VWF_CANLF
ID VWF_CANLF Reviewed; 2813 AA.
AC Q28295; Q28311; Q9TSI4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=von Willebrand factor;
DE Short=vWF;
DE Flags: Precursor;
GN Name=VWF; Synonyms=F8VWF;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stoy S.J., Shibuya H., Nonneman D.J., Holzhauer J., Mohammed I.H.,
RA Johnson G.S.;
RT "Canine vWF cDNA sequence.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=10961880;
RA Haberichter S.L., Fahs S.A., Montgomery R.R.;
RT "von Willebrand factor storage and multimerization: 2 independent
RT intracellular processes.";
RL Blood 96:1808-1815(2000).
RN [3]
RP SEQUENCE REVISION TO 55.
RA Montgomery R.R., Fahs S., Montgomery M.W.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC STRAIN=Scottish terrier; TISSUE=Uterus;
RX PubMed=10668811; DOI=10.1892/0891-6640(2000)014<0010:mcvwdi>2.3.co;2;
RA Venta P.J., Li J., Yuzbasiyan-Gurkan V., Brewer G.J., Schall W.D.;
RT "Mutation causing von Willebrand's disease in Scottish Terriers.";
RL J. Vet. Intern. Med. 14:10-19(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1234-1669.
RC TISSUE=Blood;
RA Mancuso D.J., Christopherson P.A., Kroner P.A., Montgomery R.R.;
RT "The canine von Willebrand factor gene: sequence and expression of a region
RT encoding the glycoprotein Ib/IX binding domain.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
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, glycoprotein Ibalpha/IX/V. Also acts as a
CC chaperone for coagulation factor VIII, delivering it to the site of
CC injury, stabilizing its heterodimeric structure and protecting it from
CC premature clearance from plasma (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Multimeric. Interacts with F8. {ECO:0000269|PubMed:10961880}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DOMAIN: The propeptide is required for multimerization of vWF and for
CC its targeting to storage granules.
CC -!- PTM: All cysteine residues are involved in intrachain or interchain
CC disulfide bonds. {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in VWF are the cause of von Willebrand disease
CC (VWD) in the Scottish Terrier. VWD is characterized by frequent
CC bleeding. Type I VWD is associated with a deficiency of VWF; type II by
CC normal to decreased plasma level of VWF; type III by a virtual absence
CC of VWF. {ECO:0000269|PubMed:10668811}.
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DR EMBL; L76227; AAB05549.1; -; mRNA.
DR EMBL; U66246; AAB93766.2; -; mRNA.
DR EMBL; AF099154; AAD04919.1; -; mRNA.
DR EMBL; L16903; AAA30903.1; -; Genomic_DNA.
DR RefSeq; NP_001002932.1; NM_001002932.1.
DR SMR; Q28295; -.
DR STRING; 9615.ENSCAFP00000053390; -.
DR MEROPS; I08.950; -.
DR MEROPS; I08.954; -.
DR PaxDb; Q28295; -.
DR PRIDE; Q28295; -.
DR Ensembl; ENSCAFT00000083915; ENSCAFP00000065165; ENSCAFG00000015228.
DR GeneID; 399544; -.
DR KEGG; cfa:399544; -.
DR CTD; 7450; -.
DR VGNC; VGNC:48329; VWF.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q28295; -.
DR OrthoDB; 12226at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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 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; 2.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF01826; TIL; 3.
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; 5.
DR SMART; SM00215; VWC_out; 2.
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 Blood coagulation; Cell adhesion; Cleavage on pair of basic residues;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hemostasis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PROPEP 23..763
FT /evidence="ECO:0000250"
FT /id="PRO_0000022680"
FT CHAIN 764..2813
FT /note="von Willebrand factor"
FT /id="PRO_0000022681"
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 776..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"
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"
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 531..533
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 698..700
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2507..2509
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
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 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2790
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"
FT DISULFID 776..804
FT /evidence="ECO:0000250"
FT DISULFID 810..821
FT /evidence="ECO:0000250"
FT DISULFID 867..996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
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 1060..1084
FT /evidence="ECO:0000250"
FT DISULFID 1071..1111
FT /evidence="ECO:0000250"
FT DISULFID 1089..1091
FT /evidence="ECO:0000250"
FT DISULFID 1126..1130
FT /evidence="ECO:0000250"
FT DISULFID 1149..1169
FT /evidence="ECO:0000250"
FT DISULFID 1153..1165
FT /evidence="ECO:0000250"
FT DISULFID 1196..1199
FT /evidence="ECO:0000250"
FT DISULFID 1234..1237
FT /evidence="ECO:0000250"
FT DISULFID 1272..1458
FT /evidence="ECO:0000250"
FT DISULFID 1669..1670
FT /evidence="ECO:0000250"
FT DISULFID 1686..1872
FT /evidence="ECO:0000250"
FT DISULFID 1879..1904
FT /evidence="ECO:0000250"
FT DISULFID 1899..1940
FT /note="Or C-1899 with C-1942"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039,
FT ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1927..2088
FT /evidence="ECO:0000250"
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"
FT DISULFID 2739..2788
FT /evidence="ECO:0000250"
FT DISULFID 2750..2804
FT /evidence="ECO:0000250"
FT DISULFID 2754..2806
FT /evidence="ECO:0000250"
FT DISULFID ?..2811
FT /evidence="ECO:0000250"
FT CONFLICT 70
FT /note="V -> I (in Ref. 4; AAD04919)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> G (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="I -> V (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
FT CONFLICT 409..411
FT /note="VCH -> ICQ (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="G -> A (in Ref. 1; AAB05549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="F -> L (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
FT CONFLICT 2381
FT /note="L -> P (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
FT CONFLICT 2406
FT /note="P -> L (in Ref. 2; AAB93766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2813 AA; 309719 MW; 5DF93E1E5E72F80C CRC64;
MSPTRLVRVL LALALILPGK LCTKGTVGRS SMARCSLFGG DFINTFDESM YSFAGDCSYL
LAGDCQEHSV SLIGGFQNGK RVSLSVYLGE FFDIHLFVNG TMLQGTQSIS MPYASNGLYL
EAEAGYYKLS SEAYGFVARI DGNGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFRTQEGTL
TSDPYDFANS WALSSGEQRC KRVSPPSSPC NVSSDEVQQV LWEQCQLLKS ASVFARCHPL
VDPEPFVALC ERTLCTCVQG MECPCAVLLE YARACAQQGI VLYGWTDHSV CRPACPAGME
YKECVSPCTR TCQSLHVKEV CQEQCVDGCS CPEGQLLDEG HCVGSAECSC VHAGQRYPPG
ASLLQDCHTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGVC HYLLAQDCQD
HTFSVVIETV QCADDLDAVC TRSVTVRLPG HHNSLVKLKH GGGVSMDGQD IQIPLLQGDL
RIQHTVMASV RLSYGEDLQM DWDGRGRLLV TLSPAYAGKT CGLCGNYNGN RGDDFVTPAG
LAEPLVEDFG NAWKLLGACE NLQKQHRDPC SLNPRQARFA EEACALLTSS KFEPCHRAVG
PQPYVQNCRY DVCSCSDGRD CLCSAVANYA AACARRGVHI AWREPGFCAL SCPQGQVYLQ
CGTPCNMTCR SLSYPEEDCN EVCLEGCFCP PGLYLDERGD CVPKAQCPCY YDGEIFQPED
IFSDHHTMCY CEDGFMHCTT SGGLGSLLPN PVLSSPRSHR SKRSLSCRPP MVKLVCPADN
PRAEGLECAK TCQNYDLQCM STGCVSGCLC PQGMVRHENR CVALERCPCF HQGQEYAPGE
TVKIDCNTCV CRDRKWNCTD HVCDATCSAI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS
NPGTFRILVG NEGCSYPSVK CKKRVTILVE GGEIELFDGE VNVKKPMKDE THFEVVESGQ
YVILLLGKAL SVVWDHRLSI SVTLKRTYQE QVCGLCGNFD GIQNNDFTSS SLQIEEDPVD
FGNSWKVNPQ CADTKKVPLD SSPAVCHNNI MKQTMVDSSC RILTSDIFQD CNRLVDPEPF
LDICIYDTCS CESIGDCTCF CDTIAAYAHV CAQHGKVVAW RTATFCPQNC EERNLHENGY
ECEWRYNSCA PACPITCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC IDPEDCPVCE
VAGRRLAPGK KIILNPSDPE HCQICHCDGV NFTCQACREP GSLVVPPTEG PIGSTTSYVE
DTPEPPLHDF HCSRLLDLVF LLDGSSKLSE DEFEVLKVFV VGMMEHLHIS QKRIRVAVVE
YHDGSHAYIE LKDRKRPSEL RRITSQVKYA GSEVASTSEV LKYTLFQIFG KIDRPEASRI
ALLLMASQEP SRLARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIHLIEK QAPENKAFVF
SGVDELEQRR DEIINYLCDL APEAPAPTQH PPMAQVTVGS ELLGVSSPGP KRNSMVLDVV
FVLEGSDKIG EANFNKSREF MEEVIQRMDV GQDRIHVTVL QYSYMVTVEY TFSEAQSKGE
VLQQVRDIRY RGGNRTNTGL ALQYLSEHSF SVSQGDREQV PNLVYMVTGN PASDEIKRMP
GDIQVVPIGV GPHANVQELE KIGWPNAPIL IHDFEMLPRE APDLVLQRCC SGEGLQIPTL
SPTPDCSQPL DVVLLLDGSS SIPASYFDEM KSFTKAFISR ANIGPRLTQV SVLQYGSITT
IDVPWNVAYE KVHLLSLVDL MQQEGGPSQI GDALSFAVRY VTSEVHGARP GASKAVVILV
TDVSVDSVDA AAEAARSNRV TVFPIGIGDR YSEAQLSSLA GPKAGSNMVR LQRIEDLPTV
ATLGNSFFHK LCSGFDRVCV DEDGNEKRPG DVWTLPDQCH TVTCLPDGQT LLKSHRVNCD
RGPRPSCPNG QPPLRVEETC GCRWTCPCVC MGSSTRHIVT FDGQNFKLTG SCSYVLFQNK
EQDLEVILHN GACSPGAKET CMKSIEVKHD GLSVELHSDM QMTVNGRLVS IPYVGGDMEV
NVYGTIMYEV RFNHLGHIFT FTPQNNEFQL QLSPRTFASK TYGLCGICDE NGANDFILRD
GTVTTDWKAL IQEWTVQQLG KTCQPVPEEQ CPVSSSSHCQ VLLSELFAEC HKVLAPATFY
AMCQPDSCHP KKVCEAIALY AHLCRTKGVC VDWRRANFCA MSCPPSLVYN HCEHGCPRLC
EGNTSSCGDQ PSEGCFCPPN QVMLEGSCVP EEACTQCISE DGVRHQFLET WVPAHQPCQI
CTCLSGRKVN CTLQPCPTAR APTCGPCEVA RLRQNAEQCC PEYECVCDLV SCDLPPVPPC
EDGLQMTLTN PGECRPNFTC ACRKDECRRE SPPSCPPHRT LALRKTQCCD EYECACNCVN
STVSCPLGYL ASAVTNDCGC TTTTCFPDKV CVHRGTIYPV GQFWEEACDV CTCTDLEDSV
MGLRVAQCSQ KPCEDNCLSG FTYVLHEGEC CGRCLPSACE VVIGSPRGDA QSHWKNVGSH
WASPDNPCLI NECVRVKEEV FVQQRNVSCP QLNVPTCPTG FQLSCKTSEC CPTCHCEPLE
ACLLNGTIIG PGKSLMIDVC TTCRCTVQVG VISGFKLECR KTTCEACPLG YKEEKNQGEC
CGRCLPIACT IQLRGGQIMT LKRDETIQDG CDSHFCKVNE RGEYIWEKRV TGCPPFDEHK
CLAEGGKIMK IPGTCCDTCE EPECKDIIAK LQRVKVGDCK SEEEVDIHYC EGKCASKAVY
SIHMEDVQDQ CSCCSPTQTE PMQVPLRCTN GSLIYHEILN AMQCRCSPRK CSK
