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Database: UniProt
Entry: P08709
LinkDB: P08709
Original site: P08709 
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   08-MAY-2019, entry version 256.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Woodbury R.G., Hart C.E., Insley M.Y., Kisiel W., Kurachi K.,
RA   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.,
RA   Hagen F.S., Murray M.J.;
RT   "Nucleotide sequence of the gene coding for human factor VII, a
RT   vitamin K-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
RT   FVII 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.,
RA   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.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   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.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   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.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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
RT   project: 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;
RP   GLU-67; GLU-74; GLU-76; GLU-79; GLU-80; GLU-85; GLU-86; GLU-89 AND
RP   GLU-95, HYDROXYLATION AT ASP-123, AND GLYCOSYLATION AT ASN-205 AND
RP   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
RT   factor 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
RT   missense 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;
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-
RT   Glc) O-glycosidically linked to a serine residue in the first
RT   epidermal growth factor-like domain of human factors VII and IX and
RT   protein Z and bovine 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;
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
RT   first 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;
RA   Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M.,
RA   Komiyama Y., 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-
RT   directed 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
RT   by 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
RT   O-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.,
RA   Konigsberg W.H., Nemreson Y., Kirchhofer D.;
RT   "The crystal structure of the complex of blood coagulation factor VIIa
RT   with 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.,
RA   Drakenberg T.;
RT   "Solution structure of the N-terminal EGF-like domain from human
RT   factor 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
RT   (115His and 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.,
RA   von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H.,
RA   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
RT   coagulation 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
RT   cleavage 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
RT   human 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
RT   an amino acid substitution of His (CAC) for Arg(247) (CGC) in the
RT   catalytic 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
RP   VARIANT 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.,
RA   Kisiel W.;
RT   "Factor VII central. A novel mutation in the catalytic domain that
RT   reduces tissue factor binding, impairs activation by factor Xa, and
RT   abolishes 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.,
RA   Yang D., Clarke B.J.;
RT   "Factor VII deficiency caused by a structural variant N57D of the
RT   first 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
RT   the signal sequence identified in a patient with factor VII
RT   deficiency.";
RL   Br. J. Haematol. 101:47-49(1998).
RN   [35]
RP   VARIANTS FA7D THR-194 AND VAL-304.
RX   PubMed=9452082;
RA   Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.;
RT   "Two new missense mutations (P134T and A244V) in the coagulation
RT   factor VII 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
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [37]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [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
RT   VII 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;
RP   SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302;
RP   THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370;
RP   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.,
RA   Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A.,
RA   Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R.,
RA   Krawczak M., Cooper D.N.;
RT   "Molecular analysis of the genotype-phenotype relationship in factor
RT   VII 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;
RP   ARG-195; GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304;
RP   CYS-307; MET-312; LYS-325; PHE-341; VAL-354; ILE-358; ARG-363;
RP   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
RT   infarction 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
RT   results in severely impaired secretion of the molecule, but not
RT   complete 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;
RP   ARG-344; 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;
RP   PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157;
RP   ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194;
RP   THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254;
RP   TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298;
RP   GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307;
RP   MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343;
RP   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;
RP   SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413;
RP   MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND
RP   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
RT   Europe 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.,
RA   Kapelushnik J.;
RT   "Familial factor VII deficiency with foetal and neonatal fatal
RT   cerebral haemorrhage associated with homozygosis to Gly180Arg
RT   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.
CC       Serine protease that circulates in the blood in a zymogen form.
CC       Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
CC       factor IXa, or thrombin by minor proteolysis. In the presence of
CC       tissue factor and calcium ions, factor VIIa then converts factor X
CC       to factor Xa by limited proteolysis. Factor VIIa will also convert
CC       factor IX to factor IXa in the presence of tissue factor and
CC       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
CC       a disulfide bond. {ECO:0000269|PubMed:8598903,
CC       ECO:0000269|PubMed:9925787}.
CC   -!- INTERACTION:
CC       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
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000269|PubMed:3264725}.
CC   -!- PTM: O- and N-glycosylated. N-glycosylation at Asn-205 occurs
CC       cotranslationally and is mediated by STT3A-containing complexes,
CC       while glycosylation at Asn-382 is post-translational and is
CC       mediated STT3B-containing complexes before folding. O-fucosylated
CC       by POFUT1 on a conserved serine or threonine residue found in the
CC       consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and
CC       C3 are the second and third conserved cysteines.
CC       {ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:19167329,
CC       ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:3264725,
CC       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
CC       very severe, with the early occurrence of intracerebral
CC       hemorrhages or repeated hemarthroses, or, in contrast, moderate
CC       with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or
CC       hemorrhages provoked by a surgical intervention. Finally, numerous
CC       subjects are completely asymptomatic despite very low factor VII
CC       levels. {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 mutations affecting the gene represented in
CC       this entry.
CC   -!- PHARMACEUTICAL: Available under the names Niastase or Novoseven
CC       (Novo Nordisk). Used for the treatment of bleeding episodes in
CC       hemophilia A or B patients with antibodies to coagulation factors
CC       VIII or IX.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-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   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F7";
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; 1NL8; Model; -; H=213-466, M=61-202.
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; 1NL8; -.
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   SMR; P08709; -.
DR   BioGrid; 108453; 19.
DR   ComplexPortal; CPX-2808; Factor VII - TF complex.
DR   CORUM; P08709; -.
DR   DIP; DIP-6135N; -.
DR   ELM; P08709; -.
DR   IntAct; P08709; 10.
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; DB00100; Coagulation Factor IX (Recombinant).
DR   DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB04767; N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID.
DR   GuidetoPHARMACOLOGY; 2363; -.
DR   MEROPS; S01.215; -.
DR   GlyConnect; 98; -.
DR   iPTMnet; P08709; -.
DR   PhosphoSitePlus; P08709; -.
DR   UniCarbKB; P08709; -.
DR   BioMuta; F7; -.
DR   DMDM; 119766; -.
DR   jPOST; P08709; -.
DR   MaxQB; P08709; -.
DR   PaxDb; P08709; -.
DR   PeptideAtlas; P08709; -.
DR   PRIDE; P08709; -.
DR   ProteomicsDB; 52160; -.
DR   ProteomicsDB; 52161; -. [P08709-2]
DR   Ensembl; ENST00000346342; ENSP00000329546; ENSG00000057593. [P08709-2]
DR   Ensembl; ENST00000375581; ENSP00000364731; ENSG00000057593. [P08709-1]
DR   GeneID; 2155; -.
DR   KEGG; hsa:2155; -.
DR   UCSC; uc001vsv.5; human. [P08709-1]
DR   CTD; 2155; -.
DR   DisGeNET; 2155; -.
DR   GeneCards; F7; -.
DR   HGNC; HGNC:3544; F7.
DR   HPA; HPA004826; -.
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   eggNOG; ENOG410IIMB; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000154474; -.
DR   InParanoid; P08709; -.
DR   KO; K01320; -.
DR   OMA; SKDACKG; -.
DR   OrthoDB; 265965at2759; -.
DR   PhylomeDB; P08709; -.
DR   TreeFam; TF327329; -.
DR   BRENDA; 3.4.21.21; 2681.
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   EvolutionaryTrace; P08709; -.
DR   GeneWiki; Factor_VII; -.
DR   GenomeRNAi; 2155; -.
DR   PMAP-CutDB; P08709; -.
DR   PRO; PR:P08709; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000057593; Expressed in 127 organ(s), highest expression level in right lobe of liver.
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:0005886; C:plasma membrane; TAS:Reactome.
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: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; TAS:Reactome.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
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:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; 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   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; 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; 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; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW   Hydrolase; Hydroxylation; Pharmaceutical; Polymorphism; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     60       {ECO:0000269|PubMed:3264725}.
FT                                /FTId=PRO_0000027729.
FT   CHAIN        61    212       Factor VII light chain.
FT                                /FTId=PRO_0000027730.
FT   CHAIN       213    466       Factor VII heavy chain.
FT                                /FTId=PRO_0000027731.
FT   DOMAIN       61    105       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN      106    142       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      147    188       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      213    452       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    253    253       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    302    302       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    404    404       Charge relay system. {ECO:0000250}.
FT   BINDING     398    398       Substrate. {ECO:0000250}.
FT   SITE        113    113       Important for S-112 for O-xylosylation.
FT   SITE        212    213       Cleavage; by factor Xa, factor XIIa,
FT                                factor IXa, or thrombin.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      67     67       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      74     74       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      76     76       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      79     79       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725}.
FT   MOD_RES      80     80       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      85     85       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      86     86       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      89     89       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES      95     95       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3264725,
FT                                ECO:0000269|PubMed:3486420}.
FT   MOD_RES     123    123       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000269|PubMed:3264725}.
FT   CARBOHYD    112    112       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000269|PubMed:1904059,
FT                                ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:21949356,
FT                                ECO:0000269|PubMed:2511201}.
FT                                /FTId=CAR_000007.
FT   CARBOHYD    112    112       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000269|PubMed:1904059,
FT                                ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:21949356,
FT                                ECO:0000269|PubMed:2511201}.
FT   CARBOHYD    120    120       O-linked (Fuc) serine.
FT                                {ECO:0000269|PubMed:1904059,
FT                                ECO:0000269|PubMed:9023546}.
FT                                /FTId=CAR_000180.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19167329,
FT                                ECO:0000269|PubMed:3264725}.
FT   CARBOHYD    382    382       N-linked (GlcNAc...) asparagine.
FT                                {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       Missing (in isoform B).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:3486420}.
FT                                /FTId=VSP_005387.
FT   VARIANT      13     13       L -> P (in FA7D; Morioka;
FT                                dbSNP:rs387906507).
FT                                {ECO:0000269|PubMed:9576180}.
FT                                /FTId=VAR_014391.
FT   VARIANT      59     59       R -> RR (in FA7D).
FT                                {ECO:0000269|PubMed:21206266}.
FT                                /FTId=VAR_065369.
FT   VARIANT      64     64       F -> L (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015135.
FT   VARIANT      73     73       L -> Q (in FA7D; dbSNP:rs45572939).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014405.
FT   VARIANT      79     79       E -> Q (in FA7D).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014406.
FT   VARIANT      82     82       C -> F (in FA7D; dbSNP:rs1448296564).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065370.
FT   VARIANT      82     82       C -> R (in FA7D; dbSNP:rs745374448).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065371.
FT   VARIANT      84     84       Missing (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065372.
FT   VARIANT      85     85       E -> K (in FA7D; dbSNP:rs121964935).
FT                                {ECO:0000269|PubMed:12472587}.
FT                                /FTId=VAR_065373.
FT   VARIANT      88     88       R -> G (in FA7D; dbSNP:rs776354144).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065374.
FT   VARIANT      88     88       R -> P (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065375.
FT   VARIANT     117    117       N -> D (in FA7D; exhibits no procoagulant
FT                                activity and is unable to bind tissue
FT                                factor; dbSNP:rs121964932).
FT                                {ECO:0000269|PubMed:9414278}.
FT                                /FTId=VAR_065376.
FT   VARIANT     120    120       S -> P (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015136.
FT   VARIANT     121    121       C -> F (in FA7D).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014407.
FT   VARIANT     125    125       L -> P (in FA7D).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014408.
FT   VARIANT     128    128       Y -> C (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014409.
FT   VARIANT     138    138       G -> D (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065377.
FT   VARIANT     139    139       R -> K (in FA7D).
FT                                /FTId=VAR_006497.
FT   VARIANT     139    139       R -> Q (in FA7D; Charlotte;
FT                                dbSNP:rs150525536).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8204879,
FT                                ECO:0000269|PubMed:8242057}.
FT                                /FTId=VAR_006498.
FT   VARIANT     139    139       R -> W (in FA7D; dbSNP:rs776796178).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:8242057}.
FT                                /FTId=VAR_006499.
FT   VARIANT     151    151       C -> S (in FA7D).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014410.
FT   VARIANT     154    154       E -> K (in FA7D; dbSNP:rs146795869).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015137.
FT   VARIANT     156    156       G -> S (in FA7D; dbSNP:rs563972504).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065378.
FT   VARIANT     157    157       G -> C (in FA7D).
FT                                /FTId=VAR_006501.
FT   VARIANT     157    157       G -> S (in FA7D; dbSNP:rs763458490).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_006500.
FT   VARIANT     157    157       G -> V (in FA7D; dbSNP:rs771335282).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014411.
FT   VARIANT     160    160       Q -> R (in FA7D; dbSNP:rs200016360).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8242057}.
FT                                /FTId=VAR_006502.
FT   VARIANT     171    171       S -> F (in FA7D; dbSNP:rs143855920).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065379.
FT   VARIANT     177    177       G -> R (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065380.
FT   VARIANT     181    181       L -> P (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065381.
FT   VARIANT     183    183       D -> N (in FA7D; dbSNP:rs1258691292).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065382.
FT   VARIANT     186    186       S -> F (in FA7D; dbSNP:rs764971156).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065383.
FT   VARIANT     189    189       P -> S (in FA7D; dbSNP:rs1479693459).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065384.
FT   VARIANT     194    194       P -> L (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065385.
FT   VARIANT     194    194       P -> T (in FA7D; Malta-I;
FT                                dbSNP:rs1234759020).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:9452082}.
FT                                /FTId=VAR_006503.
FT   VARIANT     195    195       C -> R (in FA7D; dbSNP:rs372577568).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014412.
FT   VARIANT     197    197       K -> E (in FA7D; dbSNP:rs1250204261).
FT                                {ECO:0000269|PubMed:8242057}.
FT                                /FTId=VAR_006504.
FT   VARIANT     198    198       I -> T (in FA7D; dbSNP:rs762621913).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065386.
FT   VARIANT     212    212       R -> Q (in FA7D; Charlotte;
FT                                dbSNP:rs868044209).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:19751712,
FT                                ECO:0000269|PubMed:8204879}.
FT                                /FTId=VAR_006505.
FT   VARIANT     216    216       G -> D (in FA7D; dbSNP:rs1438503836).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015138.
FT   VARIANT     238    238       C -> Y (in FA7D; dbSNP:rs121964928).
FT                                {ECO:0000269|PubMed:8364544}.
FT                                /FTId=VAR_006506.
FT   VARIANT     240    240       G -> R (in FA7D).
FT                                {ECO:0000269|PubMed:19432927}.
FT                                /FTId=VAR_065387.
FT   VARIANT     241    241       T -> N (in FA7D; dbSNP:rs1160146175).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014413.
FT   VARIANT     250    250       S -> F (in FA7D).
FT                                {ECO:0000269|PubMed:21372693}.
FT                                /FTId=VAR_065388.
FT   VARIANT     251    251       A -> P (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065389.
FT   VARIANT     251    251       A -> T (in FA7D; dbSNP:rs1269916662).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065390.
FT   VARIANT     254    254       C -> R (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065391.
FT   VARIANT     254    254       C -> Y (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015139.
FT   VARIANT     264    264       L -> P (in FA7D; dbSNP:rs753266903).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065392.
FT   VARIANT     266    266       A -> T (in FA7D; dbSNP:rs764807079).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015140.
FT   VARIANT     272    272       D -> N (in FA7D; dbSNP:rs751028917).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065393.
FT   VARIANT     277    277       D -> N (in FA7D; dbSNP:rs550074221).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065394.
FT   VARIANT     283    283       R -> W (in FA7D; dbSNP:rs779589651).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8844208}.
FT                                /FTId=VAR_006507.
FT   VARIANT     295    295       V -> D (in dbSNP:rs6045).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013936.
FT   VARIANT     298    298       T -> I (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065395.
FT   VARIANT     301    301       H -> Q (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065396.
FT   VARIANT     302    302       D -> H (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014414.
FT   VARIANT     302    302       D -> N (in FA7D; dbSNP:rs770328850).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014415.
FT   VARIANT     304    304       A -> T (in FA7D; dbSNP:rs773627551).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014416.
FT   VARIANT     304    304       A -> V (in FA7D; Malta-II;
FT                                dbSNP:rs121964931).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8883260,
FT                                ECO:0000269|PubMed:9452082}.
FT                                /FTId=VAR_006508.
FT   VARIANT     307    307       R -> C (in FA7D; dbSNP:rs147680958).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014417.
FT   VARIANT     307    307       R -> H (in FA7D; Mie; dbSNP:rs121964929).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:7974346}.
FT                                /FTId=VAR_006509.
FT   VARIANT     312    312       V -> M (in FA7D; dbSNP:rs201991361).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015141.
FT   VARIANT     314    314       L -> V (in FA7D).
FT                                {ECO:0000269|PubMed:21206266}.
FT                                /FTId=VAR_065397.
FT   VARIANT     321    321       L -> F (in FA7D; dbSNP:rs778138366).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065398.
FT   VARIANT     323    323       L -> R (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065399.
FT   VARIANT     325    325       E -> K (in FA7D; dbSNP:rs749760143).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8844208}.
FT                                /FTId=VAR_006510.
FT   VARIANT     326    326       R -> Q (in FA7D; dbSNP:rs146698837).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065400.
FT   VARIANT     332    332       T -> M (in FA7D; dbSNP:rs200212201).
FT                                {ECO:0000269|PubMed:11129332}.
FT                                /FTId=VAR_014418.
FT   VARIANT     337    337       R -> C (in FA7D; dbSNP:rs139372641).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065401.
FT   VARIANT     341    341       V -> F (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015142.
FT   VARIANT     343    343       G -> S (in FA7D; dbSNP:rs1250853566).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:21206266}.
FT                                /FTId=VAR_065402.
FT   VARIANT     344    344       W -> G (in FA7D).
FT                                {ECO:0000269|PubMed:26761581}.
FT                                /FTId=VAR_076570.
FT   VARIANT     344    344       W -> R (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065403.
FT   VARIANT     345    345       G -> S (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065404.
FT   VARIANT     350    350       R -> C (in FA7D; dbSNP:rs747876824).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065405.
FT   VARIANT     352    352       A -> T (in dbSNP:rs3093267).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_013122.
FT   VARIANT     354    354       A -> V (in FA7D; dbSNP:rs36209567).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:16292673,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:7981691}.
FT                                /FTId=VAR_006511.
FT   VARIANT     358    358       M -> I (in FA7D; dbSNP:rs149283257).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8043443}.
FT                                /FTId=VAR_006512.
FT   VARIANT     358    358       M -> V (in FA7D; dbSNP:rs928183869).
FT                                {ECO:0000269|PubMed:8844208}.
FT                                /FTId=VAR_006513.
FT   VARIANT     360    360       L -> P (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065406.
FT   VARIANT     363    363       P -> H (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065407.
FT   VARIANT     363    363       P -> R (in FA7D; dbSNP:rs963430078).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015143.
FT   VARIANT     364    364       R -> Q (in FA7D; Harrow/Padua;
FT                                dbSNP:rs121964926).
FT                                {ECO:0000269|PubMed:1634227,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:2070047,
FT                                ECO:0000269|PubMed:8043443,
FT                                ECO:0000269|PubMed:8242057,
FT                                ECO:0000269|PubMed:8844208}.
FT                                /FTId=VAR_006514.
FT   VARIANT     364    364       R -> W (in FA7D; dbSNP:rs750980786).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065408.
FT   VARIANT     367    367       T -> S (in dbSNP:rs747673406).
FT                                {ECO:0000269|PubMed:7860081}.
FT                                /FTId=VAR_018671.
FT   VARIANT     370    370       C -> F (in FA7D; dbSNP:rs121964927).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:1634227,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:19751712,
FT                                ECO:0000269|PubMed:8043443}.
FT                                /FTId=VAR_006515.
FT   VARIANT     375    375       R -> W (in FA7D; dbSNP:rs137919286).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065409.
FT   VARIANT     384    384       T -> M (in FA7D; dbSNP:rs531225271).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065410.
FT   VARIANT     387    387       M -> T (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065411.
FT   VARIANT     387    387       M -> V (in FA7D; dbSNP:rs1215224419).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065412.
FT   VARIANT     388    388       F -> S (in FA7D; reduces tissue factor
FT                                binding; impairs activation by factor Xa;
FT                                abolishes amidolytic and coagulant
FT                                activities; dbSNP:rs121964938).
FT                                {ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8940045}.
FT                                /FTId=VAR_065413.
FT   VARIANT     389    389       C -> G (in FA7D; dbSNP:rs121964934).
FT                                {ECO:0000269|PubMed:11091194,
FT                                ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:21206266}.
FT                                /FTId=VAR_014392.
FT   VARIANT     391    391       G -> C (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065414.
FT   VARIANT     391    391       G -> S (in FA7D; dbSNP:rs190485816).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014419.
FT   VARIANT     398    398       D -> E (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065415.
FT   VARIANT     401    401       K -> E (in FA7D; dbSNP:rs748979195).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065416.
FT   VARIANT     402    402       G -> E (in FA7D).
FT                                {ECO:0000269|PubMed:8844208}.
FT                                /FTId=VAR_006517.
FT   VARIANT     402    402       G -> R (in FA7D).
FT                                {ECO:0000269|PubMed:8043443}.
FT                                /FTId=VAR_006516.
FT   VARIANT     403    403       D -> H (in FA7D).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_015144.
FT   VARIANT     404    404       S -> N (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065417.
FT   VARIANT     408    408       H -> Q (in FA7D; dbSNP:rs121964936).
FT                                {ECO:0000269|PubMed:12472587}.
FT                                /FTId=VAR_065418.
FT   VARIANT     408    408       H -> R (in FA7D).
FT                                {ECO:0000269|PubMed:19751712}.
FT                                /FTId=VAR_065419.
FT   VARIANT     413    413       R -> G (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065420.
FT   VARIANT     413    413       R -> Q (may be associated with decreased
FT                                susceptibility to myocardial infarction;
FT                                dbSNP:rs6046).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:10984565,
FT                                ECO:0000269|PubMed:16292673,
FT                                ECO:0000269|PubMed:8043443,
FT                                ECO:0000269|PubMed:8844208,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_006518.
FT   VARIANT     414    414       G -> C (in FA7D; results in severely
FT                                impaired protein secretion;
FT                                dbSNP:rs121964937).
FT                                {ECO:0000269|PubMed:14717781}.
FT                                /FTId=VAR_065421.
FT   VARIANT     419    419       T -> M (in FA7D; dbSNP:rs121964930).
FT                                {ECO:0000269|PubMed:10862079,
FT                                ECO:0000269|PubMed:18976247,
FT                                ECO:0000269|PubMed:8652821}.
FT                                /FTId=VAR_006519.
FT   VARIANT     422    422       V -> F (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065422.
FT   VARIANT     425    425       G -> A (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065423.
FT   VARIANT     425    425       G -> C (in FA7D).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065424.
FT   VARIANT     429    429       A -> T (in FA7D; dbSNP:rs755377592).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065425.
FT   VARIANT     432    432       G -> D (in FA7D; dbSNP:rs1450120320).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065426.
FT   VARIANT     435    435       G -> E (in FA7D; dbSNP:rs756956471).
FT                                {ECO:0000269|PubMed:11129332,
FT                                ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_014420.
FT   VARIANT     437    437       Y -> F (in FA7D; dbSNP:rs758213652).
FT                                {ECO:0000269|PubMed:18976247}.
FT                                /FTId=VAR_065427.
FT   VARIANT     445    445       E -> K (in dbSNP:rs3093248).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_013123.
FT   MUTAGEN     112    112       S->A: Complete loss of O-glycosylation
FT                                and O-xylosylation by POGLUT1.
FT                                {ECO:0000269|PubMed:21949356}.
FT   MUTAGEN     113    113       S->A: No effect on O-glycosylation by
FT                                POGLUT1. Drastic decrease in O-
FT                                xylosylation.
FT                                {ECO:0000269|PubMed:21949356}.
FT   HELIX        66     68       {ECO:0000244|PDB:4YLQ}.
FT   HELIX        73     77       {ECO:0000244|PDB:4YLQ}.
FT   HELIX        84     91       {ECO:0000244|PDB:4YLQ}.
FT   HELIX        94    104       {ECO:0000244|PDB:4YLQ}.
FT   TURN        109    112       {ECO:0000244|PDB:4YLQ}.
FT   TURN        116    118       {ECO:0000244|PDB:1QFK}.
FT   STRAND      120    124       {ECO:0000244|PDB:4YLQ}.
FT   STRAND      127    131       {ECO:0000244|PDB:4YLQ}.
FT   STRAND      136    138       {ECO:0000244|PDB:4YLQ}.
FT   HELIX       145    147       {ECO:0000244|PDB:2C4F}.
FT   STRAND      148    150       {ECO:0000244|PDB:1QFK}.
FT   TURN        151    153       {ECO:0000244|PDB:4YLQ}.
FT   HELIX       154    157       {ECO:0000244|PDB:5PAG}.
FT   STRAND      159    165       {ECO:0000244|PDB:5PAG}.
FT   TURN        166    168       {ECO:0000244|PDB:5PAG}.
FT   STRAND      169    173       {ECO:0000244|PDB:5PAG}.
FT   STRAND      178    180       {ECO:0000244|PDB:5PAG}.
FT   STRAND      187    189       {ECO:0000244|PDB:5PAG}.
FT   STRAND      191    193       {ECO:0000244|PDB:5PAG}.
FT   HELIX       199    205       {ECO:0000244|PDB:5PAG}.
FT   HELIX       220    222       {ECO:0000244|PDB:1JBU}.
FT   STRAND      227    232       {ECO:0000244|PDB:5PAG}.
FT   STRAND      235    242       {ECO:0000244|PDB:5PAG}.
FT   STRAND      244    250       {ECO:0000244|PDB:5PAG}.
FT   HELIX       252    255       {ECO:0000244|PDB:5PAG}.
FT   HELIX       261    263       {ECO:0000244|PDB:5PAG}.
FT   STRAND      264    269       {ECO:0000244|PDB:5PAG}.
FT   STRAND      272    274       {ECO:0000244|PDB:2FLB}.
FT   STRAND      281    291       {ECO:0000244|PDB:5PAG}.
FT   STRAND      298    301       {ECO:0000244|PDB:1JBU}.
FT   STRAND      304    310       {ECO:0000244|PDB:5PAG}.
FT   HELIX       326    331       {ECO:0000244|PDB:5PAG}.
FT   HELIX       333    335       {ECO:0000244|PDB:5PAG}.
FT   STRAND      338    344       {ECO:0000244|PDB:5PAG}.
FT   STRAND      346    348       {ECO:0000244|PDB:5PAG}.
FT   TURN        352    355       {ECO:0000244|PDB:1DVA}.
FT   STRAND      358    365       {ECO:0000244|PDB:5PAG}.
FT   HELIX       367    373       {ECO:0000244|PDB:5PAG}.
FT   TURN        376    378       {ECO:0000244|PDB:4YLQ}.
FT   TURN        380    382       {ECO:0000244|PDB:4YLQ}.
FT   HELIX       383    386       {ECO:0000244|PDB:1JBU}.
FT   STRAND      387    391       {ECO:0000244|PDB:5PAG}.
FT   STRAND      393    398       {ECO:0000244|PDB:5PAG}.
FT   HELIX       401    403       {ECO:0000244|PDB:5PAK}.
FT   STRAND      407    412       {ECO:0000244|PDB:5PAG}.
FT   STRAND      415    422       {ECO:0000244|PDB:5PAG}.
FT   TURN        427    429       {ECO:0000244|PDB:5PAX}.
FT   STRAND      435    439       {ECO:0000244|PDB:5PAG}.
FT   HELIX       440    443       {ECO:0000244|PDB:5PAG}.
FT   HELIX       444    451       {ECO:0000244|PDB:5PAG}.
FT   STRAND      457    463       {ECO:0000244|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
//
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