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 24-JAN-2024, entry version 270. 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://vwf.hemobase.com/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Von Willebrand factor entry; CC URL="https://en.wikipedia.org/wiki/Von_Willebrand_factor"; 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; 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; 7P4N; NMR; -; A=2647-2720. 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 PDB; 7ZWH; EM; 3.20 A; D/E=1-1197, G/H=1265-1463. DR PDB; 8D3C; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-1464. DR PDB; 8D3D; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-1464. 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; 7P4N; -. DR PDBsum; 7PMV; -. DR PDBsum; 7PNF; -. DR PDBsum; 7ZWH; -. DR PDBsum; 8D3C; -. DR PDBsum; 8D3D; -. DR EMDB; EMD-13541; -. DR EMDB; EMD-13547; -. DR EMDB; EMD-14998; -. DR EMDB; EMD-23057; -. DR EMDB; EMD-27156; -. DR EMDB; EMD-27157; -. DR EMDB; EMD-27158; -. DR EMDB; EMD-32620; -. DR EMDB; EMD-32621; -. DR EMDB; EMD-32622; -. DR EMDB; EMD-32687; -. DR EMDB; EMD-32688; -. DR EMDB; EMD-32689; -. DR EMDB; EMD-32690; -. DR EMDB; EMD-32713; -. DR SASBDB; P04275; -. DR SMR; P04275; -. DR BioGRID; 113289; 26. DR CORUM; P04275; -. DR DIP; DIP-29667N; -. DR ELM; P04275; -. DR IntAct; P04275; 63. 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; DB16007; Rurioctocog alfa pegol. 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 GlyCosmos; P04275; 28 sites, 120 glycans. DR GlyGen; P04275; 30 sites, 112 N-linked glycans (12 sites), 10 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; 9606-ENSP00000261405; -. DR PeptideAtlas; P04275; -. DR ProteomicsDB; 51696; -. [P04275-1] DR ProteomicsDB; 74127; -. DR ABCD; P04275; 56 sequenced antibodies. DR Antibodypedia; 789; 2353 antibodies from 51 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 AGR; HGNC:12726; -. 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; 2872912at2759; -. DR PhylomeDB; P04275; -. DR TreeFam; TF300299; -. DR BioCyc; MetaCyc:ENSG00000110799-MONOMER; -. 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 1161 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 196 other cell types or tissues. DR ExpressionAtlas; P04275; baseline and differential. 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: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:0051087; F:protein-folding chaperone binding; IDA: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 CDD; cd19941; TIL; 5. DR CDD; cd01450; vWFA_subfamily_ECM; 3. DR DisProt; DP02981; -. DR Gene3D; 2.10.25.10; Laminin; 5. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR036084; Ser_inhib-like_sf. DR InterPro; IPR002919; TIL_dom. DR InterPro; IPR037578; Von_Willebrand_factor. DR InterPro; IPR032361; VWA_N2. DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom. 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; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1. DR PANTHER; PTHR11339:SF361; VON WILLEBRAND FACTOR; 1. DR Pfam; PF08742; C8; 4. DR Pfam; PF01826; TIL; 3. DR Pfam; PF00092; VWA; 3. DR Pfam; PF16164; VWA_N2; 1. DR Pfam; PF00093; VWC; 2. DR Pfam; PF00094; VWD; 4. DR PIRSF; PIRSF002495; VWF; 1. DR PRINTS; PR00453; VWFADOMAIN. 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; SSF57603; FnI-like domain; 1. DR SUPFAM; SSF57567; Serine protease inhibitors; 5. DR SUPFAM; SSF53300; vWA-like; 3. 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. DR Genevisible; P04275; HS. 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:rs1800382)" 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; 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 TURN 39..41 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 69..77 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 80..88 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 119..131 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 224..229 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 244..256 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 265..278 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 333..337 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 410..413 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 439..444 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 449..451 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 486..488 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 532..535 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 546..552 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 554..556 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 577..584 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 585..588 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 593..596 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 602..614 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 615..617 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 618..636 FT /evidence="ECO:0007829|PDB:7ZWH" FT TURN 645..647 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 665..667 FT /evidence="ECO:0007829|PDB:7ZWH" FT HELIX 669..673 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 697..699 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 722..724 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 727..732 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 735..739 FT /evidence="ECO:0007829|PDB:7ZWH" FT STRAND 769..771 FT /evidence="ECO:0007829|PDB:7ZWH" 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:7ZWH" 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 1089..1091 FT /evidence="ECO:0007829|PDB:7ZWH" 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 1179..1181 FT /evidence="ECO:0007829|PDB:7ZWH" 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 2648..2653 FT /evidence="ECO:0007829|PDB:7P4N" FT TURN 2654..2656 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2657..2661 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2669..2678 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2684..2689 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2698..2702 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2708..2710 FT /evidence="ECO:0007829|PDB:7P4N" FT STRAND 2717..2719 FT /evidence="ECO:0007829|PDB:7P4N" 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 //