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Q8CIZ8 (VWF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
von Willebrand factor
Short name=vWF

Cleaved into the following chain:

  1. von Willebrand antigen 2
    Alternative name(s):
    von Willebrand antigen II
Gene names
Name:Vwf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length2813 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. UniProtKB P04275

Subunit structure

Multimeric. Interacts with F8 By similarity.

Subcellular location

Secreted By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Localized to storage granules By similarity.

Tissue specificity

Plasma. Expressed in liver. Ref.7

Domain

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

Post-translational modification

All cysteine residues are involved in intrachain or interchain disulfide bonds By similarity. UniProtKB P04275

N- and O-glycosylated By similarity.

Sequence similarities

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 4 TIL (trypsin inhibitory-like) domains.

Contains 3 VWFA domains.

Contains 3 VWFC domains.

Contains 4 VWFD domains.

Sequence caution

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

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
Hemostasis
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

liver development

Inferred from mutant phenotype PubMed 7854452. Source: MGI

placenta development

Inferred from mutant phenotype PubMed 7854452. Source: MGI

platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentWeibel-Palade body

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay PubMed 8562500. Source: MGI

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

collagen binding

Inferred from sequence or structural similarity. Source: UniProtKB

glycoprotein binding

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

integrin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protease binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein N-terminus binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.7 (identifier: Q8CIZ8-1)

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.
Isoform 2 (identifier: Q8CIZ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     387-402: ECLVTGQSHFKSFDNR → RLGTFSPFLPVLCGEV
     403-2813: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity UniProtKB P04275
Chain23 – 763741von Willebrand antigen 2 UniProtKB P04275
PRO_0000022684
Chain764 – 28132050von Willebrand factor UniProtKB P04275
PRO_0000022685

Regions

Domain34 – 240207VWFD 1
Domain295 – 34854TIL 1
Domain387 – 598212VWFD 2
Domain652 – 70756TIL 2
Domain804 – 82724TIL 3
Domain866 – 1074209VWFD 3
Domain1146 – 119651TIL 4
Domain1277 – 1453177VWFA 1; binding site for platelet glycoprotein Ib Ref.7
Domain1498 – 1665168VWFA 2
Domain1691 – 1871181VWFA 3; principal binding site for collagens type I and III Ref.7
Domain1949 – 2153205VWFD 4
Domain2255 – 232874VWFC 1
Domain2429 – 249567VWFC 2
Domain2580 – 264566VWFC 3
Domain2724 – 281289CTCK
Region764 – 78724Amino-terminal
Region788 – 83346E1
Region826 – 85328CX
Region2216 – 226146E2
Motif2507 – 25093Cell attachment site By similarity UniProtKB P04275

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation10051N-linked (GlcNAc...) Potential
Glycosylation11471N-linked (GlcNAc...); atypical By similarity UniProtKB P04275
Glycosylation12311N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation12481O-linked (GalNAc...) By similarity
Glycosylation12551O-linked (GalNAc...) By similarity
Glycosylation12561O-linked (GalNAc...) By similarity
Glycosylation14681O-linked (GalNAc...) By similarity
Glycosylation14771O-linked (GalNAc...) By similarity
Glycosylation14861O-linked (GalNAc...) By similarity
Glycosylation15151N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation15741N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation16791O-linked (GalNAc...) By similarity
Glycosylation22231N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation22901N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation22981O-linked (GalNAc...) By similarity
Glycosylation24001N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation25461N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation25851N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation27901N-linked (GlcNAc...) By similarity UniProtKB P04275
Glycosylation28101N-linked (GlcNAc...) Potential
Disulfide bond767 ↔ 808 By similarity UniProtKB P04275
Disulfide bond776 ↔ 804 By similarity UniProtKB P04275
Disulfide bond810 ↔ 821 By similarity UniProtKB P04275
Disulfide bond889 ↔ 1031 By similarity UniProtKB P04275
Disulfide bond898 ↔ 993 By similarity UniProtKB P04275
Disulfide bond914 ↔ 921 By similarity UniProtKB P04275
Disulfide bond? ↔ 996 By similarity UniProtKB P04275
Disulfide bond1060 ↔ 1084 By similarity UniProtKB P04275
Disulfide bond1071 ↔ 1111 By similarity UniProtKB P04275
Disulfide bond1089 ↔ 1091 By similarity UniProtKB P04275
Disulfide bond1126 ↔ 1130 By similarity UniProtKB P04275
Disulfide bond1149 ↔ 1169 By similarity UniProtKB P04275
Disulfide bond1153 ↔ 1165 By similarity UniProtKB P04275
Disulfide bond1196 ↔ 1199 By similarity UniProtKB P04275
Disulfide bond1234 ↔ 1237 By similarity UniProtKB P04275
Disulfide bond1272 ↔ 1458 Ref.9 UniProtKB P04275
Disulfide bond1669 ↔ 1670 By similarity UniProtKB P04275
Disulfide bond1686 ↔ 1872 By similarity UniProtKB P04275
Disulfide bond1879 ↔ 1904 By similarity UniProtKB P04275
Disulfide bond1899 ↔ 1940Or C-1899 with C-1942 By similarity UniProtKB P04275
Disulfide bond1927 ↔ 2088 By similarity UniProtKB P04275
Disulfide bond1950 ↔ 2085 By similarity UniProtKB P04275
Disulfide bond1972 ↔ 2123 By similarity UniProtKB P04275
Disulfide bond1993 ↔ 2001 By similarity UniProtKB P04275
Disulfide bond2724 ↔ 2774 By similarity UniProtKB P04275
Disulfide bond2739 ↔ 2788 By similarity UniProtKB P04275
Disulfide bond2750 ↔ 2804 By similarity UniProtKB P04275
Disulfide bond2754 ↔ 2806 By similarity UniProtKB P04275
Disulfide bond? ↔ 2811 By similarity UniProtKB P04275
Cross-link1720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence387 – 40216ECLVT…SFDNR → RLGTFSPFLPVLCGEV in isoform 2.
VSP_051618
Alternative sequence403 – 28132411Missing in isoform 2.
VSP_051619

Experimental info

Mutagenesis12051R → H: Accelerated clearance of VWF from blood plasma. Ref.7
Sequence conflict1031M → T in AAP41950. Ref.1
Sequence conflict1221L → R in AAP41950. Ref.1
Sequence conflict7991R → C in AAP41950. Ref.1
Sequence conflict8671R → C in AAP41950. Ref.1
Sequence conflict8951Y → Q in AAP41950. Ref.1
Sequence conflict10071S → F in AAP41950. Ref.1
Sequence conflict12451A → V in CAB86200. Ref.4
Sequence conflict14211S → D in AAA82929. Ref.5
Sequence conflict1485 – 14862IS → TL in AAA82929. Ref.5
Sequence conflict23611D → A in AAP41950. Ref.1

Secondary structure

1 ........................... 2813
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2003. Version 2.
Checksum: 3EE2C7D8FF21FFA6

FASTA2,813309,269
        10         20         30         40         50         60 
MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM YSFAGGCSYL 

        70         80         90        100        110        120 
LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG TVMQGDQSIS MPYASQGLYL 

       130        140        150        160        170        180 
ELEAGYYKLS SETFGFAARI DGNGNFQVLM SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL 

       190        200        210        220        230        240 
TSDPYDFANS WALSSEEQRC KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL 

       250        260        270        280        290        300 
VDPESFVALC EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME 

       310        320        330        340        350        360 
YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC VHAGKRYPPG 

       370        380        390        400        410        420 
TSLSQDCNTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCED 

       430        440        450        460        470        480 
HTFSIVIETM QCADDPDAVC TRSVSVRLSA LHNSLVKLKH GGAVGIDGQD VQLPFLQGDL 

       490        500        510        520        530        540 
RIQHTVMASV RLSYAEDLQM DWDGRGRLLV KLSPVYSGKT CGLCGNYNGN KGDDFLTPAG 

       550        560        570        580        590        600 
LVEPLVVDFG NAWKLQGDCS DLRRQHSDPC SLNPRLTRFA EEACALLTSS KFEACHHAVS 

       610        620        630        640        650        660 
PLPYLQNCRY DVCSCSDSRD CLCNAVANYA AECARKGVHI GWREPGFCAL GCPQGQVYLQ 

       670        680        690        700        710        720 
CGNSCNLTCR SLSLPDEECS EVCLEGCYCP PGLYQDERGD CVPKAQCPCY YDGELFQPAD 

       730        740        750        760        770        780 
IFSDHHTMCY CEDGFMHCTT SGTLGSLLPD TVLSSPLSHR SKRSLSCRPP MVKLVCPADN 

       790        800        810        820        830        840 
PRAQGLECAK TCQNYDLERM SLGCVSGCLC PPGMVRHENK CVALERCPCF HQGAEYAPGD 

       850        860        870        880        890        900 
TVKIGCNTCV CRERKWNCTN HVCDATRSAI GMAHYLTFDG LKYLFPGECQ YVLVYDYCGS 

       910        920        930        940        950        960 
NPGTFQILVG NEGCSYPSVK CRKRVTILVD GGELELFDGE VNVKRPLRDE SHFEVVESGR 

       970        980        990       1000       1010       1020 
YVILLLGQAL SVVWDHHLSI SVVLKHTYQE QVCGLCGNFD GIQNNDSTTS SLQVEEDPVN 

      1030       1040       1050       1060       1070       1080 
FGNSWKVSSQ CADTRKLSLD VSPATCHNNI MKQTMVDSAC RILTSDVFQG CNRLVDPEPY 

      1090       1100       1110       1120       1130       1140 
LDICIYDTCS CESIGDCACF CDTIAAYAHV CAQHGQVVAW RTPTLCPQSC EEKNVRENGY 

      1150       1160       1170       1180       1190       1200 
ECEWRYNSCA PACPVTCQHP EPLACPVQCV EGCHAHCPPG RILDELLQTC VDPQDCPVCE 

      1210       1220       1230       1240       1250       1260 
VAGRRLAPGK KITLSPDDPA HCQNCHCDGV NLTCEACQEP GGLVAPPTDA PVSSTTPYVE 

      1270       1280       1290       1300       1310       1320 
DTPEPPLHNF YCSKLLDLVF LLDGSSMLSE AEFEVLKAFV VGMMERLHIS QKRIRVAVVE 

      1330       1340       1350       1360       1370       1380 
YHDGSRAYLE LKARKRPSEL RRITSQIKYT GSQVASTSEV LKYTLFQIFG KIDRPEASHI 

      1390       1400       1410       1420       1430       1440 
TLLLTASQEP PRMARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIRLIEK QAPENKAFLL 

      1450       1460       1470       1480       1490       1500 
SGVDELEQRR DEIVSYLCDL APEAPAPTQP PQVAHVTVSP GIAGISSPGP KRKSMVLDVV 

      1510       1520       1530       1540       1550       1560 
FVLEGSDEVG EANFNKSKEF VEEVIQRMDV SPDATRISVL QYSYTVTMEY AFNGAQSKEE 

      1570       1580       1590       1600       1610       1620 
VLRHVREIRY QGGNRTNTGQ ALQYLSEHSF SPSQGDRVEA PNLVYMVTGN PASDEIKRLP 

      1630       1640       1650       1660       1670       1680 
GDIQVVPIGV GPHANMQELE RISRPIAPIF IRDFETLPRE APDLVLQTCC SKEGLQLPTL 

      1690       1700       1710       1720       1730       1740 
PPLPDCSQPL DVVLLLDGSS SLPESSFDKM KSFAKAFISK ANIGPHLTQV SVIQYGSINT 

      1750       1760       1770       1780       1790       1800 
IDVPWNVVQE KAHLQSLVDL MQQEGGPSQI GDALAFAVRY VTSQIHGARP GASKAVVIII 

      1810       1820       1830       1840       1850       1860 
MDTSLDPVDT AADAARSNRV AVFPVGVGDR YDEAQLRILA GPGASSNVVK LQQVEDLSTM 

      1870       1880       1890       1900       1910       1920 
ATLGNSFFHK LCSGFSGVCV DEDGNEKRPG DVWTLPDQCH TVTCLANGQT LLQSHRVNCD 

      1930       1940       1950       1960       1970       1980 
HGPRPSCANS QSPVRVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVIFQNK 

      1990       2000       2010       2020       2030       2040 
EQDLEVLLHN GACSPGAKQA CMKSIEIKHA GVSAELHSNM EMAVDGRLVL APYVGENMEV 

      2050       2060       2070       2080       2090       2100 
SIYGAIMYEV RFTHLGHILT YTPQNNEFQL QLSPKTFASK MHGLCGICDE NGANDFTLRD 

      2110       2120       2130       2140       2150       2160 
GTVTTDWKRL VQEWTVQQPG YTCQAVPEEQ CPVSDSSHCQ VLLSASFAEC HKVIAPATFH 

      2170       2180       2190       2200       2210       2220 
TICQQDSCHQ ERVCEVIASY AHLCRTSGVC VDWRTTDFCA MSCPPSLVYN HCERGCPRHC 

      2230       2240       2250       2260       2270       2280 
DGNTSFCGDH PSEGCFCPQH QVFLEGSCVP EEACTQCVGE DGVRHQFLET WVPDHQPCQI 

      2290       2300       2310       2320       2330       2340 
CMCLSGRKIN CTAQPCPTAR APTCGPCEVA RLKQSTNLCC PEYECVCDLF NCNLPPVPPC 

      2350       2360       2370       2380       2390       2400 
EGGLQPTLTN PGECRPTFTC DCRKEECKRV SPPSCPPHRT PTLRKTQCCD EYECACSCVN 

      2410       2420       2430       2440       2450       2460 
STLSCPLGYL ASATTNDCGC TTTTCLPDKV CVHRGTVYPV GQFWEEGCDT CTCTDMEDTV 

      2470       2480       2490       2500       2510       2520 
VGLRVVQCSQ RPCEDSCQPG FSYVLHEGEC CGRCLPSACK VVAGSLRGDS HSSWKSVGSR 

      2530       2540       2550       2560       2570       2580 
WAVPENPCLV NECVRVEDAV FVQQRNISCP QLAVPTCPTG FQLNCETSEC CPSCHCEPVE 

      2590       2600       2610       2620       2630       2640 
ACLLNGTIIG PGKSVMVDLC TTCRCIVQTD AISRFKLECR KTTCEACPMG YREEKSQGEC 

      2650       2660       2670       2680       2690       2700 
CGRCLPTACT IQLRGGRIMT LKQDETFQDG CDSHLCRVNE RGEYIWEKRV TGCPPFDEHK 

      2710       2720       2730       2740       2750       2760 
CLAEGGKIVK IPGTCCDTCE EPDCKDITAK VQYIKVGDCK SQEEVDIHYC QGKCASKAVY 

      2770       2780       2790       2800       2810 
SIDIEDVQEQ CSCCLPSRTE PMRVPLHCTN GSVVYHEVIN AMQCRCSPRN CSK

« Hide

Isoform 2 [UniParc].

Checksum: 36201FC93F1EE915
Show »

FASTA40244,467

References

« Hide 'large scale' references
[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/6.
Tissue: Lung.
[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/c.
[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. expand/collapse author list , 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/c.
[6]Erratum
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 86:2461-2461(1995) [PubMed] [Europe PMC] [Abstract]
[7]"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/6J.
[8]"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.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00798576.
IPI00830789.
RefSeqNP_035838.3. NM_011708.4.
UniGeneMm.22339.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U0OX-ray2.70C1261-1468[»]
ProteinModelPortalQ8CIZ8.
SMRQ8CIZ8. Positions 1270-1464, 1494-1671, 1685-1873.
ModBaseSearch...

Protein family/group databases

MEROPSI08.950.

PTM databases

PhosphoSiteQ8CIZ8.

Proteomic databases

PaxDbQ8CIZ8.
PRIDEQ8CIZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001995; ENSMUSP00000001995; ENSMUSG00000001930.
GeneID22371.
KEGGmmu:22371.

Organism-specific databases

CTD7450.
MGIMGI:98941. Vwf.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00700000104340.
HOGENOMHOG000169747.
HOVERGENHBG004380.
InParanoidQ8CIZ8.
KOK03900.
OrthoDBEOG44TP6X.

Gene expression databases

ArrayExpressQ8CIZ8.
BgeeQ8CIZ8.
CleanExMM_VWF.
GenevestigatorQ8CIZ8.
GermOnlineENSMUSG00000001930. Mus musculus.

Family and domain databases

InterProIPR006207. 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]
PfamPF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view]
PIRSFPIRSF002495. VWF. 1 hit.
SMARTSM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]
SUPFAMSSF57567. Cysrich_TIL. 5 hits.
PROSITEPS01185. 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]
ProtoNetSearch...

Other

ChiTaRSVWF. mouse.
EvolutionaryTraceQ8CIZ8.
NextBio302707.
SOURCESearch...

Entry information

Entry nameVWF_MOUSE
AccessionPrimary (citable) accession number: Q8CIZ8
Secondary accession number(s): Q60863 expand/collapse secondary AC list , Q6XUV6, Q8BIU9, Q8CGN0, Q9JK16
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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