ID FA5_HUMAN Reviewed; 2224 AA. AC P12259; A8K6E8; Q14285; Q2EHR5; Q5R346; Q5R347; Q6UPU6; Q8WWQ6; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 27-MAR-2024, entry version 252. DE RecName: Full=Coagulation factor V; DE AltName: Full=Activated protein C cofactor; DE AltName: Full=Proaccelerin, labile factor; DE Contains: DE RecName: Full=Coagulation factor V heavy chain; DE Contains: DE RecName: Full=Coagulation factor V light chain; DE Flags: Precursor; GN Name=F5; 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], PROTEOLYTIC CLEAVAGE AT ARG-737; ARG-1046 AND RP ARG-1573 BY THROMBIN, AND VARIANTS ARG-858; ARG-865; GLU-925; PHE-1397 AND RP VAL-1764. RX PubMed=3110773; DOI=10.1073/pnas.84.14.4846; RA Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A., Hewick R.M., RA Kaufman R.J., Mann K.G.; RT "Complete cDNA and derived amino acid sequence of human factor V."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1567832; DOI=10.1021/bi00130a007; RA Cripe L.D., Moore K.D., Kane W.H.; RT "Structure of the gene for human coagulation factor V."; RL Biochemistry 31:3777-3785(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THPH2 GLN-534, AND VARIANTS RP SER-15; HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865; RP SER-915; GLU-925; SER-969; LEU-980; GLN-1146; ILE-1285; SER-1404; ALA-1530 RP AND THR-2148. RG SeattleSNPs variation discovery resource; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THPH2 GLN-534. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1030, AND VARIANT LYS-513. RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1600, AND VARIANTS ARG-858; ARG-865; RP GLU-925 AND ILE-1285. RX PubMed=2827731; DOI=10.1021/bi00394a033; RA Kane W.H., Ichinose A., Hagen F.S., Davie E.W.; RT "Cloning of cDNAs coding for the heavy chain region and connecting region RT of human factor V, a blood coagulation factor with four types of internal RT repeats."; RL Biochemistry 26:6508-6514(1987). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-1598. RA Kostka H.; RT "Human coagulation factor V, exon 13, missense mutation Asn713Ser."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 660-1598, AND VARIANTS ARG-858; ARG-865; RP GLU-925 AND PHE-1397. RX PubMed=11758222; RA Xie F., Cheng F., Zhu X.; RT "Studies on hereditary deficiency of coagulation factor V."; RL Zhonghua Xue Ye Xue Za Zhi 22:453-456(2001). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1215 AND 1315-2224. RX PubMed=3092220; DOI=10.1073/pnas.83.18.6800; RA Kane W.H., Davie E.W.; RT "Cloning of a cDNA coding for human factor V, a blood coagulation factor RT homologous to factor VIII and ceruloplasmin."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6800-6804(1986). RN [10] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=8454869; RA Shen N.L.L., Fan S.-T., Pyati J., Graff R., Lapolla R.J., Edgington T.S.; RT "The serine protease cofactor factor V is synthesized by lymphocytes."; RL J. Immunol. 150:2992-3001(1993). RN [11] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583; RA Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.; RT "Mechanism of inhibition of activated protein C by protein C inhibitor."; RL J. Biochem. 95:187-195(1984). RN [12] RP COPPER-BINDING. RX PubMed=6490642; DOI=10.1016/s0021-9258(18)90637-x; RA Mann K.G., Lawler C.M., Vehar G.A., Church W.R.; RT "Coagulation Factor V contains copper ion."; RL J. Biol. Chem. 259:12949-12951(1984). RN [13] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=2844223; DOI=10.1021/bi00412a005; RA Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., RA Bouma B.N.; RT "Inactivation of human plasma kallikrein and factor XIa by protein C RT inhibitor."; RL Biochemistry 27:4231-4237(1988). RN [14] RP SULFATION. RX PubMed=8204629; DOI=10.1021/bi00188a026; RA Pittman D.D., Tomkinson K.N., Michnick D., Selighsohn U., Kaufman R.J.; RT "Posttranslational sulfation of factor V is required for efficient thrombin RT cleavage and activation and for full procoagulant activity."; RL Biochemistry 33:6952-6959(1994). RN [15] RP SULFATION. RX PubMed=2168225; RA Hortin G.L.; RT "Sulfation of tyrosine residues in coagulation factor V."; RL Blood 76:946-952(1990). RN [16] RP PROTEOLYTIC CLEAVAGE AT ARG-334; ARG-534; ARG-707 AND LYS-1022 BY ACTIVATED RP PROTEIN C. RX PubMed=7989361; DOI=10.1016/s0021-9258(18)31776-9; RA Kalafatis M., Rand M.D., Mann K.G.; RT "The mechanism of inactivation of human factor V and human factor Va by RT activated protein C."; RL J. Biol. Chem. 269:31869-31880(1994). RN [17] RP HETERODIMER WITH SERPINA5. RX PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x; RA Kise H., Nishioka J., Kawamura J., Suzuki K.; RT "Characterization of semenogelin II and its molecular interaction with RT prostate-specific antigen and protein C inhibitor."; RL Eur. J. Biochem. 238:88-96(1996). RN [18] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=9556620; DOI=10.1074/jbc.273.18.11281; RA Nishioka J., Ning M., Hayashi T., Suzuki K.; RT "Protein C inhibitor secreted from activated platelets efficiently inhibits RT activated protein C on phosphatidylethanolamine of platelet membrane and RT microvesicles."; RL J. Biol. Chem. 273:11281-11287(1998). RN [19] RP INVOLVEMENT IN RPRGL1 SUSCEPTIBILITY. RX PubMed=11018168; DOI=10.1056/nejm200010053431405; RA Martinelli I., Taioli E., Cetin I., Marinoni A., Gerosa S., Villa M.V., RA Bozzo M., Mannucci P.M.; RT "Mutations in coagulation factors in women with unexplained late fetal RT loss."; RL N. Engl. J. Med. 343:1015-1018(2000). RN [20] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=15140131; DOI=10.1111/j.1538-7836.2004.00733.x; RA Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C., RA Ido M., Suzuki K.; RT "Characterization of a novel human protein C inhibitor (PCI) gene RT transgenic mouse useful for studying the role of PCI in physiological and RT pathological conditions."; RL J. Thromb. Haemost. 2:949-961(2004). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-460; ASN-821; ASN-977 RP AND ASN-1559. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-640, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [25] RP PHOSPHORYLATION AT SER-859. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2065-2224. RX PubMed=10586886; DOI=10.1038/46594; RA Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W., RA Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H., RA Fuentes-Prior P.; RT "Crystal structures of the membrane-binding C2 domain of human coagulation RT factor V."; RL Nature 402:434-439(1999). RN [27] RP VARIANT VAL-1764. RX PubMed=7874144; RA Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A.; RT "A polymorphism in the human coagulation factor V gene."; RL Hum. Mol. Genet. 3:2085-2085(1994). RN [28] RP VARIANT THPH2 GLN-534. RX PubMed=8164741; DOI=10.1038/369064a0; RA Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J., RA de Ronde H., van der Velden P.A., Reitsma P.H.; RT "Mutation in blood coagulation factor V associated with resistance to RT activated protein C."; RL Nature 369:64-67(1994). RN [29] RP VARIANTS ILE-1285 AND ARG-1327. RX PubMed=8713778; RA Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E., RA Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G., RA Bernardi F.; RT "Detection of new polymorphic markers in the factor V gene: association RT with factor V levels in plasma."; RL Thromb. Haemost. 75:45-48(1996). RN [30] RP ASSOCIATION OF VARIANT LEIDEN GLN-534 WITH SUSCEPTIBILITY TO BUDD-CHIARI RP SYNDROME. RX PubMed=9245936; DOI=10.1136/gut.40.6.798; RA Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T.; RT "Prevalence of the factor V Leiden mutation in hepatic and portal vein RT thrombosis."; RL Gut 40:798-800(1997). RN [31] RP VARIANT HONG KONG GLY-334, AND VARIANT LYS-513. RX PubMed=9454741; RA Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R.; RT "A novel mutation of Arg306 of factor V gene in Hong Kong Chinese."; RL Blood 91:1135-1139(1998). RN [32] RP VARIANT THPH2 THR-334. RX PubMed=9454742; RA Williamson D., Brown K., Luddington R., Baglin C., Baglin T.; RT "Factor V Cambridge: a new mutation (Arg306-to-Thr) associated with RT resistance to activated protein C."; RL Blood 91:1140-1144(1998). RN [33] RP VARIANT HONG KONG GLY-334. RX PubMed=9746807; RA Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W.; RT "Clinical significance of Arg306 mutations of factor V gene."; RL Blood 92:2599-2600(1998). RN [34] RP VARIANT THPH2 GLN-534, AND VARIANTS HIS-107; THR-413; LYS-513; SER-809; RP THR-817; ARG-858; ARG-865; GLU-925; GLN-1146; ALA-1530; SER-1685; VAL-1749; RP VAL-1764; ILE-1820 AND GLY-2222. 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 [35] 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 [36] RP VARIANT FA5D CYS-1730, VARIANT THPH2 GLN-534, AND VARIANT ARG-1327. RX PubMed=10942390; RA Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D., Girelli D., RA Girolami A., Bernardi F.; RT "Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT 20210G/A) RT affecting the prothrombinase complex in a thrombophilic family."; RL Blood 96:1443-1448(2000). RN [37] RP VARIANTS THPH2 ARG-613 AND CYS-1730. RX PubMed=11435304; DOI=10.1182/blood.v98.2.358; RA van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G., RA van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W.; RT "Five novel mutations in the gene for human blood coagulation factor V RT associated with type I factor V deficiency."; RL Blood 98:358-367(2001). RN [38] RP VARIANT THPH2 HIS-2102. RX PubMed=11858490; RA Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C., Zehnder J.L.; RT "Novel factor V C2-domain mutation (R2074H) in two families with factor V RT deficiency and bleeding."; RL Thromb. Haemost. 87:294-299(2002). RN [39] RP VARIANT FA5D CYS-2102, AND CHARACTERIZATION OF VARIANT FA5D CYS-2102. RX PubMed=12393490; DOI=10.1182/blood-2002-06-1928; RA Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F., RA Santagostino E., Mannucci P.M., Tenchini M.L.; RT "Arg2074Cys missense mutation in the C2 domain of factor V causing RT moderately severe factor V deficiency: molecular characterization by RT expression of the recombinant protein."; RL Blood 101:173-177(2003). RN [40] RP VARIANT THPH2 THR-387. RX PubMed=14617013; DOI=10.1046/j.1365-2141.2003.04624.x; RA Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M., Norstrom E.A., RA Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B.; RT "Factor V I359T: a novel mutation associated with thrombosis and resistance RT to activated protein C."; RL Br. J. Haematol. 123:496-501(2003). RN [41] RP ASSOCIATION OF VARIANT GLN-534 WITH SUSCEPTIBILITY TO ISCHSTR. RX PubMed=15534175; DOI=10.1001/archneur.61.11.1652; RA Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.; RT "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes RT involving approximately 18,000 cases and 58,000 controls."; RL Arch. Neurol. 61:1652-1661(2004). RN [42] RP CHARACTERIZATION OF VARIANT THPH2 THR-387. RX PubMed=14695241; DOI=10.1182/blood-2003-06-2092; RA Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B., Mumford A., RA McVey J.H., Tuddenham E.G.D., Dahlbaeck B.; RT "Functional characterization of factor V-Ile359Thr: a novel mutation RT associated with thrombosis."; RL Blood 103:3381-3387(2004). RN [43] RP VARIANT [LARGE SCALE ANALYSIS] ALA-775. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Central regulator of hemostasis. It serves as a critical CC cofactor for the prothrombinase activity of factor Xa that results in CC the activation of prothrombin to thrombin. CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. CC {ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:2844223, CC ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:9556620}. CC -!- SUBUNIT: Factor Va, the activated form of factor V, is composed of a CC heavy chain and a light chain, non-covalently bound. The interaction CC between the two chains is calcium-dependent. Forms heterodimer with CC SERPINA5. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA CC repeats. CC -!- PTM: Thrombin activates factor V proteolytically to the active CC cofactor, factor Va (formation of a heavy chain at the N-terminus and a CC light chain at the C-terminus). CC -!- PTM: Sulfation is required for efficient thrombin cleavage and CC activation and for full procoagulant activity. CC {ECO:0000269|PubMed:2168225, ECO:0000269|PubMed:7989361, CC ECO:0000269|PubMed:8204629}. CC -!- PTM: Activated protein C inactivates factor V and factor Va by CC proteolytic degradation. {ECO:0000269|PubMed:7989361}. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000269|PubMed:26091039}. CC -!- DISEASE: Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation CC disorder leading to a hemorrhagic diathesis known as parahemophilia. CC {ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:12393490}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Thrombophilia due to activated protein C resistance (THPH2) CC [MIM:188055]: A hemostatic disorder due to defective degradation of CC factor V by activated protein C. It is characterized by a poor CC anticoagulant response to activated protein C resulting in tendency to CC thrombosis. {ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10942390, CC ECO:0000269|PubMed:11435304, ECO:0000269|PubMed:11858490, CC ECO:0000269|PubMed:14617013, ECO:0000269|PubMed:14695241, CC ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:8164741, CC ECO:0000269|PubMed:9454742}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused CC by obstruction of hepatic venous outflow involving either the hepatic CC veins or the terminal segment of the inferior vena cava. Obstructions CC are generally caused by thrombosis and lead to hepatic congestion and CC ischemic necrosis. Clinical manifestations observed in the majority of CC patients include hepatomegaly, right upper quadrant pain and abdominal CC ascites. Budd-Chiari syndrome is associated with a combination of CC disease states including primary myeloproliferative syndromes and CC thrombophilia due to factor V Leiden, protein C deficiency and CC antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical CC complication in patients with polycythemia vera. CC {ECO:0000269|PubMed:9245936}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute CC neurologic event leading to death of neural tissue of the brain and CC resulting in loss of motor, sensory and/or cognitive function. Ischemic CC strokes, resulting from vascular occlusion, is considered to be a CC highly complex disease consisting of a group of heterogeneous disorders CC with multiple genetic and environmental risk factors. CC {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- DISEASE: Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common CC complication of pregnancy, resulting in spontaneous abortion before the CC fetus has reached viability. The term includes all miscarriages from CC the time of conception until 24 weeks of gestation. Recurrent pregnancy CC loss is defined as 3 or more consecutive spontaneous abortions. CC {ECO:0000269|PubMed:11018168}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABD23003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor V entry; CC URL="https://en.wikipedia.org/wiki/Factor_V"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/f5/"; 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; M16967; AAA52424.1; -; mRNA. DR EMBL; L32779; AAB59401.1; -; Genomic_DNA. DR EMBL; L32755; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32756; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32757; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32758; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32759; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32760; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32761; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32762; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32763; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32764; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32765; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32766; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32767; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32768; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32769; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32770; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32771; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32772; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32773; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32774; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32775; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32776; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32777; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; L32778; AAB59401.1; JOINED; Genomic_DNA. DR EMBL; AY364535; AAQ55063.1; -; Genomic_DNA. DR EMBL; Z99572; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK291613; BAF84302.1; -; mRNA. DR EMBL; M14335; AAB59532.1; -; mRNA. DR EMBL; DQ377944; ABD23003.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ297255; CAC82573.1; -; mRNA. DR CCDS; CCDS1281.1; -. DR PIR; A56172; KFHU5. DR RefSeq; NP_000121.2; NM_000130.4. DR PDB; 1CZS; X-ray; 1.90 A; A=2065-2224. DR PDB; 1CZT; X-ray; 1.87 A; A=2065-2224. DR PDB; 1CZV; X-ray; 2.40 A; A/B=2065-2224. DR PDB; 3P6Z; X-ray; 1.70 A; C/I=685-737. DR PDB; 3P70; X-ray; 2.55 A; M/N/O/P=685-737. DR PDB; 3S9C; X-ray; 1.80 A; B=1561-1574. DR PDB; 7KVE; EM; 3.30 A; B=29-2224. DR PDB; 7KVF; EM; 3.60 A; B=29-2224. DR PDB; 7KXY; EM; 4.40 A; A=29-737, B=1574-2224. DR PDB; 7TPP; EM; 4.10 A; C=29-737, D=1574-2224. DR PDB; 7TPQ; EM; 5.30 A; C=29-737, D=1574-2224. DR PDB; 8FDG; EM; 3.20 A; A=29-2224. DR PDB; 8TN9; EM; 3.05 A; A=29-2224. DR PDBsum; 1CZS; -. DR PDBsum; 1CZT; -. DR PDBsum; 1CZV; -. DR PDBsum; 3P6Z; -. DR PDBsum; 3P70; -. DR PDBsum; 3S9C; -. DR PDBsum; 7KVE; -. DR PDBsum; 7KVF; -. DR PDBsum; 7KXY; -. DR PDBsum; 7TPP; -. DR PDBsum; 7TPQ; -. DR PDBsum; 8FDG; -. DR PDBsum; 8TN9; -. DR AlphaFoldDB; P12259; -. DR EMDB; EMD-23048; -. DR EMDB; EMD-23049; -. DR EMDB; EMD-23067; -. DR EMDB; EMD-29008; -. DR EMDB; EMD-29009; -. DR EMDB; EMD-29010; -. DR EMDB; EMD-29011; -. DR EMDB; EMD-41400; -. DR EMDB; EMD-41401; -. DR EMDB; EMD-41402; -. DR EMDB; EMD-41403; -. DR EMDB; EMD-41407; -. DR EMDB; EMD-41408; -. DR EMDB; EMD-41411; -. DR SMR; P12259; -. DR BioGRID; 108452; 17. DR ComplexPortal; CPX-6216; Coagulation factor Va complex. DR DIP; DIP-47331N; -. DR IntAct; P12259; 9. DR MINT; P12259; -. DR STRING; 9606.ENSP00000356771; -. DR BindingDB; P12259; -. DR ChEMBL; CHEMBL3618; -. DR DrugBank; DB13151; Anti-inhibitor coagulant complex. DR DrugBank; DB09130; Copper. DR DrugBank; DB00055; Drotrecogin alfa. DR DrugBank; DB11571; Human thrombin. DR DrugBank; DB11312; Protein C. DR DrugBank; DB13149; Protein S human. DR DrugBank; DB11300; Thrombin. DR DrugBank; DB11572; Thrombin alfa. DR DrugBank; DB05777; Thrombomodulin Alfa. DR CarbonylDB; P12259; -. DR GlyConnect; 1120; 55 N-Linked glycans (15 sites), 17 O-Linked glycans (26 sites). DR GlyCosmos; P12259; 59 sites, 24 glycans. DR GlyGen; P12259; 77 sites, 19 N-linked glycans (10 sites), 7 O-linked glycans (48 sites). DR iPTMnet; P12259; -. DR PhosphoSitePlus; P12259; -. DR BioMuta; F5; -. DR DMDM; 308153653; -. DR CPTAC; non-CPTAC-2648; -. DR jPOST; P12259; -. DR MassIVE; P12259; -. DR MaxQB; P12259; -. DR PaxDb; 9606-ENSP00000356771; -. DR PeptideAtlas; P12259; -. DR ProteomicsDB; 52838; -. DR Antibodypedia; 863; 437 antibodies from 32 providers. DR DNASU; 2153; -. DR Ensembl; ENST00000367797.9; ENSP00000356771.3; ENSG00000198734.12. DR GeneID; 2153; -. DR KEGG; hsa:2153; -. DR MANE-Select; ENST00000367797.9; ENSP00000356771.3; NM_000130.5; NP_000121.2. DR UCSC; uc001ggg.2; human. DR AGR; HGNC:3542; -. DR CTD; 2153; -. DR DisGeNET; 2153; -. DR GeneCards; F5; -. DR GeneReviews; F5; -. DR HGNC; HGNC:3542; F5. DR HPA; ENSG00000198734; Group enriched (choroid plexus, liver, placenta). DR MalaCards; F5; -. DR MIM; 188055; phenotype. DR MIM; 227400; phenotype. DR MIM; 600880; phenotype. DR MIM; 601367; phenotype. DR MIM; 612309; gene. DR MIM; 614389; phenotype. DR neXtProt; NX_P12259; -. DR OpenTargets; ENSG00000198734; -. DR Orphanet; 131; Budd-Chiari syndrome. DR Orphanet; 329217; Cerebral sinovenous thrombosis. DR Orphanet; 326; Congenital factor V deficiency. DR Orphanet; 391320; East Texas bleeding disorder. DR Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia. DR PharmGKB; PA159; -. DR VEuPathDB; HostDB:ENSG00000198734; -. DR eggNOG; ENOG502QSUG; Eukaryota. DR GeneTree; ENSGT00940000158556; -. DR HOGENOM; CLU_000948_0_0_1; -. DR InParanoid; P12259; -. DR OMA; SYNAWSI; -. DR OrthoDB; 537265at2759; -. DR PhylomeDB; P12259; -. DR TreeFam; TF329807; -. DR BioCyc; MetaCyc:G66-30677-MONOMER; -. DR PathwayCommons; P12259; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-5694530; Cargo concentration in the ER. DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SignaLink; P12259; -. DR SIGNOR; P12259; -. DR BioGRID-ORCS; 2153; 9 hits in 1156 CRISPR screens. DR ChiTaRS; F5; human. DR EvolutionaryTrace; P12259; -. DR GeneWiki; Factor_V; -. DR GenomeRNAi; 2153; -. DR Pharos; P12259; Tbio. DR PRO; PR:P12259; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P12259; Protein. DR Bgee; ENSG00000198734; Expressed in right lobe of liver and 144 other cell types or tissues. DR ExpressionAtlas; P12259; baseline and differential. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0031091; C:platelet alpha granule; IBA:GO_Central. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0008015; P:blood circulation; IBA:GO_Central. DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central. DR GO; GO:0032571; P:response to vitamin K; IEA:Ensembl. DR CDD; cd14450; CuRO_3_FV_like; 1. DR CDD; cd14454; CuRO_4_FV_like; 1. DR CDD; cd14451; CuRO_5_FV_like; 1. DR CDD; cd00057; FA58C; 2. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR000421; FA58C. DR InterPro; IPR024715; Factor_5/8-like. DR InterPro; IPR008979; Galactose-bd-like_sf. DR PANTHER; PTHR46806:SF9; COAGULATION FACTOR V; 1. DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF07732; Cu-oxidase_3; 2. DR Pfam; PF00754; F5_F8_type_C; 2. DR PIRSF; PIRSF000354; Factors_V_VIII; 1. DR SMART; SM00231; FA58C; 2. DR SUPFAM; SSF49503; Cupredoxins; 6. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS01285; FA58C_1; 2. DR PROSITE; PS01286; FA58C_2; 2. DR PROSITE; PS50022; FA58C_3; 2. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2. DR Genevisible; P12259; HS. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation; Calcium; Copper; Disease variant; KW Disulfide bond; Glycoprotein; Hemostasis; Metal-binding; Phosphoprotein; KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Thrombophilia; KW Zymogen. FT SIGNAL 1..28 FT CHAIN 29..2224 FT /note="Coagulation factor V" FT /id="PRO_0000002978" FT CHAIN 29..737 FT /note="Coagulation factor V heavy chain" FT /id="PRO_0000002979" FT PROPEP 738..1573 FT /note="Activation peptide (connecting region)" FT /id="PRO_0000002980" FT CHAIN 1574..2224 FT /note="Coagulation factor V light chain" FT /id="PRO_0000002981" FT DOMAIN 30..329 FT /note="F5/8 type A 1" FT DOMAIN 30..193 FT /note="Plastocyanin-like 1" FT DOMAIN 203..329 FT /note="Plastocyanin-like 2" FT DOMAIN 348..684 FT /note="F5/8 type A 2" FT DOMAIN 348..526 FT /note="Plastocyanin-like 3" FT DOMAIN 536..684 FT /note="Plastocyanin-like 4" FT REPEAT 895..911 FT /note="1-1" FT REPEAT 912..928 FT /note="1-2" FT REPEAT 1185..1193 FT /note="2-1" FT REPEAT 1194..1202 FT /note="2-2" FT REPEAT 1203..1211 FT /note="2-3" FT REPEAT 1212..1220 FT /note="2-4" FT REPEAT 1221..1229 FT /note="2-5" FT REPEAT 1230..1238 FT /note="2-6" FT REPEAT 1239..1247 FT /note="2-7" FT REPEAT 1248..1256 FT /note="2-8" FT REPEAT 1257..1265 FT /note="2-9" FT REPEAT 1266..1274 FT /note="2-10" FT REPEAT 1275..1283 FT /note="2-11" FT REPEAT 1284..1292 FT /note="2-12" FT REPEAT 1293..1301 FT /note="2-13" FT REPEAT 1302..1310 FT /note="2-14" FT REPEAT 1311..1319 FT /note="2-15" FT REPEAT 1320..1328 FT /note="2-16" FT REPEAT 1329..1337 FT /note="2-17" FT REPEAT 1338..1346 FT /note="2-18" FT REPEAT 1347..1355 FT /note="2-19" FT REPEAT 1356..1364 FT /note="2-20" FT REPEAT 1365..1373 FT /note="2-21" FT REPEAT 1374..1382 FT /note="2-22" FT REPEAT 1383..1391 FT /note="2-23" FT REPEAT 1392..1400 FT /note="2-24" FT REPEAT 1401..1409 FT /note="2-25" FT REPEAT 1410..1418 FT /note="2-26" FT REPEAT 1419..1427 FT /note="2-27" FT REPEAT 1428..1436 FT /note="2-28" FT REPEAT 1437..1445 FT /note="2-29" FT REPEAT 1446..1454 FT /note="2-30" FT REPEAT 1455..1463 FT /note="2-31" FT REPEAT 1464..1472 FT /note="2-32" FT REPEAT 1473..1481 FT /note="2-33" FT REPEAT 1482..1490 FT /note="2-34" FT REPEAT 1493..1501 FT /note="2-35" FT DOMAIN 1578..1907 FT /note="F5/8 type A 3" FT DOMAIN 1578..1751 FT /note="Plastocyanin-like 5" FT DOMAIN 1761..1907 FT /note="Plastocyanin-like 6" FT DOMAIN 1907..2061 FT /note="F5/8 type C 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DOMAIN 2066..2221 FT /note="F5/8 type C 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT REGION 692..1573 FT /note="B" FT REGION 822..842 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 894..927 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 895..928 FT /note="2 X 17 AA tandem repeats" FT REGION 982..1001 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1029..1048 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1097..1157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1185..1501 FT /note="35 X 9 AA approximate tandem repeats of [TNP]-L-S-P- FT D-L-S-Q-T" FT REGION 1341..1367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1097..1115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1133..1152 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 140 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1843 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000250" FT BINDING 1845 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000250" FT SITE 334..335 FT /note="Cleavage; by activated protein C" FT /evidence="ECO:0000269|PubMed:7989361" FT SITE 534..535 FT /note="Cleavage; by activated protein C" FT /evidence="ECO:0000269|PubMed:7989361" FT SITE 707..708 FT /note="Cleavage; by activated protein C" FT /evidence="ECO:0000269|PubMed:7989361" FT SITE 737..738 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000269|PubMed:3110773" FT SITE 1022..1023 FT /note="Cleavage; by activated protein C" FT /evidence="ECO:0000269|PubMed:7989361" FT SITE 1046..1047 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000269|PubMed:3110773" FT SITE 1573..1574 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000269|PubMed:3110773" FT MOD_RES 640 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 693 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 724 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 726 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 859 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 1522 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 1538 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 1543 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 1593 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 55 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16263699, FT ECO:0000269|PubMed:16335952" FT CARBOHYD 382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 468 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 554 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 741 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 752 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 760 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 776 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 782 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 821 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 938 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 977 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1074 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1083 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1106 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1479 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1499 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1559 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 1703 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2010 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 167..193 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 248..329 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 500..526 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 603..684 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 1725..1751 FT /evidence="ECO:0000305" FT DISULFID 1907..2061 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 2066..2221 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT VARIANT 15 FT /note="G -> S (in dbSNP:rs9332485)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021297" FT VARIANT 107 FT /note="D -> H (in dbSNP:rs6019)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013886" FT VARIANT 334 FT /note="R -> G (in Hong Kong; does not predispose to FT clinical thrombosis; dbSNP:rs118203905)" FT /evidence="ECO:0000269|PubMed:9454741, FT ECO:0000269|PubMed:9746807" FT /id="VAR_013620" FT VARIANT 334 FT /note="R -> T (in THPH2; Cambridge; dbSNP:rs118203906)" FT /evidence="ECO:0000269|PubMed:9454742" FT /id="VAR_013621" FT VARIANT 387 FT /note="I -> T (in THPH2; Liverpool; mutant protein is FT expressed with an additional carbohydrate chain; FT dbSNP:rs118203911)" FT /evidence="ECO:0000269|PubMed:14617013, FT ECO:0000269|PubMed:14695241" FT /id="VAR_032698" FT VARIANT 413 FT /note="M -> T (in dbSNP:rs6033)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013887" FT VARIANT 513 FT /note="R -> K (in dbSNP:rs6020)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9454741, FT ECO:0000269|Ref.3" FT /id="VAR_013622" FT VARIANT 534 FT /note="R -> Q (in THPH2; factor VLeiden; risk factor for FT Budd-Chiari syndrome; risk factor for ischemic stroke; FT dbSNP:rs6025)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:16710414, FT ECO:0000269|PubMed:8164741, ECO:0000269|Ref.3" FT /id="VAR_001213" FT VARIANT 613 FT /note="C -> R (in THPH2; Nijkerk; dbSNP:rs1453479152)" FT /evidence="ECO:0000269|PubMed:11435304" FT /id="VAR_032699" FT VARIANT 775 FT /note="S -> A (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035817" FT VARIANT 781 FT /note="S -> R (in dbSNP:rs13306350)" FT /id="VAR_047740" FT VARIANT 809 FT /note="P -> S (in dbSNP:rs6031)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013888" FT VARIANT 817 FT /note="N -> T (in dbSNP:rs6018)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013889" FT VARIANT 858 FT /note="K -> R (in dbSNP:rs4524)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731, FT ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3" FT /id="VAR_001214" FT VARIANT 865 FT /note="H -> R (in dbSNP:rs4525)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731, FT ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3" FT /id="VAR_001215" FT VARIANT 915 FT /note="T -> S (in dbSNP:rs9332695)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021298" FT VARIANT 925 FT /note="K -> E (in dbSNP:rs6032)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731, FT ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3" FT /id="VAR_013890" FT VARIANT 969 FT /note="N -> S (in dbSNP:rs9332604)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021299" FT VARIANT 980 FT /note="R -> L (in dbSNP:rs9332605)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021300" FT VARIANT 1146 FT /note="H -> Q (in dbSNP:rs6005)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013891" FT VARIANT 1285 FT /note="L -> I (in dbSNP:rs1046712)" FT /evidence="ECO:0000269|PubMed:2827731, FT ECO:0000269|PubMed:8713778, ECO:0000269|Ref.3" FT /id="VAR_013892" FT VARIANT 1327 FT /note="H -> R (in dbSNP:rs1800595)" FT /evidence="ECO:0000269|PubMed:10942390, FT ECO:0000269|PubMed:8713778" FT /id="VAR_013893" FT VARIANT 1397 FT /note="L -> F (in dbSNP:rs13306334)" FT /evidence="ECO:0000269|PubMed:11758222, FT ECO:0000269|PubMed:3110773" FT /id="VAR_047741" FT VARIANT 1404 FT /note="P -> S (in dbSNP:rs9332608)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021301" FT VARIANT 1530 FT /note="E -> A (in dbSNP:rs6007)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3" FT /id="VAR_013894" FT VARIANT 1685 FT /note="T -> S (in dbSNP:rs6011)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013895" FT VARIANT 1730 FT /note="Y -> C (in FA5D; Seoul 2; dbSNP:rs118203907)" FT /evidence="ECO:0000269|PubMed:10942390, FT ECO:0000269|PubMed:11435304" FT /id="VAR_032700" FT VARIANT 1749 FT /note="L -> V (in dbSNP:rs6034)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013896" FT VARIANT 1764 FT /note="M -> V (in dbSNP:rs6030)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:3110773, ECO:0000269|PubMed:7874144" FT /id="VAR_013897" FT VARIANT 1820 FT /note="M -> I (in dbSNP:rs6026)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013898" FT VARIANT 2102 FT /note="R -> C (in FA5D; impairs both factor V secretion and FT activity; dbSNP:rs118203910)" FT /evidence="ECO:0000269|PubMed:12393490" FT /id="VAR_032701" FT VARIANT 2102 FT /note="R -> H (in THPH2)" FT /evidence="ECO:0000269|PubMed:11858490" FT /id="VAR_017329" FT VARIANT 2148 FT /note="M -> T (in dbSNP:rs9332701)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021302" FT VARIANT 2185 FT /note="K -> R (in dbSNP:rs6679078)" FT /id="VAR_034603" FT VARIANT 2222 FT /note="D -> G (in dbSNP:rs6027)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013899" FT CONFLICT 741 FT /note="N -> S (in Ref. 7; ABD23003)" FT /evidence="ECO:0000305" FT CONFLICT 908 FT /note="E -> K (in Ref. 1; AAA52424 and 8; CAC82573)" FT /evidence="ECO:0000305" FT CONFLICT 991 FT /note="K -> E (in Ref. 5; BAF84302)" FT /evidence="ECO:0000305" FT CONFLICT 2213 FT /note="A -> T (in Ref. 1; AAA52424)" FT /evidence="ECO:0000305" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 61..69 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 178..182 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 266..271 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 281..291 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 302..310 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 313..317 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 321..326 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 352..361 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 373..379 FT /evidence="ECO:0007829|PDB:7KVE" FT TURN 382..385 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 391..398 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 427..441 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 446..453 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 456..458 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 461..463 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 467..469 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 480..487 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 489..491 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 499..506 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 511..516 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 528..530 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 536..543 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 547..552 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 559..566 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 578..581 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 582..584 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 585..589 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 600..603 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 607..614 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 622..625 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 641..643 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 648..654 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 659..664 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 669..674 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 676..682 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 685..688 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 698..702 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 707..712 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 714..718 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 732..735 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 767..769 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 1492..1494 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1515..1519 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1531..1534 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1536..1538 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1543..1545 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1553..1556 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1560..1562 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1569..1571 FT /evidence="ECO:0007829|PDB:3S9C" FT STRAND 1580..1593 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1596..1600 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1607..1611 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1613..1625 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1638..1643 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1648..1651 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1655..1662 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1664..1666 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1674..1676 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1679..1681 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1689..1691 FT /evidence="ECO:0007829|PDB:7KVE" FT HELIX 1694..1696 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 1702..1711 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 1714..1716 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1720..1722 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1724..1728 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1729..1731 FT /evidence="ECO:0007829|PDB:7KVE" FT TURN 1736..1743 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1748..1751 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1758..1760 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1764..1772 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1783..1785 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 1789..1792 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1799..1801 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1808..1810 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1825..1832 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1840..1844 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1853..1855 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1862..1864 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1868..1875 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1880..1885 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 1890..1894 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1897..1902 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1912..1916 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 1920..1922 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1923..1927 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 1930..1932 FT /evidence="ECO:0007829|PDB:8FDG" FT HELIX 1935..1937 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1955..1957 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1963..1978 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1981..1983 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 1986..2002 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 2008..2010 FT /evidence="ECO:0007829|PDB:7KVE" FT STRAND 2012..2015 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 2022..2025 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 2028..2051 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 2056..2065 FT /evidence="ECO:0007829|PDB:8FDG" FT TURN 2072..2074 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2075..2077 FT /evidence="ECO:0007829|PDB:1CZV" FT HELIX 2079..2081 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2082..2085 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2093..2095 FT /evidence="ECO:0007829|PDB:1CZV" FT HELIX 2098..2100 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2107..2109 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2111..2113 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2123..2139 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2141..2143 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2146..2163 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2170..2173 FT /evidence="ECO:0007829|PDB:8FDG" FT STRAND 2182..2185 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2188..2211 FT /evidence="ECO:0007829|PDB:1CZT" FT STRAND 2213..2222 FT /evidence="ECO:0007829|PDB:1CZT" SQ SEQUENCE 2224 AA; 251703 MW; 24AEF3FEA7332E37 CRC64; MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT NSSLNLSVTS FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV HFKNKADKPL SIHPQGIRYS KLSEGASYLD HTFPAEKMDD AVAPGREYTY EWSISEDSGP THDDPPCLTH IYYSHENLIE DFNSGLIGPL LICKKGTLTE GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG TMPDITVCAH DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW EYFIAAEEVI WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE DESFTKHTVN PNMKEDGILG PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSPYEDEVN SSFTSGRNNT MIRAVQPGET YTYKWNILEF DEPTENDAQC LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA DIEQQAVFAV FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES VTVTMDNVGT WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEEEE FNLTALALEN GTEFVSSNTD IIVGSNYSSP SNISKFTVNN LAEPQKAPSH QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL QPDVTGIRLL SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA SEKGSYEIIQ DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK FPRVRHKSLQ VRQDGGKSRL KKSQFLIKTR KKKKEKHTHH APLSPRTFHP LRSEAYNTFS ERRLKHSLVL HKSNETSLPT DLNQTLPSMD FGWIASLPDH NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS TSDPSHRSSS PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS LDLSQTNLSP ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH MTLSPELSQT NLSPALGQMP ISPDLSHTTL SLDFSQTNLS PELSQTNLSP ALGQMPLSPD PSHTTLSLDL SQTNLSPELS QTNLSPDLSE MPLFADLSQI PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP DISDTTLLPD LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY KTDVRTNINS SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE TDIEDSDDIP EDTTYKKVVF RKYLDSTFTK RDPRGEYEEH LGILGPIIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDDS PEWFKEDNAV QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI HSGLIGPLLI CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL ENGNKQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF LIMDRDCRMP MGLSTGIISD SQIKASEFLG YWEPRLARLN NGGSYNAWSV EKLAAEFASK PWIQVDMQKE VIITGIQTQG AKHYLKSCYT TEFYVAYSSN QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY IRISPTRAYN RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV KSYTIHYSEQ GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF IRVIPKTWNQ SIALRLELFG CDIY //