VWF_RAT
ID VWF_RAT Reviewed; 430 AA.
AC Q62935; Q78E31; Q9Z0P2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=von Willebrand factor;
DE Short=vWF;
DE Flags: Fragment;
GN Name=Vwf {ECO:0000312|EMBL:CAB37852.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA96311.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-372.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAA96311.1};
RC TISSUE=Aortic endothelium {ECO:0000312|EMBL:AAA96311.1};
RA Senis Y.A., Slack A., Giles A.R., Maurice D.H.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB37852.1}
RP NUCLEOTIDE SEQUENCE OF 13-430.
RX PubMed=10335651; DOI=10.1093/oxfordjournals.molbev.a026140;
RA Huchon D., Catzeflis F.M., Douzery E.J.P.;
RT "Molecular evolution of the nuclear von Willebrand factor gene in mammals
RT and the phylogeny of rodents.";
RL Mol. Biol. Evol. 16:577-589(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAA96311.1}
RP NUCLEOTIDE SEQUENCE OF 131-267.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAB39496.1};
RC TISSUE=Aorta {ECO:0000312|EMBL:AAB39496.1};
RA Adams L.D., Werny I., Schwartz S.M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P04275}.
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 -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; U50044; AAA96311.1; -; mRNA.
DR EMBL; AJ224673; CAB37852.1; -; Genomic_DNA.
DR EMBL; U81240; AAB39496.1; -; mRNA.
DR AlphaFoldDB; Q62935; -.
DR SMR; Q62935; -.
DR STRING; 10116.ENSRNOP00000026643; -.
DR GlyGen; Q62935; 8 sites.
DR PhosphoSitePlus; Q62935; -.
DR PaxDb; Q62935; -.
DR PeptideAtlas; Q62935; -.
DR UCSC; RGD:621759; rat.
DR RGD; 621759; Vwf.
DR eggNOG; KOG1216; Eukaryota.
DR PhylomeDB; Q62935; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0033093; C:Weibel-Palade body; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019865; F:immunoglobulin binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; IMP:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0070417; P:cellular response to cold; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007599; P:hemostasis; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0030168; P:platelet activation; IMP:RGD.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0010165; P:response to X-ray; IEP:RGD.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR037578; Von_Willebrand_factor.
DR InterPro; IPR032361; VWA_N2.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR11339:SF361; PTHR11339:SF361; 1.
DR Pfam; PF00092; VWA; 2.
DR Pfam; PF16164; VWA_N2; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR PROSITE; PS50234; VWFA; 2.
PE 2: Evidence at transcript level;
KW Blood coagulation; Cell adhesion; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hemostasis; Reference proteome; Repeat; Secreted.
FT CHAIN <1..>430
FT /note="von Willebrand factor"
FT /id="PRO_0000065939"
FT DOMAIN 52..228
FT /note="VWFA 1; binding site for platelet glycoprotein Ib"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 273..>430
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 30
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 252
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 261
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 9..12
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 47..233
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT CONFLICT 243
FT /note="S -> T (in Ref. 1; AAA96311/AAB39496)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAA96311.1"
FT NON_TER 430
FT /evidence="ECO:0000312|EMBL:CAB37852.1"
SQ SEQUENCE 430 AA; 48139 MW; 1DCF3148D85DCB69 CRC64;
HCDGVNLTCE ACQEPGGLVV PPTDAPVSST TPYVEDTPEP PLHNFYCSKL LDLVFLLDGS
YRLSEAEFEV LKAFVVGTME RLHISQKRIR VAVVEYHDGS HAYLELRARK RPSELRRIAS
QIKYVGSQLA STSEVLKYTL FQIFGKIDRP EASRVILLLT ASQEPQRMAR YFTRYLQGFK
KKKVILIPVG IGPHANLKQI RLIEKQAPEN KAFLLSGVDE LEQRRDEIIN YLCDLAPEAP
APSKPPQVAH ITVSPGISGV SSPGPKRKSL VLDVVFVLEA SDEVGEANFN KSKEFLEEVI
QRMDVSPAGT HIAVLQYSYT VNVEYTFKEA QSKEDVLRHV REIRYQGGNR TNTGQALQYL
SEHSFSPSQG DREQAPNLVY MVTGNPASDE IRRLPGDIQV VPIGVGSRAN LQELERISRP
ITPIFIQDFE
