VWF_MOUSE
ID VWF_MOUSE Reviewed; 2813 AA.
AC Q8CIZ8; Q60863; Q6XUV6; Q8BIU9; Q8CGN0; Q9JK16;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 158.
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 {ECO:0000312|MGI:MGI:98941};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP41950.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP41950.1};
RC TISSUE=Lung {ECO:0000312|EMBL:AAP41950.1};
RA Chitta M.S., Duhe R.J., Kermode J.C.;
RT "Cloning of full-length murine von Willebrand factor cDNA.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP41950.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAN07781.2};
RA Lenting P.J., Westein E., de Groot P.G., Denis C.V.;
RT "Murine von Willebrand factor.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAB86200.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1238-1658 (ISOFORM 1).
RX PubMed=10722222; DOI=10.1098/rspb.2000.1014;
RA Huchon D., Catzeflis F.M., Douzery E.J.P.;
RT "Variance of molecular datings, evolution of rodents and the phylogenetic
RT affinities between Ctenodactylidae and Hystricognathi.";
RL Proc. R. Soc. B 267:393-402(2000).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAA82929.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1298-1684 (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAA82929.1};
RX PubMed=8193357;
RA Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E.,
RA Reddington M., Novak E.K., Swank R.T., Ginsburg D.;
RT "von Willebrand disease in the RIIIS/J mouse is caused by a defect outside
RT of the von Willebrand factor gene.";
RL Blood 83:3225-3231(1994).
RN [6]
RP ERRATUM OF PUBMED:8193357.
RX PubMed=7662996;
RA Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E.,
RA Reddington M., Novak E.K., Swank R.T., Ginsburg D.;
RL Blood 86:2461-2461(1995).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10930441; DOI=10.1172/jci9896;
RA Ni H., Denis C.V., Subbarao S., Degen J.L., Sato T.N., Hynes R.O.,
RA Wagner D.D.;
RT "Persistence of platelet thrombus formation in arterioles of mice lacking
RT both von Willebrand factor and fibrinogen.";
RL J. Clin. Invest. 106:385-392(2000).
RN [8]
RP MUTAGENESIS OF ARG-1205, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:14613933};
RX PubMed=14613933; DOI=10.1074/jbc.m310436200;
RA Lenting P.J., Westein E., Terraube V., Ribba A.-S., Huizinga E.G.,
RA Meyer D., de Groot P.G., Denis C.V.;
RT "An experimental model to study the in vivo survival of von Willebrand
RT factor. Basic aspects and application to the R1205H mutation.";
RL J. Biol. Chem. 279:12102-12109(2004).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1261-1468 IN COMPLEX WITH SNAKE
RP VENOM BOTROCETIN, AND DISULFIDE BOND.
RX PubMed=15665869; DOI=10.1038/nsmb892;
RA Fukuda K., Doggett T., Laurenzi I.J., Liddington R.C., Diacovo T.G.;
RT "The snake venom protein botrocetin acts as a biological brace to promote
RT dysfunctional platelet aggregation.";
RL Nat. Struct. Mol. Biol. 12:152-159(2005).
CC -!- FUNCTION: Important in the maintenance of hemostasis, it promotes
CC adhesion of platelets to the sites of vascular injury by forming a
CC molecular bridge between sub-endothelial collagen matrix and platelet-
CC surface receptor complex GPIb-IX-V. Also acts as a chaperone for
CC coagulation factor VIII, delivering it to the site of injury,
CC stabilizing its heterodimeric structure and protecting it from
CC premature clearance from plasma. {ECO:0000250|UniProtKB:P04275,
CC ECO:0000269|PubMed:10930441}.
CC -!- SUBUNIT: Multimeric. Interacts with F8 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular
CC space, extracellular matrix {ECO:0000250}. Note=Localized to storage
CC granules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.1};
CC IsoId=Q8CIZ8-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8CIZ8-2; Sequence=VSP_051618, VSP_051619;
CC -!- TISSUE SPECIFICITY: Plasma. Expressed in liver.
CC {ECO:0000269|PubMed:14613933}.
CC -!- DOMAIN: The von Willebrand antigen 2 is required for multimerization of
CC vWF and for its targeting to storage granules. {ECO:0000250}.
CC -!- PTM: All cysteine residues are involved in intrachain or interchain
CC disulfide bonds. {ECO:0000250|UniProtKB:P04275}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Platelet deposition and thrombus formation is
CC significantly delayed, but despite this small thrombi do eventually
CC form. At later stages, thrombus growth frequently arrests leaving open
CC channels within arterioles. In double knockouts of FGA and VWF, in
CC addition to delayed platelet deposition, thrombi are fragile and
CC frequently embolize. {ECO:0000269|PubMed:10930441}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38822.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY208897; AAP41950.1; -; mRNA.
DR EMBL; AY162409; AAN73055.1; -; mRNA.
DR EMBL; AF539800; AAN07781.2; -; mRNA.
DR EMBL; AK083237; BAC38822.1; ALT_INIT; mRNA.
DR EMBL; AJ238390; CAB86200.1; -; Genomic_DNA.
DR EMBL; U27810; AAA82929.1; -; Genomic_DNA.
DR CCDS; CCDS20552.1; -. [Q8CIZ8-1]
DR RefSeq; NP_035838.3; NM_011708.4.
DR PDB; 1U0O; X-ray; 2.70 A; C=1261-1468.
DR PDBsum; 1U0O; -.
DR SMR; Q8CIZ8; -.
DR STRING; 10090.ENSMUSP00000107873; -.
DR MEROPS; I08.950; -.
DR MEROPS; I08.954; -.
DR GlyGen; Q8CIZ8; 24 sites.
DR PhosphoSitePlus; Q8CIZ8; -.
DR SwissPalm; Q8CIZ8; -.
DR CPTAC; non-CPTAC-3613; -.
DR MaxQB; Q8CIZ8; -.
DR PaxDb; Q8CIZ8; -.
DR PRIDE; Q8CIZ8; -.
DR ProteomicsDB; 299740; -. [Q8CIZ8-1]
DR ProteomicsDB; 299741; -. [Q8CIZ8-2]
DR DNASU; 22371; -.
DR GeneID; 22371; -.
DR KEGG; mmu:22371; -.
DR CTD; 7450; -.
DR MGI; MGI:98941; Vwf.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q8CIZ8; -.
DR PhylomeDB; Q8CIZ8; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
DR BioGRID-ORCS; 22371; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Vwf; mouse.
DR EvolutionaryTrace; Q8CIZ8; -.
DR PRO; PR:Q8CIZ8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CIZ8; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0033093; C:Weibel-Palade body; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019865; F:immunoglobulin binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:MGI.
DR GO; GO:0007599; P:hemostasis; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR037578; Von_Willebrand_factor.
DR InterPro; IPR032361; VWA_N2.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR11339:SF361; PTHR11339:SF361; 3.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF01826; TIL; 4.
DR Pfam; PF00092; VWA; 3.
DR Pfam; PF16164; VWA_N2; 1.
DR Pfam; PF00093; VWC; 2.
DR Pfam; PF00094; VWD; 4.
DR PIRSF; PIRSF002495; VWF; 1.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00327; VWA; 3.
DR SMART; SM00214; VWC; 7.
DR SMART; SM00215; VWC_out; 3.
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; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hemostasis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CHAIN 23..763
FT /note="von Willebrand antigen 2"
FT /id="PRO_0000022684"
FT CHAIN 764..2813
FT /note="von Willebrand factor"
FT /id="PRO_0000022685"
FT DOMAIN 33..201
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 295..348
FT /note="TIL 1"
FT DOMAIN 386..560
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 652..707
FT /note="TIL 2"
FT DOMAIN 804..827
FT /note="TIL 3"
FT DOMAIN 865..1032
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1146..1196
FT /note="TIL 4"
FT DOMAIN 1277..1453
FT /note="VWFA 1; binding site for platelet glycoprotein Ib"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1498..1665
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1691..1871
FT /note="VWFA 3; principal binding site for collagens type I
FT and III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1948..2124
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2255..2328
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2429..2495
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2580..2645
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2724..2812
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 764..787
FT /note="Amino-terminal"
FT REGION 788..833
FT /note="E1"
FT REGION 826..853
FT /note="CX"
FT REGION 2216..2261
FT /note="E2"
FT MOTIF 2507..2509
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 1005
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000250"
FT CARBOHYD 1231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 1248
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1255
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1256
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1468
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1477
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1486
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 1515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 1574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 1679
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 2223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2298
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250, ECO:0000305"
FT CARBOHYD 2400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 2810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 57..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 388..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 410..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 432..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 767..808
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 776..804
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 810..821
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 889..1031
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 898..993
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 914..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID ?..996
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1060..1084
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1071..1111
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1089..1091
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1126..1130
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1149..1169
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1153..1165
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1196..1199
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1234..1237
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1272..1458
FT /evidence="ECO:0000269|PubMed:15665869"
FT DISULFID 1669..1670
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1686..1872
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1879..1904
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1899..1940
FT /note="Or C-1899 with C-1942"
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039, ECO:0000255|PROSITE-
FT ProRule:PRU00580"
FT DISULFID 1927..2088
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 1950..2085
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1972..2123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1993..2001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2724..2774
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 2739..2788
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 2750..2804
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 2754..2806
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID ?..2811
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT VAR_SEQ 387..402
FT /note="ECLVTGQSHFKSFDNR -> RLGTFSPFLPVLCGEV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051618"
FT VAR_SEQ 403..2813
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051619"
FT MUTAGEN 1205
FT /note="R->H: Accelerated clearance of VWF from blood
FT plasma."
FT /evidence="ECO:0000269|PubMed:14613933"
FT CONFLICT 103
FT /note="M -> T (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="L -> R (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="R -> C (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="R -> C (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="Y -> Q (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 1007
FT /note="S -> F (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="A -> V (in Ref. 4; CAB86200)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="S -> D (in Ref. 5; AAA82929)"
FT /evidence="ECO:0000305"
FT CONFLICT 1485..1486
FT /note="IS -> TL (in Ref. 5; AAA82929)"
FT /evidence="ECO:0000305"
FT CONFLICT 2361
FT /note="D -> A (in Ref. 1; AAP41950)"
FT /evidence="ECO:0000305"
FT STRAND 1274..1283
FT /evidence="ECO:0007829|PDB:1U0O"
FT STRAND 1285..1288
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1290..1304
FT /evidence="ECO:0007829|PDB:1U0O"
FT STRAND 1311..1329
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1337..1345
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1357..1366
FT /evidence="ECO:0007829|PDB:1U0O"
FT TURN 1367..1369
FT /evidence="ECO:0007829|PDB:1U0O"
FT STRAND 1377..1385
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1391..1394
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1397..1406
FT /evidence="ECO:0007829|PDB:1U0O"
FT STRAND 1409..1420
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1422..1430
FT /evidence="ECO:0007829|PDB:1U0O"
FT STRAND 1438..1442
FT /evidence="ECO:0007829|PDB:1U0O"
FT HELIX 1443..1458
FT /evidence="ECO:0007829|PDB:1U0O"
SQ SEQUENCE 2813 AA; 309269 MW; 3EE2C7D8FF21FFA6 CRC64;
MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM YSFAGGCSYL
LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG TVMQGDQSIS MPYASQGLYL
ELEAGYYKLS SETFGFAARI DGNGNFQVLM SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL
TSDPYDFANS WALSSEEQRC KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL
VDPESFVALC EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME
YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC VHAGKRYPPG
TSLSQDCNTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCED
HTFSIVIETM QCADDPDAVC TRSVSVRLSA LHNSLVKLKH GGAVGIDGQD VQLPFLQGDL
RIQHTVMASV RLSYAEDLQM DWDGRGRLLV KLSPVYSGKT CGLCGNYNGN KGDDFLTPAG
LVEPLVVDFG NAWKLQGDCS DLRRQHSDPC SLNPRLTRFA EEACALLTSS KFEACHHAVS
PLPYLQNCRY DVCSCSDSRD CLCNAVANYA AECARKGVHI GWREPGFCAL GCPQGQVYLQ
CGNSCNLTCR SLSLPDEECS EVCLEGCYCP PGLYQDERGD CVPKAQCPCY YDGELFQPAD
IFSDHHTMCY CEDGFMHCTT SGTLGSLLPD TVLSSPLSHR SKRSLSCRPP MVKLVCPADN
PRAQGLECAK TCQNYDLERM SLGCVSGCLC PPGMVRHENK CVALERCPCF HQGAEYAPGD
TVKIGCNTCV CRERKWNCTN HVCDATRSAI GMAHYLTFDG LKYLFPGECQ YVLVYDYCGS
NPGTFQILVG NEGCSYPSVK CRKRVTILVD GGELELFDGE VNVKRPLRDE SHFEVVESGR
YVILLLGQAL SVVWDHHLSI SVVLKHTYQE QVCGLCGNFD GIQNNDSTTS SLQVEEDPVN
FGNSWKVSSQ CADTRKLSLD VSPATCHNNI MKQTMVDSAC RILTSDVFQG CNRLVDPEPY
LDICIYDTCS CESIGDCACF CDTIAAYAHV CAQHGQVVAW RTPTLCPQSC EEKNVRENGY
ECEWRYNSCA PACPVTCQHP EPLACPVQCV EGCHAHCPPG RILDELLQTC VDPQDCPVCE
VAGRRLAPGK KITLSPDDPA HCQNCHCDGV NLTCEACQEP GGLVAPPTDA PVSSTTPYVE
DTPEPPLHNF YCSKLLDLVF LLDGSSMLSE AEFEVLKAFV VGMMERLHIS QKRIRVAVVE
YHDGSRAYLE LKARKRPSEL RRITSQIKYT GSQVASTSEV LKYTLFQIFG KIDRPEASHI
TLLLTASQEP PRMARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIRLIEK QAPENKAFLL
SGVDELEQRR DEIVSYLCDL APEAPAPTQP PQVAHVTVSP GIAGISSPGP KRKSMVLDVV
FVLEGSDEVG EANFNKSKEF VEEVIQRMDV SPDATRISVL QYSYTVTMEY AFNGAQSKEE
VLRHVREIRY QGGNRTNTGQ ALQYLSEHSF SPSQGDRVEA PNLVYMVTGN PASDEIKRLP
GDIQVVPIGV GPHANMQELE RISRPIAPIF IRDFETLPRE APDLVLQTCC SKEGLQLPTL
PPLPDCSQPL DVVLLLDGSS SLPESSFDKM KSFAKAFISK ANIGPHLTQV SVIQYGSINT
IDVPWNVVQE KAHLQSLVDL MQQEGGPSQI GDALAFAVRY VTSQIHGARP GASKAVVIII
MDTSLDPVDT AADAARSNRV AVFPVGVGDR YDEAQLRILA GPGASSNVVK LQQVEDLSTM
ATLGNSFFHK LCSGFSGVCV DEDGNEKRPG DVWTLPDQCH TVTCLANGQT LLQSHRVNCD
HGPRPSCANS QSPVRVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVIFQNK
EQDLEVLLHN GACSPGAKQA CMKSIEIKHA GVSAELHSNM EMAVDGRLVL APYVGENMEV
SIYGAIMYEV RFTHLGHILT YTPQNNEFQL QLSPKTFASK MHGLCGICDE NGANDFTLRD
GTVTTDWKRL VQEWTVQQPG YTCQAVPEEQ CPVSDSSHCQ VLLSASFAEC HKVIAPATFH
TICQQDSCHQ ERVCEVIASY AHLCRTSGVC VDWRTTDFCA MSCPPSLVYN HCERGCPRHC
DGNTSFCGDH PSEGCFCPQH QVFLEGSCVP EEACTQCVGE DGVRHQFLET WVPDHQPCQI
CMCLSGRKIN CTAQPCPTAR APTCGPCEVA RLKQSTNLCC PEYECVCDLF NCNLPPVPPC
EGGLQPTLTN PGECRPTFTC DCRKEECKRV SPPSCPPHRT PTLRKTQCCD EYECACSCVN
STLSCPLGYL ASATTNDCGC TTTTCLPDKV CVHRGTVYPV GQFWEEGCDT CTCTDMEDTV
VGLRVVQCSQ RPCEDSCQPG FSYVLHEGEC CGRCLPSACK VVAGSLRGDS HSSWKSVGSR
WAVPENPCLV NECVRVEDAV FVQQRNISCP QLAVPTCPTG FQLNCETSEC CPSCHCEPVE
ACLLNGTIIG PGKSVMVDLC TTCRCIVQTD AISRFKLECR KTTCEACPMG YREEKSQGEC
CGRCLPTACT IQLRGGRIMT LKQDETFQDG CDSHLCRVNE RGEYIWEKRV TGCPPFDEHK
CLAEGGKIVK IPGTCCDTCE EPDCKDITAK VQYIKVGDCK SQEEVDIHYC QGKCASKAVY
SIDIEDVQEQ CSCCLPSRTE PMRVPLHCTN GSVVYHEVIN AMQCRCSPRN CSK
