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Q8CIZ8

- VWF_MOUSE

UniProt

Q8CIZ8 - VWF_MOUSE

Protein

von Willebrand factor

Gene

Vwf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (01 Oct 2003)
      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 GPIb-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 binding Source: MGI
    8. protein homodimerization activity Source: UniProtKB
    9. 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. liver development Source: MGI
    6. placenta development Source: MGI
    7. platelet activation Source: UniProtKB
    8. protein homooligomerization Source: UniProtKB

    Keywords - Biological processi

    Blood coagulation, Cell adhesion, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_216309. Integrin cell surface interactions.
    REACT_225107. Platelet Adhesion to exposed collagen.

    Protein family/group databases

    MEROPSiI08.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    von Willebrand factor
    Short name:
    vWF
    Cleaved into the following chain:
    Alternative name(s):
    von Willebrand antigen II
    Gene namesi
    Name:VwfImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:98941. Vwf.

    Subcellular locationi

    Secreted By similarity. Secretedextracellular spaceextracellular matrix By similarity
    Note: Localized to storage granules.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. external side of plasma membrane Source: MGI
    3. extracellular matrix Source: UniProtKB
    4. extracellular region Source: UniProtKB
    5. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    6. Weibel-Palade body Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1205 – 12051R → H: Accelerated clearance of VWF from blood plasma. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 763741von Willebrand antigen 2PRO_0000022684Add
    BLAST
    Chaini764 – 28132050von Willebrand factorPRO_0000022685Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi? ↔ 2811By similarity
    Disulfide bondi? ↔ 996By similarity
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi156 – 1561N-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...)By similarity
    Disulfide bondi889 ↔ 1031By similarity
    Disulfide bondi898 ↔ 993By similarity
    Disulfide bondi914 ↔ 921By similarity
    Glycosylationi1005 – 10051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1060 ↔ 1084By similarity
    Disulfide bondi1071 ↔ 1111By similarity
    Disulfide bondi1089 ↔ 1091By similarity
    Disulfide bondi1126 ↔ 1130By similarity
    Glycosylationi1147 – 11471N-linked (GlcNAc...); atypicalBy similarity
    Disulfide bondi1149 ↔ 1169By similarity
    Disulfide bondi1153 ↔ 1165By similarity
    Disulfide bondi1196 ↔ 1199By similarity
    Glycosylationi1231 – 12311N-linked (GlcNAc...)By similarity
    Disulfide bondi1234 ↔ 1237By similarity
    Glycosylationi1248 – 12481O-linked (GalNAc...)By similarityCurated
    Glycosylationi1255 – 12551O-linked (GalNAc...)By similarityCurated
    Glycosylationi1256 – 12561O-linked (GalNAc...)By similarityCurated
    Disulfide bondi1272 ↔ 14581 Publication
    Glycosylationi1468 – 14681O-linked (GalNAc...)By similarityCurated
    Glycosylationi1477 – 14771O-linked (GalNAc...)By similarityCurated
    Glycosylationi1486 – 14861O-linked (GalNAc...)By similarityCurated
    Glycosylationi1515 – 15151N-linked (GlcNAc...)By similarity
    Glycosylationi1574 – 15741N-linked (GlcNAc...)By similarity
    Disulfide bondi1669 ↔ 1670By similarity
    Glycosylationi1679 – 16791O-linked (GalNAc...)By similarityCurated
    Disulfide bondi1686 ↔ 1872By similarity
    Cross-linki1720 – 1720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Disulfide bondi1879 ↔ 1904By similarity
    Disulfide bondi1899 ↔ 1940Or C-1899 with C-1942By similarityPROSITE-ProRule annotation
    Disulfide bondi1927 ↔ 2088By similarity
    Disulfide bondi1950 ↔ 2085By similarity
    Disulfide bondi1972 ↔ 2123By similarity
    Disulfide bondi1993 ↔ 2001By similarity
    Glycosylationi2223 – 22231N-linked (GlcNAc...)By similarity
    Glycosylationi2290 – 22901N-linked (GlcNAc...)By similarity
    Glycosylationi2298 – 22981O-linked (GalNAc...)By similarityCurated
    Glycosylationi2400 – 24001N-linked (GlcNAc...)By similarity
    Glycosylationi2546 – 25461N-linked (GlcNAc...)By similarity
    Glycosylationi2585 – 25851N-linked (GlcNAc...)By similarity
    Disulfide bondi2724 ↔ 2774By similarity
    Disulfide bondi2739 ↔ 2788By similarity
    Disulfide bondi2750 ↔ 2804By similarity
    Disulfide bondi2754 ↔ 2806By similarity
    Glycosylationi2790 – 27901N-linked (GlcNAc...)By similarity
    Glycosylationi2810 – 28101N-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, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ8CIZ8.
    PaxDbiQ8CIZ8.
    PRIDEiQ8CIZ8.

    PTM databases

    PhosphoSiteiQ8CIZ8.

    Expressioni

    Tissue specificityi

    Plasma. Expressed in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ8CIZ8.
    BgeeiQ8CIZ8.
    CleanExiMM_VWF.
    GenevestigatoriQ8CIZ8.

    Interactioni

    Subunit structurei

    Multimeric. Interacts with F8 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8CIZ8. 1 interaction.
    MINTiMINT-4140177.

    Structurei

    Secondary structure

    1
    2813
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1274 – 128310
    Beta strandi1285 – 12884
    Helixi1290 – 130415
    Beta strandi1311 – 132919
    Helixi1337 – 13459
    Helixi1357 – 136610
    Turni1367 – 13693
    Beta strandi1377 – 13859
    Helixi1391 – 13944
    Helixi1397 – 140610
    Beta strandi1409 – 142012
    Helixi1422 – 14309
    Beta strandi1438 – 14425
    Helixi1443 – 145816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U0OX-ray2.70C1261-1468[»]
    ProteinModelPortaliQ8CIZ8.
    SMRiQ8CIZ8. Positions 1270-1464, 1494-1671, 1685-1873, 2721-2813.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8CIZ8.

    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
    Domaini804 – 82724TIL 3Add
    BLAST
    Domaini866 – 1074209VWFD 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1146 – 119651TIL 4Add
    BLAST
    Domaini1277 – 1453177VWFA 1; binding site for platelet glycoprotein IbPROSITE-ProRule annotationAdd
    BLAST
    Domaini1498 – 1665168VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1691 – 1871181VWFA 3; principal binding site for collagens type I and IIIPROSITE-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
    Motifi2507 – 25093Cell attachment siteBy similarity

    Domaini

    The von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules.By similarity

    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.
    GeneTreeiENSGT00730000110607.
    HOGENOMiHOG000169747.
    HOVERGENiHBG004380.
    InParanoidiQ8CIZ8.
    KOiK03900.
    PhylomeDBiQ8CIZ8.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q8CIZ8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM     50
    YSFAGGCSYL LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG 100
    TVMQGDQSIS MPYASQGLYL ELEAGYYKLS SETFGFAARI DGNGNFQVLM 150
    SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL TSDPYDFANS WALSSEEQRC 200
    KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL VDPESFVALC 250
    EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME 300
    YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC 350
    VHAGKRYPPG TSLSQDCNTC ICRNSLWICS NEECPGECLV TGQSHFKSFD 400
    NRYFTFSGIC QYLLARDCED HTFSIVIETM QCADDPDAVC TRSVSVRLSA 450
    LHNSLVKLKH GGAVGIDGQD VQLPFLQGDL RIQHTVMASV RLSYAEDLQM 500
    DWDGRGRLLV KLSPVYSGKT CGLCGNYNGN KGDDFLTPAG LVEPLVVDFG 550
    NAWKLQGDCS DLRRQHSDPC SLNPRLTRFA EEACALLTSS KFEACHHAVS 600
    PLPYLQNCRY DVCSCSDSRD CLCNAVANYA AECARKGVHI GWREPGFCAL 650
    GCPQGQVYLQ CGNSCNLTCR SLSLPDEECS EVCLEGCYCP PGLYQDERGD 700
    CVPKAQCPCY YDGELFQPAD IFSDHHTMCY CEDGFMHCTT SGTLGSLLPD 750
    TVLSSPLSHR SKRSLSCRPP MVKLVCPADN PRAQGLECAK TCQNYDLERM 800
    SLGCVSGCLC PPGMVRHENK CVALERCPCF HQGAEYAPGD TVKIGCNTCV 850
    CRERKWNCTN HVCDATRSAI GMAHYLTFDG LKYLFPGECQ YVLVYDYCGS 900
    NPGTFQILVG NEGCSYPSVK CRKRVTILVD GGELELFDGE VNVKRPLRDE 950
    SHFEVVESGR YVILLLGQAL SVVWDHHLSI SVVLKHTYQE QVCGLCGNFD 1000
    GIQNNDSTTS SLQVEEDPVN FGNSWKVSSQ CADTRKLSLD VSPATCHNNI 1050
    MKQTMVDSAC RILTSDVFQG CNRLVDPEPY LDICIYDTCS CESIGDCACF 1100
    CDTIAAYAHV CAQHGQVVAW RTPTLCPQSC EEKNVRENGY ECEWRYNSCA 1150
    PACPVTCQHP EPLACPVQCV EGCHAHCPPG RILDELLQTC VDPQDCPVCE 1200
    VAGRRLAPGK KITLSPDDPA HCQNCHCDGV NLTCEACQEP GGLVAPPTDA 1250
    PVSSTTPYVE DTPEPPLHNF YCSKLLDLVF LLDGSSMLSE AEFEVLKAFV 1300
    VGMMERLHIS QKRIRVAVVE YHDGSRAYLE LKARKRPSEL RRITSQIKYT 1350
    GSQVASTSEV LKYTLFQIFG KIDRPEASHI TLLLTASQEP PRMARNLVRY 1400
    VQGLKKKKVI VIPVGIGPHA SLKQIRLIEK QAPENKAFLL SGVDELEQRR 1450
    DEIVSYLCDL APEAPAPTQP PQVAHVTVSP GIAGISSPGP KRKSMVLDVV 1500
    FVLEGSDEVG EANFNKSKEF VEEVIQRMDV SPDATRISVL QYSYTVTMEY 1550
    AFNGAQSKEE VLRHVREIRY QGGNRTNTGQ ALQYLSEHSF SPSQGDRVEA 1600
    PNLVYMVTGN PASDEIKRLP GDIQVVPIGV GPHANMQELE RISRPIAPIF 1650
    IRDFETLPRE APDLVLQTCC SKEGLQLPTL PPLPDCSQPL DVVLLLDGSS 1700
    SLPESSFDKM KSFAKAFISK ANIGPHLTQV SVIQYGSINT IDVPWNVVQE 1750
    KAHLQSLVDL MQQEGGPSQI GDALAFAVRY VTSQIHGARP GASKAVVIII 1800
    MDTSLDPVDT AADAARSNRV AVFPVGVGDR YDEAQLRILA GPGASSNVVK 1850
    LQQVEDLSTM ATLGNSFFHK LCSGFSGVCV DEDGNEKRPG DVWTLPDQCH 1900
    TVTCLANGQT LLQSHRVNCD HGPRPSCANS QSPVRVEETC GCRWTCPCVC 1950
    TGSSTRHIVT FDGQNFKLTG SCSYVIFQNK EQDLEVLLHN GACSPGAKQA 2000
    CMKSIEIKHA GVSAELHSNM EMAVDGRLVL APYVGENMEV SIYGAIMYEV 2050
    RFTHLGHILT YTPQNNEFQL QLSPKTFASK MHGLCGICDE NGANDFTLRD 2100
    GTVTTDWKRL VQEWTVQQPG YTCQAVPEEQ CPVSDSSHCQ VLLSASFAEC 2150
    HKVIAPATFH TICQQDSCHQ ERVCEVIASY AHLCRTSGVC VDWRTTDFCA 2200
    MSCPPSLVYN HCERGCPRHC DGNTSFCGDH PSEGCFCPQH QVFLEGSCVP 2250
    EEACTQCVGE DGVRHQFLET WVPDHQPCQI CMCLSGRKIN CTAQPCPTAR 2300
    APTCGPCEVA RLKQSTNLCC PEYECVCDLF NCNLPPVPPC EGGLQPTLTN 2350
    PGECRPTFTC DCRKEECKRV SPPSCPPHRT PTLRKTQCCD EYECACSCVN 2400
    STLSCPLGYL ASATTNDCGC TTTTCLPDKV CVHRGTVYPV GQFWEEGCDT 2450
    CTCTDMEDTV VGLRVVQCSQ RPCEDSCQPG FSYVLHEGEC CGRCLPSACK 2500
    VVAGSLRGDS HSSWKSVGSR WAVPENPCLV NECVRVEDAV FVQQRNISCP 2550
    QLAVPTCPTG FQLNCETSEC CPSCHCEPVE ACLLNGTIIG PGKSVMVDLC 2600
    TTCRCIVQTD AISRFKLECR KTTCEACPMG YREEKSQGEC CGRCLPTACT 2650
    IQLRGGRIMT LKQDETFQDG CDSHLCRVNE RGEYIWEKRV TGCPPFDEHK 2700
    CLAEGGKIVK IPGTCCDTCE EPDCKDITAK VQYIKVGDCK SQEEVDIHYC 2750
    QGKCASKAVY SIDIEDVQEQ CSCCLPSRTE PMRVPLHCTN GSVVYHEVIN 2800
    AMQCRCSPRN CSK 2813
    Length:2,813
    Mass (Da):309,269
    Last modified:October 1, 2003 - v2
    Checksum:i3EE2C7D8FF21FFA6
    GO
    Isoform 2Curated (identifier: Q8CIZ8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         387-402: ECLVTGQSHFKSFDNR → RLGTFSPFLPVLCGEV
         403-2813: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:402
    Mass (Da):44,467
    Checksum:i36201FC93F1EE915
    GO

    Sequence cautioni

    The sequence BAC38822.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031M → T in AAP41950. 1 PublicationCurated
    Sequence conflicti122 – 1221L → R in AAP41950. 1 PublicationCurated
    Sequence conflicti799 – 7991R → C in AAP41950. 1 PublicationCurated
    Sequence conflicti867 – 8671R → C in AAP41950. 1 PublicationCurated
    Sequence conflicti895 – 8951Y → Q in AAP41950. 1 PublicationCurated
    Sequence conflicti1007 – 10071S → F in AAP41950. 1 PublicationCurated
    Sequence conflicti1245 – 12451A → V in CAB86200. (PubMed:10722222)Curated
    Sequence conflicti1421 – 14211S → D in AAA82929. (PubMed:8193357)Curated
    Sequence conflicti1485 – 14862IS → TL in AAA82929. (PubMed:8193357)Curated
    Sequence conflicti2361 – 23611D → A in AAP41950. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei387 – 40216ECLVT…SFDNR → RLGTFSPFLPVLCGEV in isoform 2. 1 PublicationVSP_051618Add
    BLAST
    Alternative sequencei403 – 28132411Missing in isoform 2. 1 PublicationVSP_051619Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY208897 mRNA. Translation: AAP41950.1.
    AY162409 mRNA. Translation: AAN73055.1.
    AF539800 mRNA. Translation: AAN07781.2.
    AK083237 mRNA. Translation: BAC38822.1. Different initiation.
    AJ238390 Genomic DNA. Translation: CAB86200.1.
    U27810 Genomic DNA. Translation: AAA82929.1.
    CCDSiCCDS20552.1. [Q8CIZ8-1]
    RefSeqiNP_035838.3. NM_011708.4.
    UniGeneiMm.22339.

    Genome annotation databases

    EnsembliENSMUST00000001995; ENSMUSP00000001995; ENSMUSG00000001930.
    GeneIDi22371.
    KEGGimmu:22371.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY208897 mRNA. Translation: AAP41950.1 .
    AY162409 mRNA. Translation: AAN73055.1 .
    AF539800 mRNA. Translation: AAN07781.2 .
    AK083237 mRNA. Translation: BAC38822.1 . Different initiation.
    AJ238390 Genomic DNA. Translation: CAB86200.1 .
    U27810 Genomic DNA. Translation: AAA82929.1 .
    CCDSi CCDS20552.1. [Q8CIZ8-1 ]
    RefSeqi NP_035838.3. NM_011708.4.
    UniGenei Mm.22339.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U0O X-ray 2.70 C 1261-1468 [» ]
    ProteinModelPortali Q8CIZ8.
    SMRi Q8CIZ8. Positions 1270-1464, 1494-1671, 1685-1873, 2721-2813.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8CIZ8. 1 interaction.
    MINTi MINT-4140177.

    Protein family/group databases

    MEROPSi I08.950.

    PTM databases

    PhosphoSitei Q8CIZ8.

    Proteomic databases

    MaxQBi Q8CIZ8.
    PaxDbi Q8CIZ8.
    PRIDEi Q8CIZ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001995 ; ENSMUSP00000001995 ; ENSMUSG00000001930 .
    GeneIDi 22371.
    KEGGi mmu:22371.

    Organism-specific databases

    CTDi 7450.
    MGIi MGI:98941. Vwf.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00730000110607.
    HOGENOMi HOG000169747.
    HOVERGENi HBG004380.
    InParanoidi Q8CIZ8.
    KOi K03900.
    PhylomeDBi Q8CIZ8.

    Enzyme and pathway databases

    Reactomei REACT_216309. Integrin cell surface interactions.
    REACT_225107. Platelet Adhesion to exposed collagen.

    Miscellaneous databases

    ChiTaRSi VWF. mouse.
    EvolutionaryTracei Q8CIZ8.
    NextBioi 302707.
    PROi Q8CIZ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CIZ8.
    Bgeei Q8CIZ8.
    CleanExi MM_VWF.
    Genevestigatori Q8CIZ8.

    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. "Cloning of full-length murine von Willebrand factor cDNA."
      Chitta M.S., Duhe R.J., Kermode J.C.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6Imported.
      Tissue: LungImported.
    2. "Murine von Willebrand factor."
      Lenting P.J., Westein E., de Groot P.G., Denis C.V.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/cImported.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Hippocampus.
    4. "Variance of molecular datings, evolution of rodents and the phylogenetic affinities between Ctenodactylidae and Hystricognathi."
      Huchon D., Catzeflis F.M., Douzery E.J.P.
      Proc. R. Soc. B 267:393-402(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1238-1658 (ISOFORM 1).
    5. "von Willebrand disease in the RIIIS/J mouse is caused by a defect outside of the von Willebrand factor gene."
      Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E., Reddington M., Novak E.K., Swank R.T., Ginsburg D.
      Blood 83:3225-3231(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1298-1684 (ISOFORM 1).
      Strain: BALB/cImported.
    6. "An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation."
      Lenting P.J., Westein E., Terraube V., Ribba A.-S., Huizinga E.G., Meyer D., de Groot P.G., Denis C.V.
      J. Biol. Chem. 279:12102-12109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-1205, TISSUE SPECIFICITY.
      Strain: C57BL/6J1 Publication.
    7. "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.
    8. "The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation."
      Fukuda K., Doggett T., Laurenzi I.J., Liddington R.C., Diacovo T.G.
      Nat. Struct. Mol. Biol. 12:152-159(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1261-1468 IN COMPLEX WITH SNAKE VENOM BOTROCETIN, DISULFIDE BOND.

    Entry informationi

    Entry nameiVWF_MOUSE
    AccessioniPrimary (citable) accession number: Q8CIZ8
    Secondary accession number(s): Q60863
    , Q6XUV6, Q8BIU9, Q8CGN0, Q9JK16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 109 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3