FA5_HUMAN
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 03-AUG-2022, entry version 243.
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 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 AlphaFoldDB; P12259; -.
DR SMR; P12259; -.
DR BioGRID; 108452; 16.
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; 16 N-Linked glycans (9 sites).
DR GlyGen; P12259; 59 sites, 19 N-linked glycans (10 sites), 6 O-linked glycans (31 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; P12259; -.
DR PeptideAtlas; P12259; -.
DR PRIDE; P12259; -.
DR ProteomicsDB; 52838; -.
DR Antibodypedia; 863; 395 antibodies from 31 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 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; GDYWEPS; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; P12259; -.
DR TreeFam; TF329807; -.
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; 7 hits in 1070 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 tissues.
DR ExpressionAtlas; P12259; baseline and differential.
DR Genevisible; P12259; HS.
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; IC:ComplexPortal.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:0032991; C:protein-containing complex; IC:ComplexPortal.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IC:ComplexPortal.
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:0072377; P:blood coagulation, common pathway; IC:ComplexPortal.
DR GO; GO:0007598; P:blood coagulation, extrinsic pathway; IC:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
DR GO; GO:0031638; P:zymogen activation; IDA:ComplexPortal.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR011707; Cu-oxidase_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 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; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 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.
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 V Leiden; associated with
FT susceptibility to Budd-Chiari syndrome; associated with
FT susceptibility to ischemic stroke; 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..40
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 134..140
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 178..185
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 252..263
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 511..517
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 560..564
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 578..583
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 607..614
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 669..674
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1569..1571
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 1578..1582
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1584..1591
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1596..1600
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1615..1627
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1637..1639
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1654..1660
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1664..1666
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1679..1681
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1689..1691
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1694..1696
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1706..1711
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1714..1716
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1724..1726
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1729..1731
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1736..1740
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1741..1743
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1745..1748
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1758..1761
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1768..1782
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1792..1796
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1797..1799
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1800..1803
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1804..1813
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1827..1831
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1840..1844
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1853..1855
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1860..1864
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1869..1873
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1884..1886
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1889..1892
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1893..1895
FT /evidence="ECO:0007829|PDB:7KVE"
FT TURN 1913..1915
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1916..1918
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1920..1922
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1923..1927
FT /evidence="ECO:0007829|PDB:7KVE"
FT HELIX 1934..1936
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1957..1959
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1963..1965
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1971..1978
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1983..1985
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 1990..2003
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2008..2010
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2012..2016
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2023..2025
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2028..2051
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2058..2060
FT /evidence="ECO:0007829|PDB:7KVE"
FT STRAND 2063..2065
FT /evidence="ECO:0007829|PDB:7KVE"
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 2172..2175
FT /evidence="ECO:0007829|PDB:7KVE"
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
