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 11-NOV-2015, entry version 210. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-852; ALA-1381 RP AND 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., RA 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; RP ALA-1381 AND HIS-1472. RX PubMed=2584182; 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., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA 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., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA 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., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP ARG-484; ARG-852 AND ALA-1381. RX PubMed=3019665; RA Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.; RT "Full-length von Willebrand factor (vWF) cDNA encodes a highly RT repetitive protein considerably larger than the mature vWF subunit."; RL EMBO J. 5:1839-1847(1986). RN [7] RP ERRATUM. 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 RP OF 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 RT polymorphisms, repeated domains, and relationship to von Willebrand RT 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 RT Willebrand 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., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric 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 RP ARG-852 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 RP AND 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 RT and differentiation by polymerase chain reaction."; RL Biochemistry 30:253-269(1991). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1236-1476 (ISOFORM 1), AND VARIANT RP ALA-1381. RX PubMed=9373253; RA Schulte am Esch J. II, Cruz M.A., Siegel J.B., Anrather J., RA Robson S.C.; RT "Activation of human platelets by the membrane-expressed A1 domain of RT von 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 RT (cDNA) 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., RA Ling E.H., Livingston D.M.; RT "Molecular cloning of cDNA for human von Willebrand factor: RT authentication 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 RT antibody probes for colony-screening and mapping of the chromosomal RT 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 RT 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1720. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [27] 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [28] 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., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [29] 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 RT implications for the binding of platelet glycoprotein Ib."; RL J. Biol. Chem. 273:10396-10401(1998). RN [30] 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 [31] 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- RT dependent adhesion site motif."; RL J. Biol. Chem. 272:25162-25167(1997). RN [32] 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 [33] 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., RA Bockenstedt P.L., Johnson T.A., Yang A.Y.; RT "Molecular basis of human von Willebrand disease: analysis of platelet RT von Willebrand factor mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 86:3723-3727(1989). RN [34] RP VARIANT VWD2 THR-1628. RX PubMed=1673047; RA Iannuzzi M.C., Hidaka N., Boehnke M., Bruck M.E., Hanna W.T., RA Collins F.S., Ginsburg D.; RT "Analysis of the relationship of von Willebrand disease (vWD) and RT hereditary hemorrhagic telangiectasia and identification of a RT potential type IIA vWD mutation (IIe865 to Thr)."; RL Am. J. Hum. Genet. 48:757-763(1991). RN [35] 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 RT gene of three families with the 'Normandy' variant of von Willebrand RT disease."; RL Br. J. Haematol. 78:506-514(1991). RN [36] RP VARIANT VWD2 CYS-1308. RX PubMed=1761120; 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 RT in type IIB von Willebrand's disease."; RL Eur. J. Haematol. 47:342-345(1991). RN [37] 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 RT mutations cluster in one disulfide loop between proposed platelet RT glycoprotein Ib binding sequences."; RL J. Clin. Invest. 87:1220-1226(1991). RN [38] 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. RT Identification of four potential missense mutations within the RT putative GpIb binding domain."; RL J. Clin. Invest. 87:1227-1233(1991). RN [39] 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 [40] 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., RA Mazurier C.; RT "Expression of von Willebrand factor 'Normandy': an autosomal mutation RT that mimics hemophilia A."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6377-6381(1991). RN [41] 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 RT residue 553 in the glycoprotein Ib-binding domain of von Willebrand RT factor, causing type IIB von Willebrand disease."; RL Am. J. Hum. Genet. 50:199-207(1992). RN [42] 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 RT potential mutations in patients with type IIA and type IIB."; RL Blood Coagul. Fibrinolysis 3:415-421(1992). RN [43] 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 [44] 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., RA Fressinaud E., Meyer D., Pietu G.; RT "Defects in type IIA von Willebrand disease: a cysteine 509 to RT arginine substitution in the mature von Willebrand factor disrupts a RT disulphide loop involved in the interaction with platelet glycoprotein RT Ib-IX."; RL Br. J. Haematol. 82:66-72(1992). RN [45] RP VARIANT VWD2 LYS-1638. RX PubMed=1429668; RA Ribba A.S., Voorberg J., Meyer D., Pannekoek H., Pietu G.; RT "Characterization of recombinant von Willebrand factor corresponding RT to mutations in type IIA and type IIB von Willebrand disease."; RL J. Biol. Chem. 267:23209-23215(1992). RN [46] 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 RT abolishes ristocetin-induced von Willebrand factor binding to platelet RT glycoprotein Ib."; RL Proc. Natl. Acad. Sci. U.S.A. 89:9846-9849(1992). RN [47] 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 [48] 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 RT Willebrand factor is a novel candidate mutation in a family with type RT IIA von Willebrand disease."; RL Br. J. Haematol. 83:94-99(1993). RN [49] 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 RT the A2 region of the von Willebrand factor."; RL Eur. J. Haematol. 51:38-44(1993). RN [50] RP VARIANT VWD2 ASP-1268. RX PubMed=8376405; 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 RT control of von Willebrand factor binding to platelet glycoprotein RT Ib."; RL J. Biol. Chem. 268:20497-20501(1993). RN [51] RP VARIANT VWD2 LEU-1266. RX PubMed=8486782; DOI=10.1172/JCI116443; RA Holmberg L., Dent J.A., Schneppenheim R., Budde U., Ware J., RA Ruggeri Z.M.; RT "von Willebrand factor mutation enhancing interaction with platelets RT in patients with normal multimeric structure."; RL J. Clin. Invest. 91:2169-2177(1993). RN [52] RP VARIANT VWD2 VAL-1460. RX PubMed=8123843; RA Hilbert L., Gaucher C., de Romeuf C., Horellou M.H., Vink T., RA Mazurier C.; RT "Leu 697-->Val mutation in mature von Willebrand factor is responsible RT for type IIB von Willebrand disease."; RL Blood 83:1542-1550(1994). RN [53] 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 [54] 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 RT Willebrand disease type III patients from 24 families of Swedish and RT Finnish origin."; RL Genomics 21:188-193(1994). RN [55] 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., RA Simeoni E.; RT "Genetic heterogeneity of severe von Willebrand disease type III in RT the German population."; RL Hum. Genet. 94:640-652(1994). RN [56] 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 [57] 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 RT loop of von Willebrand factor (vWF) responsible for type 2 von RT Willebrand disease with decreased platelet-dependent function of RT vWF."; RL Blood 86:1010-1018(1995). RN [58] 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 RT discordant' von Willebrand's disease with desmopressin-induced RT thrombocytopenia."; RL Br. J. Haematol. 89:656-658(1995). RN [59] 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- RT proline 708 segment of recombinant von Willebrand factor."; RL Br. J. Haematol. 91:983-990(1995). RN [60] RP VARIANT VWD2 ARG-550. RX PubMed=7789955; DOI=10.1007/BF00209487; RA Schneppenheim R., Thomas K.B., Krey S., Budde U., Jessat U., RA Sutor A.H., 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 [61] 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 RT Cys-> Arg mutation in type IID von Willebrand disease."; RL Proc. Natl. Acad. Sci. U.S.A. 93:3581-3586(1996). RN [62] 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., RA Ingerslev J., Goodeve A.C., Peake I.R., Daly M.E.; RT "A novel von Willebrand disease-causing mutation (Arg273Trp) in the RT von Willebrand factor propeptide that results in defective RT multimerization and secretion."; RL Blood 96:560-568(2000). RN [63] 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 RT intracellular retention and degradation of heterodimers: a possible RT general mechanism for dominant mutations of oligomeric proteins."; RL Blood 98:2973-2979(2001). RN [64] 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., RA 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 [65] 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., RA Grundy P., Enayat S.M., Bolton-Maggs P.H., Keeling D.M., Khair K., RA Tait R.C., Wilde J.T., Pasi K.J., Hill F.G.; RT "The prevalence of the cysteine1584 variant of von Willebrand factor RT is increased in type 1 von Willebrand disease: co-segregation with RT increased susceptibility to ADAMTS13 proteolysis but not clinical RT phenotype."; RL Br. J. Haematol. 128:830-836(2005). RN [66] 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [67] 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., RA Lazzari M.A.; RT "C1272F: a novel type 2A von Willebrand's disease mutation in A1 RT domain; 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 CC platelet-surface receptor complex GPIb-IX-V. Also acts as a CC chaperone for coagulation factor VIII, delivering it to the site CC of injury, stabilizing its heterodimeric structure and protecting CC it from premature clearance from plasma. CC -!- SUBUNIT: Multimeric. Interacts with F8. CC {ECO:0000269|PubMed:10961880, ECO:0000269|PubMed:9218428}. CC -!- INTERACTION: CC Self; NbExp=15; IntAct=EBI-981819, EBI-981819; CC Q76LX8:ADAMTS13; NbExp=5; IntAct=EBI-981819, EBI-981764; CC P07359:GP1BA; NbExp=2; IntAct=EBI-981819, EBI-297082; CC Q96CV9:OPTN; NbExp=2; IntAct=EBI-981819, EBI-748974; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. CC Secreted, 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The von Willebrand antigen 2 is required for CC multimerization of vWF and for its targeting to storage granules. CC -!- PTM: All cysteine residues are involved in intrachain or CC interchain 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 CC protein and resulting in impaired platelet aggregation. Von CC Willebrand disease type 1 is characterized by partial quantitative CC deficiency of circulating von Willebrand factor, that is otherwise CC structurally and functionally normal. Clinical manifestations are CC mucocutaneous bleeding, such as epistaxis and menorrhagia, and CC prolonged bleeding after surgery or trauma. CC {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:11698279}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: von Willebrand disease 2 (VWD2) [MIM:613554]: A CC hemorrhagic disorder due to defects in von Willebrand factor CC protein and resulting in altered platelet aggregation. Von CC Willebrand disease type 2 is characterized by qualitative CC deficiency and functional anomalies of von Willebrand factor. It CC is divided in different subtypes including 2A, 2B, 2M and 2N CC (Normandy variant). The mutant VWF protein in types 2A, 2B and 2M CC are defective in their platelet-dependent function, whereas the CC mutant protein in type 2N is defective in its ability to bind CC factor VIII. Clinical manifestations are mucocutaneous bleeding, CC such as epistaxis and menorrhagia, and prolonged bleeding after CC surgery or trauma. {ECO:0000269|PubMed:12406074, CC ECO:0000269|PubMed:1409710, ECO:0000269|PubMed:1419803, CC ECO:0000269|PubMed:1419804, ECO:0000269|PubMed:1420817, CC ECO:0000269|PubMed:1429668, ECO:0000269|PubMed:1672694, CC ECO:0000269|PubMed:1673047, ECO:0000269|PubMed:1729889, CC ECO:0000269|PubMed:1761120, ECO:0000269|PubMed:1832934, CC ECO:0000269|PubMed:1906179, ECO:0000269|PubMed:2010538, CC ECO:0000269|PubMed:2011604, ECO:0000269|PubMed:21592258, CC ECO:0000269|PubMed:2786201, ECO:0000269|PubMed:7620154, CC ECO:0000269|PubMed:7734373, ECO:0000269|PubMed:7789955, CC ECO:0000269|PubMed:8011991, ECO:0000269|PubMed:8123843, CC ECO:0000269|PubMed:8123844, ECO:0000269|PubMed:8338947, CC ECO:0000269|PubMed:8348943, ECO:0000269|PubMed:8376405, CC ECO:0000269|PubMed:8435341, ECO:0000269|PubMed:8486782, CC ECO:0000269|PubMed:8547152, ECO:0000269|PubMed:8622978}. Note=The CC disease is caused by mutations affecting the gene represented in CC 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 CC leading to a profound deficiency of plasmatic factor VIII. CC Bleeding usually starts in infancy and can include epistaxis, CC recurrent mucocutaneous bleeding, excessive bleeding after minor CC trauma, and hemarthroses. {ECO:0000269|PubMed:10887119, CC ECO:0000269|PubMed:7989040, ECO:0000269|PubMed:8088787}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00039}. CC -!- SIMILARITY: Contains 4 TIL (trypsin inhibitory-like) domains. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 3 VWFA domains. {ECO:0000255|PROSITE- CC ProRule:PRU00219}. CC -!- SIMILARITY: Contains 3 VWFC domains. {ECO:0000255|PROSITE- CC ProRule:PRU00220}. CC -!- SIMILARITY: Contains 4 VWFD domains. {ECO:0000255|PROSITE- CC ProRule:PRU00580}. 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 CC 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 --------------------------------------------------------------------------- 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_000552.3. DR UniGene; Hs.440848; -. 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 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 ProteinModelPortal; P04275; -. DR SMR; P04275; 766-864, 1261-1468, 1495-1671, 1685-1873, 2721-2813. DR BioGrid; 113289; 14. DR DIP; DIP-29667N; -. DR IntAct; P04275; 49. DR MINT; MINT-244925; -. DR STRING; 9606.ENSP00000261405; -. DR ChEMBL; CHEMBL2021748; -. DR DrugBank; DB00025; Antihemophilic Factor. DR MEROPS; I08.950; -. DR PhosphoSite; P04275; -. DR UniCarbKB; P04275; -. DR BioMuta; VWF; -. DR DMDM; 317373549; -. DR PaxDb; P04275; -. DR PRIDE; P04275; -. DR Ensembl; ENST00000261405; ENSP00000261405; ENSG00000110799. [P04275-1] DR GeneID; 7450; -. DR KEGG; hsa:7450; -. DR UCSC; uc001qnn.1; human. [P04275-1] DR UCSC; uc001qno.1; human. DR CTD; 7450; -. DR GeneCards; VWF; -. DR GeneReviews; VWF; -. DR H-InvDB; HIX0010356; -. DR H-InvDB; HIX0171640; -. DR HGNC; HGNC:12726; VWF. DR HPA; CAB001694; -. DR HPA; HPA001815; -. DR HPA; HPA002082; -. DR MIM; 193400; phenotype. DR MIM; 277480; phenotype. DR MIM; 613160; gene. DR MIM; 613554; phenotype. DR neXtProt; NX_P04275; -. 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 eggNOG; ENOG410IR8A; Eukaryota. DR eggNOG; ENOG41100RZ; LUCA. DR GeneTree; ENSGT00760000118896; -. DR HOGENOM; HOG000169747; -. DR HOVERGEN; HBG004380; -. DR InParanoid; P04275; -. DR KO; K03900; -. DR OMA; ECCGRCL; -. DR OrthoDB; EOG73V6J9; -. DR PhylomeDB; P04275; -. DR TreeFam; TF300299; -. 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 alphaIIb beta3 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-75892; Platelet Adhesion to exposed collagen. DR ChiTaRS; VWF; human. DR EvolutionaryTrace; P04275; -. DR GeneWiki; Von_Willebrand_factor; -. DR GenomeRNAi; 7450; -. DR NextBio; 29172; -. DR PRO; PR:P04275; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P04275; -. DR CleanEx; HS_VWF; -. DR ExpressionAtlas; P04275; baseline and differential. DR Genevisible; P04275; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0031091; C:platelet alpha granule; NAS:UniProtKB. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. 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:0001948; F:glycoprotein binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0007596; P:blood coagulation; IMP:UniProtKB. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0031589; P:cell-substrate adhesion; IDA:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007599; P:hemostasis; IMP:UniProtKB. DR GO; GO:0030168; P:platelet activation; IDA:UniProtKB. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0009611; P:response to wounding; TAS:UniProtKB. DR Gene3D; 3.40.50.410; -; 3. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR002919; TIL_dom. DR InterPro; IPR014853; Unchr_dom_Cys-rich. DR InterPro; IPR032361; VWA_N2. DR InterPro; IPR012011; VWF. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR001007; VWF_dom. DR InterPro; IPR001846; VWF_type-D. DR PANTHER; PTHR11339:SF259; PTHR11339:SF259; 4. DR Pfam; PF08742; C8; 4. DR Pfam; PF01826; TIL; 5. DR Pfam; PF00092; VWA; 3. DR Pfam; PF16164; VWA_N2; 1. DR Pfam; PF00093; VWC; 3. DR Pfam; PF00094; VWD; 4. DR SMART; SM00832; C8; 4. DR SMART; SM00041; CT; 1. DR SMART; SM00327; VWA; 3. DR SMART; SM00214; VWC; 5. 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; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Extracellular matrix; Glycoprotein; Hemostasis; Isopeptide bond; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal; KW Ubl conjugation; von Willebrand disease. FT SIGNAL 1 22 {ECO:0000269|PubMed:3495266}. FT CHAIN 23 763 von Willebrand antigen 2. FT /FTId=PRO_0000022682. FT CHAIN 764 2813 von Willebrand factor. FT /FTId=PRO_0000022683. FT DOMAIN 34 240 VWFD 1. {ECO:0000255|PROSITE- FT ProRule:PRU00580}. FT DOMAIN 295 348 TIL 1. FT DOMAIN 387 598 VWFD 2. {ECO:0000255|PROSITE- FT ProRule:PRU00580}. FT DOMAIN 652 707 TIL 2. FT DOMAIN 776 827 TIL 3. FT DOMAIN 866 1074 VWFD 3. {ECO:0000255|PROSITE- FT ProRule:PRU00580}. FT DOMAIN 1146 1196 TIL 4. FT DOMAIN 1277 1453 VWFA 1; binding site for platelet FT glycoprotein Ib. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT DOMAIN 1498 1665 VWFA 2. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT DOMAIN 1691 1871 VWFA 3; main binding site for collagens FT type I and III. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT DOMAIN 1949 2153 VWFD 4. {ECO:0000255|PROSITE- FT ProRule:PRU00580}. FT DOMAIN 2255 2328 VWFC 1. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 2429 2495 VWFC 2. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 2580 2645 VWFC 3. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 2724 2812 CTCK. {ECO:0000255|PROSITE- FT ProRule:PRU00039}. FT REGION 764 787 Amino-terminal. FT REGION 788 833 E1. FT REGION 826 853 CX. FT REGION 2216 2261 E2. FT MOTIF 2507 2509 Cell attachment site. FT CARBOHYD 99 99 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 156 156 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 211 211 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 666 666 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 857 857 N-linked (GlcNAc...). FT CARBOHYD 1147 1147 N-linked (GlcNAc...); atypical. FT CARBOHYD 1231 1231 N-linked (GlcNAc...). FT CARBOHYD 1248 1248 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1255 1255 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1256 1256 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1263 1263 O-linked (GalNAc...). FT {ECO:0000269|PubMed:3524673}. FT CARBOHYD 1468 1468 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1477 1477 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1486 1486 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1487 1487 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 1515 1515 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:19139490}. FT CARBOHYD 1574 1574 N-linked (GlcNAc...). FT CARBOHYD 1679 1679 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 2223 2223 N-linked (GlcNAc...). FT CARBOHYD 2290 2290 N-linked (GlcNAc...). FT CARBOHYD 2298 2298 O-linked (GalNAc...). {ECO:0000305}. FT CARBOHYD 2357 2357 N-linked (GlcNAc...). FT CARBOHYD 2400 2400 N-linked (GlcNAc...). FT CARBOHYD 2546 2546 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2585 2585 N-linked (GlcNAc...). FT CARBOHYD 2790 2790 N-linked (GlcNAc...). FT DISULFID 767 808 {ECO:0000269|PubMed:3502076}. FT DISULFID 776 804 {ECO:0000269|PubMed:3502076}. FT DISULFID 810 821 {ECO:0000269|PubMed:3502076}. FT DISULFID 867 996 {ECO:0000269|PubMed:3502076}. FT DISULFID 889 1031 {ECO:0000269|PubMed:3502076}. FT DISULFID 898 993 {ECO:0000269|PubMed:3502076}. FT DISULFID 914 921 {ECO:0000269|PubMed:3502076}. FT DISULFID 1060 1084 {ECO:0000269|PubMed:3502076}. FT DISULFID 1071 1111 {ECO:0000269|PubMed:3502076}. FT DISULFID 1089 1091 {ECO:0000269|PubMed:3502076}. FT DISULFID 1126 1130 {ECO:0000269|PubMed:3502076}. FT DISULFID 1149 1169 {ECO:0000269|PubMed:3502076}. FT DISULFID 1153 1165 {ECO:0000269|PubMed:3502076}. FT DISULFID 1196 1199 {ECO:0000269|PubMed:3502076}. FT DISULFID 1234 1237 {ECO:0000269|PubMed:3502076}. FT DISULFID 1272 1458 {ECO:0000269|PubMed:3502076}. FT DISULFID 1669 1670 {ECO:0000269|PubMed:3502076}. FT DISULFID 1686 1872 {ECO:0000269|PubMed:3502076}. FT DISULFID 1879 1904 {ECO:0000269|PubMed:3502076}. FT DISULFID 1899 1940 Or C-1899 with C-1942. FT {ECO:0000255|PROSITE-ProRule:PRU00039, FT ECO:0000255|PROSITE-ProRule:PRU00580, FT ECO:0000269|PubMed:3502076}. FT DISULFID 1927 2088 {ECO:0000269|PubMed:3502076}. FT DISULFID 1950 2085 {ECO:0000269|PubMed:3502076}. FT DISULFID 1972 2123 {ECO:0000269|PubMed:3502076}. FT DISULFID 1993 2001 {ECO:0000269|PubMed:3502076}. FT DISULFID 2724 2774 {ECO:0000250}. FT DISULFID 2739 2788 {ECO:0000250}. FT DISULFID 2750 2804 {ECO:0000250}. FT DISULFID 2754 2806 {ECO:0000250}. FT DISULFID ? 2811 {ECO:0000250}. FT CROSSLNK 1720 1720 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000269|PubMed:17370265}. FT VAR_SEQ 1 18 MIPARFAGVLLALALILP -> MGAQDEEEGIQDLDGLLVF FT DKIVEVTLLNLPWYNEETEGQRGEMTAPKSPRAKIR (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056527. FT VAR_SEQ 220 314 GLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGG FT LECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEY FT RQCVSPCARTCQS -> EEPECNDITARLQYVKVGSCKSEV FT EVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQV FT ALHCTNGSVVYHEVLNAMECKCSPRKCSKI (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056528. FT VAR_SEQ 315 2813 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056529. FT VARIANT 273 273 R -> W (in VWD1 and VWD3; defect in FT secretion and formation of multimers; FT dbSNP:rs61753997). FT {ECO:0000269|PubMed:10887119}. FT /FTId=VAR_010242. FT VARIANT 318 318 N -> K (in dbSNP:rs1800387). FT /FTId=VAR_057023. FT VARIANT 377 377 W -> C (in VWD3). FT {ECO:0000269|PubMed:7989040}. FT /FTId=VAR_005782. FT VARIANT 471 471 V -> I (in dbSNP:rs1800377). FT {ECO:0000269|PubMed:2584182}. FT /FTId=VAR_060591. FT VARIANT 484 484 H -> R (in dbSNP:rs1800378). FT {ECO:0000269|PubMed:3019665}. FT /FTId=VAR_024553. FT VARIANT 528 528 N -> S (in VWD2). FT {ECO:0000269|PubMed:8011991}. FT /FTId=VAR_005783. FT VARIANT 550 550 G -> R (in VWD2). FT {ECO:0000269|PubMed:7789955}. FT /FTId=VAR_005784. FT VARIANT 740 740 M -> I (in dbSNP:rs16932374). FT /FTId=VAR_057024. FT VARIANT 788 788 C -> Y (in VWD2). FT /FTId=VAR_009141. FT VARIANT 789 789 T -> A (in dbSNP:rs1063856). FT {ECO:0000269|PubMed:2864688}. FT /FTId=VAR_005785. FT VARIANT 791 791 T -> M (in VWD2; Normandy type). FT {ECO:0000269|PubMed:1906179}. FT /FTId=VAR_005786. FT VARIANT 816 816 R -> W (in VWD2; Normandy type). FT {ECO:0000269|PubMed:1832934}. FT /FTId=VAR_005787. FT VARIANT 852 852 Q -> R (in dbSNP:rs216321). FT {ECO:0000269|PubMed:2584182, FT ECO:0000269|PubMed:2864688, FT ECO:0000269|PubMed:3019665, FT ECO:0000269|PubMed:3488076, FT ECO:0000269|PubMed:3489923, FT ECO:0000269|PubMed:3524673}. FT /FTId=VAR_005788. FT VARIANT 854 854 R -> Q (in VWD2; Normandy type; FT dbSNP:rs41276738). FT {ECO:0000269|PubMed:1832934}. FT /FTId=VAR_005789. FT VARIANT 857 857 N -> D. FT /FTId=VAR_005790. FT VARIANT 885 885 F -> S (in dbSNP:rs11064002). FT /FTId=VAR_057025. FT VARIANT 1060 1060 C -> R (in VWD2). FT {ECO:0000269|PubMed:12406074}. FT /FTId=VAR_028446. FT VARIANT 1149 1149 C -> R (in VWD1; reduced secretion of FT homodimers and heterodimers with wild FT type VWD and increased degradation by the FT proteasome). FT {ECO:0000269|PubMed:11698279}. FT /FTId=VAR_064925. FT VARIANT 1266 1266 P -> L (in VWD2). FT {ECO:0000269|PubMed:8486782}. FT /FTId=VAR_005791. FT VARIANT 1268 1268 H -> D (in VWD2). FT {ECO:0000269|PubMed:8376405}. FT /FTId=VAR_005792. FT VARIANT 1272 1272 C -> F (in VWD2; subtype 2A). FT {ECO:0000269|PubMed:21592258}. FT /FTId=VAR_067340. FT VARIANT 1272 1272 C -> R (in VWD2). FT {ECO:0000269|PubMed:1419804}. FT /FTId=VAR_005793. FT VARIANT 1306 1306 R -> W (in VWD2). FT {ECO:0000269|PubMed:1419803, FT ECO:0000269|PubMed:1420817, FT ECO:0000269|PubMed:1672694, FT ECO:0000269|PubMed:2010538}. FT /FTId=VAR_005794. FT VARIANT 1308 1308 R -> C (in VWD2). FT {ECO:0000269|PubMed:1419803, FT ECO:0000269|PubMed:1672694, FT ECO:0000269|PubMed:1761120, FT ECO:0000269|PubMed:2010538}. FT /FTId=VAR_005795. FT VARIANT 1313 1313 W -> C (in VWD2). FT {ECO:0000269|PubMed:2011604}. FT /FTId=VAR_005796. FT VARIANT 1314 1314 V -> L (in VWD2). FT {ECO:0000269|PubMed:1419803}. FT /FTId=VAR_005797. FT VARIANT 1316 1316 V -> M (in VWD2). FT {ECO:0000269|PubMed:1420817, FT ECO:0000269|PubMed:1672694, FT ECO:0000269|PubMed:1729889}. FT /FTId=VAR_005798. FT VARIANT 1318 1318 V -> L (in VWD2). FT {ECO:0000269|PubMed:1419803}. FT /FTId=VAR_005799. FT VARIANT 1324 1324 G -> S (in VWD2). FT {ECO:0000269|PubMed:1409710}. FT /FTId=VAR_005800. FT VARIANT 1341 1341 R -> Q (in VWD2). FT {ECO:0000269|PubMed:1672694}. FT /FTId=VAR_005801. FT VARIANT 1374 1374 R -> C (in VWD2). FT {ECO:0000269|PubMed:7620154}. FT /FTId=VAR_005802. FT VARIANT 1374 1374 R -> H (in VWD2). FT {ECO:0000269|PubMed:7620154, FT ECO:0000269|PubMed:7734373}. FT /FTId=VAR_005803. FT VARIANT 1381 1381 T -> A (in dbSNP:rs216311). FT {ECO:0000269|PubMed:1988024, FT ECO:0000269|PubMed:2584182, FT ECO:0000269|PubMed:2864688, FT ECO:0000269|PubMed:3019665, FT ECO:0000269|PubMed:3488076, FT ECO:0000269|PubMed:3489923, FT ECO:0000269|PubMed:3524673, FT ECO:0000269|PubMed:9373253}. FT /FTId=VAR_005804. FT VARIANT 1399 1399 R -> H (in dbSNP:rs216312). FT {ECO:0000269|PubMed:1672694}. FT /FTId=VAR_005805. FT VARIANT 1460 1460 L -> V (in VWD2). FT {ECO:0000269|PubMed:8123843}. FT /FTId=VAR_005806. FT VARIANT 1461 1461 A -> V (in VWD2). FT {ECO:0000269|PubMed:8547152}. FT /FTId=VAR_005807. FT VARIANT 1472 1472 D -> H (in dbSNP:rs1800383). FT {ECO:0000269|PubMed:1988024, FT ECO:0000269|PubMed:2584182, FT ECO:0000269|PubMed:3489923}. FT /FTId=VAR_029656. FT VARIANT 1514 1514 F -> C (in VWD2). FT {ECO:0000269|PubMed:8435341}. FT /FTId=VAR_005808. FT VARIANT 1540 1540 L -> P (in VWD2). FT {ECO:0000269|PubMed:8123844}. FT /FTId=VAR_005809. FT VARIANT 1565 1565 V -> L (in dbSNP:rs1800385). FT /FTId=VAR_014630. FT VARIANT 1570 1570 Y -> C (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036276. FT VARIANT 1584 1584 Y -> C (exhibits increased in FT susceptibility to proteolysis by FT ADAMTS13; dbSNP:rs1800386). FT {ECO:0000269|PubMed:15755288, FT ECO:0000269|PubMed:8348943}. FT /FTId=VAR_005810. FT VARIANT 1597 1597 R -> G (in VWD2). FT {ECO:0000269|PubMed:8348943}. FT /FTId=VAR_005811. FT VARIANT 1597 1597 R -> Q (in VWD2). FT {ECO:0000269|PubMed:8338947}. FT /FTId=VAR_005812. FT VARIANT 1597 1597 R -> W (in VWD2). FT {ECO:0000269|PubMed:2786201}. FT /FTId=VAR_005813. FT VARIANT 1607 1607 V -> D (in VWD2). FT {ECO:0000269|PubMed:2786201}. FT /FTId=VAR_005814. FT VARIANT 1609 1609 G -> R (in VWD2). FT {ECO:0000269|PubMed:8338947, FT ECO:0000269|PubMed:8348943}. FT /FTId=VAR_005815. FT VARIANT 1613 1613 S -> P (in VWD2). FT {ECO:0000269|PubMed:2010538}. FT /FTId=VAR_005816. FT VARIANT 1628 1628 I -> T (in VWD2). FT {ECO:0000269|PubMed:1420817, FT ECO:0000269|PubMed:1673047, FT ECO:0000269|PubMed:8123844}. FT /FTId=VAR_005817. FT VARIANT 1638 1638 E -> K (in VWD2). FT {ECO:0000269|PubMed:1429668}. FT /FTId=VAR_005818. FT VARIANT 1648 1648 P -> S (in VWD2). FT {ECO:0000269|PubMed:1420817}. FT /FTId=VAR_005819. FT VARIANT 1665 1665 V -> E (in VWD2). FT {ECO:0000269|PubMed:8338947}. FT /FTId=VAR_005820. FT VARIANT 2063 2063 P -> S (in VWD3; dbSNP:rs61750615). FT /FTId=VAR_009142. FT VARIANT 2178 2178 A -> S (in dbSNP:rs34230288). FT /FTId=VAR_057026. FT VARIANT 2185 2185 R -> Q (in dbSNP:rs2229446). FT /FTId=VAR_057027. FT VARIANT 2362 2362 C -> F (in VWD3). FT /FTId=VAR_009143. FT VARIANT 2546 2546 N -> Y (in VWD3). FT /FTId=VAR_009144. FT VARIANT 2705 2705 G -> R (in dbSNP:rs7962217). FT /FTId=VAR_057028. FT VARIANT 2739 2739 C -> Y (in VWD3). FT {ECO:0000269|PubMed:8088787}. FT /FTId=VAR_005821. FT VARIANT 2773 2773 C -> R (in VWD2). FT {ECO:0000269|PubMed:8622978}. FT /FTId=VAR_005822. FT MUTAGEN 1149 1149 C->R: Reduced secretion and increased FT intracellular retention. Similar FT phenotype; when associated with S-1169. FT {ECO:0000269|PubMed:11698279}. FT MUTAGEN 1169 1169 C->S: Reduced secretion and increased FT intracellular retention. Similar FT phenotype; when associated with R-1149. FT {ECO:0000269|PubMed:11698279}. FT CONFLICT 770 770 P -> H (in Ref. 11; AAB59512). FT {ECO:0000305}. FT CONFLICT 804 804 C -> S (in Ref. 10; AA sequence and 11; FT AAB59512). {ECO:0000305}. FT CONFLICT 1914 1914 S -> T (in Ref. 1; CAA27972). FT {ECO:0000305}. FT CONFLICT 2168 2168 C -> S (in Ref. 10; AA sequence). FT {ECO:0000305}. FT STRAND 767 769 {ECO:0000244|PDB:2MHP}. FT STRAND 771 774 {ECO:0000244|PDB:2MHP}. FT TURN 781 786 {ECO:0000244|PDB:2MHP}. FT TURN 792 794 {ECO:0000244|PDB:2MHP}. FT STRAND 795 797 {ECO:0000244|PDB:2MHP}. FT STRAND 804 809 {ECO:0000244|PDB:2MHP}. FT STRAND 814 817 {ECO:0000244|PDB:2MHP}. FT STRAND 820 823 {ECO:0000244|PDB:2MHP}. FT HELIX 824 826 {ECO:0000244|PDB:2MHP}. FT STRAND 829 833 {ECO:0000244|PDB:2MHP}. FT STRAND 841 844 {ECO:0000244|PDB:2MHP}. FT STRAND 847 852 {ECO:0000244|PDB:2MHP}. FT STRAND 855 858 {ECO:0000244|PDB:2MHP}. FT STRAND 1267 1269 {ECO:0000244|PDB:1IJB}. FT TURN 1270 1273 {ECO:0000244|PDB:4C29}. FT STRAND 1276 1283 {ECO:0000244|PDB:1IJB}. FT STRAND 1285 1288 {ECO:0000244|PDB:4C2B}. FT HELIX 1290 1305 {ECO:0000244|PDB:1IJB}. FT TURN 1307 1310 {ECO:0000244|PDB:1SQ0}. FT STRAND 1313 1329 {ECO:0000244|PDB:1IJB}. FT HELIX 1337 1345 {ECO:0000244|PDB:1IJB}. FT HELIX 1357 1367 {ECO:0000244|PDB:1IJB}. FT STRAND 1369 1371 {ECO:0000244|PDB:1IJB}. FT STRAND 1377 1385 {ECO:0000244|PDB:1IJB}. FT HELIX 1391 1393 {ECO:0000244|PDB:1IJB}. FT HELIX 1394 1396 {ECO:0000244|PDB:1U0N}. FT HELIX 1397 1406 {ECO:0000244|PDB:1IJB}. FT STRAND 1409 1417 {ECO:0000244|PDB:1IJB}. FT HELIX 1422 1431 {ECO:0000244|PDB:1IJB}. FT HELIX 1433 1435 {ECO:0000244|PDB:4C29}. FT STRAND 1438 1442 {ECO:0000244|PDB:1IJB}. FT HELIX 1443 1445 {ECO:0000244|PDB:1IJB}. FT HELIX 1446 1460 {ECO:0000244|PDB:1IJB}. FT STRAND 1498 1504 {ECO:0000244|PDB:3ZQK}. FT TURN 1507 1509 {ECO:0000244|PDB:3ZQK}. FT HELIX 1511 1527 {ECO:0000244|PDB:3ZQK}. FT STRAND 1534 1550 {ECO:0000244|PDB:3ZQK}. FT HELIX 1558 1567 {ECO:0000244|PDB:3ZQK}. FT HELIX 1578 1587 {ECO:0000244|PDB:3ZQK}. FT TURN 1588 1590 {ECO:0000244|PDB:3ZQK}. FT HELIX 1592 1594 {ECO:0000244|PDB:3ZQK}. FT HELIX 1595 1599 {ECO:0000244|PDB:3GXB}. FT STRAND 1602 1608 {ECO:0000244|PDB:3ZQK}. FT STRAND 1623 1631 {ECO:0000244|PDB:3ZQK}. FT HELIX 1636 1643 {ECO:0000244|PDB:3ZQK}. FT STRAND 1649 1652 {ECO:0000244|PDB:3ZQK}. FT TURN 1654 1656 {ECO:0000244|PDB:3ZQK}. FT HELIX 1657 1670 {ECO:0000244|PDB:3ZQK}. FT STRAND 1690 1697 {ECO:0000244|PDB:1ATZ}. FT STRAND 1699 1702 {ECO:0000244|PDB:1ATZ}. FT HELIX 1704 1720 {ECO:0000244|PDB:1ATZ}. FT STRAND 1727 1743 {ECO:0000244|PDB:1ATZ}. FT STRAND 1745 1747 {ECO:0000244|PDB:4DMU}. FT HELIX 1751 1759 {ECO:0000244|PDB:1ATZ}. FT HELIX 1770 1782 {ECO:0000244|PDB:1ATZ}. FT HELIX 1784 1786 {ECO:0000244|PDB:2ADF}. FT STRAND 1792 1800 {ECO:0000244|PDB:1ATZ}. FT HELIX 1809 1817 {ECO:0000244|PDB:1ATZ}. FT STRAND 1820 1831 {ECO:0000244|PDB:1ATZ}. FT HELIX 1833 1839 {ECO:0000244|PDB:1ATZ}. FT HELIX 1841 1847 {ECO:0000244|PDB:1ATZ}. FT STRAND 1849 1853 {ECO:0000244|PDB:1ATZ}. FT HELIX 1856 1862 {ECO:0000244|PDB:1ATZ}. FT STRAND 1863 1865 {ECO:0000244|PDB:2ADF}. FT HELIX 1866 1870 {ECO:0000244|PDB:1ATZ}. FT STRAND 2728 2732 {ECO:0000244|PDB:4NT5}. FT STRAND 2739 2743 {ECO:0000244|PDB:4NT5}. FT STRAND 2745 2749 {ECO:0000244|PDB:4NT5}. FT STRAND 2756 2761 {ECO:0000244|PDB:4NT5}. FT TURN 2762 2765 {ECO:0000244|PDB:4NT5}. FT STRAND 2766 2787 {ECO:0000244|PDB:4NT5}. FT STRAND 2793 2801 {ECO:0000244|PDB:4NT5}. FT STRAND 2804 2809 {ECO:0000244|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 //