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Q28295

- VWF_CANFA

UniProt

Q28295 - VWF_CANFA

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Protein
von Willebrand factor
Gene
VWF, F8VWF
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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, glycoprotein Ibalpha/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 By similarity.

GO - Molecular functioni

  1. chaperone binding Source: UniProtKB
  2. collagen binding Source: UniProtKB
  3. glycoprotein binding Source: UniProtKB
  4. immunoglobulin binding Source: UniProtKB
  5. integrin binding Source: UniProtKB
  6. protease binding Source: UniProtKB
  7. protein N-terminus binding Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: UniProtKB
  2. cell adhesion Source: UniProtKB
  3. cell-substrate adhesion Source: UniProtKB
  4. hemostasis Source: UniProtKB
  5. platelet activation Source: UniProtKB
  6. protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Cell adhesion, Hemostasis

Protein family/group databases

MEROPSiI08.950.

Names & Taxonomyi

Protein namesi
Recommended name:
von Willebrand factor
Short name:
vWF
Gene namesi
Name:VWF
Synonyms:F8VWF
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

Secreted. Secretedextracellular spaceextracellular matrix
Note: Localized to storage granules.1 Publication

GO - Cellular componenti

  1. Weibel-Palade body Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: UniProtKB
  5. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in VWF are the cause of von Willebrand disease (VWD) in the Scottish Terrier. VWD is characterized by frequent bleeding. Type I VWD is associated with a deficiency of VWF; type II by normal to decreased plasma level of VWF; type III by a virtual absence of VWF.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 By similarity
Add
BLAST
Propeptidei23 – 763741 By similarity
PRO_0000022680Add
BLAST
Chaini764 – 28132050von Willebrand factor
PRO_0000022681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi? ↔ 2811 By similarity
Glycosylationi99 – 991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi156 – 1561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi211 – 2111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi666 – 6661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi767 ↔ 808 By similarity
Disulfide bondi776 ↔ 804 By similarity
Disulfide bondi810 ↔ 821 By similarity
Glycosylationi857 – 8571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi867 ↔ 996 By similarity
Disulfide bondi889 ↔ 1031 By similarity
Disulfide bondi898 ↔ 993 By similarity
Disulfide bondi914 ↔ 921 By similarity
Disulfide bondi1060 ↔ 1084 By similarity
Disulfide bondi1071 ↔ 1111 By similarity
Disulfide bondi1089 ↔ 1091 By similarity
Disulfide bondi1126 ↔ 1130 By similarity
Disulfide bondi1149 ↔ 1169 By similarity
Disulfide bondi1153 ↔ 1165 By similarity
Disulfide bondi1196 ↔ 1199 By similarity
Glycosylationi1231 – 12311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1234 ↔ 1237 By similarity
Disulfide bondi1272 ↔ 1458 By similarity
Glycosylationi1515 – 15151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1574 – 15741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1669 ↔ 1670 By similarity
Disulfide bondi1686 ↔ 1872 By similarity
Disulfide bondi1879 ↔ 1904 By similarity
Disulfide bondi1899 ↔ 1940Or C-1899 with C-1942 By similarity
Disulfide bondi1927 ↔ 2088 By similarity
Disulfide bondi1950 ↔ 2085 By similarity
Disulfide bondi1972 ↔ 2123 By similarity
Disulfide bondi1993 ↔ 2001 By similarity
Glycosylationi2223 – 22231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2290 – 22901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2357 – 23571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2400 – 24001N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2546 – 25461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2585 – 25851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2724 ↔ 2774 By similarity
Disulfide bondi2739 ↔ 2788 By similarity
Disulfide bondi2750 ↔ 2804 By similarity
Disulfide bondi2754 ↔ 2806 By similarity
Glycosylationi2790 – 27901N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

All cysteine residues are involved in intrachain or interchain disulfide bonds By similarity.
N- and O-glycosylated By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ28295.
PRIDEiQ28295.

Expressioni

Tissue specificityi

Plasma.

Interactioni

Subunit structurei

Multimeric. Interacts with F8.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ28295.
SMRiQ28295. Positions 1261-1468, 1684-1873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 240207VWFD 1
Add
BLAST
Domaini295 – 34854TIL 1
Add
BLAST
Domaini387 – 598212VWFD 2
Add
BLAST
Domaini652 – 70756TIL 2
Add
BLAST
Domaini776 – 82752TIL 3
Add
BLAST
Domaini866 – 1074209VWFD 3
Add
BLAST
Domaini1146 – 119651TIL 4
Add
BLAST
Domaini1277 – 1453177VWFA 1
Add
BLAST
Domaini1498 – 1665168VWFA 2
Add
BLAST
Domaini1691 – 1871181VWFA 3
Add
BLAST
Domaini1949 – 2153205VWFD 4
Add
BLAST
Domaini2255 – 232874VWFC 1
Add
BLAST
Domaini2429 – 249567VWFC 2
Add
BLAST
Domaini2580 – 264566VWFC 3
Add
BLAST
Domaini2724 – 281289CTCK
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni764 – 78724Amino-terminal
Add
BLAST
Regioni788 – 83346E1
Add
BLAST
Regioni826 – 85328CX
Add
BLAST
Regioni2216 – 226146E2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi531 – 5333Cell attachment site Reviewed prediction
Motifi698 – 7003Cell attachment site Reviewed prediction
Motifi2507 – 25093Cell attachment site Reviewed prediction

Domaini

The propeptide is required for multimerization of vWF and for its targeting to storage granules.

Sequence similaritiesi

Contains 3 VWFA domains.
Contains 3 VWFC domains.
Contains 4 VWFD domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000169747.
HOVERGENiHBG004380.
InParanoidiQ28295.
KOiK03900.

Family and domain databases

Gene3Di3.40.50.410. 3 hits.
InterProiIPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view]
PIRSFiPIRSF002495. VWF. 1 hit.
SMARTiSM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 5 hits.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS50234. VWFA. 3 hits.
PS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
PS51233. VWFD. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q28295-1 [UniParc]FASTAAdd to Basket

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MSPTRLVRVL LALALILPGK LCTKGTVGRS SMARCSLFGG DFINTFDESM     50
YSFAGDCSYL LAGDCQEHSV SLIGGFQNGK RVSLSVYLGE FFDIHLFVNG 100
TMLQGTQSIS MPYASNGLYL EAEAGYYKLS SEAYGFVARI DGNGNFQVLL 150
SDRYFNKTCG LCGNFNIFAE DDFRTQEGTL TSDPYDFANS WALSSGEQRC 200
KRVSPPSSPC NVSSDEVQQV LWEQCQLLKS ASVFARCHPL VDPEPFVALC 250
ERTLCTCVQG MECPCAVLLE YARACAQQGI VLYGWTDHSV CRPACPAGME 300
YKECVSPCTR TCQSLHVKEV CQEQCVDGCS CPEGQLLDEG HCVGSAECSC 350
VHAGQRYPPG ASLLQDCHTC ICRNSLWICS NEECPGECLV TGQSHFKSFD 400
NRYFTFSGVC HYLLAQDCQD HTFSVVIETV QCADDLDAVC TRSVTVRLPG 450
HHNSLVKLKH GGGVSMDGQD IQIPLLQGDL RIQHTVMASV RLSYGEDLQM 500
DWDGRGRLLV TLSPAYAGKT CGLCGNYNGN RGDDFVTPAG LAEPLVEDFG 550
NAWKLLGACE NLQKQHRDPC SLNPRQARFA EEACALLTSS KFEPCHRAVG 600
PQPYVQNCRY DVCSCSDGRD CLCSAVANYA AACARRGVHI AWREPGFCAL 650
SCPQGQVYLQ CGTPCNMTCR SLSYPEEDCN EVCLEGCFCP PGLYLDERGD 700
CVPKAQCPCY YDGEIFQPED IFSDHHTMCY CEDGFMHCTT SGGLGSLLPN 750
PVLSSPRSHR SKRSLSCRPP MVKLVCPADN PRAEGLECAK TCQNYDLQCM 800
STGCVSGCLC PQGMVRHENR CVALERCPCF HQGQEYAPGE TVKIDCNTCV 850
CRDRKWNCTD HVCDATCSAI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS 900
NPGTFRILVG NEGCSYPSVK CKKRVTILVE GGEIELFDGE VNVKKPMKDE 950
THFEVVESGQ YVILLLGKAL SVVWDHRLSI SVTLKRTYQE QVCGLCGNFD 1000
GIQNNDFTSS SLQIEEDPVD FGNSWKVNPQ CADTKKVPLD SSPAVCHNNI 1050
MKQTMVDSSC RILTSDIFQD CNRLVDPEPF LDICIYDTCS CESIGDCTCF 1100
CDTIAAYAHV CAQHGKVVAW RTATFCPQNC EERNLHENGY ECEWRYNSCA 1150
PACPITCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC IDPEDCPVCE 1200
VAGRRLAPGK KIILNPSDPE HCQICHCDGV NFTCQACREP GSLVVPPTEG 1250
PIGSTTSYVE DTPEPPLHDF HCSRLLDLVF LLDGSSKLSE DEFEVLKVFV 1300
VGMMEHLHIS QKRIRVAVVE YHDGSHAYIE LKDRKRPSEL RRITSQVKYA 1350
GSEVASTSEV LKYTLFQIFG KIDRPEASRI ALLLMASQEP SRLARNLVRY 1400
VQGLKKKKVI VIPVGIGPHA SLKQIHLIEK QAPENKAFVF SGVDELEQRR 1450
DEIINYLCDL APEAPAPTQH PPMAQVTVGS ELLGVSSPGP KRNSMVLDVV 1500
FVLEGSDKIG EANFNKSREF MEEVIQRMDV GQDRIHVTVL QYSYMVTVEY 1550
TFSEAQSKGE VLQQVRDIRY RGGNRTNTGL ALQYLSEHSF SVSQGDREQV 1600
PNLVYMVTGN PASDEIKRMP GDIQVVPIGV GPHANVQELE KIGWPNAPIL 1650
IHDFEMLPRE APDLVLQRCC SGEGLQIPTL SPTPDCSQPL DVVLLLDGSS 1700
SIPASYFDEM KSFTKAFISR ANIGPRLTQV SVLQYGSITT IDVPWNVAYE 1750
KVHLLSLVDL MQQEGGPSQI GDALSFAVRY VTSEVHGARP GASKAVVILV 1800
TDVSVDSVDA AAEAARSNRV TVFPIGIGDR YSEAQLSSLA GPKAGSNMVR 1850
LQRIEDLPTV ATLGNSFFHK LCSGFDRVCV DEDGNEKRPG DVWTLPDQCH 1900
TVTCLPDGQT LLKSHRVNCD RGPRPSCPNG QPPLRVEETC GCRWTCPCVC 1950
MGSSTRHIVT FDGQNFKLTG SCSYVLFQNK EQDLEVILHN GACSPGAKET 2000
CMKSIEVKHD GLSVELHSDM QMTVNGRLVS IPYVGGDMEV NVYGTIMYEV 2050
RFNHLGHIFT FTPQNNEFQL QLSPRTFASK TYGLCGICDE NGANDFILRD 2100
GTVTTDWKAL IQEWTVQQLG KTCQPVPEEQ CPVSSSSHCQ VLLSELFAEC 2150
HKVLAPATFY AMCQPDSCHP KKVCEAIALY AHLCRTKGVC VDWRRANFCA 2200
MSCPPSLVYN HCEHGCPRLC EGNTSSCGDQ PSEGCFCPPN QVMLEGSCVP 2250
EEACTQCISE DGVRHQFLET WVPAHQPCQI CTCLSGRKVN CTLQPCPTAR 2300
APTCGPCEVA RLRQNAEQCC PEYECVCDLV SCDLPPVPPC EDGLQMTLTN 2350
PGECRPNFTC ACRKDECRRE SPPSCPPHRT LALRKTQCCD EYECACNCVN 2400
STVSCPLGYL ASAVTNDCGC TTTTCFPDKV CVHRGTIYPV GQFWEEACDV 2450
CTCTDLEDSV MGLRVAQCSQ KPCEDNCLSG FTYVLHEGEC CGRCLPSACE 2500
VVIGSPRGDA QSHWKNVGSH WASPDNPCLI NECVRVKEEV FVQQRNVSCP 2550
QLNVPTCPTG FQLSCKTSEC CPTCHCEPLE ACLLNGTIIG PGKSLMIDVC 2600
TTCRCTVQVG VISGFKLECR KTTCEACPLG YKEEKNQGEC CGRCLPIACT 2650
IQLRGGQIMT LKRDETIQDG CDSHFCKVNE RGEYIWEKRV TGCPPFDEHK 2700
CLAEGGKIMK IPGTCCDTCE EPECKDIIAK LQRVKVGDCK SEEEVDIHYC 2750
EGKCASKAVY SIHMEDVQDQ CSCCSPTQTE PMQVPLRCTN GSLIYHEILN 2800
AMQCRCSPRK CSK 2813
Length:2,813
Mass (Da):309,719
Last modified:January 11, 2001 - v2
Checksum:i5DF93E1E5E72F80C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701V → I in AAD04919. 1 Publication
Sequence conflicti266 – 2661A → G in AAB93766. 1 Publication
Sequence conflicti280 – 2801I → V in AAB93766. 1 Publication
Sequence conflicti409 – 4113VCH → ICQ in AAB93766. 1 Publication
Sequence conflicti994 – 9941G → A in AAB05549. 1 Publication
Sequence conflicti1021 – 10211F → L in AAB93766. 1 Publication
Sequence conflicti2381 – 23811L → P in AAB93766. 1 Publication
Sequence conflicti2406 – 24061P → L in AAB93766. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L76227 mRNA. Translation: AAB05549.1.
U66246 mRNA. Translation: AAB93766.2.
AF099154 mRNA. Translation: AAD04919.1.
L16903 Genomic DNA. Translation: AAA30903.1.
RefSeqiNP_001002932.1. NM_001002932.1.
UniGeneiCfa.111.

Genome annotation databases

GeneIDi399544.
KEGGicfa:399544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L76227 mRNA. Translation: AAB05549.1 .
U66246 mRNA. Translation: AAB93766.2 .
AF099154 mRNA. Translation: AAD04919.1 .
L16903 Genomic DNA. Translation: AAA30903.1 .
RefSeqi NP_001002932.1. NM_001002932.1.
UniGenei Cfa.111.

3D structure databases

ProteinModelPortali Q28295.
SMRi Q28295. Positions 1261-1468, 1684-1873.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I08.950.

Proteomic databases

PaxDbi Q28295.
PRIDEi Q28295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399544.
KEGGi cfa:399544.

Organism-specific databases

CTDi 7450.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000169747.
HOVERGENi HBG004380.
InParanoidi Q28295.
KOi K03900.

Miscellaneous databases

NextBioi 20816602.

Family and domain databases

Gene3Di 3.40.50.410. 3 hits.
InterProi IPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view ]
Pfami PF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view ]
PIRSFi PIRSF002495. VWF. 1 hit.
SMARTi SM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view ]
SUPFAMi SSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 5 hits.
PROSITEi PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS50234. VWFA. 3 hits.
PS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
PS51233. VWFD. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Canine vWF cDNA sequence."
    Stoy S.J., Shibuya H., Nonneman D.J., Holzhauer J., Mohammed I.H., Johnson G.S.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "von Willebrand factor storage and multimerization: 2 independent intracellular processes."
    Haberichter S.L., Fahs S.A., Montgomery R.R.
    Blood 96:1808-1815(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION.
    Tissue: Heart.
  3. Montgomery R.R., Fahs S., Montgomery M.W.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 55.
  4. "Mutation causing von Willebrand's disease in Scottish Terriers."
    Venta P.J., Li J., Yuzbasiyan-Gurkan V., Brewer G.J., Schall W.D.
    J. Vet. Intern. Med. 14:10-19(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE.
    Strain: Scottish terrier.
    Tissue: Uterus.
  5. "The canine von Willebrand factor gene: sequence and expression of a region encoding the glycoprotein Ib/IX binding domain."
    Mancuso D.J., Christopherson P.A., Kroner P.A., Montgomery R.R.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1234-1669.
    Tissue: Blood.
  6. "von Willebrand factor, platelets and endothelial cell interactions."
    Ruggeri Z.M.
    J. Thromb. Haemost. 1:1335-1342(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiVWF_CANFA
AccessioniPrimary (citable) accession number: Q28295
Secondary accession number(s): Q28311, Q9TSI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: June 11, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi