO:0000244|PDB:4YLQ}.
STRAND 272 274 {ECO:0000244|PDB:2FLB}.
STRAND 281 291 {ECO:0000244|PDB:4YLQ}.
STRAND 298 301 {ECO:0000244|PDB:1JBU}.
STRAND 304 310 {ECO:0000244|PDB:4YLQ}.
HELIX 326 331 {ECO:0000244|PDB:4YLQ}.
HELIX 333 335 {ECO:0000244|PDB:4YLQ}.
STRAND 337 348 {ECO:0000244|PDB:4YLQ}.
TURN 352 355 {ECO:0000244|PDB:1DVA}.
STRAND 358 365 {ECO:0000244|PDB:4YLQ}.
HELIX 367 370 {ECO:0000244|PDB:4YLQ}.
HELIX 372 374 {ECO:0000244|PDB:1JBU}.
TURN 376 378 {ECO:0000244|PDB:4YLQ}.
TURN 380 382 {ECO:0000244|PDB:4YLQ}.
HELIX 383 386 {ECO:0000244|PDB:1JBU}.
STRAND 387 391 {ECO:0000244|PDB:4YLQ}.
STRAND 393 396 {ECO:0000244|PDB:4JZE}.
HELIX 401 403 {ECO:0000244|PDB:2BZ6}.
STRAND 407 412 {ECO:0000244|PDB:4YLQ}.
STRAND 415 424 {ECO:0000244|PDB:4YLQ}.
STRAND 426 429 {ECO:0000244|PDB:4YLQ}.
STRAND 435 439 {ECO:0000244|PDB:4YLQ}.
HELIX 440 443 {ECO:0000244|PDB:4YLQ}.
HELIX 444 452 {ECO:0000244|PDB:4YLQ}.
STRAND 459 463 {ECO:0000244|PDB:4YLQ}.
SEQUENCE 466 AA; 51594 MW; 9B5D501669D67B06 CRC64;
MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE AHGVLHRRRR
ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF WISYSDGDQC ASSPCQNGGS
CKDQLQSYIC FCLPAFEGRN CETHKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL
LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG
TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN
HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL
NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG
IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP


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