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von Willebrand factor (vWF) [Cleaved into: von Willebrand antigen 2 (von Willebrand antigen II)]

 VWF_HUMAN               Reviewed;        2813 AA.
P04275; Q8TCE8; Q99806;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-OCT-2017, entry version 229.
RecName: Full=von Willebrand factor;
Short=vWF;
Contains:
RecName: Full=von Willebrand antigen 2;
AltName: Full=von Willebrand antigen II;
Flags: Precursor;
Name=VWF; Synonyms=F8VWF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-852; ALA-1381
AND HIS-1472.
PubMed=3489923; DOI=10.1093/nar/14.17.7125;
Bonthron D., Orr E.C., Mitsock L.M., Ginsburg D., Handin R.I.,
Orkin S.H.;
"Nucleotide sequence of pre-pro-von Willebrand factor cDNA.";
Nucleic Acids Res. 14:7125-7128(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-471; ARG-852;
ALA-1381 AND HIS-1472.
PubMed=2584182;
Mancuso D.J., Tuley E.A., Westfield L.A., Worrall N.K.,
Shelton-Inloes B.B., Sorace J.M., Alevy Y.G., Sadler J.E.;
"Structure of the gene for human von Willebrand factor.";
J. Biol. Chem. 264:19514-19527(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1400 (ISOFORM 1), AND VARIANTS
ARG-484; ARG-852 AND ALA-1381.
PubMed=3019665;
Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.;
"Full-length von Willebrand factor (vWF) cDNA encodes a highly
repetitive protein considerably larger than the mature vWF subunit.";
EMBO J. 5:1839-1847(1986).
[7]
ERRATUM.
Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.;
EMBO J. 5:3074-3074(1986).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178.
PubMed=2828057; DOI=10.1111/j.1432-1033.1988.tb13757.x;
Bonthron D., Orkin S.H.;
"The human von Willebrand factor gene. Structure of the 5' region.";
Eur. J. Biochem. 171:51-57(1988).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 1), AND PROTEIN SEQUENCE
OF 23-56.
TISSUE=Umbilical vein endothelial cell;
PubMed=3495266; DOI=10.1016/S0006-291X(87)80016-5;
Shelton-Inloes B.B., Broze G.J. Jr., Miletich J.P., Sadler J.E.;
"Evolution of human von Willebrand factor: cDNA sequence
polymorphisms, repeated domains, and relationship to von Willebrand
antigen II.";
Biochem. Biophys. Res. Commun. 144:657-665(1987).
[10]
PROTEIN SEQUENCE OF 764-2813, AND VARIANTS ARG-852 AND ALA-1381.
PubMed=3524673; DOI=10.1021/bi00359a015;
Titani K., Kumar S., Takio K., Ericsson L.H., Wade R.D., Ashida K.,
Walsh K.A., Chopek M.W., Sadler J.E., Fujikawa K.;
"Amino acid sequence of human von Willebrand factor.";
Biochemistry 25:3171-3184(1986).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 744-873 AND 1289-2813 (ISOFORM 1), AND
VARIANTS ALA-789; ARG-852 AND ALA-1381.
PubMed=2864688; DOI=10.1073/pnas.82.19.6394;
Sadler J.E., Shelton-Inloes B.B., Sorace J.M., Harlan J.M., Titani K.,
Davie E.W.;
"Cloning and characterization of two cDNAs coding for human von
Willebrand factor.";
Proc. Natl. Acad. Sci. U.S.A. 82:6394-6398(1985).
[12]
PROTEIN SEQUENCE OF 764-782.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 781-1424 (ISOFORM 1), AND VARIANTS
ARG-852 AND ALA-1381.
PubMed=3488076; DOI=10.1021/bi00359a014;
Shelton-Inloes B.B., Titani K., Sadler J.E.;
"cDNA sequences for human von Willebrand factor reveal five types of
repeated domains and five possible protein sequence polymorphisms.";
Biochemistry 25:3164-3171(1986).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 990-1947, AND VARIANTS ALA-1381
AND HIS-1472.
PubMed=1988024; DOI=10.1021/bi00215a036;
Mancuso D.J., Tuley E.A., Westfield L.A., Lester-Mancuso T.L.,
Le Beau M.M., Sorace J.M., Sadler J.E.;
"Human von Willebrand factor gene and pseudogene: structural analysis
and differentiation by polymerase chain reaction.";
Biochemistry 30:253-269(1991).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1236-1476 (ISOFORM 1), AND VARIANT
ALA-1381.
PubMed=9373253;
Schulte am Esch J. II, Cruz M.A., Siegel J.B., Anrather J.,
Robson S.C.;
"Activation of human platelets by the membrane-expressed A1 domain of
von Willebrand factor.";
Blood 90:4425-4437(1997).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 2621-2813 (ISOFORM 1).
PubMed=3874428; DOI=10.1126/science.3874428;
Ginsburg D., Handin R.I., Bonthron D.T., Donlon T.A., Bruns G.A.P.,
Latt S.A., Orkin S.H.;
"Human von Willebrand factor (vWF): isolation of complementary DNA
(cDNA) clones and chromosomal localization.";
Science 228:1401-1406(1985).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
PubMed=3873280; DOI=10.1016/0092-8674(85)90060-1;
Lynch D.C., Zimmerman T.S., Collins C.J., Brown M., Morin M.J.,
Ling E.H., Livingston D.M.;
"Molecular cloning of cDNA for human von Willebrand factor:
authentication by a new method.";
Cell 41:49-56(1985).
[18]
SEQUENCE REVISION.
Lynch D.C.;
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
PubMed=3875078; DOI=10.1093/nar/13.13.4699;
Verweij C.L., de Vries C.J.M., Distel B., van Zonneveld A.-J.,
Geurts van Kessel A., van Mourik J.A., Pannekoek H.;
"Construction of cDNA coding for human von Willebrand factor using
antibody probes for colony-screening and mapping of the chromosomal
gene.";
Nucleic Acids Res. 13:4699-4717(1985).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2731-2813.
PubMed=3496594; DOI=10.1073/pnas.84.13.4393;
Collins C.J., Underdahl J.P., Levene R.B., Ravera C.P., Morin M.J.,
Dombalagian M.J., Ricca G., Livingston D.M., Lynch D.C.;
"Molecular cloning of the human gene for von Willebrand factor and
identification of the transcription initiation site.";
Proc. Natl. Acad. Sci. U.S.A. 84:4393-4397(1987).
[21]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=10961880;
Haberichter S.L., Fahs S.A., Montgomery R.R.;
"von Willebrand factor storage and multimerization: 2 independent
intracellular processes.";
Blood 96:1808-1815(2000).
[22]
DISULFIDE BONDS.
PubMed=3502076; DOI=10.1021/bi00399a013;
Marti T., Rosselet S.J., Titani K., Walsh K.A.;
"Identification of disulfide-bridged substructures within human von
Willebrand factor.";
Biochemistry 26:8099-8109(1987).
[23]
STRUCTURE OF CARBOHYDRATES.
PubMed=3089784; DOI=10.1111/j.1432-1033.1986.tb09750.x;
Samor B., Michalski J.C., Debray H., Mazurier C., Goudemand M.,
van Halbeek H., Vliegenthart J.F.G., Montreuil J.;
"Primary structure of a new tetraantennary glycan of the N-
acetyllactosaminic type isolated from human factor VIII/von Willebrand
factor.";
Eur. J. Biochem. 158:295-298(1986).
[24]
INTERACTION WITH F8.
PubMed=9218428; DOI=10.1074/jbc.272.29.18007;
Saenko E.L., Scandella D.;
"The acidic region of the factor VIII light chain and the C2 domain
together form the high affinity binding site for von Willebrand
factor.";
J. Biol. Chem. 272:18007-18014(1997).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1515.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2546.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[27]
GLYCOSYLATION AT ASN-1515.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1261-1468.
PubMed=9553097; DOI=10.1074/jbc.273.17.10396;
Emsley J., Cruz M., Handin R., Liddington R.;
"Crystal structure of the von Willebrand factor A1 domain and
implications for the binding of platelet glycoprotein Ib.";
J. Biol. Chem. 273:10396-10401(1998).
[29]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-1873.
PubMed=9331419; DOI=10.1016/S0969-2126(97)00266-9;
Huizinga E.G., Martijn van der Plas R., Kroon J., Sixma J.J., Gros P.;
"Crystal structure of the A3 domain of human von Willebrand factor:
implications for collagen binding.";
Structure 5:1147-1156(1997).
[30]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1686-1872.
PubMed=9312128; DOI=10.1074/jbc.272.40.25162;
Bienkowska J., Cruz M., Atiemo A., Handin R., Liddington R.;
"The von Willebrand factor A3 domain does not contain a metal ion-
dependent adhesion site motif.";
J. Biol. Chem. 272:25162-25167(1997).
[31]
REVIEW.
PubMed=12871266; DOI=10.1046/j.1538-7836.2003.00260.x;
Ruggeri Z.M.;
"von Willebrand factor, platelets and endothelial cell interactions.";
J. Thromb. Haemost. 1:1335-1342(2003).
[32]
VARIANTS VWD2 TRP-1597 AND ASP-1607.
PubMed=2786201; DOI=10.1073/pnas.86.10.3723;
Ginsburg D., Konkle B.A., Gill J.C., Montgomery R.R.,
Bockenstedt P.L., Johnson T.A., Yang A.Y.;
"Molecular basis of human von Willebrand disease: analysis of platelet
von Willebrand factor mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 86:3723-3727(1989).
[33]
VARIANT VWD2 THR-1628.
PubMed=1673047;
Iannuzzi M.C., Hidaka N., Boehnke M., Bruck M.E., Hanna W.T.,
Collins F.S., Ginsburg D.;
"Analysis of the relationship of von Willebrand disease (vWD) and
hereditary hemorrhagic telangiectasia and identification of a
potential type IIA vWD mutation (IIe865 to Thr).";
Am. J. Hum. Genet. 48:757-763(1991).
[34]
VARIANTS VWD2 TRP-816 AND GLN-854.
PubMed=1832934; DOI=10.1111/j.1365-2141.1991.tb04480.x;
Gaucher C., Mercier B., Jorieux S., Oufkir D., Mazurier C.;
"Identification of two point mutations in the von Willebrand factor
gene of three families with the 'Normandy' variant of von Willebrand
disease.";
Br. J. Haematol. 78:506-514(1991).
[35]
VARIANT VWD2 CYS-1308.
PubMed=1761120;
Donner M., Andersson A.-M., Kristoffersson A.-C., Nilsson I.M.,
Dahlback B., Holmberg L.;
"An Arg545-->Cys545 substitution mutation of the von Willebrand factor
in type IIB von Willebrand's disease.";
Eur. J. Haematol. 47:342-345(1991).
[36]
VARIANTS VWD2 TRP-1306; CYS-1308 AND PRO-1613.
PubMed=2010538; DOI=10.1172/JCI115122;
Randi A.M., Rabinowitz I., Mancuso D.J., Mannucci P.M., Sadler J.E.;
"Molecular basis of von Willebrand disease type IIB. Candidate
mutations cluster in one disulfide loop between proposed platelet
glycoprotein Ib binding sequences.";
J. Clin. Invest. 87:1220-1226(1991).
[37]
VARIANTS VWD2 TRP-1306; CYS-1308; MET-1316 AND GLN-1341, AND VARIANT
HIS-1399.
PubMed=1672694; DOI=10.1172/JCI115123;
Cooney K.A., Nichols W.C., Bruck M.E., Bahou W.F., Shapiro A.D.,
Bowie E.J.W., Gralnick H.R., Ginsburg D.;
"The molecular defect in type IIB von Willebrand disease.
Identification of four potential missense mutations within the
putative GpIb binding domain.";
J. Clin. Invest. 87:1227-1233(1991).
[38]
VARIANT VWD2 CYS-1313.
PubMed=2011604; DOI=10.1073/pnas.88.7.2946;
Ware J., Dent J.A., Azuma H., Sugimoto M., Kyrle P.A., Yoshioka A.,
Ruggeri Z.M.;
"Identification of a point mutation in type IIB von Willebrand disease
illustrating the regulation of von Willebrand factor affinity for the
platelet membrane glycoprotein Ib-IX receptor.";
Proc. Natl. Acad. Sci. U.S.A. 88:2946-2950(1991).
[39]
VARIANT VWD2 MET-791.
PubMed=1906179; DOI=10.1073/pnas.88.14.6377;
Tuley E.A., Gaucher C., Jorieux S., Worrall N.K., Sadler J.E.,
Mazurier C.;
"Expression of von Willebrand factor 'Normandy': an autosomal mutation
that mimics hemophilia A.";
Proc. Natl. Acad. Sci. U.S.A. 88:6377-6381(1991).
[40]
VARIANT VWD2 MET-1316.
PubMed=1729889;
Murray E.W., Giles A.R., Lillicrap D.;
"Germ-line mosaicism for a valine-to-methionine substitution at
residue 553 in the glycoprotein Ib-binding domain of von Willebrand
factor, causing type IIB von Willebrand disease.";
Am. J. Hum. Genet. 50:199-207(1992).
[41]
VARIANTS VWD2 TRP-1306; MET-1316; THR-1628 AND SER-1648.
PubMed=1420817;
Pietu G., Ribba A.S., de Paillette L., Cherel G., Lavergne J.-M.,
Bahnak B.R., Meyer D.;
"Molecular study of von Willebrand disease: identification of
potential mutations in patients with type IIA and type IIB.";
Blood Coagul. Fibrinolysis 3:415-421(1992).
[42]
VARIANTS VWD2 TRP-1306; CYS-1308; LEU-1314 AND LEU-1318.
PubMed=1419803; DOI=10.1111/j.1365-2141.1992.tb04594.x;
Donner M., Kristoffersson A.-C., Lenk H., Scheibel E., Dahlback B.,
Nilsson I.M., Holmberg L.;
"Type IIB von Willebrand's disease: gene mutations and clinical
presentation in nine families from Denmark, Germany and Sweden.";
Br. J. Haematol. 82:58-65(1992).
[43]
VARIANT VWD2 ARG-1272.
PubMed=1419804; DOI=10.1111/j.1365-2141.1992.tb04595.x;
Lavergne J.-M., de Paillette L., Bahnak B.R., Ribba A.-S.,
Fressinaud E., Meyer D., Pietu G.;
"Defects in type IIA von Willebrand disease: a cysteine 509 to
arginine substitution in the mature von Willebrand factor disrupts a
disulphide loop involved in the interaction with platelet glycoprotein
Ib-IX.";
Br. J. Haematol. 82:66-72(1992).
[44]
VARIANT VWD2 LYS-1638.
PubMed=1429668;
Ribba A.S., Voorberg J., Meyer D., Pannekoek H., Pietu G.;
"Characterization of recombinant von Willebrand factor corresponding
to mutations in type IIA and type IIB von Willebrand disease.";
J. Biol. Chem. 267:23209-23215(1992).
[45]
VARIANT VWD2 SER-1324.
PubMed=1409710; DOI=10.1073/pnas.89.20.9846;
Rabinowitz I., Tuley E.A., Mancuso D.J., Randi A.M., Firkin B.G.,
Howard M.A., Sadler J.E.;
"von Willebrand disease type B: a missense mutation selectively
abolishes ristocetin-induced von Willebrand factor binding to platelet
glycoprotein Ib.";
Proc. Natl. Acad. Sci. U.S.A. 89:9846-9849(1992).
[46]
VARIANTS VWD2 GLN-1597; ARG-1609 AND GLU-1665.
PubMed=8338947;
Inbal A., Englender T., Kornbrot N., Randi A.M., Castaman G.,
Mannucci P.M., Sadler J.E.;
"Identification of three candidate mutations causing type IIA von
Willebrand disease using a rapid, nonradioactive, allele-specific
hybridization method.";
Blood 82:830-836(1993).
[47]
VARIANT VWD2 CYS-1514.
PubMed=8435341; DOI=10.1111/j.1365-2141.1993.tb04637.x;
Gaucher C., Hanss M., Dechavanne M., Mazurier C.;
"Substitution of cysteine for phenylalanine 751 in mature von
Willebrand factor is a novel candidate mutation in a family with type
IIA von Willebrand disease.";
Br. J. Haematol. 83:94-99(1993).
[48]
VARIANTS VWD2 GLY-1597 AND ARG-1609, AND VARIANT CYS-1584.
PubMed=8348943;
Donner M., Kristoffersson A.C., Berntorp E., Scheibel E., Thorsen S.,
Dahlback B., Nilsson I.M., Holmberg L.;
"Two new candidate mutations in type IIA von Willebrand's disease
(Arg834-->Gly, Gly846-->Arg) and one polymorphism (Tyr821-->Cys) in
the A2 region of the von Willebrand factor.";
Eur. J. Haematol. 51:38-44(1993).
[49]
VARIANT VWD2 ASP-1268.
PubMed=8376405;
Rabinowitz I., Randi A.M., Shindler K.S., Tuley E.A., Rustagi P.K.,
Sadler J.E.;
"Type IIB mutation His-505-->Asp implicates a new segment in the
control of von Willebrand factor binding to platelet glycoprotein
Ib.";
J. Biol. Chem. 268:20497-20501(1993).
[50]
VARIANT VWD2 LEU-1266.
PubMed=8486782; DOI=10.1172/JCI116443;
Holmberg L., Dent J.A., Schneppenheim R., Budde U., Ware J.,
Ruggeri Z.M.;
"von Willebrand factor mutation enhancing interaction with platelets
in patients with normal multimeric structure.";
J. Clin. Invest. 91:2169-2177(1993).
[51]
VARIANT VWD2 VAL-1460.
PubMed=8123843;
Hilbert L., Gaucher C., de Romeuf C., Horellou M.H., Vink T.,
Mazurier C.;
"Leu 697-->Val mutation in mature von Willebrand factor is responsible
for type IIB von Willebrand disease.";
Blood 83:1542-1550(1994).
[52]
VARIANTS VWD2 PRO-1540 AND THR-1628.
PubMed=8123844;
Lyons S.E., Cooney K.A., Bockenstedt P., Ginsburg D.;
"Characterization of Leu777Pro and Ile865Thr type IIA von Willebrand
disease mutations.";
Blood 83:1551-1557(1994).
[53]
VARIANT VWD3 TYR-2739.
PubMed=8088787; DOI=10.1006/geno.1994.1241;
Zhang Z.P., Blombaeck M., Egberg N., Falk G., Anvret M.;
"Characterization of the von Willebrand factor gene (VWF) in von
Willebrand disease type III patients from 24 families of Swedish and
Finnish origin.";
Genomics 21:188-193(1994).
[54]
VARIANT VWD3 CYS-377.
PubMed=7989040; DOI=10.1007/BF00206958;
Schneppenheim R., Krey S., Bergmann F., Bock D., Budde U., Lange M.,
Linde R., Mittler U., Meili E., Mertes G., Olek K., Plendl H.,
Simeoni E.;
"Genetic heterogeneity of severe von Willebrand disease type III in
the German population.";
Hum. Genet. 94:640-652(1994).
[55]
VARIANT VWD2 SER-528.
PubMed=8011991;
Uno H., Nishida N., Ishizaki J., Suzuki M., Nishikubo T., Miyata S.,
Takahashi Y., Yoshioka A., Tsuda K.;
"Investigation of type IIC von Willebrand disease.";
Int. J. Hematol. 59:219-225(1994).
[56]
VARIANTS VWD2 CYS-1374 AND HIS-1374.
PubMed=7620154;
Hilbert L., Gaucher C., Mazurier C.;
"Identification of two mutations (Arg611Cys and Arg611His) in the A1
loop of von Willebrand factor (vWF) responsible for type 2 von
Willebrand disease with decreased platelet-dependent function of
vWF.";
Blood 86:1010-1018(1995).
[57]
VARIANT VWD2 HIS-1374.
PubMed=7734373; DOI=10.1111/j.1365-2141.1995.tb08383.x;
Castaman G., Eikenboom C.J.C., Rodeghiero F., Briet K., Reitsma P.H.;
"A novel candidate mutation (Arg611-->His) in type I 'platelet
discordant' von Willebrand's disease with desmopressin-induced
thrombocytopenia.";
Br. J. Haematol. 89:656-658(1995).
[58]
VARIANT VWD2 VAL-1461.
PubMed=8547152; DOI=10.1111/j.1365-2141.1995.tb05423.x;
Hilbert L., Gaucher C., Mazurier C.;
"Effects of different amino-acid substitutions in the leucine 694-
proline 708 segment of recombinant von Willebrand factor.";
Br. J. Haematol. 91:983-990(1995).
[59]
VARIANT VWD2 ARG-550.
PubMed=7789955; DOI=10.1007/BF00209487;
Schneppenheim R., Thomas K.B., Krey S., Budde U., Jessat U.,
Sutor A.H., Zeiger B.;
"Identification of a candidate missense mutation in a family with von
Willebrand disease type IIC.";
Hum. Genet. 95:681-686(1995).
[60]
VARIANT VWD2 ARG-2773.
PubMed=8622978; DOI=10.1073/pnas.93.8.3581;
Schneppenheim R., Brassard J., Krey S., Budde U., Kunicki T.J.,
Holmberg L., Ware J., Ruggeri Z.M.;
"Defective dimerization of von Willebrand factor subunits due to a
Cys-> Arg mutation in type IID von Willebrand disease.";
Proc. Natl. Acad. Sci. U.S.A. 93:3581-3586(1996).
[61]
VARIANT VWD1 TRP-273, AND VARIANT VWD3 TRP-273.
PubMed=10887119;
Allen S., Abuzenadah A.M., Hinks J., Blagg J.L., Gursel T.,
Ingerslev J., Goodeve A.C., Peake I.R., Daly M.E.;
"A novel von Willebrand disease-causing mutation (Arg273Trp) in the
von Willebrand factor propeptide that results in defective
multimerization and secretion.";
Blood 96:560-568(2000).
[62]
VARIANT VWD1 ARG-1149, AND MUTAGENESIS OF CYS-1149 AND CYS-1169.
PubMed=11698279; DOI=10.1182/blood.V98.10.2973;
Bodo I., Katsumi A., Tuley E.A., Eikenboom J.C., Dong Z., Sadler J.E.;
"Type 1 von Willebrand disease mutation Cys1149Arg causes
intracellular retention and degradation of heterodimers: a possible
general mechanism for dominant mutations of oligomeric proteins.";
Blood 98:2973-2979(2001).
[63]
VARIANT VWD2 ARG-1060.
PubMed=12406074; DOI=10.1046/j.1365-2141.2002.03819.x;
Mazurier C., Parquet-Gernez A., Gaucher C., Lavergne J.-M.,
Goudemand J.;
"Factor VIII deficiency not induced by FVIII gene mutation in a female
first cousin of two brothers with haemophilia A.";
Br. J. Haematol. 119:390-392(2002).
[64]
VARIANT CYS-1584.
PubMed=15755288; DOI=10.1111/j.1365-2141.2005.05375.x;
Bowen D.J., Collins P.W., Lester W., Cumming A.M., Keeney S.,
Grundy P., Enayat S.M., Bolton-Maggs P.H., Keeling D.M., Khair K.,
Tait R.C., Wilde J.T., Pasi K.J., Hill F.G.;
"The prevalence of the cysteine1584 variant of von Willebrand factor
is increased in type 1 von Willebrand disease: co-segregation with
increased susceptibility to ADAMTS13 proteolysis but not clinical
phenotype.";
Br. J. Haematol. 128:830-836(2005).
[65]
VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[66]
VARIANT VWD2 PHE-1272.
PubMed=21592258; DOI=10.1111/j.1365-2516.2011.02569.x;
Woods A.I., Sanchez-Luceros A., Kempfer A.C., Powazniak Y.,
Calderazzo Pereyra J.C., Blanco A.N., Meschengieser S.S.,
Lazzari M.A.;
"C1272F: a novel type 2A von Willebrand's disease mutation in A1
domain; its clinical significance.";
Haemophilia 18:112-116(2012).
-!- FUNCTION: Important in the maintenance of hemostasis, it promotes
adhesion of platelets to the sites of vascular injury by forming a
molecular bridge between sub-endothelial collagen matrix and
platelet-surface receptor complex GPIb-IX-V. Also acts as a
chaperone for coagulation factor VIII, delivering it to the site
of injury, stabilizing its heterodimeric structure and protecting
it from premature clearance from plasma.
-!- SUBUNIT: Multimeric. Interacts with F8.
{ECO:0000269|PubMed:10961880, ECO:0000269|PubMed:9218428}.
-!- INTERACTION:
Self; NbExp=21; IntAct=EBI-981819, EBI-981819;
Q76LX8:ADAMTS13; NbExp=19; IntAct=EBI-981819, EBI-981764;
P07359:GP1BA; NbExp=2; IntAct=EBI-981819, EBI-297082;
Q96CV9:OPTN; NbExp=2; IntAct=EBI-981819, EBI-748974;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}.
Secreted, extracellular space, extracellular matrix
{ECO:0000269|PubMed:10961880}. Note=Localized to storage granules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P04275-1; Sequence=Displayed;
Name=2;
IsoId=P04275-2; Sequence=VSP_056527, VSP_056528, VSP_056529;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Plasma.
-!- DOMAIN: The von Willebrand antigen 2 is required for
multimerization of vWF and for its targeting to storage granules.
-!- PTM: All cysteine residues are involved in intrachain or
interchain disulfide bonds.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.
-!- DISEASE: von Willebrand disease 1 (VWD1) [MIM:193400]: A common
hemorrhagic disorder due to defects in von Willebrand factor
protein and resulting in impaired platelet aggregation. Von
Willebrand disease type 1 is characterized by partial quantitative
deficiency of circulating von Willebrand factor, that is otherwise
structurally and functionally normal. Clinical manifestations are
mucocutaneous bleeding, such as epistaxis and menorrhagia, and
prolonged bleeding after surgery or trauma.
{ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:11698279}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: von Willebrand disease 2 (VWD2) [MIM:613554]: A
hemorrhagic disorder due to defects in von Willebrand factor
protein and resulting in altered platelet aggregation. Von
Willebrand disease type 2 is characterized by qualitative
deficiency and functional anomalies of von Willebrand factor. It
is divided in different subtypes including 2A, 2B, 2M and 2N
(Normandy variant). The mutant VWF protein in types 2A, 2B and 2M
are defective in their platelet-dependent function, whereas the
mutant protein in type 2N is defective in its ability to bind
factor VIII. Clinical manifestations are mucocutaneous bleeding,
such as epistaxis and menorrhagia, and prolonged bleeding after
surgery or trauma. {ECO:0000269|PubMed:12406074,
ECO:0000269|PubMed:1409710, ECO:0000269|PubMed:1419803,
ECO:0000269|PubMed:1419804, ECO:0000269|PubMed:1420817,
ECO:0000269|PubMed:1429668, ECO:0000269|PubMed:1672694,
ECO:0000269|PubMed:1673047, ECO:0000269|PubMed:1729889,
ECO:0000269|PubMed:1761120, ECO:0000269|PubMed:1832934,
ECO:0000269|PubMed:1906179, ECO:0000269|PubMed:2010538,
ECO:0000269|PubMed:2011604, ECO:0000269|PubMed:21592258,
ECO:0000269|PubMed:2786201, ECO:0000269|PubMed:7620154,
ECO:0000269|PubMed:7734373, ECO:0000269|PubMed:7789955,
ECO:0000269|PubMed:8011991, ECO:0000269|PubMed:8123843,
ECO:0000269|PubMed:8123844, ECO:0000269|PubMed:8338947,
ECO:0000269|PubMed:8348943, ECO:0000269|PubMed:8376405,
ECO:0000269|PubMed:8435341, ECO:0000269|PubMed:8486782,
ECO:0000269|PubMed:8547152, ECO:0000269|PubMed:8622978}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: von Willebrand disease 3 (VWD3) [MIM:277480]: A severe
hemorrhagic disorder due to a total or near total absence of von
Willebrand factor in the plasma and cellular compartments, also
leading to a profound deficiency of plasmatic factor VIII.
Bleeding usually starts in infancy and can include epistaxis,
recurrent mucocutaneous bleeding, excessive bleeding after minor
trauma, and hemarthroses. {ECO:0000269|PubMed:10887119,
ECO:0000269|PubMed:7989040, ECO:0000269|PubMed:8088787}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SEQUENCE CAUTION:
Sequence=AAB59512.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=vWF; Note=von Willebrand factor (vWF) mutation
db;
URL="http://www.vwf.group.shef.ac.uk/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Von Willebrand factor entry;
URL="https://en.wikipedia.org/wiki/Von_Willebrand_factor";
-----------------------------------------------------------------------
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EMBL; X04385; CAA27972.1; -; mRNA.
EMBL; M25865; AAB59458.1; -; Genomic_DNA.
EMBL; M25828; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25829; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25830; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25831; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25832; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25833; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25834; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25835; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25836; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25837; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25838; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25839; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25840; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25841; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25842; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25843; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25844; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25845; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25846; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25847; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25848; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25849; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25850; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25851; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25852; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25853; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25854; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25855; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25856; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25857; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25858; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25859; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25860; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25861; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25862; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25863; AAB59458.1; JOINED; Genomic_DNA.
EMBL; M25864; AAB59458.1; JOINED; Genomic_DNA.
EMBL; AC005845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88817.1; -; Genomic_DNA.
EMBL; BC022258; AAH22258.1; -; mRNA.
EMBL; X04146; CAA27765.1; -; mRNA.
EMBL; X06828; CAA29985.1; -; Genomic_DNA.
EMBL; X06829; CAA29985.1; JOINED; Genomic_DNA.
EMBL; M17588; AAA65940.1; -; mRNA.
EMBL; M10321; AAB59512.1; ALT_SEQ; mRNA.
EMBL; M60675; AAA61295.1; -; Genomic_DNA.
EMBL; U81237; AAB39987.1; -; mRNA.
EMBL; K03028; AAA61293.1; -; mRNA.
EMBL; X02672; CAA26503.1; -; mRNA.
EMBL; M16946; AAA61294.1; -; Genomic_DNA.
EMBL; M16945; AAA61294.1; JOINED; Genomic_DNA.
CCDS; CCDS8539.1; -. [P04275-1]
PIR; A34480; VWHU.
RefSeq; NP_000543.2; NM_000552.4.
UniGene; Hs.440848; -.
PDB; 1AO3; X-ray; 2.20 A; A/B=1686-1872.
PDB; 1ATZ; X-ray; 1.80 A; A/B=1685-1873.
PDB; 1AUQ; X-ray; 2.30 A; A=1261-1468.
PDB; 1FE8; X-ray; 2.03 A; A/B/C=1683-1874.
PDB; 1FNS; X-ray; 2.00 A; A=1271-1465.
PDB; 1IJB; X-ray; 1.80 A; A=1263-1464.
PDB; 1IJK; X-ray; 2.60 A; A=1263-1464.
PDB; 1M10; X-ray; 3.10 A; A=1261-1468.
PDB; 1OAK; X-ray; 2.20 A; A=1271-1465.
PDB; 1SQ0; X-ray; 2.60 A; A=1259-1471.
PDB; 1U0N; X-ray; 2.95 A; A=1261-1468.
PDB; 1UEX; X-ray; 2.85 A; C=1260-1468.
PDB; 2ADF; X-ray; 1.90 A; A=1683-1874.
PDB; 2MHP; NMR; -; A=766-864.
PDB; 2MHQ; NMR; -; A=766-864.
PDB; 3GXB; X-ray; 1.90 A; A/B=1495-1671.
PDB; 3HXO; X-ray; 2.40 A; A=1260-1468.
PDB; 3HXQ; X-ray; 2.69 A; A=1260-1468.
PDB; 3PPV; X-ray; 1.90 A; A=1488-1674.
PDB; 3PPW; X-ray; 1.90 A; A=1488-1674.
PDB; 3PPX; X-ray; 1.91 A; A=1488-1674.
PDB; 3PPY; X-ray; 2.00 A; A=1488-1674.
PDB; 3ZQK; X-ray; 1.70 A; A/B/C=1478-1674.
PDB; 4C29; X-ray; 2.20 A; A/B=1264-1471.
PDB; 4C2A; X-ray; 2.08 A; A=1264-1471.
PDB; 4C2B; X-ray; 2.80 A; A/C/E/G=1264-1471.
PDB; 4DMU; X-ray; 2.80 A; B/D/F/H/J/L=1683-1874.
PDB; 4NT5; X-ray; 3.28 A; A=2721-2813.
PDB; 5BV8; X-ray; 1.59 A; A=1238-1471.
PDBsum; 1AO3; -.
PDBsum; 1ATZ; -.
PDBsum; 1AUQ; -.
PDBsum; 1FE8; -.
PDBsum; 1FNS; -.
PDBsum; 1IJB; -.
PDBsum; 1IJK; -.
PDBsum; 1M10; -.
PDBsum; 1OAK; -.
PDBsum; 1SQ0; -.
PDBsum; 1U0N; -.
PDBsum; 1UEX; -.
PDBsum; 2ADF; -.
PDBsum; 2MHP; -.
PDBsum; 2MHQ; -.
PDBsum; 3GXB; -.
PDBsum; 3HXO; -.
PDBsum; 3HXQ; -.
PDBsum; 3PPV; -.
PDBsum; 3PPW; -.
PDBsum; 3PPX; -.
PDBsum; 3PPY; -.
PDBsum; 3ZQK; -.
PDBsum; 4C29; -.
PDBsum; 4C2A; -.
PDBsum; 4C2B; -.
PDBsum; 4DMU; -.
PDBsum; 4NT5; -.
PDBsum; 5BV8; -.
ProteinModelPortal; P04275; -.
SMR; P04275; -.
BioGrid; 113289; 15.
CORUM; P04275; -.
DIP; DIP-29667N; -.
ELM; P04275; -.
IntAct; P04275; 51.
MINT; MINT-244925; -.
STRING; 9606.ENSP00000261405; -.
ChEMBL; CHEMBL2021748; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB05202; ARC1779.
MEROPS; I08.950; -.
iPTMnet; P04275; -.
PhosphoSitePlus; P04275; -.
SwissPalm; P04275; -.
UniCarbKB; P04275; -.
BioMuta; VWF; -.
DMDM; 317373549; -.
PaxDb; P04275; -.
PeptideAtlas; P04275; -.
PRIDE; P04275; -.
Ensembl; ENST00000261405; ENSP00000261405; ENSG00000110799. [P04275-1]
GeneID; 7450; -.
KEGG; hsa:7450; -.
UCSC; uc001qnn.2; human. [P04275-1]
CTD; 7450; -.
DisGeNET; 7450; -.
EuPathDB; HostDB:ENSG00000110799.13; -.
GeneCards; VWF; -.
GeneReviews; VWF; -.
H-InvDB; HIX0010356; -.
H-InvDB; HIX0171640; -.
HGNC; HGNC:12726; VWF.
HPA; CAB001694; -.
HPA; CAB072874; -.
HPA; CAB072875; -.
HPA; HPA001815; -.
HPA; HPA002082; -.
MalaCards; VWF; -.
MIM; 193400; phenotype.
MIM; 277480; phenotype.
MIM; 613160; gene.
MIM; 613554; phenotype.
neXtProt; NX_P04275; -.
OpenTargets; ENSG00000110799; -.
Orphanet; 166078; Von Willebrand disease type 1.
Orphanet; 166084; Von Willebrand disease type 2A.
Orphanet; 166087; Von Willebrand disease type 2B.
Orphanet; 166090; Von Willebrand disease type 2M.
Orphanet; 166093; Von Willebrand disease type 2N.
Orphanet; 166096; Von Willebrand disease type 3.
PharmGKB; PA37337; -.
eggNOG; ENOG410IR8A; Eukaryota.
eggNOG; ENOG41100RZ; LUCA.
GeneTree; ENSGT00760000118896; -.
HOGENOM; HOG000169747; -.
HOVERGEN; HBG004380; -.
InParanoid; P04275; -.
KO; K03900; -.
OMA; ECCGRCL; -.
OrthoDB; EOG091G0006; -.
PhylomeDB; P04275; -.
TreeFam; TF300299; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
SIGNOR; P04275; -.
ChiTaRS; VWF; human.
EvolutionaryTrace; P04275; -.
GeneWiki; Von_Willebrand_factor; -.
GenomeRNAi; 7450; -.
PRO; PR:P04275; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110799; -.
CleanEx; HS_VWF; -.
ExpressionAtlas; P04275; baseline and differential.
Genevisible; P04275; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0031091; C:platelet alpha granule; NAS:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0033093; C:Weibel-Palade body; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019865; F:immunoglobulin binding; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0002020; F:protease binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0007596; P:blood coagulation; IMP:UniProtKB.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IDA:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007599; P:hemostasis; IMP:UniProtKB.
GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0009611; P:response to wounding; TAS:UniProtKB.
Gene3D; 3.40.50.410; -; 3.
InterPro; IPR006207; Cys_knot_C.
InterPro; IPR036084; Ser_inhib-like_sf.
InterPro; IPR002919; TIL_dom.
InterPro; IPR014853; Unchr_dom_Cys-rich.
InterPro; IPR032361; VWA_N2.
InterPro; IPR002035; VWF_A.
InterPro; IPR001007; VWF_dom.
InterPro; IPR001846; VWF_type-D.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF08742; C8; 4.
Pfam; PF01826; TIL; 5.
Pfam; PF00092; VWA; 3.
Pfam; PF16164; VWA_N2; 1.
Pfam; PF00093; VWC; 3.
Pfam; PF00094; VWD; 4.
SMART; SM00832; C8; 4.
SMART; SM00041; CT; 1.
SMART; SM00327; VWA; 3.
SMART; SM00214; VWC; 5.
SMART; SM00215; VWC_out; 2.
SMART; SM00216; VWD; 4.
SUPFAM; SSF53300; SSF53300; 3.
SUPFAM; SSF57567; SSF57567; 5.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS50234; VWFA; 3.
PROSITE; PS01208; VWFC_1; 3.
PROSITE; PS50184; VWFC_2; 3.
PROSITE; PS51233; VWFD; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Cell adhesion;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Hemostasis; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; von Willebrand disease.
SIGNAL 1 22 {ECO:0000269|PubMed:3495266}.
CHAIN 23 763 von Willebrand antigen 2.
/FTId=PRO_0000022682.
CHAIN 764 2813 von Willebrand factor.
/FTId=PRO_0000022683.
DOMAIN 34 240 VWFD 1. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 295 348 TIL 1.
DOMAIN 387 598 VWFD 2. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 652 707 TIL 2.
DOMAIN 776 827 TIL 3.
DOMAIN 866 1074 VWFD 3. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 1146 1196 TIL 4.
DOMAIN 1277 1453 VWFA 1; binding site for platelet
glycoprotein Ib. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1498 1665 VWFA 2. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1691 1871 VWFA 3; main binding site for collagens
type I and III. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1949 2153 VWFD 4. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 2255 2328 VWFC 1. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 2429 2495 VWFC 2. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 2580 2645 VWFC 3. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 2724 2812 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
REGION 764 787 Amino-terminal.
REGION 788 833 E1.
REGION 826 853 CX.
REGION 2216 2261 E2.
MOTIF 2507 2509 Cell attachment site.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 666 666 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 857 857 N-linked (GlcNAc...) asparagine.
CARBOHYD 1147 1147 N-linked (GlcNAc...) asparagine;
atypical.
CARBOHYD 1231 1231 N-linked (GlcNAc...) asparagine.
CARBOHYD 1248 1248 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1255 1255 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1256 1256 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1263 1263 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3524673}.
CARBOHYD 1468 1468 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1477 1477 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1486 1486 O-linked (GalNAc...) serine.
{ECO:0000305}.
CARBOHYD 1487 1487 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 1515 1515 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:19139490}.
CARBOHYD 1574 1574 N-linked (GlcNAc...) asparagine.
CARBOHYD 1679 1679 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 2223 2223 N-linked (GlcNAc...) asparagine.
CARBOHYD 2290 2290 N-linked (GlcNAc...) asparagine.
CARBOHYD 2298 2298 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 2357 2357 N-linked (GlcNAc...) asparagine.
CARBOHYD 2400 2400 N-linked (GlcNAc...) asparagine.
CARBOHYD 2546 2546 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 2585 2585 N-linked (GlcNAc...) asparagine.
CARBOHYD 2790 2790 N-linked (GlcNAc...) asparagine.
DISULFID 767 808 {ECO:0000269|PubMed:3502076}.
DISULFID 776 804 {ECO:0000269|PubMed:3502076}.
DISULFID 810 821 {ECO:0000269|PubMed:3502076}.
DISULFID 867 996 {ECO:0000269|PubMed:3502076}.
DISULFID 889 1031 {ECO:0000269|PubMed:3502076}.
DISULFID 898 993 {ECO:0000269|PubMed:3502076}.
DISULFID 914 921 {ECO:0000269|PubMed:3502076}.
DISULFID 1060 1084 {ECO:0000269|PubMed:3502076}.
DISULFID 1071 1111 {ECO:0000269|PubMed:3502076}.
DISULFID 1089 1091 {ECO:0000269|PubMed:3502076}.
DISULFID 1126 1130 {ECO:0000269|PubMed:3502076}.
DISULFID 1149 1169 {ECO:0000269|PubMed:3502076}.
DISULFID 1153 1165 {ECO:0000269|PubMed:3502076}.
DISULFID 1196 1199 {ECO:0000269|PubMed:3502076}.
DISULFID 1234 1237 {ECO:0000269|PubMed:3502076}.
DISULFID 1272 1458 {ECO:0000269|PubMed:3502076}.
DISULFID 1669 1670 {ECO:0000269|PubMed:3502076}.
DISULFID 1686 1872 {ECO:0000269|PubMed:3502076}.
DISULFID 1879 1904 {ECO:0000269|PubMed:3502076}.
DISULFID 1899 1940 Or C-1899 with C-1942.
{ECO:0000255|PROSITE-ProRule:PRU00039,
ECO:0000255|PROSITE-ProRule:PRU00580,
ECO:0000269|PubMed:3502076}.
DISULFID 1927 2088 {ECO:0000269|PubMed:3502076}.
DISULFID 1950 2085 {ECO:0000269|PubMed:3502076}.
DISULFID 1972 2123 {ECO:0000269|PubMed:3502076}.
DISULFID 1993 2001 {ECO:0000269|PubMed:3502076}.
DISULFID 2724 2774 {ECO:0000250}.
DISULFID 2739 2788 {ECO:0000250}.
DISULFID 2750 2804 {ECO:0000250}.
DISULFID 2754 2806 {ECO:0000250}.
DISULFID ? 2811 {ECO:0000250}.
VAR_SEQ 1 18 MIPARFAGVLLALALILP -> MGAQDEEEGIQDLDGLLVF
DKIVEVTLLNLPWYNEETEGQRGEMTAPKSPRAKIR (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056527.
VAR_SEQ 220 314 GLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGG
LECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEY
RQCVSPCARTCQS -> EEPECNDITARLQYVKVGSCKSEV
EVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQV
ALHCTNGSVVYHEVLNAMECKCSPRKCSKI (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056528.
VAR_SEQ 315 2813 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056529.
VARIANT 273 273 R -> W (in VWD1 and VWD3; defect in
secretion and formation of multimers;
dbSNP:rs61753997).
{ECO:0000269|PubMed:10887119}.
/FTId=VAR_010242.
VARIANT 318 318 N -> K (in dbSNP:rs1800387).
/FTId=VAR_057023.
VARIANT 377 377 W -> C (in VWD3; dbSNP:rs62643626).
{ECO:0000269|PubMed:7989040}.
/FTId=VAR_005782.
VARIANT 471 471 V -> I (in dbSNP:rs1800377).
{ECO:0000269|PubMed:2584182}.
/FTId=VAR_060591.
VARIANT 484 484 H -> R (in dbSNP:rs1800378).
{ECO:0000269|PubMed:3019665}.
/FTId=VAR_024553.
VARIANT 528 528 N -> S (in VWD2; dbSNP:rs61754010).
{ECO:0000269|PubMed:8011991}.
/FTId=VAR_005783.
VARIANT 550 550 G -> R (in VWD2; dbSNP:rs61754011).
{ECO:0000269|PubMed:7789955}.
/FTId=VAR_005784.
VARIANT 740 740 M -> I (in dbSNP:rs16932374).
/FTId=VAR_057024.
VARIANT 788 788 C -> Y (in VWD2; dbSNP:rs61748476).
/FTId=VAR_009141.
VARIANT 789 789 T -> A (in dbSNP:rs1063856).
{ECO:0000269|PubMed:2864688}.
/FTId=VAR_005785.
VARIANT 791 791 T -> M (in VWD2; Normandy type;
dbSNP:rs61748477).
{ECO:0000269|PubMed:1906179}.
/FTId=VAR_005786.
VARIANT 816 816 R -> W (in VWD2; Normandy type;
dbSNP:rs121964894).
{ECO:0000269|PubMed:1832934}.
/FTId=VAR_005787.
VARIANT 852 852 Q -> R (in dbSNP:rs216321).
{ECO:0000269|PubMed:2584182,
ECO:0000269|PubMed:2864688,
ECO:0000269|PubMed:3019665,
ECO:0000269|PubMed:3488076,
ECO:0000269|PubMed:3489923,
ECO:0000269|PubMed:3524673}.
/FTId=VAR_005788.
VARIANT 854 854 R -> Q (in VWD2; Normandy type;
dbSNP:rs41276738).
{ECO:0000269|PubMed:1832934}.
/FTId=VAR_005789.
VARIANT 857 857 N -> D.
/FTId=VAR_005790.
VARIANT 885 885 F -> S (in dbSNP:rs11064002).
/FTId=VAR_057025.
VARIANT 1060 1060 C -> R (in VWD2; dbSNP:rs61748497).
{ECO:0000269|PubMed:12406074}.
/FTId=VAR_028446.
VARIANT 1149 1149 C -> R (in VWD1; reduced secretion of
homodimers and heterodimers with wild
type VWD and increased degradation by the
proteasome; dbSNP:rs61748511).
{ECO:0000269|PubMed:11698279}.
/FTId=VAR_064925.
VARIANT 1266 1266 P -> L (in VWD2; dbSNP:rs61749370).
{ECO:0000269|PubMed:8486782}.
/FTId=VAR_005791.
VARIANT 1268 1268 H -> D (in VWD2; dbSNP:rs61749371).
{ECO:0000269|PubMed:8376405}.
/FTId=VAR_005792.
VARIANT 1272 1272 C -> F (in VWD2; subtype 2A;
dbSNP:rs63524161).
{ECO:0000269|PubMed:21592258}.
/FTId=VAR_067340.
VARIANT 1272 1272 C -> R (in VWD2; dbSNP:rs61749372).
{ECO:0000269|PubMed:1419804}.
/FTId=VAR_005793.
VARIANT 1306 1306 R -> W (in VWD2; dbSNP:rs61749384).
{ECO:0000269|PubMed:1419803,
ECO:0000269|PubMed:1420817,
ECO:0000269|PubMed:1672694,
ECO:0000269|PubMed:2010538}.
/FTId=VAR_005794.
VARIANT 1308 1308 R -> C (in VWD2; dbSNP:rs61749387).
{ECO:0000269|PubMed:1419803,
ECO:0000269|PubMed:1672694,
ECO:0000269|PubMed:1761120,
ECO:0000269|PubMed:2010538}.
/FTId=VAR_005795.
VARIANT 1313 1313 W -> C (in VWD2; dbSNP:rs61749392).
{ECO:0000269|PubMed:2011604}.
/FTId=VAR_005796.
VARIANT 1314 1314 V -> L (in VWD2; dbSNP:rs61749393).
{ECO:0000269|PubMed:1419803}.
/FTId=VAR_005797.
VARIANT 1316 1316 V -> M (in VWD2; dbSNP:rs61749397).
{ECO:0000269|PubMed:1420817,
ECO:0000269|PubMed:1672694,
ECO:0000269|PubMed:1729889}.
/FTId=VAR_005798.
VARIANT 1318 1318 V -> L (in VWD2).
{ECO:0000269|PubMed:1419803}.
/FTId=VAR_005799.
VARIANT 1324 1324 G -> S (in VWD2; dbSNP:rs61749398).
{ECO:0000269|PubMed:1409710}.
/FTId=VAR_005800.
VARIANT 1341 1341 R -> Q (in VWD2; dbSNP:rs61749403).
{ECO:0000269|PubMed:1672694}.
/FTId=VAR_005801.
VARIANT 1374 1374 R -> C (in VWD2; dbSNP:rs61750071).
{ECO:0000269|PubMed:7620154}.
/FTId=VAR_005802.
VARIANT 1374 1374 R -> H (in VWD2; dbSNP:rs61750072).
{ECO:0000269|PubMed:7620154,
ECO:0000269|PubMed:7734373}.
/FTId=VAR_005803.
VARIANT 1381 1381 T -> A (in dbSNP:rs216311).
{ECO:0000269|PubMed:1988024,
ECO:0000269|PubMed:2584182,
ECO:0000269|PubMed:2864688,
ECO:0000269|PubMed:3019665,
ECO:0000269|PubMed:3488076,
ECO:0000269|PubMed:3489923,
ECO:0000269|PubMed:3524673,
ECO:0000269|PubMed:9373253}.
/FTId=VAR_005804.
VARIANT 1399 1399 R -> H (in dbSNP:rs216312).
{ECO:0000269|PubMed:1672694}.
/FTId=VAR_005805.
VARIANT 1460 1460 L -> V (in VWD2; dbSNP:rs61750088).
{ECO:0000269|PubMed:8123843}.
/FTId=VAR_005806.
VARIANT 1461 1461 A -> V (in VWD2; dbSNP:rs61750089).
{ECO:0000269|PubMed:8547152}.
/FTId=VAR_005807.
VARIANT 1472 1472 D -> H (in dbSNP:rs1800383).
{ECO:0000269|PubMed:1988024,
ECO:0000269|PubMed:2584182,
ECO:0000269|PubMed:3489923}.
/FTId=VAR_029656.
VARIANT 1514 1514 F -> C (in VWD2; dbSNP:rs61750101).
{ECO:0000269|PubMed:8435341}.
/FTId=VAR_005808.
VARIANT 1540 1540 L -> P (in VWD2; dbSNP:rs267607342).
{ECO:0000269|PubMed:8123844}.
/FTId=VAR_005809.
VARIANT 1565 1565 V -> L (in dbSNP:rs1800385).
/FTId=VAR_014630.
VARIANT 1570 1570 Y -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036276.
VARIANT 1584 1584 Y -> C (exhibits increased in
susceptibility to proteolysis by
ADAMTS13; dbSNP:rs1800386).
{ECO:0000269|PubMed:15755288,
ECO:0000269|PubMed:8348943}.
/FTId=VAR_005810.
VARIANT 1597 1597 R -> G (in VWD2; dbSNP:rs61750117).
{ECO:0000269|PubMed:8348943}.
/FTId=VAR_005811.
VARIANT 1597 1597 R -> Q (in VWD2; dbSNP:rs61750577).
{ECO:0000269|PubMed:8338947}.
/FTId=VAR_005812.
VARIANT 1597 1597 R -> W (in VWD2; dbSNP:rs61750117).
{ECO:0000269|PubMed:2786201}.
/FTId=VAR_005813.
VARIANT 1607 1607 V -> D (in VWD2; dbSNP:rs61750579).
{ECO:0000269|PubMed:2786201}.
/FTId=VAR_005814.
VARIANT 1609 1609 G -> R (in VWD2; dbSNP:rs61750580).
{ECO:0000269|PubMed:8338947,
ECO:0000269|PubMed:8348943}.
/FTId=VAR_005815.
VARIANT 1613 1613 S -> P (in VWD2; dbSNP:rs61750581).
{ECO:0000269|PubMed:2010538}.
/FTId=VAR_005816.
VARIANT 1628 1628 I -> T (in VWD2; dbSNP:rs61750584).
{ECO:0000269|PubMed:1420817,
ECO:0000269|PubMed:1673047,
ECO:0000269|PubMed:8123844}.
/FTId=VAR_005817.
VARIANT 1638 1638 E -> K (in VWD2; dbSNP:rs61750588).
{ECO:0000269|PubMed:1429668}.
/FTId=VAR_005818.
VARIANT 1648 1648 P -> S (in VWD2; dbSNP:rs61750590).
{ECO:0000269|PubMed:1420817}.
/FTId=VAR_005819.
VARIANT 1665 1665 V -> E (in VWD2; dbSNP:rs61750596).
{ECO:0000269|PubMed:8338947}.
/FTId=VAR_005820.
VARIANT 2063 2063 P -> S (in VWD3; dbSNP:rs61750615).
/FTId=VAR_009142.
VARIANT 2178 2178 A -> S (in dbSNP:rs34230288).
/FTId=VAR_057026.
VARIANT 2185 2185 R -> Q (in dbSNP:rs2229446).
/FTId=VAR_057027.
VARIANT 2362 2362 C -> F (in VWD3; dbSNP:rs61750630).
/FTId=VAR_009143.
VARIANT 2546 2546 N -> Y (in VWD3; dbSNP:rs61751298).
/FTId=VAR_009144.
VARIANT 2705 2705 G -> R (in dbSNP:rs7962217).
/FTId=VAR_057028.
VARIANT 2739 2739 C -> Y (in VWD3; dbSNP:rs61751305).
{ECO:0000269|PubMed:8088787}.
/FTId=VAR_005821.
VARIANT 2773 2773 C -> R (in VWD2; dbSNP:rs61751310).
{ECO:0000269|PubMed:8622978}.
/FTId=VAR_005822.
MUTAGEN 1149 1149 C->R: Reduced secretion and increased
intracellular retention. Similar
phenotype; when associated with S-1169.
{ECO:0000269|PubMed:11698279}.
MUTAGEN 1169 1169 C->S: Reduced secretion and increased
intracellular retention. Similar
phenotype; when associated with R-1149.
{ECO:0000269|PubMed:11698279}.
CONFLICT 770 770 P -> H (in Ref. 11; AAB59512).
{ECO:0000305}.
CONFLICT 804 804 C -> S (in Ref. 10; AA sequence and 11;
AAB59512). {ECO:0000305}.
CONFLICT 1914 1914 S -> T (in Ref. 1; CAA27972).
{ECO:0000305}.
CONFLICT 2168 2168 C -> S (in Ref. 10; AA sequence).
{ECO:0000305}.
STRAND 767 769 {ECO:0000244|PDB:2MHP}.
STRAND 771 774 {ECO:0000244|PDB:2MHP}.
TURN 781 786 {ECO:0000244|PDB:2MHP}.
TURN 792 794 {ECO:0000244|PDB:2MHP}.
STRAND 795 797 {ECO:0000244|PDB:2MHP}.
STRAND 804 809 {ECO:0000244|PDB:2MHP}.
STRAND 814 817 {ECO:0000244|PDB:2MHP}.
STRAND 820 823 {ECO:0000244|PDB:2MHP}.
HELIX 824 826 {ECO:0000244|PDB:2MHP}.
STRAND 829 833 {ECO:0000244|PDB:2MHP}.
STRAND 841 844 {ECO:0000244|PDB:2MHP}.
STRAND 847 852 {ECO:0000244|PDB:2MHP}.
STRAND 855 858 {ECO:0000244|PDB:2MHP}.
STRAND 1267 1269 {ECO:0000244|PDB:5BV8}.
TURN 1270 1273 {ECO:0000244|PDB:4C29}.
STRAND 1276 1283 {ECO:0000244|PDB:5BV8}.
STRAND 1285 1288 {ECO:0000244|PDB:4C2B}.
HELIX 1290 1305 {ECO:0000244|PDB:5BV8}.
TURN 1307 1310 {ECO:0000244|PDB:1SQ0}.
STRAND 1313 1329 {ECO:0000244|PDB:5BV8}.
HELIX 1337 1345 {ECO:0000244|PDB:5BV8}.
HELIX 1357 1366 {ECO:0000244|PDB:5BV8}.
STRAND 1369 1371 {ECO:0000244|PDB:5BV8}.
STRAND 1377 1385 {ECO:0000244|PDB:5BV8}.
HELIX 1391 1393 {ECO:0000244|PDB:5BV8}.
HELIX 1394 1396 {ECO:0000244|PDB:1U0N}.
HELIX 1397 1406 {ECO:0000244|PDB:5BV8}.
STRAND 1409 1417 {ECO:0000244|PDB:5BV8}.
HELIX 1422 1431 {ECO:0000244|PDB:5BV8}.
HELIX 1433 1435 {ECO:0000244|PDB:4C29}.
STRAND 1438 1442 {ECO:0000244|PDB:5BV8}.
HELIX 1443 1445 {ECO:0000244|PDB:5BV8}.
HELIX 1446 1460 {ECO:0000244|PDB:5BV8}.
STRAND 1498 1504 {ECO:0000244|PDB:3ZQK}.
TURN 1507 1509 {ECO:0000244|PDB:3ZQK}.
HELIX 1511 1527 {ECO:0000244|PDB:3ZQK}.
STRAND 1534 1550 {ECO:0000244|PDB:3ZQK}.
HELIX 1558 1567 {ECO:0000244|PDB:3ZQK}.
HELIX 1578 1587 {ECO:0000244|PDB:3ZQK}.
TURN 1588 1590 {ECO:0000244|PDB:3ZQK}.
HELIX 1592 1594 {ECO:0000244|PDB:3ZQK}.
HELIX 1595 1599 {ECO:0000244|PDB:3GXB}.
STRAND 1602 1608 {ECO:0000244|PDB:3ZQK}.
STRAND 1623 1631 {ECO:0000244|PDB:3ZQK}.
HELIX 1636 1643 {ECO:0000244|PDB:3ZQK}.
STRAND 1649 1652 {ECO:0000244|PDB:3ZQK}.
TURN 1654 1656 {ECO:0000244|PDB:3ZQK}.
HELIX 1657 1670 {ECO:0000244|PDB:3ZQK}.
STRAND 1690 1697 {ECO:0000244|PDB:1ATZ}.
STRAND 1699 1702 {ECO:0000244|PDB:1ATZ}.
HELIX 1704 1720 {ECO:0000244|PDB:1ATZ}.
STRAND 1727 1743 {ECO:0000244|PDB:1ATZ}.
STRAND 1745 1747 {ECO:0000244|PDB:4DMU}.
HELIX 1751 1759 {ECO:0000244|PDB:1ATZ}.
HELIX 1770 1782 {ECO:0000244|PDB:1ATZ}.
HELIX 1784 1786 {ECO:0000244|PDB:2ADF}.
STRAND 1792 1800 {ECO:0000244|PDB:1ATZ}.
HELIX 1809 1817 {ECO:0000244|PDB:1ATZ}.
STRAND 1820 1831 {ECO:0000244|PDB:1ATZ}.
HELIX 1833 1839 {ECO:0000244|PDB:1ATZ}.
HELIX 1841 1847 {ECO:0000244|PDB:1ATZ}.
STRAND 1849 1853 {ECO:0000244|PDB:1ATZ}.
HELIX 1856 1862 {ECO:0000244|PDB:1ATZ}.
STRAND 1863 1865 {ECO:0000244|PDB:2ADF}.
HELIX 1866 1870 {ECO:0000244|PDB:1ATZ}.
STRAND 2728 2732 {ECO:0000244|PDB:4NT5}.
STRAND 2739 2743 {ECO:0000244|PDB:4NT5}.
STRAND 2745 2749 {ECO:0000244|PDB:4NT5}.
STRAND 2756 2761 {ECO:0000244|PDB:4NT5}.
TURN 2762 2765 {ECO:0000244|PDB:4NT5}.
STRAND 2766 2787 {ECO:0000244|PDB:4NT5}.
STRAND 2793 2801 {ECO:0000244|PDB:4NT5}.
STRAND 2804 2809 {ECO:0000244|PDB:4NT5}.
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


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