VWF_HUMAN
ID VWF_HUMAN Reviewed; 2813 AA.
AC P04275; Q8TCE8; Q99806;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 262.
DE RecName: Full=von Willebrand factor;
DE Short=vWF;
DE Contains:
DE RecName: Full=von Willebrand antigen 2;
DE AltName: Full=von Willebrand antigen II;
DE Flags: Precursor;
GN Name=VWF; Synonyms=F8VWF;
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] (ISOFORM 1), AND VARIANTS ARG-852; ALA-1381 AND
RP HIS-1472.
RX PubMed=3489923; DOI=10.1093/nar/14.17.7125;
RA Bonthron D., Orr E.C., Mitsock L.M., Ginsburg D., Handin R.I., Orkin S.H.;
RT "Nucleotide sequence of pre-pro-von Willebrand factor cDNA.";
RL Nucleic Acids Res. 14:7125-7128(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-471; ARG-852; ALA-1381
RP AND HIS-1472.
RX PubMed=2584182; DOI=10.1016/s0021-9258(19)47144-5;
RA Mancuso D.J., Tuley E.A., Westfield L.A., Worrall N.K.,
RA Shelton-Inloes B.B., Sorace J.M., Alevy Y.G., Sadler J.E.;
RT "Structure of the gene for human von Willebrand factor.";
RL J. Biol. Chem. 264:19514-19527(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1400 (ISOFORM 1), AND VARIANTS ARG-484;
RP ARG-852 AND ALA-1381.
RX PubMed=3019665; DOI=10.1002/j.1460-2075.1986.tb04435.x;
RA Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.;
RT "Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive
RT protein considerably larger than the mature vWF subunit.";
RL EMBO J. 5:1839-1847(1986).
RN [7]
RP ERRATUM OF PUBMED:3019665.
RA Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.;
RL EMBO J. 5:3074-3074(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178.
RX PubMed=2828057; DOI=10.1111/j.1432-1033.1988.tb13757.x;
RA Bonthron D., Orkin S.H.;
RT "The human von Willebrand factor gene. Structure of the 5' region.";
RL Eur. J. Biochem. 171:51-57(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP 23-56.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=3495266; DOI=10.1016/s0006-291x(87)80016-5;
RA Shelton-Inloes B.B., Broze G.J. Jr., Miletich J.P., Sadler J.E.;
RT "Evolution of human von Willebrand factor: cDNA sequence polymorphisms,
RT repeated domains, and relationship to von Willebrand antigen II.";
RL Biochem. Biophys. Res. Commun. 144:657-665(1987).
RN [10]
RP PROTEIN SEQUENCE OF 764-2813, AND VARIANTS ARG-852 AND ALA-1381.
RX PubMed=3524673; DOI=10.1021/bi00359a015;
RA Titani K., Kumar S., Takio K., Ericsson L.H., Wade R.D., Ashida K.,
RA Walsh K.A., Chopek M.W., Sadler J.E., Fujikawa K.;
RT "Amino acid sequence of human von Willebrand factor.";
RL Biochemistry 25:3171-3184(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 744-873 AND 1289-2813 (ISOFORM 1), AND
RP VARIANTS ALA-789; ARG-852 AND ALA-1381.
RX PubMed=2864688; DOI=10.1073/pnas.82.19.6394;
RA Sadler J.E., Shelton-Inloes B.B., Sorace J.M., Harlan J.M., Titani K.,
RA Davie E.W.;
RT "Cloning and characterization of two cDNAs coding for human von Willebrand
RT factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6394-6398(1985).
RN [12]
RP PROTEIN SEQUENCE OF 764-782.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 781-1424 (ISOFORM 1), AND VARIANTS ARG-852
RP AND ALA-1381.
RX PubMed=3488076; DOI=10.1021/bi00359a014;
RA Shelton-Inloes B.B., Titani K., Sadler J.E.;
RT "cDNA sequences for human von Willebrand factor reveal five types of
RT repeated domains and five possible protein sequence polymorphisms.";
RL Biochemistry 25:3164-3171(1986).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 990-1947, AND VARIANTS ALA-1381 AND
RP HIS-1472.
RX PubMed=1988024; DOI=10.1021/bi00215a036;
RA Mancuso D.J., Tuley E.A., Westfield L.A., Lester-Mancuso T.L.,
RA Le Beau M.M., Sorace J.M., Sadler J.E.;
RT "Human von Willebrand factor gene and pseudogene: structural analysis and
RT differentiation by polymerase chain reaction.";
RL Biochemistry 30:253-269(1991).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1236-1476 (ISOFORM 1), AND VARIANT ALA-1381.
RX PubMed=9373253;
RA Schulte am Esch J. II, Cruz M.A., Siegel J.B., Anrather J., Robson S.C.;
RT "Activation of human platelets by the membrane-expressed A1 domain of von
RT Willebrand factor.";
RL Blood 90:4425-4437(1997).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2621-2813 (ISOFORM 1).
RX PubMed=3874428; DOI=10.1126/science.3874428;
RA Ginsburg D., Handin R.I., Bonthron D.T., Donlon T.A., Bruns G.A.P.,
RA Latt S.A., Orkin S.H.;
RT "Human von Willebrand factor (vWF): isolation of complementary DNA (cDNA)
RT clones and chromosomal localization.";
RL Science 228:1401-1406(1985).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
RX PubMed=3873280; DOI=10.1016/0092-8674(85)90060-1;
RA Lynch D.C., Zimmerman T.S., Collins C.J., Brown M., Morin M.J., Ling E.H.,
RA Livingston D.M.;
RT "Molecular cloning of cDNA for human von Willebrand factor: authentication
RT by a new method.";
RL Cell 41:49-56(1985).
RN [18]
RP SEQUENCE REVISION.
RA Lynch D.C.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
RX PubMed=3875078; DOI=10.1093/nar/13.13.4699;
RA Verweij C.L., de Vries C.J.M., Distel B., van Zonneveld A.-J.,
RA Geurts van Kessel A., van Mourik J.A., Pannekoek H.;
RT "Construction of cDNA coding for human von Willebrand factor using antibody
RT probes for colony-screening and mapping of the chromosomal gene.";
RL Nucleic Acids Res. 13:4699-4717(1985).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2731-2813.
RX PubMed=3496594; DOI=10.1073/pnas.84.13.4393;
RA Collins C.J., Underdahl J.P., Levene R.B., Ravera C.P., Morin M.J.,
RA Dombalagian M.J., Ricca G., Livingston D.M., Lynch D.C.;
RT "Molecular cloning of the human gene for von Willebrand factor and
RT identification of the transcription initiation site.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4393-4397(1987).
RN [21]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10961880;
RA Haberichter S.L., Fahs S.A., Montgomery R.R.;
RT "von Willebrand factor storage and multimerization: 2 independent
RT intracellular processes.";
RL Blood 96:1808-1815(2000).
RN [22]
RP DISULFIDE BONDS.
RX PubMed=3502076; DOI=10.1021/bi00399a013;
RA Marti T., Rosselet S.J., Titani K., Walsh K.A.;
RT "Identification of disulfide-bridged substructures within human von
RT Willebrand factor.";
RL Biochemistry 26:8099-8109(1987).
RN [23]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=3089784; DOI=10.1111/j.1432-1033.1986.tb09750.x;
RA Samor B., Michalski J.C., Debray H., Mazurier C., Goudemand M.,
RA van Halbeek H., Vliegenthart J.F.G., Montreuil J.;
RT "Primary structure of a new tetraantennary glycan of the N-
RT acetyllactosaminic type isolated from human factor VIII/von Willebrand
RT factor.";
RL Eur. J. Biochem. 158:295-298(1986).
RN [24]
RP INTERACTION WITH F8.
RX PubMed=9218428; DOI=10.1074/jbc.272.29.18007;
RA Saenko E.L., Scandella D.;
RT "The acidic region of the factor VIII light chain and the C2 domain
RT together form the high affinity binding site for von Willebrand factor.";
RL J. Biol. Chem. 272:18007-18014(1997).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1515.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [26]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2546.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [27]
RP GLYCOSYLATION AT ASN-1515.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1261-1468.
RX PubMed=9553097; DOI=10.1074/jbc.273.17.10396;
RA Emsley J., Cruz M., Handin R., Liddington R.;
RT "Crystal structure of the von Willebrand factor A1 domain and implications
RT for the binding of platelet glycoprotein Ib.";
RL J. Biol. Chem. 273:10396-10401(1998).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-1873.
RX PubMed=9331419; DOI=10.1016/s0969-2126(97)00266-9;
RA Huizinga E.G., Martijn van der Plas R., Kroon J., Sixma J.J., Gros P.;
RT "Crystal structure of the A3 domain of human von Willebrand factor:
RT implications for collagen binding.";
RL Structure 5:1147-1156(1997).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1686-1872.
RX PubMed=9312128; DOI=10.1074/jbc.272.40.25162;
RA Bienkowska J., Cruz M., Atiemo A., Handin R., Liddington R.;
RT "The von Willebrand factor A3 domain does not contain a metal ion-dependent
RT adhesion site motif.";
RL J. Biol. Chem. 272:25162-25167(1997).
RN [31]
RP REVIEW.
RX PubMed=12871266; DOI=10.1046/j.1538-7836.2003.00260.x;
RA Ruggeri Z.M.;
RT "von Willebrand factor, platelets and endothelial cell interactions.";
RL J. Thromb. Haemost. 1:1335-1342(2003).
RN [32]
RP VARIANTS VWD2 TRP-1597 AND ASP-1607.
RX PubMed=2786201; DOI=10.1073/pnas.86.10.3723;
RA Ginsburg D., Konkle B.A., Gill J.C., Montgomery R.R., Bockenstedt P.L.,
RA Johnson T.A., Yang A.Y.;
RT "Molecular basis of human von Willebrand disease: analysis of platelet von
RT Willebrand factor mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3723-3727(1989).
RN [33]
RP VARIANT VWD2 THR-1628.
RX PubMed=1673047;
RA Iannuzzi M.C., Hidaka N., Boehnke M., Bruck M.E., Hanna W.T., Collins F.S.,
RA Ginsburg D.;
RT "Analysis of the relationship of von Willebrand disease (vWD) and
RT hereditary hemorrhagic telangiectasia and identification of a potential
RT type IIA vWD mutation (IIe865 to Thr).";
RL Am. J. Hum. Genet. 48:757-763(1991).
RN [34]
RP VARIANTS VWD2 TRP-816 AND GLN-854.
RX PubMed=1832934; DOI=10.1111/j.1365-2141.1991.tb04480.x;
RA Gaucher C., Mercier B., Jorieux S., Oufkir D., Mazurier C.;
RT "Identification of two point mutations in the von Willebrand factor gene of
RT three families with the 'Normandy' variant of von Willebrand disease.";
RL Br. J. Haematol. 78:506-514(1991).
RN [35]
RP VARIANT VWD2 CYS-1308.
RX PubMed=1761120; DOI=10.1111/j.1600-0609.1991.tb01858.x;
RA Donner M., Andersson A.-M., Kristoffersson A.-C., Nilsson I.M.,
RA Dahlback B., Holmberg L.;
RT "An Arg545-->Cys545 substitution mutation of the von Willebrand factor in
RT type IIB von Willebrand's disease.";
RL Eur. J. Haematol. 47:342-345(1991).
RN [36]
RP VARIANTS VWD2 TRP-1306; CYS-1308 AND PRO-1613.
RX PubMed=2010538; DOI=10.1172/jci115122;
RA Randi A.M., Rabinowitz I., Mancuso D.J., Mannucci P.M., Sadler J.E.;
RT "Molecular basis of von Willebrand disease type IIB. Candidate mutations
RT cluster in one disulfide loop between proposed platelet glycoprotein Ib
RT binding sequences.";
RL J. Clin. Invest. 87:1220-1226(1991).
RN [37]
RP VARIANTS VWD2 TRP-1306; CYS-1308; MET-1316 AND GLN-1341, AND VARIANT
RP HIS-1399.
RX PubMed=1672694; DOI=10.1172/jci115123;
RA Cooney K.A., Nichols W.C., Bruck M.E., Bahou W.F., Shapiro A.D.,
RA Bowie E.J.W., Gralnick H.R., Ginsburg D.;
RT "The molecular defect in type IIB von Willebrand disease. Identification of
RT four potential missense mutations within the putative GpIb binding
RT domain.";
RL J. Clin. Invest. 87:1227-1233(1991).
RN [38]
RP VARIANT VWD2 CYS-1313.
RX PubMed=2011604; DOI=10.1073/pnas.88.7.2946;
RA Ware J., Dent J.A., Azuma H., Sugimoto M., Kyrle P.A., Yoshioka A.,
RA Ruggeri Z.M.;
RT "Identification of a point mutation in type IIB von Willebrand disease
RT illustrating the regulation of von Willebrand factor affinity for the
RT platelet membrane glycoprotein Ib-IX receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2946-2950(1991).
RN [39]
RP VARIANT VWD2 MET-791.
RX PubMed=1906179; DOI=10.1073/pnas.88.14.6377;
RA Tuley E.A., Gaucher C., Jorieux S., Worrall N.K., Sadler J.E., Mazurier C.;
RT "Expression of von Willebrand factor 'Normandy': an autosomal mutation that
RT mimics hemophilia A.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6377-6381(1991).
RN [40]
RP VARIANT VWD2 MET-1316.
RX PubMed=1729889;
RA Murray E.W., Giles A.R., Lillicrap D.;
RT "Germ-line mosaicism for a valine-to-methionine substitution at residue 553
RT in the glycoprotein Ib-binding domain of von Willebrand factor, causing
RT type IIB von Willebrand disease.";
RL Am. J. Hum. Genet. 50:199-207(1992).
RN [41]
RP VARIANTS VWD2 TRP-1306; MET-1316; THR-1628 AND SER-1648.
RX PubMed=1420817;
RA Pietu G., Ribba A.S., de Paillette L., Cherel G., Lavergne J.-M.,
RA Bahnak B.R., Meyer D.;
RT "Molecular study of von Willebrand disease: identification of potential
RT mutations in patients with type IIA and type IIB.";
RL Blood Coagul. Fibrinolysis 3:415-421(1992).
RN [42]
RP VARIANTS VWD2 TRP-1306; CYS-1308; LEU-1314 AND LEU-1318.
RX PubMed=1419803; DOI=10.1111/j.1365-2141.1992.tb04594.x;
RA Donner M., Kristoffersson A.-C., Lenk H., Scheibel E., Dahlback B.,
RA Nilsson I.M., Holmberg L.;
RT "Type IIB von Willebrand's disease: gene mutations and clinical
RT presentation in nine families from Denmark, Germany and Sweden.";
RL Br. J. Haematol. 82:58-65(1992).
RN [43]
RP VARIANT VWD2 ARG-1272.
RX PubMed=1419804; DOI=10.1111/j.1365-2141.1992.tb04595.x;
RA Lavergne J.-M., de Paillette L., Bahnak B.R., Ribba A.-S., Fressinaud E.,
RA Meyer D., Pietu G.;
RT "Defects in type IIA von Willebrand disease: a cysteine 509 to arginine
RT substitution in the mature von Willebrand factor disrupts a disulphide loop
RT involved in the interaction with platelet glycoprotein Ib-IX.";
RL Br. J. Haematol. 82:66-72(1992).
RN [44]
RP VARIANT VWD2 LYS-1638.
RX PubMed=1429668; DOI=10.1016/s0021-9258(18)50078-8;
RA Ribba A.S., Voorberg J., Meyer D., Pannekoek H., Pietu G.;
RT "Characterization of recombinant von Willebrand factor corresponding to
RT mutations in type IIA and type IIB von Willebrand disease.";
RL J. Biol. Chem. 267:23209-23215(1992).
RN [45]
RP VARIANT VWD2 SER-1324.
RX PubMed=1409710; DOI=10.1073/pnas.89.20.9846;
RA Rabinowitz I., Tuley E.A., Mancuso D.J., Randi A.M., Firkin B.G.,
RA Howard M.A., Sadler J.E.;
RT "von Willebrand disease type B: a missense mutation selectively abolishes
RT ristocetin-induced von Willebrand factor binding to platelet glycoprotein
RT Ib.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9846-9849(1992).
RN [46]
RP VARIANTS VWD2 GLN-1597; ARG-1609 AND GLU-1665.
RX PubMed=8338947;
RA Inbal A., Englender T., Kornbrot N., Randi A.M., Castaman G.,
RA Mannucci P.M., Sadler J.E.;
RT "Identification of three candidate mutations causing type IIA von
RT Willebrand disease using a rapid, nonradioactive, allele-specific
RT hybridization method.";
RL Blood 82:830-836(1993).
RN [47]
RP VARIANT VWD2 CYS-1514.
RX PubMed=8435341; DOI=10.1111/j.1365-2141.1993.tb04637.x;
RA Gaucher C., Hanss M., Dechavanne M., Mazurier C.;
RT "Substitution of cysteine for phenylalanine 751 in mature von Willebrand
RT factor is a novel candidate mutation in a family with type IIA von
RT Willebrand disease.";
RL Br. J. Haematol. 83:94-99(1993).
RN [48]
RP VARIANTS VWD2 GLY-1597 AND ARG-1609, AND VARIANT CYS-1584.
RX PubMed=8348943;
RA Donner M., Kristoffersson A.C., Berntorp E., Scheibel E., Thorsen S.,
RA Dahlback B., Nilsson I.M., Holmberg L.;
RT "Two new candidate mutations in type IIA von Willebrand's disease
RT (Arg834-->Gly, Gly846-->Arg) and one polymorphism (Tyr821-->Cys) in the A2
RT region of the von Willebrand factor.";
RL Eur. J. Haematol. 51:38-44(1993).
RN [49]
RP VARIANT VWD2 ASP-1268.
RX PubMed=8376405; DOI=10.1016/s0021-9258(20)80753-4;
RA Rabinowitz I., Randi A.M., Shindler K.S., Tuley E.A., Rustagi P.K.,
RA Sadler J.E.;
RT "Type IIB mutation His-505-->Asp implicates a new segment in the control of
RT von Willebrand factor binding to platelet glycoprotein Ib.";
RL J. Biol. Chem. 268:20497-20501(1993).
RN [50]
RP VARIANT VWD2 LEU-1266.
RX PubMed=8486782; DOI=10.1172/jci116443;
RA Holmberg L., Dent J.A., Schneppenheim R., Budde U., Ware J., Ruggeri Z.M.;
RT "von Willebrand factor mutation enhancing interaction with platelets in
RT patients with normal multimeric structure.";
RL J. Clin. Invest. 91:2169-2177(1993).
RN [51]
RP VARIANT VWD2 VAL-1460.
RX PubMed=8123843;
RA Hilbert L., Gaucher C., de Romeuf C., Horellou M.H., Vink T., Mazurier C.;
RT "Leu 697-->Val mutation in mature von Willebrand factor is responsible for
RT type IIB von Willebrand disease.";
RL Blood 83:1542-1550(1994).
RN [52]
RP VARIANTS VWD2 PRO-1540 AND THR-1628.
RX PubMed=8123844;
RA Lyons S.E., Cooney K.A., Bockenstedt P., Ginsburg D.;
RT "Characterization of Leu777Pro and Ile865Thr type IIA von Willebrand
RT disease mutations.";
RL Blood 83:1551-1557(1994).
RN [53]
RP VARIANT VWD3 TYR-2739.
RX PubMed=8088787; DOI=10.1006/geno.1994.1241;
RA Zhang Z.P., Blombaeck M., Egberg N., Falk G., Anvret M.;
RT "Characterization of the von Willebrand factor gene (VWF) in von Willebrand
RT disease type III patients from 24 families of Swedish and Finnish origin.";
RL Genomics 21:188-193(1994).
RN [54]
RP VARIANT VWD3 CYS-377.
RX PubMed=7989040; DOI=10.1007/bf00206958;
RA Schneppenheim R., Krey S., Bergmann F., Bock D., Budde U., Lange M.,
RA Linde R., Mittler U., Meili E., Mertes G., Olek K., Plendl H., Simeoni E.;
RT "Genetic heterogeneity of severe von Willebrand disease type III in the
RT German population.";
RL Hum. Genet. 94:640-652(1994).
RN [55]
RP VARIANT VWD2 SER-528.
RX PubMed=8011991;
RA Uno H., Nishida N., Ishizaki J., Suzuki M., Nishikubo T., Miyata S.,
RA Takahashi Y., Yoshioka A., Tsuda K.;
RT "Investigation of type IIC von Willebrand disease.";
RL Int. J. Hematol. 59:219-225(1994).
RN [56]
RP VARIANTS VWD2 CYS-1374 AND HIS-1374.
RX PubMed=7620154;
RA Hilbert L., Gaucher C., Mazurier C.;
RT "Identification of two mutations (Arg611Cys and Arg611His) in the A1 loop
RT of von Willebrand factor (vWF) responsible for type 2 von Willebrand
RT disease with decreased platelet-dependent function of vWF.";
RL Blood 86:1010-1018(1995).
RN [57]
RP VARIANT VWD2 HIS-1374.
RX PubMed=7734373; DOI=10.1111/j.1365-2141.1995.tb08383.x;
RA Castaman G., Eikenboom C.J.C., Rodeghiero F., Briet K., Reitsma P.H.;
RT "A novel candidate mutation (Arg611-->His) in type I 'platelet discordant'
RT von Willebrand's disease with desmopressin-induced thrombocytopenia.";
RL Br. J. Haematol. 89:656-658(1995).
RN [58]
RP VARIANT VWD2 VAL-1461.
RX PubMed=8547152; DOI=10.1111/j.1365-2141.1995.tb05423.x;
RA Hilbert L., Gaucher C., Mazurier C.;
RT "Effects of different amino-acid substitutions in the leucine 694-proline
RT 708 segment of recombinant von Willebrand factor.";
RL Br. J. Haematol. 91:983-990(1995).
RN [59]
RP VARIANT VWD2 ARG-550.
RX PubMed=7789955; DOI=10.1007/bf00209487;
RA Schneppenheim R., Thomas K.B., Krey S., Budde U., Jessat U., Sutor A.H.,
RA Zeiger B.;
RT "Identification of a candidate missense mutation in a family with von
RT Willebrand disease type IIC.";
RL Hum. Genet. 95:681-686(1995).
RN [60]
RP VARIANT VWD2 ARG-2773.
RX PubMed=8622978; DOI=10.1073/pnas.93.8.3581;
RA Schneppenheim R., Brassard J., Krey S., Budde U., Kunicki T.J.,
RA Holmberg L., Ware J., Ruggeri Z.M.;
RT "Defective dimerization of von Willebrand factor subunits due to a Cys->
RT Arg mutation in type IID von Willebrand disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3581-3586(1996).
RN [61]
RP VARIANT VWD1 TRP-273, AND VARIANT VWD3 TRP-273.
RX PubMed=10887119;
RA Allen S., Abuzenadah A.M., Hinks J., Blagg J.L., Gursel T., Ingerslev J.,
RA Goodeve A.C., Peake I.R., Daly M.E.;
RT "A novel von Willebrand disease-causing mutation (Arg273Trp) in the von
RT Willebrand factor propeptide that results in defective multimerization and
RT secretion.";
RL Blood 96:560-568(2000).
RN [62]
RP VARIANT VWD1 ARG-1149, AND MUTAGENESIS OF CYS-1149 AND CYS-1169.
RX PubMed=11698279; DOI=10.1182/blood.v98.10.2973;
RA Bodo I., Katsumi A., Tuley E.A., Eikenboom J.C., Dong Z., Sadler J.E.;
RT "Type 1 von Willebrand disease mutation Cys1149Arg causes intracellular
RT retention and degradation of heterodimers: a possible general mechanism for
RT dominant mutations of oligomeric proteins.";
RL Blood 98:2973-2979(2001).
RN [63]
RP VARIANT VWD2 ARG-1060.
RX PubMed=12406074; DOI=10.1046/j.1365-2141.2002.03819.x;
RA Mazurier C., Parquet-Gernez A., Gaucher C., Lavergne J.-M., Goudemand J.;
RT "Factor VIII deficiency not induced by FVIII gene mutation in a female
RT first cousin of two brothers with haemophilia A.";
RL Br. J. Haematol. 119:390-392(2002).
RN [64]
RP VARIANT CYS-1584.
RX PubMed=15755288; DOI=10.1111/j.1365-2141.2005.05375.x;
RA Bowen D.J., Collins P.W., Lester W., Cumming A.M., Keeney S., Grundy P.,
RA Enayat S.M., Bolton-Maggs P.H., Keeling D.M., Khair K., Tait R.C.,
RA Wilde J.T., Pasi K.J., Hill F.G.;
RT "The prevalence of the cysteine1584 variant of von Willebrand factor is
RT increased in type 1 von Willebrand disease: co-segregation with increased
RT susceptibility to ADAMTS13 proteolysis but not clinical phenotype.";
RL Br. J. Haematol. 128:830-836(2005).
RN [65]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
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).
RN [66]
RP VARIANT VWD2 PHE-1272.
RX PubMed=21592258; DOI=10.1111/j.1365-2516.2011.02569.x;
RA Woods A.I., Sanchez-Luceros A., Kempfer A.C., Powazniak Y.,
RA Calderazzo Pereyra J.C., Blanco A.N., Meschengieser S.S., Lazzari M.A.;
RT "C1272F: a novel type 2A von Willebrand's disease mutation in A1 domain;
RT its clinical significance.";
RL Haemophilia 18:112-116(2012).
CC -!- FUNCTION: Important in the maintenance of hemostasis, it promotes
CC adhesion of platelets to the sites of vascular injury by forming a
CC molecular bridge between sub-endothelial collagen matrix and platelet-
CC surface receptor complex GPIb-IX-V. Also acts as a chaperone for
CC coagulation factor VIII, delivering it to the site of injury,
CC stabilizing its heterodimeric structure and protecting it from
CC premature clearance from plasma.
CC -!- SUBUNIT: Multimeric. Interacts with F8. {ECO:0000269|PubMed:10961880,
CC ECO:0000269|PubMed:9218428}.
CC -!- INTERACTION:
CC P04275; Q76LX8: ADAMTS13; NbExp=19; IntAct=EBI-981819, EBI-981764;
CC P04275; P00451: F8; NbExp=2; IntAct=EBI-981819, EBI-1046394;
CC P04275; PRO_0000002967 [P00451]: F8; NbExp=2; IntAct=EBI-981819, EBI-21454065;
CC P04275; P07359: GP1BA; NbExp=2; IntAct=EBI-981819, EBI-297082;
CC P04275; P04275: VWF; NbExp=21; IntAct=EBI-981819, EBI-981819;
CC P04275-2; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-25896548, EBI-10254793;
CC P04275-2; Q99944: EGFL8; NbExp=3; IntAct=EBI-25896548, EBI-3924130;
CC P04275-2; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-25896548, EBI-25830459;
CC P04275-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-25896548, EBI-396540;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04275-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04275-2; Sequence=VSP_056527, VSP_056528, VSP_056529;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DOMAIN: The von Willebrand antigen 2 is required for multimerization of
CC vWF and for its targeting to storage granules.
CC -!- PTM: All cysteine residues are involved in intrachain or interchain
CC disulfide bonds.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.
CC -!- DISEASE: von Willebrand disease 1 (VWD1) [MIM:193400]: A common
CC hemorrhagic disorder due to defects in von Willebrand factor protein
CC and resulting in impaired platelet aggregation. Von Willebrand disease
CC type 1 is characterized by partial quantitative deficiency of
CC circulating von Willebrand factor, that is otherwise structurally and
CC functionally normal. Clinical manifestations are mucocutaneous
CC bleeding, such as epistaxis and menorrhagia, and prolonged bleeding
CC after surgery or trauma. {ECO:0000269|PubMed:10887119,
CC ECO:0000269|PubMed:11698279}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: von Willebrand disease 2 (VWD2) [MIM:613554]: A hemorrhagic
CC disorder due to defects in von Willebrand factor protein and resulting
CC in altered platelet aggregation. Von Willebrand disease type 2 is
CC characterized by qualitative deficiency and functional anomalies of von
CC Willebrand factor. It is divided in different subtypes including 2A,
CC 2B, 2M and 2N (Normandy variant). The mutant VWF protein in types 2A,
CC 2B and 2M are defective in their platelet-dependent function, whereas
CC the mutant protein in type 2N is defective in its ability to bind
CC factor VIII. Clinical manifestations are mucocutaneous bleeding, such
CC as epistaxis and menorrhagia, and prolonged bleeding after surgery or
CC trauma. {ECO:0000269|PubMed:12406074, ECO:0000269|PubMed:1409710,
CC ECO:0000269|PubMed:1419803, ECO:0000269|PubMed:1419804,
CC ECO:0000269|PubMed:1420817, ECO:0000269|PubMed:1429668,
CC ECO:0000269|PubMed:1672694, ECO:0000269|PubMed:1673047,
CC ECO:0000269|PubMed:1729889, ECO:0000269|PubMed:1761120,
CC ECO:0000269|PubMed:1832934, ECO:0000269|PubMed:1906179,
CC ECO:0000269|PubMed:2010538, ECO:0000269|PubMed:2011604,
CC ECO:0000269|PubMed:21592258, ECO:0000269|PubMed:2786201,
CC ECO:0000269|PubMed:7620154, ECO:0000269|PubMed:7734373,
CC ECO:0000269|PubMed:7789955, ECO:0000269|PubMed:8011991,
CC ECO:0000269|PubMed:8123843, ECO:0000269|PubMed:8123844,
CC ECO:0000269|PubMed:8338947, ECO:0000269|PubMed:8348943,
CC ECO:0000269|PubMed:8376405, ECO:0000269|PubMed:8435341,
CC ECO:0000269|PubMed:8486782, ECO:0000269|PubMed:8547152,
CC ECO:0000269|PubMed:8622978}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: von Willebrand disease 3 (VWD3) [MIM:277480]: A severe
CC hemorrhagic disorder due to a total or near total absence of von
CC Willebrand factor in the plasma and cellular compartments, also leading
CC to a profound deficiency of plasmatic factor VIII. Bleeding usually
CC starts in infancy and can include epistaxis, recurrent mucocutaneous
CC bleeding, excessive bleeding after minor trauma, and hemarthroses.
CC {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:7989040,
CC ECO:0000269|PubMed:8088787}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59512.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=vWF; Note=von Willebrand factor (vWF) mutation db;
CC URL="http://www.vwf.group.shef.ac.uk/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Von Willebrand factor entry;
CC URL="https://en.wikipedia.org/wiki/Von_Willebrand_factor";
CC ---------------------------------------------------------------------------
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DR EMBL; X04385; CAA27972.1; -; mRNA.
DR EMBL; M25865; AAB59458.1; -; Genomic_DNA.
DR EMBL; M25828; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25829; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25830; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25831; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25832; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25833; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25834; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25835; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25836; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25837; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25838; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25839; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25840; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25841; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25842; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25843; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25844; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25845; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25846; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25847; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25848; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25849; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25850; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25851; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25852; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25853; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25854; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25855; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25856; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25857; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25858; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25859; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25860; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25861; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25862; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25863; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; M25864; AAB59458.1; JOINED; Genomic_DNA.
DR EMBL; AC005845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88817.1; -; Genomic_DNA.
DR EMBL; BC022258; AAH22258.1; -; mRNA.
DR EMBL; X04146; CAA27765.1; -; mRNA.
DR EMBL; X06828; CAA29985.1; -; Genomic_DNA.
DR EMBL; X06829; CAA29985.1; JOINED; Genomic_DNA.
DR EMBL; M17588; AAA65940.1; -; mRNA.
DR EMBL; M10321; AAB59512.1; ALT_SEQ; mRNA.
DR EMBL; M60675; AAA61295.1; -; Genomic_DNA.
DR EMBL; U81237; AAB39987.1; -; mRNA.
DR EMBL; K03028; AAA61293.1; -; mRNA.
DR EMBL; X02672; CAA26503.1; -; mRNA.
DR EMBL; M16946; AAA61294.1; -; Genomic_DNA.
DR EMBL; M16945; AAA61294.1; JOINED; Genomic_DNA.
DR CCDS; CCDS8539.1; -. [P04275-1]
DR PIR; A34480; VWHU.
DR RefSeq; NP_000543.2; NM_000552.4. [P04275-1]
DR PDB; 1AO3; X-ray; 2.20 A; A/B=1686-1872.
DR PDB; 1ATZ; X-ray; 1.80 A; A/B=1685-1873.
DR PDB; 1AUQ; X-ray; 2.30 A; A=1261-1468.
DR PDB; 1FE8; X-ray; 2.03 A; A/B/C=1683-1874.
DR PDB; 1FNS; X-ray; 2.00 A; A=1271-1465.
DR PDB; 1IJB; X-ray; 1.80 A; A=1263-1464.
DR PDB; 1IJK; X-ray; 2.60 A; A=1263-1464.
DR PDB; 1M10; X-ray; 3.10 A; A=1261-1468.
DR PDB; 1OAK; X-ray; 2.20 A; A=1271-1465.
DR PDB; 1SQ0; X-ray; 2.60 A; A=1259-1471.
DR PDB; 1U0N; X-ray; 2.95 A; A=1261-1468.
DR PDB; 1UEX; X-ray; 2.85 A; C=1260-1468.
DR PDB; 2ADF; X-ray; 1.90 A; A=1683-1874.
DR PDB; 2MHP; NMR; -; A=766-864.
DR PDB; 2MHQ; NMR; -; A=766-864.
DR PDB; 3GXB; X-ray; 1.90 A; A/B=1495-1671.
DR PDB; 3HXO; X-ray; 2.40 A; A=1260-1468.
DR PDB; 3HXQ; X-ray; 2.69 A; A=1260-1468.
DR PDB; 3PPV; X-ray; 1.90 A; A=1488-1674.
DR PDB; 3PPW; X-ray; 1.90 A; A=1488-1674.
DR PDB; 3PPX; X-ray; 1.91 A; A=1488-1674.
DR PDB; 3PPY; X-ray; 2.00 A; A=1488-1674.
DR PDB; 3ZQK; X-ray; 1.70 A; A/B/C=1478-1674.
DR PDB; 4C29; X-ray; 2.20 A; A/B=1264-1471.
DR PDB; 4C2A; X-ray; 2.08 A; A=1264-1471.
DR PDB; 4C2B; X-ray; 2.80 A; A/C/E/G=1264-1471.
DR PDB; 4DMU; X-ray; 2.80 A; B/D/F/H/J/L=1683-1874.
DR PDB; 4NT5; X-ray; 3.28 A; A=2721-2813.
DR PDB; 5BV8; X-ray; 1.59 A; A=1238-1471.
DR PDB; 6FWN; NMR; -; A=2497-2577.
DR PDB; 6N29; X-ray; 2.50 A; A/B=764-1244.
DR PDB; 7EOW; X-ray; 1.60 A; A=1261-1468.
DR PDB; 7F49; X-ray; 2.09 A; A=1259-1468.
DR PDB; 7KWO; EM; 2.90 A; V=1-1256.
DR PDB; 7PMV; EM; 3.70 A; A/B/D/E=1-1241.
DR PDB; 7PNF; EM; 4.35 A; B/D=1-1241.
DR PDBsum; 1AO3; -.
DR PDBsum; 1ATZ; -.
DR PDBsum; 1AUQ; -.
DR PDBsum; 1FE8; -.
DR PDBsum; 1FNS; -.
DR PDBsum; 1IJB; -.
DR PDBsum; 1IJK; -.
DR PDBsum; 1M10; -.
DR PDBsum; 1OAK; -.
DR PDBsum; 1SQ0; -.
DR PDBsum; 1U0N; -.
DR PDBsum; 1UEX; -.
DR PDBsum; 2ADF; -.
DR PDBsum; 2MHP; -.
DR PDBsum; 2MHQ; -.
DR PDBsum; 3GXB; -.
DR PDBsum; 3HXO; -.
DR PDBsum; 3HXQ; -.
DR PDBsum; 3PPV; -.
DR PDBsum; 3PPW; -.
DR PDBsum; 3PPX; -.
DR PDBsum; 3PPY; -.
DR PDBsum; 3ZQK; -.
DR PDBsum; 4C29; -.
DR PDBsum; 4C2A; -.
DR PDBsum; 4C2B; -.
DR PDBsum; 4DMU; -.
DR PDBsum; 4NT5; -.
DR PDBsum; 5BV8; -.
DR PDBsum; 6FWN; -.
DR PDBsum; 6N29; -.
DR PDBsum; 7EOW; -.
DR PDBsum; 7F49; -.
DR PDBsum; 7KWO; -.
DR PDBsum; 7PMV; -.
DR PDBsum; 7PNF; -.
DR SASBDB; P04275; -.
DR SMR; P04275; -.
DR BioGRID; 113289; 24.
DR CORUM; P04275; -.
DR DIP; DIP-29667N; -.
DR ELM; P04275; -.
DR IntAct; P04275; 62.
DR MINT; P04275; -.
DR STRING; 9606.ENSP00000261405; -.
DR ChEMBL; CHEMBL2021748; -.
DR DrugBank; DB09329; Antihemophilic factor (recombinant), PEGylated.
DR DrugBank; DB00025; Antihemophilic factor, human recombinant.
DR DrugBank; DB06081; Caplacizumab.
DR DrugBank; DB11607; Efmoroctocog alfa.
DR DrugBank; DB05202; Egaptivon pegol.
DR DrugBank; DB13998; Lonoctocog alfa.
DR DrugBank; DB13999; Moroctocog alfa.
DR DrugBank; DB09108; Simoctocog alfa.
DR DrugBank; DB11606; Susoctocog alfa.
DR DrugBank; DB14738; Turoctocog alfa pegol.
DR DrugCentral; P04275; -.
DR MEROPS; I08.950; -.
DR MEROPS; I08.954; -.
DR GlyConnect; 627; 72 N-Linked glycans (12 sites), 2 O-Linked glycans.
DR GlyGen; P04275; 30 sites, 112 N-linked glycans (12 sites), 9 O-linked glycans (8 sites).
DR iPTMnet; P04275; -.
DR MetOSite; P04275; -.
DR PhosphoSitePlus; P04275; -.
DR SwissPalm; P04275; -.
DR BioMuta; VWF; -.
DR DMDM; 317373549; -.
DR jPOST; P04275; -.
DR MassIVE; P04275; -.
DR PaxDb; P04275; -.
DR PeptideAtlas; P04275; -.
DR PRIDE; P04275; -.
DR ProteomicsDB; 51696; -. [P04275-1]
DR ProteomicsDB; 74127; -.
DR ABCD; P04275; 56 sequenced antibodies.
DR Antibodypedia; 789; 2038 antibodies from 50 providers.
DR DNASU; 7450; -.
DR Ensembl; ENST00000261405.10; ENSP00000261405.5; ENSG00000110799.14. [P04275-1]
DR GeneID; 7450; -.
DR KEGG; hsa:7450; -.
DR MANE-Select; ENST00000261405.10; ENSP00000261405.5; NM_000552.5; NP_000543.3.
DR UCSC; uc001qnn.2; human. [P04275-1]
DR CTD; 7450; -.
DR DisGeNET; 7450; -.
DR GeneCards; VWF; -.
DR GeneReviews; VWF; -.
DR HGNC; HGNC:12726; VWF.
DR HPA; ENSG00000110799; Low tissue specificity.
DR MalaCards; VWF; -.
DR MIM; 193400; phenotype.
DR MIM; 277480; phenotype.
DR MIM; 613160; gene.
DR MIM; 613554; phenotype.
DR neXtProt; NX_P04275; -.
DR OpenTargets; ENSG00000110799; -.
DR Orphanet; 166078; Von Willebrand disease type 1.
DR Orphanet; 166084; Von Willebrand disease type 2A.
DR Orphanet; 166087; Von Willebrand disease type 2B.
DR Orphanet; 166090; Von Willebrand disease type 2M.
DR Orphanet; 166093; Von Willebrand disease type 2N.
DR Orphanet; 166096; Von Willebrand disease type 3.
DR PharmGKB; PA37337; -.
DR VEuPathDB; HostDB:ENSG00000110799; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000155810; -.
DR HOGENOM; CLU_000076_5_0_1; -.
DR InParanoid; P04275; -.
DR OMA; KFEACHH; -.
DR OrthoDB; 12226at2759; -.
DR PhylomeDB; P04275; -.
DR TreeFam; TF300299; -.
DR PathwayCommons; P04275; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR Reactome; R-HSA-9672391; Defective F8 cleavage by thrombin.
DR Reactome; R-HSA-9672393; Defective F8 binding to von Willebrand factor.
DR SignaLink; P04275; -.
DR SIGNOR; P04275; -.
DR BioGRID-ORCS; 7450; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; VWF; human.
DR EvolutionaryTrace; P04275; -.
DR GeneWiki; Von_Willebrand_factor; -.
DR GenomeRNAi; 7450; -.
DR Pharos; P04275; Tclin.
DR PRO; PR:P04275; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P04275; protein.
DR Bgee; ENSG00000110799; Expressed in urethra and 194 other tissues.
DR ExpressionAtlas; P04275; baseline and differential.
DR Genevisible; P04275; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031091; C:platelet alpha granule; NAS:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0033093; C:Weibel-Palade body; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019865; F:immunoglobulin binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0002020; F:protease binding; IDA:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:UniProtKB.
DR GO; GO:0007599; P:hemostasis; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IDA:ARUK-UCL.
DR GO; GO:0009611; P:response to wounding; TAS:UniProtKB.
DR DisProt; DP02981; -.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR037578; Von_Willebrand_factor.
DR InterPro; IPR032361; VWA_N2.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR11339:SF361; PTHR11339:SF361; 2.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF01826; TIL; 4.
DR Pfam; PF00092; VWA; 3.
DR Pfam; PF16164; VWA_N2; 1.
DR Pfam; PF00093; VWC; 3.
DR Pfam; PF00094; VWD; 4.
DR PIRSF; PIRSF002495; VWF; 1.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00327; VWA; 3.
DR SMART; SM00214; VWC; 5.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF53300; SSF53300; 3.
DR SUPFAM; SSF57567; SSF57567; 5.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS50234; VWFA; 3.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 3.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Cell adhesion;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hemostasis; Reference proteome; Repeat; Secreted; Signal;
KW von Willebrand disease.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3495266"
FT CHAIN 23..763
FT /note="von Willebrand antigen 2"
FT /id="PRO_0000022682"
FT CHAIN 764..2813
FT /note="von Willebrand factor"
FT /id="PRO_0000022683"
FT DOMAIN 33..201
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 295..348
FT /note="TIL 1"
FT DOMAIN 386..560
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 652..707
FT /note="TIL 2"
FT DOMAIN 776..827
FT /note="TIL 3"
FT DOMAIN 865..1032
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1146..1196
FT /note="TIL 4"
FT DOMAIN 1277..1453
FT /note="VWFA 1; binding site for platelet glycoprotein Ib"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1498..1665
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1691..1871
FT /note="VWFA 3; main binding site for collagens type I and
FT III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1948..2124
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2255..2328
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2429..2495
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2580..2645
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2724..2812
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 764..787
FT /note="Amino-terminal"
FT REGION 788..833
FT /note="E1"
FT REGION 826..853
FT /note="CX"
FT REGION 2216..2261
FT /note="E2"
FT MOTIF 2507..2509
FT /note="Cell attachment site"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT CARBOHYD 1231
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1248
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1255
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1256
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1263
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3524673"
FT CARBOHYD 1468
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1477
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1486
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1487
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1515
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 1574
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1679
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 2223
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 2298
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 2357
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 2400
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 2546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2585
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 2790
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 35..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 57..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 388..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 410..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 432..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 767..808
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 776..804
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 810..821
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 867..996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 889..1031
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 898..993
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 914..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 1060..1084
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1071..1111
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1089..1091
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1126..1130
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1149..1169
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1153..1165
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1196..1199
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1234..1237
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1272..1458
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1669..1670
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1686..1872
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1879..1904
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1899..1940
FT /note="Or C-1899 with C-1942"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039,
FT ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 1927..2088
FT /evidence="ECO:0000269|PubMed:3502076"
FT DISULFID 1950..2085
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 1972..2123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 1993..2001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:3502076"
FT DISULFID 2724..2774
FT /evidence="ECO:0000250"
FT DISULFID 2739..2788
FT /evidence="ECO:0000250"
FT DISULFID 2750..2804
FT /evidence="ECO:0000250"
FT DISULFID 2754..2806
FT /evidence="ECO:0000250"
FT DISULFID ?..2811
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..18
FT /note="MIPARFAGVLLALALILP -> MGAQDEEEGIQDLDGLLVFDKIVEVTLLNL
FT PWYNEETEGQRGEMTAPKSPRAKIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056527"
FT VAR_SEQ 220..314
FT /note="GLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEY
FT ARTCAQEGMVLYGWTDHSACSPVCPAGMEYRQCVSPCARTCQS -> EEPECNDITARL
FT QYVKVGSCKSEVEVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQVALHCTN
FT GSVVYHEVLNAMECKCSPRKCSKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056528"
FT VAR_SEQ 315..2813
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056529"
FT VARIANT 273
FT /note="R -> W (in VWD1 and VWD3; defect in secretion and
FT formation of multimers; dbSNP:rs61753997)"
FT /evidence="ECO:0000269|PubMed:10887119"
FT /id="VAR_010242"
FT VARIANT 318
FT /note="N -> K (in dbSNP:rs1800387)"
FT /id="VAR_057023"
FT VARIANT 377
FT /note="W -> C (in VWD3; dbSNP:rs62643626)"
FT /evidence="ECO:0000269|PubMed:7989040"
FT /id="VAR_005782"
FT VARIANT 471
FT /note="V -> I (in dbSNP:rs1800377)"
FT /evidence="ECO:0000269|PubMed:2584182"
FT /id="VAR_060591"
FT VARIANT 484
FT /note="H -> R (in dbSNP:rs1800378)"
FT /evidence="ECO:0000269|PubMed:3019665"
FT /id="VAR_024553"
FT VARIANT 528
FT /note="N -> S (in VWD2; dbSNP:rs61754010)"
FT /evidence="ECO:0000269|PubMed:8011991"
FT /id="VAR_005783"
FT VARIANT 550
FT /note="G -> R (in VWD2; dbSNP:rs61754011)"
FT /evidence="ECO:0000269|PubMed:7789955"
FT /id="VAR_005784"
FT VARIANT 740
FT /note="M -> I (in dbSNP:rs2228317)"
FT /id="VAR_057024"
FT VARIANT 788
FT /note="C -> Y (in VWD2; dbSNP:rs61748476)"
FT /id="VAR_009141"
FT VARIANT 789
FT /note="T -> A (in dbSNP:rs1063856)"
FT /evidence="ECO:0000269|PubMed:2864688"
FT /id="VAR_005785"
FT VARIANT 791
FT /note="T -> M (in VWD2; Normandy type; dbSNP:rs61748477)"
FT /evidence="ECO:0000269|PubMed:1906179"
FT /id="VAR_005786"
FT VARIANT 816
FT /note="R -> W (in VWD2; Normandy type; dbSNP:rs121964894)"
FT /evidence="ECO:0000269|PubMed:1832934"
FT /id="VAR_005787"
FT VARIANT 852
FT /note="Q -> R (in dbSNP:rs216321)"
FT /evidence="ECO:0000269|PubMed:2584182,
FT ECO:0000269|PubMed:2864688, ECO:0000269|PubMed:3019665,
FT ECO:0000269|PubMed:3488076, ECO:0000269|PubMed:3489923,
FT ECO:0000269|PubMed:3524673"
FT /id="VAR_005788"
FT VARIANT 854
FT /note="R -> Q (in VWD2; Normandy type; dbSNP:rs41276738)"
FT /evidence="ECO:0000269|PubMed:1832934"
FT /id="VAR_005789"
FT VARIANT 857
FT /note="N -> D"
FT /id="VAR_005790"
FT VARIANT 885
FT /note="F -> S (in dbSNP:rs11064002)"
FT /id="VAR_057025"
FT VARIANT 1060
FT /note="C -> R (in VWD2; dbSNP:rs61748497)"
FT /evidence="ECO:0000269|PubMed:12406074"
FT /id="VAR_028446"
FT VARIANT 1149
FT /note="C -> R (in VWD1; reduced secretion of homodimers and
FT heterodimers with wild type VWD and increased degradation
FT by the proteasome; dbSNP:rs61748511)"
FT /evidence="ECO:0000269|PubMed:11698279"
FT /id="VAR_064925"
FT VARIANT 1266
FT /note="P -> L (in VWD2; dbSNP:rs61749370)"
FT /evidence="ECO:0000269|PubMed:8486782"
FT /id="VAR_005791"
FT VARIANT 1268
FT /note="H -> D (in VWD2; dbSNP:rs61749371)"
FT /evidence="ECO:0000269|PubMed:8376405"
FT /id="VAR_005792"
FT VARIANT 1272
FT /note="C -> F (in VWD2; subtype 2A; dbSNP:rs63524161)"
FT /evidence="ECO:0000269|PubMed:21592258"
FT /id="VAR_067340"
FT VARIANT 1272
FT /note="C -> R (in VWD2; dbSNP:rs61749372)"
FT /evidence="ECO:0000269|PubMed:1419804"
FT /id="VAR_005793"
FT VARIANT 1306
FT /note="R -> W (in VWD2; dbSNP:rs61749384)"
FT /evidence="ECO:0000269|PubMed:1419803,
FT ECO:0000269|PubMed:1420817, ECO:0000269|PubMed:1672694,
FT ECO:0000269|PubMed:2010538"
FT /id="VAR_005794"
FT VARIANT 1308
FT /note="R -> C (in VWD2; dbSNP:rs61749387)"
FT /evidence="ECO:0000269|PubMed:1419803,
FT ECO:0000269|PubMed:1672694, ECO:0000269|PubMed:1761120,
FT ECO:0000269|PubMed:2010538"
FT /id="VAR_005795"
FT VARIANT 1313
FT /note="W -> C (in VWD2; dbSNP:rs61749392)"
FT /evidence="ECO:0000269|PubMed:2011604"
FT /id="VAR_005796"
FT VARIANT 1314
FT /note="V -> L (in VWD2; dbSNP:rs61749393)"
FT /evidence="ECO:0000269|PubMed:1419803"
FT /id="VAR_005797"
FT VARIANT 1316
FT /note="V -> M (in VWD2; dbSNP:rs61749397)"
FT /evidence="ECO:0000269|PubMed:1420817,
FT ECO:0000269|PubMed:1672694, ECO:0000269|PubMed:1729889"
FT /id="VAR_005798"
FT VARIANT 1318
FT /note="V -> L (in VWD2; dbSNP:rs372028373)"
FT /evidence="ECO:0000269|PubMed:1419803"
FT /id="VAR_005799"
FT VARIANT 1324
FT /note="G -> S (in VWD2; dbSNP:rs61749398)"
FT /evidence="ECO:0000269|PubMed:1409710"
FT /id="VAR_005800"
FT VARIANT 1341
FT /note="R -> Q (in VWD2; dbSNP:rs61749403)"
FT /evidence="ECO:0000269|PubMed:1672694"
FT /id="VAR_005801"
FT VARIANT 1374
FT /note="R -> C (in VWD2; dbSNP:rs61750071)"
FT /evidence="ECO:0000269|PubMed:7620154"
FT /id="VAR_005802"
FT VARIANT 1374
FT /note="R -> H (in VWD2; dbSNP:rs61750072)"
FT /evidence="ECO:0000269|PubMed:7620154,
FT ECO:0000269|PubMed:7734373"
FT /id="VAR_005803"
FT VARIANT 1381
FT /note="T -> A (in dbSNP:rs216311)"
FT /evidence="ECO:0000269|PubMed:1988024,
FT ECO:0000269|PubMed:2584182, ECO:0000269|PubMed:2864688,
FT ECO:0000269|PubMed:3019665, ECO:0000269|PubMed:3488076,
FT ECO:0000269|PubMed:3489923, ECO:0000269|PubMed:3524673,
FT ECO:0000269|PubMed:9373253"
FT /id="VAR_005804"
FT VARIANT 1399
FT /note="R -> H (in dbSNP:rs216312)"
FT /evidence="ECO:0000269|PubMed:1672694"
FT /id="VAR_005805"
FT VARIANT 1460
FT /note="L -> V (in VWD2; dbSNP:rs61750088)"
FT /evidence="ECO:0000269|PubMed:8123843"
FT /id="VAR_005806"
FT VARIANT 1461
FT /note="A -> V (in VWD2; dbSNP:rs61750089)"
FT /evidence="ECO:0000269|PubMed:8547152"
FT /id="VAR_005807"
FT VARIANT 1472
FT /note="D -> H (in dbSNP:rs1800383)"
FT /evidence="ECO:0000269|PubMed:1988024,
FT ECO:0000269|PubMed:2584182, ECO:0000269|PubMed:3489923"
FT /id="VAR_029656"
FT VARIANT 1514
FT /note="F -> C (in VWD2; dbSNP:rs61750101)"
FT /evidence="ECO:0000269|PubMed:8435341"
FT /id="VAR_005808"
FT VARIANT 1540
FT /note="L -> P (in VWD2; dbSNP:rs267607342)"
FT /evidence="ECO:0000269|PubMed:8123844"
FT /id="VAR_005809"
FT VARIANT 1565
FT /note="V -> L (in dbSNP:rs1800385)"
FT /id="VAR_014630"
FT VARIANT 1570
FT /note="Y -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036276"
FT VARIANT 1584
FT /note="Y -> C (exhibits increased in susceptibility to
FT proteolysis by ADAMTS13; dbSNP:rs1800386)"
FT /evidence="ECO:0000269|PubMed:15755288,
FT ECO:0000269|PubMed:8348943"
FT /id="VAR_005810"
FT VARIANT 1597
FT /note="R -> G (in VWD2; dbSNP:rs61750117)"
FT /evidence="ECO:0000269|PubMed:8348943"
FT /id="VAR_005811"
FT VARIANT 1597
FT /note="R -> Q (in VWD2; dbSNP:rs61750577)"
FT /evidence="ECO:0000269|PubMed:8338947"
FT /id="VAR_005812"
FT VARIANT 1597
FT /note="R -> W (in VWD2; dbSNP:rs61750117)"
FT /evidence="ECO:0000269|PubMed:2786201"
FT /id="VAR_005813"
FT VARIANT 1607
FT /note="V -> D (in VWD2; dbSNP:rs61750579)"
FT /evidence="ECO:0000269|PubMed:2786201"
FT /id="VAR_005814"
FT VARIANT 1609
FT /note="G -> R (in VWD2; dbSNP:rs61750580)"
FT /evidence="ECO:0000269|PubMed:8338947,
FT ECO:0000269|PubMed:8348943"
FT /id="VAR_005815"
FT VARIANT 1613
FT /note="S -> P (in VWD2; dbSNP:rs61750581)"
FT /evidence="ECO:0000269|PubMed:2010538"
FT /id="VAR_005816"
FT VARIANT 1628
FT /note="I -> T (in VWD2; dbSNP:rs61750584)"
FT /evidence="ECO:0000269|PubMed:1420817,
FT ECO:0000269|PubMed:1673047, ECO:0000269|PubMed:8123844"
FT /id="VAR_005817"
FT VARIANT 1638
FT /note="E -> K (in VWD2; dbSNP:rs61750588)"
FT /evidence="ECO:0000269|PubMed:1429668"
FT /id="VAR_005818"
FT VARIANT 1648
FT /note="P -> S (in VWD2; dbSNP:rs61750590)"
FT /evidence="ECO:0000269|PubMed:1420817"
FT /id="VAR_005819"
FT VARIANT 1665
FT /note="V -> E (in VWD2; dbSNP:rs61750596)"
FT /evidence="ECO:0000269|PubMed:8338947"
FT /id="VAR_005820"
FT VARIANT 2063
FT /note="P -> S (in VWD3; likely benign variant;
FT dbSNP:rs61750615)"
FT /id="VAR_009142"
FT VARIANT 2178
FT /note="A -> S (in dbSNP:rs34230288)"
FT /id="VAR_057026"
FT VARIANT 2185
FT /note="R -> Q (in dbSNP:rs2229446)"
FT /id="VAR_057027"
FT VARIANT 2362
FT /note="C -> F (in VWD3; dbSNP:rs61750630)"
FT /id="VAR_009143"
FT VARIANT 2546
FT /note="N -> Y (in VWD3; dbSNP:rs61751298)"
FT /id="VAR_009144"
FT VARIANT 2705
FT /note="G -> R (in dbSNP:rs7962217)"
FT /id="VAR_057028"
FT VARIANT 2739
FT /note="C -> Y (in VWD3; dbSNP:rs61751305)"
FT /evidence="ECO:0000269|PubMed:8088787"
FT /id="VAR_005821"
FT VARIANT 2773
FT /note="C -> R (in VWD2; dbSNP:rs61751310)"
FT /evidence="ECO:0000269|PubMed:8622978"
FT /id="VAR_005822"
FT MUTAGEN 1149
FT /note="C->R: Reduced secretion and increased intracellular
FT retention. Similar phenotype; when associated with S-1169."
FT /evidence="ECO:0000269|PubMed:11698279"
FT MUTAGEN 1169
FT /note="C->S: Reduced secretion and increased intracellular
FT retention. Similar phenotype; when associated with R-1149."
FT /evidence="ECO:0000269|PubMed:11698279"
FT CONFLICT 770
FT /note="P -> H (in Ref. 11; AAB59512)"
FT /evidence="ECO:0000305"
FT CONFLICT 804
FT /note="C -> S (in Ref. 10; AA sequence and 11; AAB59512)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="S -> T (in Ref. 1; CAA27972)"
FT /evidence="ECO:0000305"
FT CONFLICT 2168
FT /note="C -> S (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:2MHP"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 778..781
FT /evidence="ECO:0007829|PDB:7KWO"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:2MHP"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 818..823
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 824..826
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 841..844
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 847..852
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 855..858
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:6N29"
FT TURN 871..873
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 889..896
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 898..900
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 905..913
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 915..917
FT /evidence="ECO:0007829|PDB:7KWO"
FT HELIX 918..920
FT /evidence="ECO:0007829|PDB:7KWO"
FT STRAND 922..929
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 932..937
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 940..945
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 953..958
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 961..974
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 976..978
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 980..984
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 986..988
FT /evidence="ECO:0007829|PDB:6N29"
FT TURN 989..991
FT /evidence="ECO:0007829|PDB:7KWO"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1018..1023
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1029..1031
FT /evidence="ECO:0007829|PDB:7KWO"
FT HELIX 1044..1046
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1050..1060
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1061..1064
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1066..1074
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1078..1088
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1094..1096
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1098..1113
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1123..1126
FT /evidence="ECO:0007829|PDB:6N29"
FT TURN 1131..1133
FT /evidence="ECO:0007829|PDB:7KWO"
FT HELIX 1136..1138
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1143..1153
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1156..1158
FT /evidence="ECO:0007829|PDB:7KWO"
FT STRAND 1166..1176
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1182..1184
FT /evidence="ECO:0007829|PDB:6N29"
FT TURN 1185..1188
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1189..1191
FT /evidence="ECO:0007829|PDB:6N29"
FT HELIX 1193..1195
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1198..1201
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1204..1207
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1211..1215
FT /evidence="ECO:0007829|PDB:6N29"
FT TURN 1219..1221
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1223..1230
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1232..1236
FT /evidence="ECO:0007829|PDB:6N29"
FT STRAND 1267..1269
FT /evidence="ECO:0007829|PDB:5BV8"
FT TURN 1270..1273
FT /evidence="ECO:0007829|PDB:4C29"
FT STRAND 1276..1283
FT /evidence="ECO:0007829|PDB:5BV8"
FT STRAND 1285..1288
FT /evidence="ECO:0007829|PDB:4C2B"
FT HELIX 1290..1305
FT /evidence="ECO:0007829|PDB:5BV8"
FT TURN 1307..1310
FT /evidence="ECO:0007829|PDB:1SQ0"
FT STRAND 1313..1329
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1337..1345
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1357..1366
FT /evidence="ECO:0007829|PDB:5BV8"
FT STRAND 1369..1371
FT /evidence="ECO:0007829|PDB:5BV8"
FT STRAND 1377..1385
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1391..1393
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1394..1396
FT /evidence="ECO:0007829|PDB:1U0N"
FT HELIX 1397..1406
FT /evidence="ECO:0007829|PDB:5BV8"
FT STRAND 1409..1417
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1422..1431
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1433..1435
FT /evidence="ECO:0007829|PDB:4C29"
FT STRAND 1438..1442
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1443..1445
FT /evidence="ECO:0007829|PDB:5BV8"
FT HELIX 1446..1460
FT /evidence="ECO:0007829|PDB:5BV8"
FT STRAND 1498..1504
FT /evidence="ECO:0007829|PDB:3ZQK"
FT TURN 1507..1509
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1511..1527
FT /evidence="ECO:0007829|PDB:3ZQK"
FT STRAND 1534..1550
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1558..1567
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1578..1587
FT /evidence="ECO:0007829|PDB:3ZQK"
FT TURN 1588..1590
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1592..1594
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1595..1599
FT /evidence="ECO:0007829|PDB:3GXB"
FT STRAND 1602..1608
FT /evidence="ECO:0007829|PDB:3ZQK"
FT STRAND 1623..1631
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1636..1643
FT /evidence="ECO:0007829|PDB:3ZQK"
FT STRAND 1649..1652
FT /evidence="ECO:0007829|PDB:3ZQK"
FT TURN 1654..1656
FT /evidence="ECO:0007829|PDB:3ZQK"
FT HELIX 1657..1670
FT /evidence="ECO:0007829|PDB:3ZQK"
FT STRAND 1690..1697
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1699..1702
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1704..1720
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1727..1743
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1745..1747
FT /evidence="ECO:0007829|PDB:4DMU"
FT HELIX 1751..1759
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1770..1782
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1784..1786
FT /evidence="ECO:0007829|PDB:2ADF"
FT STRAND 1792..1800
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1809..1817
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1820..1831
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1833..1839
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1841..1847
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1849..1853
FT /evidence="ECO:0007829|PDB:1ATZ"
FT HELIX 1856..1862
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 1863..1865
FT /evidence="ECO:0007829|PDB:2ADF"
FT HELIX 1866..1870
FT /evidence="ECO:0007829|PDB:1ATZ"
FT STRAND 2497..2503
FT /evidence="ECO:0007829|PDB:6FWN"
FT TURN 2506..2508
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2511..2516
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2520..2522
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2524..2527
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2529..2536
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2539..2546
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2562..2565
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2568..2571
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2574..2577
FT /evidence="ECO:0007829|PDB:6FWN"
FT STRAND 2728..2732
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2739..2743
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2745..2749
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2756..2761
FT /evidence="ECO:0007829|PDB:4NT5"
FT TURN 2762..2765
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2766..2787
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2793..2801
FT /evidence="ECO:0007829|PDB:4NT5"
FT STRAND 2804..2809
FT /evidence="ECO:0007829|PDB:4NT5"
SQ SEQUENCE 2813 AA; 309265 MW; D5C1C78360917C29 CRC64;
MIPARFAGVL LALALILPGT LCAEGTRGRS STARCSLFGS DFVNTFDGSM YSFAGYCSYL
LAGGCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG TVTQGDQRVS MPYASKGLYL
ETEAGYYKLS GEAYGFVARI DGSGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFMTQEGTL
TSDPYDFANS WALSSGEQWC ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL
VDPEPFVALC EKTLCECAGG LECACPALLE YARTCAQEGM VLYGWTDHSA CSPVCPAGME
YRQCVSPCAR TCQSLHINEM CQERCVDGCS CPEGQLLDEG LCVESTECPC VHSGKRYPPG
TSLSRDCNTC ICRNSQWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCQD
HSFSIVIETV QCADDRDAVC TRSVTVRLPG LHNSLVKLKH GAGVAMDGQD VQLPLLKGDL
RIQHTVTASV RLSYGEDLQM DWDGRGRLLV KLSPVYAGKT CGLCGNYNGN QGDDFLTPSG
LAEPRVEDFG NAWKLHGDCQ DLQKQHSDPC ALNPRMTRFS EEACAVLTSP TFEACHRAVS
PLPYLRNCRY DVCSCSDGRE CLCGALASYA AACAGRGVRV AWREPGRCEL NCPKGQVYLQ
CGTPCNLTCR SLSYPDEECN EACLEGCFCP PGLYMDERGD CVPKAQCPCY YDGEIFQPED
IFSDHHTMCY CEDGFMHCTM SGVPGSLLPD AVLSSPLSHR SKRSLSCRPP MVKLVCPADN
LRAEGLECTK TCQNYDLECM SMGCVSGCLC PPGMVRHENR CVALERCPCF HQGKEYAPGE
TVKIGCNTCV CQDRKWNCTD HVCDATCSTI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS
NPGTFRILVG NKGCSHPSVK CKKRVTILVE GGEIELFDGE VNVKRPMKDE THFEVVESGR
YIILLLGKAL SVVWDRHLSI SVVLKQTYQE KVCGLCGNFD GIQNNDLTSS NLQVEEDPVD
FGNSWKVSSQ CADTRKVPLD SSPATCHNNI MKQTMVDSSC RILTSDVFQD CNKLVDPEPY
LDVCIYDTCS CESIGDCACF CDTIAAYAHV CAQHGKVVTW RTATLCPQSC EERNLRENGY
ECEWRYNSCA PACQVTCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC VDPEDCPVCE
VAGRRFASGK KVTLNPSDPE HCQICHCDVV NLTCEACQEP GGLVVPPTDA PVSPTTLYVE
DISEPPLHDF YCSRLLDLVF LLDGSSRLSE AEFEVLKAFV VDMMERLRIS QKWVRVAVVE
YHDGSHAYIG LKDRKRPSEL RRIASQVKYA GSQVASTSEV LKYTLFQIFS KIDRPEASRI
TLLLMASQEP QRMSRNFVRY VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL
SSVDELEQQR DEIVSYLCDL APEAPPPTLP PDMAQVTVGP GLLGVSTLGP KRNSMVLDVA
FVLEGSDKIG EADFNRSKEF MEEVIQRMDV GQDSIHVTVL QYSYMVTVEY PFSEAQSKGD
ILQRVREIRY QGGNRTNTGL ALRYLSDHSF LVSQGDREQA PNLVYMVTGN PASDEIKRLP
GDIQVVPIGV GPNANVQELE RIGWPNAPIL IQDFETLPRE APDLVLQRCC SGEGLQIPTL
SPAPDCSQPL DVILLLDGSS SFPASYFDEM KSFAKAFISK ANIGPRLTQV SVLQYGSITT
IDVPWNVVPE KAHLLSLVDV MQREGGPSQI GDALGFAVRY LTSEMHGARP GASKAVVILV
TDVSVDSVDA AADAARSNRV TVFPIGIGDR YDAAQLRILA GPAGDSNVVK LQRIEDLPTM
VTLGNSFLHK LCSGFVRICM DEDGNEKRPG DVWTLPDQCH TVTCQPDGQT LLKSHRVNCD
RGLRPSCPNS QSPVKVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVLFQNK
EQDLEVILHN GACSPGARQG CMKSIEVKHS ALSVELHSDM EVTVNGRLVS VPYVGGNMEV
NVYGAIMHEV RFNHLGHIFT FTPQNNEFQL QLSPKTFASK TYGLCGICDE NGANDFMLRD
GTVTTDWKTL VQEWTVQRPG QTCQPILEEQ CLVPDSSHCQ VLLLPLFAEC HKVLAPATFY
AICQQDSCHQ EQVCEVIASY AHLCRTNGVC VDWRTPDFCA MSCPPSLVYN HCEHGCPRHC
DGNVSSCGDH PSEGCFCPPD KVMLEGSCVP EEACTQCIGE DGVQHQFLEA WVPDHQPCQI
CTCLSGRKVN CTTQPCPTAK APTCGLCEVA RLRQNADQCC PEYECVCDPV SCDLPPVPHC
ERGLQPTLTN PGECRPNFTC ACRKEECKRV SPPSCPPHRL PTLRKTQCCD EYECACNCVN
STVSCPLGYL ASTATNDCGC TTTTCLPDKV CVHRSTIYPV GQFWEEGCDV CTCTDMEDAV
MGLRVAQCSQ KPCEDSCRSG FTYVLHEGEC CGRCLPSACE VVTGSPRGDS QSSWKSVGSQ
WASPENPCLI NECVRVKEEV FIQQRNVSCP QLEVPVCPSG FQLSCKTSAC CPSCRCERME
ACMLNGTVIG PGKTVMIDVC TTCRCMVQVG VISGFKLECR KTTCNPCPLG YKEENNTGEC
CGRCLPTACT IQLRGGQIMT LKRDETLQDG CDTHFCKVNE RGEYFWEKRV TGCPPFDEHK
CLAEGGKIMK IPGTCCDTCE EPECNDITAR LQYVKVGSCK SEVEVDIHYC QGKCASKAMY
SIDINDVQDQ CSCCSPTRTE PMQVALHCTN GSVVYHEVLN AMECKCSPRK CSK
