FA7_HUMAN
ID FA7_HUMAN Reviewed; 466 AA.
AC P08709; B0YJC8; Q14339; Q5JVF1; Q5JVF2; Q9UD52; Q9UD53; Q9UD54;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 274.
DE RecName: Full=Coagulation factor VII;
DE EC=3.4.21.21;
DE AltName: Full=Proconvertin;
DE AltName: Full=Serum prothrombin conversion accelerator;
DE Short=SPCA;
DE AltName: INN=Eptacog alfa;
DE Contains:
DE RecName: Full=Factor VII light chain;
DE Contains:
DE RecName: Full=Factor VII heavy chain;
DE Flags: Precursor;
GN Name=F7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Liver;
RX PubMed=3486420; DOI=10.1073/pnas.83.8.2412;
RA Hagen F.S., Gray C.L., O'Hara P.J., Grant F.J., Saari G.C., Woodbury R.G.,
RA Hart C.E., Insley M.Y., Kisiel W., Kurachi K., Davie E.W.;
RT "Characterization of a cDNA coding for human factor VII.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2412-2416(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3037537; DOI=10.1073/pnas.84.15.5158;
RA O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y., Hagen F.S.,
RA Murray M.J.;
RT "Nucleotide sequence of the gene coding for human factor VII, a vitamin K-
RT dependent protein participating in blood coagulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-354 AND GLN-413.
RX PubMed=16292673; DOI=10.1007/s00439-005-0045-5;
RA Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J.,
RA Fontcuberta J., Calafell F.;
RT "Human F7 sequence is split into three deep clades that are related to FVII
RT plasma levels.";
RL Hum. Genet. 118:741-751(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Soria J.M., Almasy L., Souto J.C., Sabater M., Fontcuberta J., Blangero J.;
RT "Complete dissection of a human quantitative trait locus: allelic
RT architecture of F7 and factor VII levels.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Masroori N., Habibi Roudkenar M., Halabian R.;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-352; GLN-413 AND
RP LYS-445.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 61-466, GAMMA-CARBOXYGLUTAMATION AT GLU-66; GLU-67;
RP GLU-74; GLU-76; GLU-79; GLU-80; GLU-85; GLU-86; GLU-89 AND GLU-95,
RP HYDROXYLATION AT ASP-123, AND GLYCOSYLATION AT ASN-205 AND ASN-382.
RX PubMed=3264725; DOI=10.1021/bi00420a030;
RA Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T.,
RA Pedersen A.H., Hedner U.;
RT "Amino acid sequence and posttranslational modifications of human factor
RT VIIa from plasma and transfected baby hamster kidney cells.";
RL Biochemistry 27:7785-7793(1988).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS FA7D ILE-358;
RP GLN-364; PHE-370 AND ARG-402, AND VARIANT GLN-413.
RX PubMed=8043443; DOI=10.1111/j.1365-2141.1994.tb04793.x;
RA Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C.,
RA Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S.,
RA Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G.;
RT "Molecular defects in CRM+ factor VII deficiencies: modelling of missense
RT mutations in the catalytic domain of FVII.";
RL Br. J. Haematol. 86:610-618(1994).
RN [12]
RP GLYCOSYLATION AT SER-112, AND STRUCTURE OF CARBOHYDRATE ON SER-112.
RX PubMed=2511201; DOI=10.1016/s0021-9258(19)47065-8;
RA Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
RA Shimonishi Y., Iwanaga S.;
RT "Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)
RT O-glycosidically linked to a serine residue in the first epidermal growth
RT factor-like domain of human factors VII and IX and protein Z and bovine
RT protein Z.";
RL J. Biol. Chem. 264:20320-20325(1989).
RN [13]
RP GLYCOSYLATION AT SER-112, AND STRUCTURE OF CARBOHYDRATE ON SER-112.
RX PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
RA Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in the first
RT EGF-like domain of clotting factors VII and IX and protein Z.";
RL Adv. Exp. Med. Biol. 281:121-131(1990).
RN [14]
RP GLYCOSYLATION AT SER-112 AND SER-120.
RX PubMed=1904059; DOI=10.1016/s0021-9258(18)99126-x;
RA Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M., Komiyama Y.,
RA Pedersen A.H., Kisiel W.;
RT "Human plasma and recombinant factor VII. Characterization of O-
RT glycosylations at serine residues 52 and 60 and effects of site-directed
RT mutagenesis of serine 52 to alanine.";
RL J. Biol. Chem. 266:11051-11057(1991).
RN [15]
RP GLYCOSYLATION AT SER-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9023546; DOI=10.1093/glycob/6.8.837;
RA Wang Y., Lee G.F., Kelley R.F., Spellman M.W.;
RT "Identification of a GDP-L-fucose:polypeptide fucosyltransferase and
RT enzymatic addition of O-linked fucose to EGF domains.";
RL Glycobiology 6:837-842(1996).
RN [16]
RP GLYCOSYLATION AT ASN-205 AND ASN-382.
RX PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
RA Ruiz-Canada C., Kelleher D.J., Gilmore R.;
RT "Cotranslational and posttranslational N-glycosylation of polypeptides by
RT distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [17]
RP GLYCOSYLATION AT SER-112, AND MUTAGENESIS OF SER-112 AND SER-113.
RX PubMed=21949356; DOI=10.1073/pnas.1109696108;
RA Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A.,
RA Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A.,
RA Jafar-Nejad H., Haltiwanger R.S.;
RT "Rumi functions as both a protein O-glucosyltransferase and a protein O-
RT xylosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
RX PubMed=8598903; DOI=10.1038/380041a0;
RA Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H.,
RA Nemreson Y., Kirchhofer D.;
RT "The crystal structure of the complex of blood coagulation factor VIIa with
RT soluble tissue factor.";
RL Nature 380:41-46(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
RX PubMed=9925787; DOI=10.1006/jmbi.1998.2452;
RA Zhang E., St Charles R., Tulinsky A.;
RT "Structure of extracellular tissue factor complexed with factor VIIa
RT inhibited with a BPTI mutant.";
RL J. Mol. Biol. 285:2089-2104(1999).
RN [20]
RP STRUCTURE BY NMR OF 105-145.
RX PubMed=9692950; DOI=10.1021/bi980522f;
RA Muranyi A., Finn B.E., Gippert G.P., Forsen S., Stenflo J., Drakenberg T.;
RT "Solution structure of the N-terminal EGF-like domain from human factor
RT VII.";
RL Biochemistry 37:10605-10615(1998).
RN [21]
RP VARIANT FA7D GLN-364.
RX PubMed=2070047;
RA O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J.,
RA Meade T.W., Tuddenham E.G.D.;
RT "Purification and characterization of factor VII 304-Gln: a variant
RT molecule with reduced activity isolated from a clinically unaffected
RT male.";
RL Blood 78:132-140(1991).
RN [22]
RP VARIANTS FA7D GLN-364 AND PHE-370.
RX PubMed=1634227; DOI=10.1007/bf00219173;
RA Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M.,
RA Rodorigo G., Casonato A., Girolami A., Bernardi F.;
RT "Detection of two missense mutations and characterization of a repeat
RT polymorphism in the factor VII gene (F7).";
RL Hum. Genet. 89:497-502(1992).
RN [23]
RP VARIANT FA7D TYR-238.
RX PubMed=8364544; DOI=10.1093/hmg/2.7.1055;
RA Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F.;
RT "A missense mutation (178Cys-->Tyr) and two neutral dimorphisms (115His and
RT 333Ser) in the human coagulation factor VII gene.";
RL Hum. Mol. Genet. 2:1055-1056(1993).
RN [24]
RP VARIANTS FA7D GLN-139; TRP-139; ARG-160; GLU-197 AND GLN-364.
RX PubMed=8242057; DOI=10.1093/hmg/2.9.1355;
RA Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N., von Felten A.,
RA Meili E., Hahn I., Prangnell D.R., Lumley H., Tuddenham E.G.D., McVey J.H.;
RT "Detection of missense mutations by single-strand conformational
RT polymorphism (SSCP) analysis in five dysfunctional variants of coagulation
RT factor VII.";
RL Hum. Mol. Genet. 2:1355-1359(1993).
RN [25]
RP VARIANTS FA7D GLN-139 AND GLN-212.
RX PubMed=8204879;
RA Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W.,
RA Roberts H.R., Blajchman M., Monroe D.M., High K.A.;
RT "Severe factor VII deficiency caused by mutations abolishing the cleavage
RT site for activation and altering binding to tissue factor.";
RL Blood 83:3524-3535(1994).
RN [26]
RP VARIANT SER-367.
RX PubMed=7860081; DOI=10.1159/000154235;
RA Dewald G., Noethen M.M., Ruther K.;
RT "A common Ser/Thr polymorphism in the perforin-homologous region of human
RT complement component C7.";
RL Hum. Hered. 44:301-304(1994).
RN [27]
RP VARIANT FA7D VAL-354.
RX PubMed=7981691; DOI=10.1093/hmg/3.7.1175;
RA Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B.,
RA Rodeghiero F., Marchetti G.;
RT "Topologically equivalent mutations causing dysfunctional coagulation
RT factors VII (294Ala-->Val) and X (334Ser-->Pro).";
RL Hum. Mol. Genet. 3:1175-1177(1994).
RN [28]
RP VARIANT FA7D HIS-307.
RX PubMed=7974346;
RA Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K.;
RT "Factor VII Mie: homozygous asymptomatic type I deficiency caused by an
RT amino acid substitution of His (CAC) for Arg(247) (CGC) in the catalytic
RT domain.";
RL Thromb. Haemost. 71:773-777(1994).
RN [29]
RP VARIANT FA7D MET-419.
RX PubMed=8652821;
RA Arbini A.A., Mannucci P.M., Bauer K.A.;
RT "A Thr359Met mutation in factor VII of a patient with a hereditary
RT deficiency causes defective secretion of the molecule.";
RL Blood 87:5085-5094(1996).
RN [30]
RP VARIANTS FA7D TRP-283; LYS-325; VAL-358; GLN-364 AND GLU-402, AND VARIANT
RP GLN-413.
RX PubMed=8844208;
RX DOI=10.1002/(sici)1098-1004(1996)8:2<108::aid-humu2>3.0.co;2-7;
RA Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G.,
RA Lunghi B., Rodeghiero F., Marchetti G.;
RT "Mutation pattern in clinically asymptomatic coagulation factor VII
RT deficiency.";
RL Hum. Mutat. 8:108-115(1996).
RN [31]
RP VARIANT FA7D SER-388, AND CHARACTERIZATION OF VARIANT FA7D SER-388.
RX PubMed=8940045; DOI=10.1074/jbc.271.48.30685;
RA Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C., Kisiel W.;
RT "Factor VII central. A novel mutation in the catalytic domain that reduces
RT tissue factor binding, impairs activation by factor Xa, and abolishes
RT amidolytic and coagulant activity.";
RL J. Biol. Chem. 271:30685-30691(1996).
RN [32]
RP VARIANT FA7D VAL-304.
RX PubMed=8883260;
RA Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N.,
RA Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R.,
RA Seligsohn U.;
RT "Ala244Val is a common, probably ancient mutation causing factor VII
RT deficiency in Moroccan and Iranian Jews.";
RL Thromb. Haemost. 76:283-291(1996).
RN [33]
RP VARIANT FA7D ASP-117, AND CHARACTERIZATION OF VARIANT FA7D ASP-117.
RX PubMed=9414278;
RA Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S., Yang D.,
RA Clarke B.J.;
RT "Factor VII deficiency caused by a structural variant N57D of the first
RT epidermal growth factor domain.";
RL Blood 91:142-148(1998).
RN [34]
RP VARIANT FA7D PRO-13.
RX PubMed=9576180; DOI=10.1046/j.1365-2141.1998.00666.x;
RA Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S.,
RA Sakuragawa N.;
RT "Factor VII Morioka (FVII L-26P): a homozygous missense mutation in the
RT signal sequence identified in a patient with factor VII deficiency.";
RL Br. J. Haematol. 101:47-49(1998).
RN [35]
RP VARIANTS FA7D THR-194 AND VAL-304.
RX PubMed=9452082; DOI=10.1002/humu.1380110161;
RA Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.;
RT "Two new missense mutations (P134T and A244V) in the coagulation factor VII
RT gene.";
RL Hum. Mutat. Suppl. 1:S189-S191(1998).
RN [36]
RP VARIANTS ASP-295 AND GLN-413.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [37]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [38]
RP VARIANT FA7D GLY-389.
RX PubMed=11091194; DOI=10.1046/j.1365-2141.2000.02332.x;
RA Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L.;
RT "Two novel factor VII gene mutations in a Chinese family with factor VII
RT deficiency.";
RL Br. J. Haematol. 111:143-145(2000).
RN [39]
RP VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151;
RP VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304;
RP CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435.
RX PubMed=11129332; DOI=10.1007/s004390000373;
RA Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D., Mumford A.D.,
RA Attock G.B., Reverter J.C., Lanir N., Parapia L.A., Reynaud J., Meili E.,
RA von Felton A., Martinowitz U., Prangnell D.R., Krawczak M., Cooper D.N.;
RT "Molecular analysis of the genotype-phenotype relationship in factor VII
RT deficiency.";
RL Hum. Genet. 107:327-342(2000).
RN [40]
RP VARIANTS FA7D LEU-64; PRO-120; CYS-128; LYS-154; SER-157; ARG-160; ARG-195;
RP GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304; CYS-307; MET-312;
RP LYS-325; PHE-341; VAL-354; ILE-358; ARG-363; PHE-370; HIS-403 AND MET-419.
RX PubMed=10862079;
RX DOI=10.1002/1098-1004(200006)15:6<489::aid-humu1>3.0.co;2-j;
RA Wulff K., Herrmann F.H.;
RT "Twenty two novel mutations of the factor VII gene in factor VII
RT deficiency.";
RL Hum. Mutat. 15:489-496(2000).
RN [41]
RP VARIANT GLN-413.
RX PubMed=10984565; DOI=10.1056/nejm200009143431104;
RA Girelli D., Russo C., Ferraresi P., Olivieri O., Pinotti M., Friso S.,
RA Manzato F., Mazzucco A., Bernardi F., Corrocher R.;
RT "Polymorphisms in the factor VII gene and the risk of myocardial infarction
RT in patients with coronary artery disease.";
RL N. Engl. J. Med. 343:774-780(2000).
RN [42]
RP VARIANTS FA7D LYS-85 AND GLN-408.
RX PubMed=12472587; DOI=10.1046/j.1365-2141.2002.03933.x;
RA Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K.,
RA Arai M., Fukutake K.;
RT "Two double heterozygous mutations in the F7 gene show different
RT manifestations.";
RL Br. J. Haematol. 119:1052-1058(2002).
RN [43]
RP VARIANT FA7D CYS-414, AND CHARACTERIZATION OF VARIANT FA7D CYS-414.
RX PubMed=14717781; DOI=10.1046/j.1365-2141.2003.04778.x;
RA Takamiya O., Hino K.;
RT "A patient homozygous for a Gly354Cys mutation in factor VII that results
RT in severely impaired secretion of the molecule, but not complete
RT deficiency.";
RL Br. J. Haematol. 124:336-342(2004).
RN [44]
RP VARIANTS FA7D ARG-82; ARG-177; THR-198; GLN-212; PRO-251; ARG-323; ARG-344;
RP PHE-370; MET-384; GLU-398 AND ARG-408.
RX PubMed=19751712; DOI=10.1016/j.cca.2009.09.007;
RA Mota L., Shetty S., Idicula-Thomas S., Ghosh K.;
RT "Phenotypic and genotypic characterization of Factor VII deficiency
RT patients from Western India.";
RL Clin. Chim. Acta 409:106-111(2009).
RN [45]
RP VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88; PRO-120;
RP CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157; ARG-160; PHE-171;
RP PRO-181; ASN-183; PHE-186; SER-189; LEU-194; THR-194; ARG-195; GLN-212;
RP ASP-216; ASN-241; THR-251; ARG-254; TYR-254; PRO-264; THR-266; ASN-272;
RP ASN-277; TRP-283; ILE-298; GLN-301; ASN-302; HIS-302; THR-304; VAL-304;
RP CYS-307; HIS-307; MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341;
RP SER-343; SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363;
RP GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387; SER-388;
RP CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413; MET-419; PHE-422;
RP ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND PHE-437.
RX PubMed=18976247; DOI=10.1111/j.1365-2516.2008.01910.x;
RA Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J.,
RA Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N.,
RA Salazar-Sanchez L.;
RT "Factor VII deficiency: clinical manifestation of 717 subjects from Europe
RT and Latin America with mutations in the factor 7 gene.";
RL Haemophilia 15:267-280(2009).
RN [46]
RP VARIANT FA7D ARG-240.
RX PubMed=19432927; DOI=10.1111/j.1365-2516.2009.02004.x;
RA Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O., Kapelushnik J.;
RT "Familial factor VII deficiency with foetal and neonatal fatal cerebral
RT haemorrhage associated with homozygosis to Gly180Arg mutation.";
RL Haemophilia 15:774-778(2009).
RN [47]
RP VARIANTS FA7D ARG-59 INS; VAL-314; SER-343 AND GLY-389.
RX PubMed=21206266; DOI=10.1097/mbc.0b013e328343641a;
RA Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J.;
RT "Recurrent mutations and genotype-phenotype correlations in hereditary
RT factor VII deficiency in Korea.";
RL Blood Coagul. Fibrinolysis 22:102-105(2011).
RN [48]
RP VARIANT FA7D PHE-250.
RX PubMed=21372693; DOI=10.1097/mbc.0b013e3283447388;
RA Jiang M., Wang Z., Yu Z., Bai X., Su J., Cao L., Zhang W., Ruan C.;
RT "A novel missense mutation close to the charge-stabilizing system in a
RT patient with congenital factor VII deficiency.";
RL Blood Coagul. Fibrinolysis 22:264-270(2011).
RN [49]
RP VARIANT FA7D GLY-344.
RX PubMed=26761581; DOI=10.1097/mbc.0000000000000499;
RA Hao X., Cheng X., Ye J., Wang Y., Yang L., Wang M., Jin Y.;
RT "Severe coagulation factor VII deficiency caused by a novel homozygous
RT mutation (p. Trp284Gly) in loop 140s.";
RL Blood Coagul. Fibrinolysis 27:461-463(2016).
CC -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine
CC protease that circulates in the blood in a zymogen form. Factor VII is
CC converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or
CC thrombin by minor proteolysis. In the presence of tissue factor and
CC calcium ions, factor VIIa then converts factor X to factor Xa by
CC limited proteolysis. Factor VIIa will also convert factor IX to factor
CC IXa in the presence of tissue factor and calcium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC factor Xa.; EC=3.4.21.21;
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a
CC disulfide bond. {ECO:0000269|PubMed:8598903,
CC ECO:0000269|PubMed:9925787}.
CC -!- INTERACTION:
CC P08709; P13726: F3; NbExp=7; IntAct=EBI-355972, EBI-1040727;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P08709-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P08709-2; Sequence=VSP_005387;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000269|PubMed:3264725}.
CC -!- PTM: O- and N-glycosylated. N-glycosylation at Asn-205 occurs
CC cotranslationally and is mediated by STT3A-containing complexes, while
CC glycosylation at Asn-382 is post-translational and is mediated STT3B-
CC containing complexes before folding. O-fucosylated by POFUT1 on a
CC conserved serine or threonine residue found in the consensus sequence
CC C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and
CC third conserved cysteines. {ECO:0000269|PubMed:1904059,
CC ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:21949356,
CC ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:9023546}.
CC -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-112 by
CC POGLUT1 in vitro.
CC -!- DISEASE: Factor VII deficiency (FA7D) [MIM:227500]: A hemorrhagic
CC disease with variable presentation. The clinical picture can be very
CC severe, with the early occurrence of intracerebral hemorrhages or
CC repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal
CC hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a
CC surgical intervention. Finally, numerous subjects are completely
CC asymptomatic despite very low factor VII levels.
CC {ECO:0000269|PubMed:10862079, ECO:0000269|PubMed:11091194,
CC ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:12472587,
CC ECO:0000269|PubMed:14717781, ECO:0000269|PubMed:1634227,
CC ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19432927,
CC ECO:0000269|PubMed:19751712, ECO:0000269|PubMed:2070047,
CC ECO:0000269|PubMed:21206266, ECO:0000269|PubMed:21372693,
CC ECO:0000269|PubMed:26761581, ECO:0000269|PubMed:7974346,
CC ECO:0000269|PubMed:7981691, ECO:0000269|PubMed:8043443,
CC ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8242057,
CC ECO:0000269|PubMed:8364544, ECO:0000269|PubMed:8652821,
CC ECO:0000269|PubMed:8844208, ECO:0000269|PubMed:8883260,
CC ECO:0000269|PubMed:8940045, ECO:0000269|PubMed:9414278,
CC ECO:0000269|PubMed:9452082, ECO:0000269|PubMed:9576180}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- PHARMACEUTICAL: Available under the names Niastase or Novoseven (Novo
CC Nordisk). Used for the treatment of bleeding episodes in hemophilia A
CC or B patients with antibodies to coagulation factors VIII or IX.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor VII entry;
CC URL="https://en.wikipedia.org/wiki/Factor_VII";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f7/";
CC ---------------------------------------------------------------------------
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DR EMBL; M13232; AAA88040.1; -; mRNA.
DR EMBL; M13232; AAA88041.1; -; mRNA.
DR EMBL; J02933; AAA51983.1; -; Genomic_DNA.
DR EMBL; DQ142911; ABD17891.1; -; Genomic_DNA.
DR EMBL; AY212252; AAP33841.1; -; Genomic_DNA.
DR EMBL; EU557239; ACB87203.1; -; mRNA.
DR EMBL; AF466933; AAL66184.1; -; Genomic_DNA.
DR EMBL; EF445049; ACA06107.1; -; Genomic_DNA.
DR EMBL; EF445049; ACA06108.1; -; Genomic_DNA.
DR EMBL; AL137002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130468; AAI30469.1; -; mRNA.
DR CCDS; CCDS9528.1; -. [P08709-1]
DR CCDS; CCDS9529.1; -. [P08709-2]
DR PIR; A28322; KFHU7.
DR RefSeq; NP_000122.1; NM_000131.4. [P08709-1]
DR RefSeq; NP_062562.1; NM_019616.3. [P08709-2]
DR PDB; 1BF9; NMR; -; A=105-145.
DR PDB; 1CVW; X-ray; 2.28 A; H=213-466, L=150-204.
DR PDB; 1DAN; X-ray; 2.00 A; H=213-466, L=61-212.
DR PDB; 1DVA; X-ray; 3.00 A; H/I=213-466, L/M=102-202.
DR PDB; 1F7E; NMR; -; A=105-147.
DR PDB; 1F7M; NMR; -; A=105-147.
DR PDB; 1FAK; X-ray; 2.10 A; H=213-466, L=61-212.
DR PDB; 1FF7; NMR; -; A=105-147.
DR PDB; 1FFM; NMR; -; A=105-147.
DR PDB; 1J9C; X-ray; 2.90 A; H=213-466, L=108-202.
DR PDB; 1JBU; X-ray; 2.00 A; H=213-466, L=150-212.
DR PDB; 1KLI; X-ray; 1.69 A; H=213-466, L=144-212.
DR PDB; 1KLJ; X-ray; 2.44 A; H=213-466, L=144-212.
DR PDB; 1O5D; X-ray; 2.05 A; H=213-466, L=61-212.
DR PDB; 1QFK; X-ray; 2.80 A; H=213-466, L=109-212.
DR PDB; 1W0Y; X-ray; 2.50 A; H=213-466, L=61-202.
DR PDB; 1W2K; X-ray; 3.00 A; H=213-466, L=61-202.
DR PDB; 1W7X; X-ray; 1.80 A; H=213-466, L=150-204.
DR PDB; 1W8B; X-ray; 3.00 A; H=213-466, L=148-204.
DR PDB; 1WQV; X-ray; 2.50 A; H=213-466, L=61-212.
DR PDB; 1WSS; X-ray; 2.60 A; H=213-466, L=61-212.
DR PDB; 1WTG; X-ray; 2.20 A; H=213-466, L=61-212.
DR PDB; 1WUN; X-ray; 2.40 A; H=213-466, L=61-212.
DR PDB; 1WV7; X-ray; 2.70 A; H=213-466, L=61-212.
DR PDB; 1YGC; X-ray; 2.00 A; H=213-466, L=150-212.
DR PDB; 1Z6J; X-ray; 2.00 A; H=213-466, L=61-202.
DR PDB; 2A2Q; X-ray; 1.80 A; H=213-466, L=61-212.
DR PDB; 2AEI; X-ray; 2.52 A; H=213-466, L=61-212.
DR PDB; 2AER; X-ray; 1.87 A; H=213-466, L=61-202.
DR PDB; 2B7D; X-ray; 2.24 A; H=213-466, L=61-212.
DR PDB; 2B8O; X-ray; 2.80 A; H=213-466, L=61-202.
DR PDB; 2BZ6; X-ray; 1.60 A; H=213-466, L=150-202.
DR PDB; 2C4F; X-ray; 1.72 A; H=213-466, L=61-202.
DR PDB; 2EC9; X-ray; 2.00 A; H=213-466, L=61-202.
DR PDB; 2F9B; X-ray; 2.54 A; H=213-466, L=61-212.
DR PDB; 2FIR; X-ray; 2.00 A; H=213-466, L=61-202.
DR PDB; 2FLB; X-ray; 1.95 A; H=213-466, L=61-212.
DR PDB; 2FLR; X-ray; 2.35 A; H=213-466, L=61-212.
DR PDB; 2PUQ; X-ray; 2.05 A; H=213-466, L=109-202.
DR PDB; 2ZP0; X-ray; 2.70 A; H=213-466, L=61-212.
DR PDB; 2ZWL; X-ray; 2.20 A; H=213-466, L=61-212.
DR PDB; 2ZZU; X-ray; 2.50 A; H=213-466, L=61-212.
DR PDB; 3ELA; X-ray; 2.20 A; H=213-466, L=61-212.
DR PDB; 3TH2; X-ray; 1.72 A; H=213-466, L=61-202.
DR PDB; 3TH3; X-ray; 2.70 A; H=213-466, L=61-202.
DR PDB; 3TH4; X-ray; 1.80 A; H=213-466, L=61-202.
DR PDB; 4IBL; X-ray; 1.80 A; H=213-466, L=61-212.
DR PDB; 4ISH; X-ray; 1.82 A; H=213-466, L=150-204.
DR PDB; 4ISI; X-ray; 1.94 A; H=213-466, L=150-204.
DR PDB; 4JYU; X-ray; 1.80 A; H=213-466, L=150-204.
DR PDB; 4JYV; X-ray; 2.19 A; H=213-466, L=150-204.
DR PDB; 4JZD; X-ray; 2.20 A; H=213-466, L=150-204.
DR PDB; 4JZE; X-ray; 1.52 A; H=213-466, L=150-204.
DR PDB; 4JZF; X-ray; 1.84 A; H=213-466, L=150-204.
DR PDB; 4NA9; X-ray; 2.24 A; H=213-466, L=150-204.
DR PDB; 4NG9; X-ray; 2.20 A; H=213-466, L=150-204.
DR PDB; 4NGA; X-ray; 2.15 A; H=213-466, L=150-204.
DR PDB; 4X8S; X-ray; 2.10 A; H=213-466, L=150-204.
DR PDB; 4X8T; X-ray; 2.20 A; H=213-466, L=150-204.
DR PDB; 4X8U; X-ray; 2.10 A; H=213-466, L=150-204.
DR PDB; 4X8V; X-ray; 2.50 A; H=213-466, L=150-204.
DR PDB; 4YLQ; X-ray; 1.40 A; H=213-466, L=61-212.
DR PDB; 4YT6; X-ray; 2.07 A; H=213-466, L=148-204.
DR PDB; 4YT7; X-ray; 2.30 A; H=213-466, L=148-204.
DR PDB; 4Z6A; X-ray; 2.25 A; H=213-466, L=108-203.
DR PDB; 4ZMA; X-ray; 2.30 A; H=213-466, L=61-212.
DR PDB; 4ZXX; X-ray; 2.60 A; H=213-466, L=150-204.
DR PDB; 4ZXY; X-ray; 2.06 A; H=213-466, L=150-204.
DR PDB; 5I46; X-ray; 2.06 A; H=213-466, L=150-204.
DR PDB; 5L0S; X-ray; 1.45 A; B=105-145.
DR PDB; 5L2Y; X-ray; 1.82 A; H=213-466, L=150-204.
DR PDB; 5L2Z; X-ray; 1.79 A; H=213-466, L=147-204.
DR PDB; 5L30; X-ray; 1.73 A; H=213-466, L=147-204.
DR PDB; 5PA8; X-ray; 1.98 A; A=149-212, C=213-466.
DR PDB; 5PA9; X-ray; 1.55 A; A=149-212, C=213-466.
DR PDB; 5PAA; X-ray; 1.98 A; A=149-212, C=213-466.
DR PDB; 5PAB; X-ray; 1.99 A; H=213-466, L=149-212.
DR PDB; 5PAC; X-ray; 1.50 A; A=149-212, B=213-466.
DR PDB; 5PAE; X-ray; 1.45 A; A=149-212, B=213-466.
DR PDB; 5PAF; X-ray; 1.50 A; A=149-212, B=213-466.
DR PDB; 5PAG; X-ray; 1.36 A; A=149-212, B=213-466.
DR PDB; 5PAI; X-ray; 1.73 A; A=149-212, B=213-466.
DR PDB; 5PAJ; X-ray; 1.70 A; A=149-212, B=213-466.
DR PDB; 5PAK; X-ray; 1.56 A; A=149-212, C=213-466.
DR PDB; 5PAM; X-ray; 1.60 A; A=149-212, B=213-466.
DR PDB; 5PAN; X-ray; 1.62 A; A=149-212, B=213-466.
DR PDB; 5PAO; X-ray; 1.40 A; A=149-212, C=213-466.
DR PDB; 5PAQ; X-ray; 1.59 A; A=149-212, B=213-466.
DR PDB; 5PAR; X-ray; 2.10 A; A=149-212, C=213-466.
DR PDB; 5PAS; X-ray; 1.48 A; A=149-212, C=213-466.
DR PDB; 5PAT; X-ray; 1.60 A; A=149-212, B=213-466.
DR PDB; 5PAU; X-ray; 1.55 A; A=149-212, C=213-466.
DR PDB; 5PAV; X-ray; 1.40 A; A=149-212, C=213-466.
DR PDB; 5PAW; X-ray; 2.20 A; A=149-212, B=213-466.
DR PDB; 5PAX; X-ray; 1.36 A; A=149-212, C=213-466.
DR PDB; 5PAY; X-ray; 1.66 A; A=149-212, C=213-466.
DR PDB; 5PB0; X-ray; 1.98 A; A=149-212, B=213-466.
DR PDB; 5PB1; X-ray; 1.90 A; A=149-212, D=213-466.
DR PDB; 5PB2; X-ray; 1.45 A; A=149-212, C=213-466.
DR PDB; 5PB3; X-ray; 1.90 A; A=149-212, C=213-466.
DR PDB; 5PB4; X-ray; 2.43 A; A=149-212, C=213-466.
DR PDB; 5PB5; X-ray; 1.84 A; A=149-212, B=213-466.
DR PDB; 5PB6; X-ray; 1.90 A; A=149-212, C=213-466.
DR PDB; 5TQE; X-ray; 1.90 A; H=213-466, L=150-204.
DR PDB; 5TQF; X-ray; 1.85 A; H=213-466, L=150-204.
DR PDB; 5TQG; X-ray; 1.90 A; H=213-466, L=150-204.
DR PDB; 5U6J; X-ray; 2.30 A; H=213-466, L=150-204.
DR PDBsum; 1BF9; -.
DR PDBsum; 1CVW; -.
DR PDBsum; 1DAN; -.
DR PDBsum; 1DVA; -.
DR PDBsum; 1F7E; -.
DR PDBsum; 1F7M; -.
DR PDBsum; 1FAK; -.
DR PDBsum; 1FF7; -.
DR PDBsum; 1FFM; -.
DR PDBsum; 1J9C; -.
DR PDBsum; 1JBU; -.
DR PDBsum; 1KLI; -.
DR PDBsum; 1KLJ; -.
DR PDBsum; 1O5D; -.
DR PDBsum; 1QFK; -.
DR PDBsum; 1W0Y; -.
DR PDBsum; 1W2K; -.
DR PDBsum; 1W7X; -.
DR PDBsum; 1W8B; -.
DR PDBsum; 1WQV; -.
DR PDBsum; 1WSS; -.
DR PDBsum; 1WTG; -.
DR PDBsum; 1WUN; -.
DR PDBsum; 1WV7; -.
DR PDBsum; 1YGC; -.
DR PDBsum; 1Z6J; -.
DR PDBsum; 2A2Q; -.
DR PDBsum; 2AEI; -.
DR PDBsum; 2AER; -.
DR PDBsum; 2B7D; -.
DR PDBsum; 2B8O; -.
DR PDBsum; 2BZ6; -.
DR PDBsum; 2C4F; -.
DR PDBsum; 2EC9; -.
DR PDBsum; 2F9B; -.
DR PDBsum; 2FIR; -.
DR PDBsum; 2FLB; -.
DR PDBsum; 2FLR; -.
DR PDBsum; 2PUQ; -.
DR PDBsum; 2ZP0; -.
DR PDBsum; 2ZWL; -.
DR PDBsum; 2ZZU; -.
DR PDBsum; 3ELA; -.
DR PDBsum; 3TH2; -.
DR PDBsum; 3TH3; -.
DR PDBsum; 3TH4; -.
DR PDBsum; 4IBL; -.
DR PDBsum; 4ISH; -.
DR PDBsum; 4ISI; -.
DR PDBsum; 4JYU; -.
DR PDBsum; 4JYV; -.
DR PDBsum; 4JZD; -.
DR PDBsum; 4JZE; -.
DR PDBsum; 4JZF; -.
DR PDBsum; 4NA9; -.
DR PDBsum; 4NG9; -.
DR PDBsum; 4NGA; -.
DR PDBsum; 4X8S; -.
DR PDBsum; 4X8T; -.
DR PDBsum; 4X8U; -.
DR PDBsum; 4X8V; -.
DR PDBsum; 4YLQ; -.
DR PDBsum; 4YT6; -.
DR PDBsum; 4YT7; -.
DR PDBsum; 4Z6A; -.
DR PDBsum; 4ZMA; -.
DR PDBsum; 4ZXX; -.
DR PDBsum; 4ZXY; -.
DR PDBsum; 5I46; -.
DR PDBsum; 5L0S; -.
DR PDBsum; 5L2Y; -.
DR PDBsum; 5L2Z; -.
DR PDBsum; 5L30; -.
DR PDBsum; 5PA8; -.
DR PDBsum; 5PA9; -.
DR PDBsum; 5PAA; -.
DR PDBsum; 5PAB; -.
DR PDBsum; 5PAC; -.
DR PDBsum; 5PAE; -.
DR PDBsum; 5PAF; -.
DR PDBsum; 5PAG; -.
DR PDBsum; 5PAI; -.
DR PDBsum; 5PAJ; -.
DR PDBsum; 5PAK; -.
DR PDBsum; 5PAM; -.
DR PDBsum; 5PAN; -.
DR PDBsum; 5PAO; -.
DR PDBsum; 5PAQ; -.
DR PDBsum; 5PAR; -.
DR PDBsum; 5PAS; -.
DR PDBsum; 5PAT; -.
DR PDBsum; 5PAU; -.
DR PDBsum; 5PAV; -.
DR PDBsum; 5PAW; -.
DR PDBsum; 5PAX; -.
DR PDBsum; 5PAY; -.
DR PDBsum; 5PB0; -.
DR PDBsum; 5PB1; -.
DR PDBsum; 5PB2; -.
DR PDBsum; 5PB3; -.
DR PDBsum; 5PB4; -.
DR PDBsum; 5PB5; -.
DR PDBsum; 5PB6; -.
DR PDBsum; 5TQE; -.
DR PDBsum; 5TQF; -.
DR PDBsum; 5TQG; -.
DR PDBsum; 5U6J; -.
DR AlphaFoldDB; P08709; -.
DR SMR; P08709; -.
DR BioGRID; 108453; 18.
DR ComplexPortal; CPX-2808; Coagulation factor VIIa - tissue factor complex.
DR ComplexPortal; CPX-6211; Coagulation factor VIIa complex.
DR CORUM; P08709; -.
DR DIP; DIP-6135N; -.
DR ELM; P08709; -.
DR IntAct; P08709; 13.
DR STRING; 9606.ENSP00000364731; -.
DR BindingDB; P08709; -.
DR ChEMBL; CHEMBL3991; -.
DR DrugBank; DB04590; (2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID.
DR DrugBank; DB07207; 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DR DrugBank; DB04758; 2-[2-ETHANESULFONYLAMINO-3-(1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIM IDOYL-BENZYLAMIDE).
DR DrugBank; DB04606; 2-[2-ETHANESULFONYLAMINO-3-(5-PROPOXY-1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIMIDOYL-BENZYLAMIDE).
DR DrugBank; DB04593; 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID.
DR DrugBank; DB07376; 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID).
DR DrugBank; DB07247; [2'-HYDROXY-3'-(1H-PYRROLO[3,2-C]PYRIDIN-2-YL)-BIPHENYL-3-YLMETHYL]-UREA.
DR DrugBank; DB08232; [5-(5-Amino-1H-pyrrolo[3,2-b]pyridin-2-yl)-6-hydroxy-3'-nitro-3-biphenylyl]acetic acid.
DR DrugBank; DB13151; Anti-inhibitor coagulant complex.
DR DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DR DrugBank; DB13152; Coagulation Factor IX Human.
DR DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DR DrugBank; DB09332; Kappadione.
DR DrugBank; DB04767; N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID.
DR DrugBank; DB13933; Nonacog beta pegol.
DR DrugBank; DB06552; rNAPc2.
DR DrugCentral; P08709; -.
DR GuidetoPHARMACOLOGY; 2363; -.
DR MEROPS; S01.215; -.
DR GlyConnect; 98; 4 O-Linked glycans (2 sites).
DR GlyGen; P08709; 5 sites, 9 N-linked glycans (2 sites), 4 O-linked glycans (3 sites).
DR iPTMnet; P08709; -.
DR MetOSite; P08709; -.
DR PhosphoSitePlus; P08709; -.
DR BioMuta; F7; -.
DR DMDM; 119766; -.
DR MassIVE; P08709; -.
DR MaxQB; P08709; -.
DR PaxDb; P08709; -.
DR PeptideAtlas; P08709; -.
DR PRIDE; P08709; -.
DR ProteomicsDB; 52160; -. [P08709-1]
DR ProteomicsDB; 52161; -. [P08709-2]
DR ABCD; P08709; 1 sequenced antibody.
DR Antibodypedia; 11679; 671 antibodies from 37 providers.
DR DNASU; 2155; -.
DR Ensembl; ENST00000346342.8; ENSP00000329546.4; ENSG00000057593.14. [P08709-2]
DR Ensembl; ENST00000375581.3; ENSP00000364731.3; ENSG00000057593.14. [P08709-1]
DR GeneID; 2155; -.
DR KEGG; hsa:2155; -.
DR MANE-Select; ENST00000346342.8; ENSP00000329546.4; NM_019616.4; NP_062562.1. [P08709-2]
DR UCSC; uc001vsv.5; human. [P08709-1]
DR CTD; 2155; -.
DR DisGeNET; 2155; -.
DR GeneCards; F7; -.
DR HGNC; HGNC:3544; F7.
DR HPA; ENSG00000057593; Tissue enriched (liver).
DR MalaCards; F7; -.
DR MIM; 227500; phenotype.
DR MIM; 613878; gene.
DR neXtProt; NX_P08709; -.
DR OpenTargets; ENSG00000057593; -.
DR Orphanet; 327; Congenital factor VII deficiency.
DR PharmGKB; PA160; -.
DR VEuPathDB; HostDB:ENSG00000057593; -.
DR eggNOG; ENOG502QRGI; Eukaryota.
DR GeneTree; ENSGT00940000154474; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P08709; -.
DR OMA; DDQFQDY; -.
DR OrthoDB; 265965at2759; -.
DR PhylomeDB; P08709; -.
DR TreeFam; TF327329; -.
DR BRENDA; 3.4.21.21; 2681.
DR PathwayCommons; P08709; -.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR SABIO-RK; P08709; -.
DR SignaLink; P08709; -.
DR SIGNOR; P08709; -.
DR BioGRID-ORCS; 2155; 13 hits in 1074 CRISPR screens.
DR EvolutionaryTrace; P08709; -.
DR GeneWiki; Factor_VII; -.
DR GenomeRNAi; 2155; -.
DR Pharos; P08709; Tchem.
DR PRO; PR:P08709; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P08709; protein.
DR Bgee; ENSG00000057593; Expressed in right lobe of liver and 123 other tissues.
DR ExpressionAtlas; P08709; baseline and differential.
DR Genevisible; P08709; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IPI:ComplexPortal.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:1905286; C:serine-type peptidase complex; IPI:BHF-UCL.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IC:ComplexPortal.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
DR GO; GO:0007598; P:blood coagulation, extrinsic pathway; IC:ComplexPortal.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IC:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:BHF-UCL.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
DR GO; GO:0061476; P:response to anticoagulant; IEA:Ensembl.
DR GO; GO:1905217; P:response to astaxanthin; IEA:Ensembl.
DR GO; GO:0010037; P:response to carbon dioxide; IEA:Ensembl.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0033595; P:response to genistein; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:1904400; P:response to Thyroid stimulating hormone; IEA:Ensembl.
DR GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEA:Ensembl.
DR GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
DR GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IC:ComplexPortal.
DR GO; GO:0031638; P:zymogen activation; IC:ComplexPortal.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR033190; F7.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278:SF26; PTHR24278:SF26; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; Disulfide bond; EGF-like domain;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW Hydroxylation; Pharmaceutical; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..60
FT /evidence="ECO:0000269|PubMed:3264725"
FT /id="PRO_0000027729"
FT CHAIN 61..212
FT /note="Factor VII light chain"
FT /id="PRO_0000027730"
FT CHAIN 213..466
FT /note="Factor VII heavy chain"
FT /id="PRO_0000027731"
FT DOMAIN 61..105
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 106..142
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..188
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 213..452
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Important for S-112 for O-xylosylation"
FT SITE 212..213
FT /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT thrombin"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 74
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725"
FT MOD_RES 80
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 85
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 86
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 89
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 95
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420"
FT MOD_RES 123
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000269|PubMed:3264725"
FT CARBOHYD 112
FT /note="O-linked (Glc...) serine; alternate"
FT /evidence="ECO:0000269|PubMed:1904059,
FT ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356,
FT ECO:0000269|PubMed:2511201"
FT /id="CAR_000007"
FT CARBOHYD 112
FT /note="O-linked (Xyl...) serine; alternate"
FT /evidence="ECO:0000269|PubMed:1904059,
FT ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356,
FT ECO:0000269|PubMed:2511201"
FT CARBOHYD 120
FT /note="O-linked (Fuc) serine"
FT /evidence="ECO:0000269|PubMed:1904059,
FT ECO:0000269|PubMed:9023546"
FT /id="CAR_000180"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167329,
FT ECO:0000269|PubMed:3264725"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167329,
FT ECO:0000269|PubMed:3264725"
FT DISULFID 77..82
FT DISULFID 110..121
FT DISULFID 115..130
FT DISULFID 132..141
FT DISULFID 151..162
FT DISULFID 158..172
FT DISULFID 174..187
FT DISULFID 195..322
FT DISULFID 219..224
FT DISULFID 238..254
FT DISULFID 370..389
FT DISULFID 400..428
FT VAR_SEQ 22..43
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3486420"
FT /id="VSP_005387"
FT VARIANT 13
FT /note="L -> P (in FA7D; Morioka; dbSNP:rs387906507)"
FT /evidence="ECO:0000269|PubMed:9576180"
FT /id="VAR_014391"
FT VARIANT 59
FT /note="R -> RR (in FA7D)"
FT /evidence="ECO:0000269|PubMed:21206266"
FT /id="VAR_065369"
FT VARIANT 64
FT /note="F -> L (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015135"
FT VARIANT 73
FT /note="L -> Q (in FA7D; dbSNP:rs45572939)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014405"
FT VARIANT 79
FT /note="E -> Q (in FA7D)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014406"
FT VARIANT 82
FT /note="C -> F (in FA7D; dbSNP:rs1448296564)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065370"
FT VARIANT 82
FT /note="C -> R (in FA7D; dbSNP:rs745374448)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065371"
FT VARIANT 84
FT /note="Missing (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065372"
FT VARIANT 85
FT /note="E -> K (in FA7D; dbSNP:rs121964935)"
FT /evidence="ECO:0000269|PubMed:12472587"
FT /id="VAR_065373"
FT VARIANT 88
FT /note="R -> G (in FA7D; dbSNP:rs776354144)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065374"
FT VARIANT 88
FT /note="R -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065375"
FT VARIANT 117
FT /note="N -> D (in FA7D; exhibits no procoagulant activity
FT and is unable to bind tissue factor; dbSNP:rs121964932)"
FT /evidence="ECO:0000269|PubMed:9414278"
FT /id="VAR_065376"
FT VARIANT 120
FT /note="S -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015136"
FT VARIANT 121
FT /note="C -> F (in FA7D)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014407"
FT VARIANT 125
FT /note="L -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014408"
FT VARIANT 128
FT /note="Y -> C (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247"
FT /id="VAR_014409"
FT VARIANT 138
FT /note="G -> D (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065377"
FT VARIANT 139
FT /note="R -> K (in FA7D)"
FT /id="VAR_006497"
FT VARIANT 139
FT /note="R -> Q (in FA7D; Charlotte; dbSNP:rs150525536)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8242057"
FT /id="VAR_006498"
FT VARIANT 139
FT /note="R -> W (in FA7D; dbSNP:rs776796178)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:8242057"
FT /id="VAR_006499"
FT VARIANT 151
FT /note="C -> S (in FA7D)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014410"
FT VARIANT 154
FT /note="E -> K (in FA7D; dbSNP:rs146795869)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015137"
FT VARIANT 156
FT /note="G -> S (in FA7D; dbSNP:rs563972504)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065378"
FT VARIANT 157
FT /note="G -> C (in FA7D)"
FT /id="VAR_006501"
FT VARIANT 157
FT /note="G -> S (in FA7D; dbSNP:rs763458490)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_006500"
FT VARIANT 157
FT /note="G -> V (in FA7D; dbSNP:rs771335282)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014411"
FT VARIANT 160
FT /note="Q -> R (in FA7D; dbSNP:rs200016360)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8242057"
FT /id="VAR_006502"
FT VARIANT 171
FT /note="S -> F (in FA7D; dbSNP:rs143855920)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065379"
FT VARIANT 177
FT /note="G -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065380"
FT VARIANT 181
FT /note="L -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065381"
FT VARIANT 183
FT /note="D -> N (in FA7D; dbSNP:rs1258691292)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065382"
FT VARIANT 186
FT /note="S -> F (in FA7D; dbSNP:rs764971156)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065383"
FT VARIANT 189
FT /note="P -> S (in FA7D; dbSNP:rs1479693459)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065384"
FT VARIANT 194
FT /note="P -> L (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065385"
FT VARIANT 194
FT /note="P -> T (in FA7D; Malta-I; dbSNP:rs1234759020)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:9452082"
FT /id="VAR_006503"
FT VARIANT 195
FT /note="C -> R (in FA7D; dbSNP:rs372577568)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247"
FT /id="VAR_014412"
FT VARIANT 197
FT /note="K -> E (in FA7D; dbSNP:rs1250204261)"
FT /evidence="ECO:0000269|PubMed:8242057"
FT /id="VAR_006504"
FT VARIANT 198
FT /note="I -> T (in FA7D; dbSNP:rs762621913)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065386"
FT VARIANT 212
FT /note="R -> Q (in FA7D; Charlotte; dbSNP:rs868044209)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19751712,
FT ECO:0000269|PubMed:8204879"
FT /id="VAR_006505"
FT VARIANT 216
FT /note="G -> D (in FA7D; dbSNP:rs1438503836)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015138"
FT VARIANT 238
FT /note="C -> Y (in FA7D; dbSNP:rs121964928)"
FT /evidence="ECO:0000269|PubMed:8364544"
FT /id="VAR_006506"
FT VARIANT 240
FT /note="G -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19432927"
FT /id="VAR_065387"
FT VARIANT 241
FT /note="T -> N (in FA7D; dbSNP:rs1160146175)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014413"
FT VARIANT 250
FT /note="S -> F (in FA7D)"
FT /evidence="ECO:0000269|PubMed:21372693"
FT /id="VAR_065388"
FT VARIANT 251
FT /note="A -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065389"
FT VARIANT 251
FT /note="A -> T (in FA7D; dbSNP:rs1269916662)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065390"
FT VARIANT 254
FT /note="C -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065391"
FT VARIANT 254
FT /note="C -> Y (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015139"
FT VARIANT 264
FT /note="L -> P (in FA7D; dbSNP:rs753266903)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065392"
FT VARIANT 266
FT /note="A -> T (in FA7D; dbSNP:rs764807079)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015140"
FT VARIANT 272
FT /note="D -> N (in FA7D; dbSNP:rs751028917)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065393"
FT VARIANT 277
FT /note="D -> N (in FA7D; dbSNP:rs550074221)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065394"
FT VARIANT 283
FT /note="R -> W (in FA7D; dbSNP:rs779589651)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8844208"
FT /id="VAR_006507"
FT VARIANT 295
FT /note="V -> D (in dbSNP:rs6045)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013936"
FT VARIANT 298
FT /note="T -> I (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065395"
FT VARIANT 301
FT /note="H -> Q (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065396"
FT VARIANT 302
FT /note="D -> H (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247"
FT /id="VAR_014414"
FT VARIANT 302
FT /note="D -> N (in FA7D; dbSNP:rs770328850)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014415"
FT VARIANT 304
FT /note="A -> T (in FA7D; dbSNP:rs773627551)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014416"
FT VARIANT 304
FT /note="A -> V (in FA7D; Malta-II; dbSNP:rs121964931)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8883260, ECO:0000269|PubMed:9452082"
FT /id="VAR_006508"
FT VARIANT 307
FT /note="R -> C (in FA7D; dbSNP:rs147680958)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247"
FT /id="VAR_014417"
FT VARIANT 307
FT /note="R -> H (in FA7D; Mie; dbSNP:rs121964929)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:7974346"
FT /id="VAR_006509"
FT VARIANT 312
FT /note="V -> M (in FA7D; dbSNP:rs201991361)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015141"
FT VARIANT 314
FT /note="L -> V (in FA7D)"
FT /evidence="ECO:0000269|PubMed:21206266"
FT /id="VAR_065397"
FT VARIANT 321
FT /note="L -> F (in FA7D; dbSNP:rs778138366)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065398"
FT VARIANT 323
FT /note="L -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065399"
FT VARIANT 325
FT /note="E -> K (in FA7D; dbSNP:rs749760143)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:8844208"
FT /id="VAR_006510"
FT VARIANT 326
FT /note="R -> Q (in FA7D; dbSNP:rs146698837)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065400"
FT VARIANT 332
FT /note="T -> M (in FA7D; dbSNP:rs200212201)"
FT /evidence="ECO:0000269|PubMed:11129332"
FT /id="VAR_014418"
FT VARIANT 337
FT /note="R -> C (in FA7D; dbSNP:rs139372641)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065401"
FT VARIANT 341
FT /note="V -> F (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015142"
FT VARIANT 343
FT /note="G -> S (in FA7D; dbSNP:rs1250853566)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:21206266"
FT /id="VAR_065402"
FT VARIANT 344
FT /note="W -> G (in FA7D)"
FT /evidence="ECO:0000269|PubMed:26761581"
FT /id="VAR_076570"
FT VARIANT 344
FT /note="W -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065403"
FT VARIANT 345
FT /note="G -> S (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065404"
FT VARIANT 350
FT /note="R -> C (in FA7D; dbSNP:rs747876824)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065405"
FT VARIANT 352
FT /note="A -> T (in dbSNP:rs3093267)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_013122"
FT VARIANT 354
FT /note="A -> V (in FA7D; dbSNP:rs36209567)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:16292673,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:7981691"
FT /id="VAR_006511"
FT VARIANT 358
FT /note="M -> I (in FA7D; dbSNP:rs149283257)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8043443"
FT /id="VAR_006512"
FT VARIANT 358
FT /note="M -> V (in FA7D; dbSNP:rs928183869)"
FT /evidence="ECO:0000269|PubMed:8844208"
FT /id="VAR_006513"
FT VARIANT 360
FT /note="L -> P (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065406"
FT VARIANT 363
FT /note="P -> H (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065407"
FT VARIANT 363
FT /note="P -> R (in FA7D; dbSNP:rs963430078)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015143"
FT VARIANT 364
FT /note="R -> Q (in FA7D; Harrow/Padua; dbSNP:rs121964926)"
FT /evidence="ECO:0000269|PubMed:1634227,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:2070047,
FT ECO:0000269|PubMed:8043443, ECO:0000269|PubMed:8242057,
FT ECO:0000269|PubMed:8844208"
FT /id="VAR_006514"
FT VARIANT 364
FT /note="R -> W (in FA7D; dbSNP:rs750980786)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065408"
FT VARIANT 367
FT /note="T -> S (in dbSNP:rs747673406)"
FT /evidence="ECO:0000269|PubMed:7860081"
FT /id="VAR_018671"
FT VARIANT 370
FT /note="C -> F (in FA7D; dbSNP:rs121964927)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:1634227,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19751712,
FT ECO:0000269|PubMed:8043443"
FT /id="VAR_006515"
FT VARIANT 375
FT /note="R -> W (in FA7D; dbSNP:rs137919286)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065409"
FT VARIANT 384
FT /note="T -> M (in FA7D; dbSNP:rs531225271)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:19751712"
FT /id="VAR_065410"
FT VARIANT 387
FT /note="M -> T (in FA7D; dbSNP:rs1595080725)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065411"
FT VARIANT 387
FT /note="M -> V (in FA7D; dbSNP:rs1215224419)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065412"
FT VARIANT 388
FT /note="F -> S (in FA7D; reduces tissue factor binding;
FT impairs activation by factor Xa; abolishes amidolytic and
FT coagulant activities; dbSNP:rs121964938)"
FT /evidence="ECO:0000269|PubMed:18976247,
FT ECO:0000269|PubMed:8940045"
FT /id="VAR_065413"
FT VARIANT 389
FT /note="C -> G (in FA7D; dbSNP:rs121964934)"
FT /evidence="ECO:0000269|PubMed:11091194,
FT ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:21206266"
FT /id="VAR_014392"
FT VARIANT 391
FT /note="G -> C (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065414"
FT VARIANT 391
FT /note="G -> S (in FA7D; dbSNP:rs190485816)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014419"
FT VARIANT 398
FT /note="D -> E (in FA7D)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065415"
FT VARIANT 401
FT /note="K -> E (in FA7D; dbSNP:rs748979195)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065416"
FT VARIANT 402
FT /note="G -> E (in FA7D)"
FT /evidence="ECO:0000269|PubMed:8844208"
FT /id="VAR_006517"
FT VARIANT 402
FT /note="G -> R (in FA7D)"
FT /evidence="ECO:0000269|PubMed:8043443"
FT /id="VAR_006516"
FT VARIANT 403
FT /note="D -> H (in FA7D)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_015144"
FT VARIANT 404
FT /note="S -> N (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065417"
FT VARIANT 408
FT /note="H -> Q (in FA7D; dbSNP:rs121964936)"
FT /evidence="ECO:0000269|PubMed:12472587"
FT /id="VAR_065418"
FT VARIANT 408
FT /note="H -> R (in FA7D; dbSNP:rs1566910847)"
FT /evidence="ECO:0000269|PubMed:19751712"
FT /id="VAR_065419"
FT VARIANT 413
FT /note="R -> G (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065420"
FT VARIANT 413
FT /note="R -> Q (may be associated with decreased
FT susceptibility to myocardial infarction; dbSNP:rs6046)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:10984565, ECO:0000269|PubMed:16292673,
FT ECO:0000269|PubMed:8043443, ECO:0000269|PubMed:8844208,
FT ECO:0000269|Ref.6"
FT /id="VAR_006518"
FT VARIANT 414
FT /note="G -> C (in FA7D; results in severely impaired
FT protein secretion; dbSNP:rs121964937)"
FT /evidence="ECO:0000269|PubMed:14717781"
FT /id="VAR_065421"
FT VARIANT 419
FT /note="T -> M (in FA7D; dbSNP:rs121964930)"
FT /evidence="ECO:0000269|PubMed:10862079,
FT ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:8652821"
FT /id="VAR_006519"
FT VARIANT 422
FT /note="V -> F (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065422"
FT VARIANT 425
FT /note="G -> A (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065423"
FT VARIANT 425
FT /note="G -> C (in FA7D)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065424"
FT VARIANT 429
FT /note="A -> T (in FA7D; dbSNP:rs755377592)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065425"
FT VARIANT 432
FT /note="G -> D (in FA7D; dbSNP:rs1450120320)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065426"
FT VARIANT 435
FT /note="G -> E (in FA7D; dbSNP:rs756956471)"
FT /evidence="ECO:0000269|PubMed:11129332,
FT ECO:0000269|PubMed:18976247"
FT /id="VAR_014420"
FT VARIANT 437
FT /note="Y -> F (in FA7D; dbSNP:rs758213652)"
FT /evidence="ECO:0000269|PubMed:18976247"
FT /id="VAR_065427"
FT VARIANT 445
FT /note="E -> K (in dbSNP:rs3093248)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_013123"
FT MUTAGEN 112
FT /note="S->A: Complete loss of O-glycosylation and O-
FT xylosylation by POGLUT1."
FT /evidence="ECO:0000269|PubMed:21949356"
FT MUTAGEN 113
FT /note="S->A: No effect on O-glycosylation by POGLUT1.
FT Drastic decrease in O-xylosylation."
FT /evidence="ECO:0000269|PubMed:21949356"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:4YLQ"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:4YLQ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1QFK"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4YLQ"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4YLQ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2C4F"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1QFK"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5PAG"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1JBU"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2FLB"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1JBU"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5PAG"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:1DVA"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:5PAG"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4YLQ"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4YLQ"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1JBU"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5PAK"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:5PAG"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:5PAX"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5PAG"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:5PAG"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:5PAG"
SQ 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
