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Q28295

- VWF_CANFA

UniProt

Q28295 - VWF_CANFA

Protein

von Willebrand factor

Gene

VWF

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    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.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 homodimerization activity Source: UniProtKB
    8. protein N-terminus binding 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

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

    GO - Cellular componenti

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

    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 – 2222By similarityAdd
    BLAST
    Propeptidei23 – 763741By similarityPRO_0000022680Add
    BLAST
    Chaini764 – 28132050von Willebrand factorPRO_0000022681Add
    BLAST

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni764 – 78724Amino-terminalAdd
    BLAST
    Regioni788 – 83346E1Add
    BLAST
    Regioni826 – 85328CXAdd
    BLAST
    Regioni2216 – 226146E2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi531 – 5333Cell attachment siteSequence Analysis
    Motifi698 – 7003Cell attachment siteSequence Analysis
    Motifi2507 – 25093Cell attachment siteSequence Analysis

    Domaini

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

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 3 VWFA domains.PROSITE-ProRule annotation
    Contains 3 VWFC domains.PROSITE-ProRule annotation
    Contains 4 VWFD domains.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701V → I in AAD04919. (PubMed:10668811)Curated
    Sequence conflicti266 – 2661A → G in AAB93766. (PubMed:10961880)Curated
    Sequence conflicti280 – 2801I → V in AAB93766. (PubMed:10961880)Curated
    Sequence conflicti409 – 4113VCH → ICQ in AAB93766. (PubMed:10961880)Curated
    Sequence conflicti994 – 9941G → A in AAB05549. 1 PublicationCurated
    Sequence conflicti1021 – 10211F → L in AAB93766. (PubMed:10961880)Curated
    Sequence conflicti2381 – 23811L → P in AAB93766. (PubMed:10961880)Curated
    Sequence conflicti2406 – 24061P → L in AAB93766. (PubMed:10961880)Curated

    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: October 1, 2014
    This is version 116 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