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 24-JAN-2024, entry version 282. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 1 O-Fuc glycan (1 site), 2 O-Glc glycans (1 site), 1 O-Linked glycan (1 site). DR GlyCosmos; P08709; 4 sites, 13 glycans. 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; 9606-ENSP00000364731; -. DR PeptideAtlas; P08709; -. DR ProteomicsDB; 52160; -. [P08709-1] DR ProteomicsDB; 52161; -. [P08709-2] DR ABCD; P08709; 1 sequenced antibody. DR Antibodypedia; 11679; 736 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 AGR; HGNC:3544; -. 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; QGRNCET; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P08709; -. DR TreeFam; TF327329; -. DR BioCyc; MetaCyc:HS00709-MONOMER; -. 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; 16 hits in 1160 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 125 other cell types or tissues. DR ExpressionAtlas; P08709; baseline and differential. 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: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:0032008; P:positive regulation of TOR 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; cd00054; EGF_CA; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. 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; 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; COAGULATION FACTOR; 1. DR PANTHER; PTHR24278:SF26; COAGULATION FACTOR VII; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001143; Factor_X; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00010; EGFBLOOD. 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; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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. DR Genevisible; P08709; HS. 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 FT O-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 //