VWF_BOVIN
ID VWF_BOVIN Reviewed; 937 AA.
AC P80012; Q28011;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=von Willebrand factor;
DE Short=vWF;
DE Flags: Precursor; Fragment;
GN Name=VWF; Synonyms=F8VWF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9165093; DOI=10.1016/s0167-4838(97)00043-5;
RA Janel N., Ribba A.S., Cherel G., Kerbiriou-Nabias D., Meyer D.;
RT "Primary structure of the propeptide and factor VIII-binding domain of
RT bovine von Willebrand factor.";
RL Biochim. Biophys. Acta 1339:4-8(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-177.
RX PubMed=8566794; DOI=10.1016/0378-1119(95)00696-6;
RA Janel N., Schwachtgen J.L., Bakhshi M.R., Barek L., Meyer D.,
RA Kerbiriou-Nabias D.;
RT "Comparison of the 5'-flanking sequences of the human and bovine von
RT Willebrand factor-encoding genes reveals alternation of highly homologous
RT domains with species-specific Alu-type repeats.";
RL Gene 167:291-295(1995).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1707363; DOI=10.1111/j.1432-1033.1991.tb15864.x;
RA Fujisawa T., Takagi J., Sekiya F., Goto A., Miake F., Saito Y.;
RT "Monoclonal antibodies that inhibit binding of propolypeptide of von
RT Willebrand factor to collagen. Localization of epitopes.";
RL Eur. J. Biochem. 196:673-677(1991).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7588715; DOI=10.1111/j.1432-1033.1995.773zz.x;
RA Takagi J., Aoyama T., Ueki S., Ohba H., Saito Y., Lorand L.;
RT "Identification of factor-XIIIa-reactive glutaminyl residues in the
RT propolypeptide of bovine von Willebrand factor.";
RL Eur. J. Biochem. 232:773-777(1995).
RN [5]
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.
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 -!- DOMAIN: The propeptide is required for multimerization of vWF and for
CC its targeting to storage granules. {ECO:0000250}.
CC -!- PTM: All cysteine residues are involved in intrachain or interchain
CC disulfide bonds. {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; Y09353; CAA70525.1; -; mRNA.
DR EMBL; U28147; AAA96953.1; -; mRNA.
DR RefSeq; NP_001192237.1; NM_001205308.1.
DR AlphaFoldDB; P80012; -.
DR SMR; P80012; -.
DR STRING; 9913.ENSBTAP00000016273; -.
DR MEROPS; I08.954; -.
DR PaxDb; P80012; -.
DR PRIDE; P80012; -.
DR GeneID; 280958; -.
DR KEGG; bta:280958; -.
DR CTD; 7450; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P80012; -.
DR OrthoDB; 12226at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0007599; P:hemostasis; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
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; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR11339:SF361; PTHR11339:SF361; 1.
DR Pfam; PF08742; C8; 2.
DR Pfam; PF01826; TIL; 2.
DR Pfam; PF00094; VWD; 3.
DR SMART; SM00832; C8; 2.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 2.
DR SUPFAM; SSF57567; SSF57567; 3.
DR PROSITE; PS51233; VWFD; 3.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hemostasis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..762
FT /evidence="ECO:0000250"
FT /id="PRO_0000022678"
FT CHAIN 763..>937
FT /note="von Willebrand factor"
FT /id="PRO_0000022679"
FT DOMAIN 33..201
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 294..347
FT /note="TIL 1"
FT DOMAIN 385..559
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 651..706
FT /note="TIL 2"
FT DOMAIN 864..>937
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 763..786
FT /note="Amino-terminal"
FT REGION 787..832
FT /note="E1"
FT REGION 825..852
FT /note="CX"
FT SITE 410
FT /note="Factor XIIIa-binding"
FT SITE 414
FT /note="Factor XIIIa-binding"
FT SITE 605
FT /note="Factor XIIIa-binding"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 856
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 387..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 409..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 431..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 766..807
FT /evidence="ECO:0000250"
FT DISULFID 775..803
FT /evidence="ECO:0000250"
FT DISULFID 913..920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 330
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="G -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 937
SQ SEQUENCE 937 AA; 102599 MW; 9BF4C94A254A5629 CRC64;
MFPTRLARLL LAVALTLPGA LCGEGALGKS SMARCSLFGA DFINTFDESM YSFSGDCSYL
LAGDCKTHSF SIVGDFQGGR RMGLSVYLGE FFDIHVFVNG TVLQGGQHVS MPYATRGLYL
ETEVGHHKLS SESYGFVARI DGSGNFQILL SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL
TSDPYDFANS WALSSEEQRC PRVSPPSSSC NVSSELQKGL WEKCQLLKTA SVFARCHALV
DPEPFVALCE RMLCACAQGL RCPCPVLLEY ARACAKQGML LYGWADHSSC RPDCPTGMEY
KECVSPCHRT CRSLSITEVC REQCVDGCSC PEGQLLDEGR CVESTECPCV HAGKPYPPGA
SLSRDCNTCI CRNSQWVCSN EDCPGECLIT GQSHFKSFDD RHFTFSGVCQ YLLAQDCQDH
SFSVVIETVQ CADDPDAVCT RSVTVRLPSP HHGLLKLKHG GGVALDGQDV QIPLLQGDLR
IQHTVTASLQ LNFGEDLQID WDGRGRLLLK LSPVYAGRTC GLCGNYNGNQ RDDFLTPAGL
VEPLVEHFGN SWKLRADCED LQEQPSDPCS LNPRLTKFAD QACAILTSPK FEACHSAVSP
LPYLRNCRYD VCACSDGRDC LCDAVANYAA ACARRGVHVG WREPSFCALS CPHGQVYQQC
GTPCNLTCRS LSHPDEECTE VCLEGCFCPP GLFLDETGSC VPKAQCPCYY DGEIFQPEDI
FSDHHTMCYC EDGFMHSATS GAPGSLLPEA VLSSPLSHRS KRSLSCRPPM VKVVCPADNP
RAEGLECTKT CQNYDLECMS TGCVSGCLPA PGMVRHENRC VALERCPCFH QGREYAPGDR
VKVDCNSCVC QDRKWNCTDH VCDASCSALG LAHYFTFDGL KYLFPGECQY VLVQDHCGSN
PGTFRVLVGN EGCSVPSLKC RKRITILVEG GEIELFD
