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Q28295 (VWF_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
von Willebrand factor

Short name=vWF
Gene names
Name:VWF
Synonyms:F8VWF
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

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, 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.

Subunit structure

Multimeric. Interacts with F8. Ref.2

Subcellular location

Secreted. Secretedextracellular spaceextracellular matrix. Note: Localized to storage granules. Ref.2

Tissue specificity

Plasma.

Domain

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

Post-translational modification

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

N- and O-glycosylated By similarity.

Involvement in disease

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. Ref.4

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.

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
Hemostasis
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

hemostasis

Inferred from sequence or structural similarity. Source: UniProtKB

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

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Propeptide23 – 763741 By similarity
PRO_0000022680
Chain764 – 28132050von Willebrand factor
PRO_0000022681

Regions

Domain34 – 240207VWFD 1
Domain295 – 34854TIL 1
Domain387 – 598212VWFD 2
Domain652 – 70756TIL 2
Domain776 – 82752TIL 3
Domain866 – 1074209VWFD 3
Domain1146 – 119651TIL 4
Domain1277 – 1453177VWFA 1
Domain1498 – 1665168VWFA 2
Domain1691 – 1871181VWFA 3
Domain1949 – 2153205VWFD 4
Domain2255 – 232874VWFC 1
Domain2429 – 249567VWFC 2
Domain2580 – 264566VWFC 3
Domain2724 – 281289CTCK
Region764 – 78724Amino-terminal
Region788 – 83346E1
Region826 – 85328CX
Region2216 – 226146E2
Motif531 – 5333Cell attachment site Potential
Motif698 – 7003Cell attachment site Potential
Motif2507 – 25093Cell attachment site Potential

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation12311N-linked (GlcNAc...) Potential
Glycosylation15151N-linked (GlcNAc...) Potential
Glycosylation15741N-linked (GlcNAc...) Potential
Glycosylation22231N-linked (GlcNAc...) Potential
Glycosylation22901N-linked (GlcNAc...) Potential
Glycosylation23571N-linked (GlcNAc...) Potential
Glycosylation24001N-linked (GlcNAc...) Potential
Glycosylation25461N-linked (GlcNAc...) Potential
Glycosylation25851N-linked (GlcNAc...) Potential
Glycosylation27901N-linked (GlcNAc...) Potential
Disulfide bond767 ↔ 808 By similarity
Disulfide bond776 ↔ 804 By similarity
Disulfide bond810 ↔ 821 By similarity
Disulfide bond867 ↔ 996 By similarity
Disulfide bond889 ↔ 1031 By similarity
Disulfide bond898 ↔ 993 By similarity
Disulfide bond914 ↔ 921 By similarity
Disulfide bond1060 ↔ 1084 By similarity
Disulfide bond1071 ↔ 1111 By similarity
Disulfide bond1089 ↔ 1091 By similarity
Disulfide bond1126 ↔ 1130 By similarity
Disulfide bond1149 ↔ 1169 By similarity
Disulfide bond1153 ↔ 1165 By similarity
Disulfide bond1196 ↔ 1199 By similarity
Disulfide bond1234 ↔ 1237 By similarity
Disulfide bond1272 ↔ 1458 By similarity
Disulfide bond1669 ↔ 1670 By similarity
Disulfide bond1686 ↔ 1872 By similarity
Disulfide bond1879 ↔ 1904 By similarity
Disulfide bond1899 ↔ 1940Or C-1899 with C-1942 By similarity
Disulfide bond1927 ↔ 2088 By similarity
Disulfide bond1950 ↔ 2085 By similarity
Disulfide bond1972 ↔ 2123 By similarity
Disulfide bond1993 ↔ 2001 By similarity
Disulfide bond2724 ↔ 2774 By similarity
Disulfide bond2739 ↔ 2788 By similarity
Disulfide bond2750 ↔ 2804 By similarity
Disulfide bond2754 ↔ 2806 By similarity
Disulfide bond? ↔ 2811 By similarity

Experimental info

Sequence conflict701V → I in AAD04919. Ref.4
Sequence conflict2661A → G in AAB93766. Ref.2
Sequence conflict2801I → V in AAB93766. Ref.2
Sequence conflict409 – 4113VCH → ICQ in AAB93766. Ref.2
Sequence conflict9941G → A in AAB05549. Ref.1
Sequence conflict10211F → L in AAB93766. Ref.2
Sequence conflict23811L → P in AAB93766. Ref.2
Sequence conflict24061P → L in AAB93766. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q28295 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 5DF93E1E5E72F80C

FASTA2,813309,719
        10         20         30         40         50         60 
MSPTRLVRVL LALALILPGK LCTKGTVGRS SMARCSLFGG DFINTFDESM YSFAGDCSYL 

        70         80         90        100        110        120 
LAGDCQEHSV SLIGGFQNGK RVSLSVYLGE FFDIHLFVNG TMLQGTQSIS MPYASNGLYL 

       130        140        150        160        170        180 
EAEAGYYKLS SEAYGFVARI DGNGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFRTQEGTL 

       190        200        210        220        230        240 
TSDPYDFANS WALSSGEQRC KRVSPPSSPC NVSSDEVQQV LWEQCQLLKS ASVFARCHPL 

       250        260        270        280        290        300 
VDPEPFVALC ERTLCTCVQG MECPCAVLLE YARACAQQGI VLYGWTDHSV CRPACPAGME 

       310        320        330        340        350        360 
YKECVSPCTR TCQSLHVKEV CQEQCVDGCS CPEGQLLDEG HCVGSAECSC VHAGQRYPPG 

       370        380        390        400        410        420 
ASLLQDCHTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGVC HYLLAQDCQD 

       430        440        450        460        470        480 
HTFSVVIETV QCADDLDAVC TRSVTVRLPG HHNSLVKLKH GGGVSMDGQD IQIPLLQGDL 

       490        500        510        520        530        540 
RIQHTVMASV RLSYGEDLQM DWDGRGRLLV TLSPAYAGKT CGLCGNYNGN RGDDFVTPAG 

       550        560        570        580        590        600 
LAEPLVEDFG NAWKLLGACE NLQKQHRDPC SLNPRQARFA EEACALLTSS KFEPCHRAVG 

       610        620        630        640        650        660 
PQPYVQNCRY DVCSCSDGRD CLCSAVANYA AACARRGVHI AWREPGFCAL SCPQGQVYLQ 

       670        680        690        700        710        720 
CGTPCNMTCR SLSYPEEDCN EVCLEGCFCP PGLYLDERGD CVPKAQCPCY YDGEIFQPED 

       730        740        750        760        770        780 
IFSDHHTMCY CEDGFMHCTT SGGLGSLLPN PVLSSPRSHR SKRSLSCRPP MVKLVCPADN 

       790        800        810        820        830        840 
PRAEGLECAK TCQNYDLQCM STGCVSGCLC PQGMVRHENR CVALERCPCF HQGQEYAPGE 

       850        860        870        880        890        900 
TVKIDCNTCV CRDRKWNCTD HVCDATCSAI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS 

       910        920        930        940        950        960 
NPGTFRILVG NEGCSYPSVK CKKRVTILVE GGEIELFDGE VNVKKPMKDE THFEVVESGQ 

       970        980        990       1000       1010       1020 
YVILLLGKAL SVVWDHRLSI SVTLKRTYQE QVCGLCGNFD GIQNNDFTSS SLQIEEDPVD 

      1030       1040       1050       1060       1070       1080 
FGNSWKVNPQ CADTKKVPLD SSPAVCHNNI MKQTMVDSSC RILTSDIFQD CNRLVDPEPF 

      1090       1100       1110       1120       1130       1140 
LDICIYDTCS CESIGDCTCF CDTIAAYAHV CAQHGKVVAW RTATFCPQNC EERNLHENGY 

      1150       1160       1170       1180       1190       1200 
ECEWRYNSCA PACPITCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC IDPEDCPVCE 

      1210       1220       1230       1240       1250       1260 
VAGRRLAPGK KIILNPSDPE HCQICHCDGV NFTCQACREP GSLVVPPTEG PIGSTTSYVE 

      1270       1280       1290       1300       1310       1320 
DTPEPPLHDF HCSRLLDLVF LLDGSSKLSE DEFEVLKVFV VGMMEHLHIS QKRIRVAVVE 

      1330       1340       1350       1360       1370       1380 
YHDGSHAYIE LKDRKRPSEL RRITSQVKYA GSEVASTSEV LKYTLFQIFG KIDRPEASRI 

      1390       1400       1410       1420       1430       1440 
ALLLMASQEP SRLARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIHLIEK QAPENKAFVF 

      1450       1460       1470       1480       1490       1500 
SGVDELEQRR DEIINYLCDL APEAPAPTQH PPMAQVTVGS ELLGVSSPGP KRNSMVLDVV 

      1510       1520       1530       1540       1550       1560 
FVLEGSDKIG EANFNKSREF MEEVIQRMDV GQDRIHVTVL QYSYMVTVEY TFSEAQSKGE 

      1570       1580       1590       1600       1610       1620 
VLQQVRDIRY RGGNRTNTGL ALQYLSEHSF SVSQGDREQV PNLVYMVTGN PASDEIKRMP 

      1630       1640       1650       1660       1670       1680 
GDIQVVPIGV GPHANVQELE KIGWPNAPIL IHDFEMLPRE APDLVLQRCC SGEGLQIPTL 

      1690       1700       1710       1720       1730       1740 
SPTPDCSQPL DVVLLLDGSS SIPASYFDEM KSFTKAFISR ANIGPRLTQV SVLQYGSITT 

      1750       1760       1770       1780       1790       1800 
IDVPWNVAYE KVHLLSLVDL MQQEGGPSQI GDALSFAVRY VTSEVHGARP GASKAVVILV 

      1810       1820       1830       1840       1850       1860 
TDVSVDSVDA AAEAARSNRV TVFPIGIGDR YSEAQLSSLA GPKAGSNMVR LQRIEDLPTV 

      1870       1880       1890       1900       1910       1920 
ATLGNSFFHK LCSGFDRVCV DEDGNEKRPG DVWTLPDQCH TVTCLPDGQT LLKSHRVNCD 

      1930       1940       1950       1960       1970       1980 
RGPRPSCPNG QPPLRVEETC GCRWTCPCVC MGSSTRHIVT FDGQNFKLTG SCSYVLFQNK 

      1990       2000       2010       2020       2030       2040 
EQDLEVILHN GACSPGAKET CMKSIEVKHD GLSVELHSDM QMTVNGRLVS IPYVGGDMEV 

      2050       2060       2070       2080       2090       2100 
NVYGTIMYEV RFNHLGHIFT FTPQNNEFQL QLSPRTFASK TYGLCGICDE NGANDFILRD 

      2110       2120       2130       2140       2150       2160 
GTVTTDWKAL IQEWTVQQLG KTCQPVPEEQ CPVSSSSHCQ VLLSELFAEC HKVLAPATFY 

      2170       2180       2190       2200       2210       2220 
AMCQPDSCHP KKVCEAIALY AHLCRTKGVC VDWRRANFCA MSCPPSLVYN HCEHGCPRLC 

      2230       2240       2250       2260       2270       2280 
EGNTSSCGDQ PSEGCFCPPN QVMLEGSCVP EEACTQCISE DGVRHQFLET WVPAHQPCQI 

      2290       2300       2310       2320       2330       2340 
CTCLSGRKVN CTLQPCPTAR APTCGPCEVA RLRQNAEQCC PEYECVCDLV SCDLPPVPPC 

      2350       2360       2370       2380       2390       2400 
EDGLQMTLTN PGECRPNFTC ACRKDECRRE SPPSCPPHRT LALRKTQCCD EYECACNCVN 

      2410       2420       2430       2440       2450       2460 
STVSCPLGYL ASAVTNDCGC TTTTCFPDKV CVHRGTIYPV GQFWEEACDV CTCTDLEDSV 

      2470       2480       2490       2500       2510       2520 
MGLRVAQCSQ KPCEDNCLSG FTYVLHEGEC CGRCLPSACE VVIGSPRGDA QSHWKNVGSH 

      2530       2540       2550       2560       2570       2580 
WASPDNPCLI NECVRVKEEV FVQQRNVSCP QLNVPTCPTG FQLSCKTSEC CPTCHCEPLE 

      2590       2600       2610       2620       2630       2640 
ACLLNGTIIG PGKSLMIDVC TTCRCTVQVG VISGFKLECR KTTCEACPLG YKEEKNQGEC 

      2650       2660       2670       2680       2690       2700 
CGRCLPIACT IQLRGGQIMT LKRDETIQDG CDSHFCKVNE RGEYIWEKRV TGCPPFDEHK 

      2710       2720       2730       2740       2750       2760 
CLAEGGKIMK IPGTCCDTCE EPECKDIIAK LQRVKVGDCK SEEEVDIHYC EGKCASKAVY 

      2770       2780       2790       2800       2810 
SIHMEDVQDQ CSCCSPTQTE PMQVPLRCTN GSLIYHEILN AMQCRCSPRK CSK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L76227 mRNA. Translation: AAB05549.1.
U66246 mRNA. Translation: AAB93766.2.
AF099154 mRNA. Translation: AAD04919.1.
L16903 Genomic DNA. Translation: AAA30903.1.
RefSeqNP_001002932.1. NM_001002932.1.
UniGeneCfa.111.

3D structure databases

ProteinModelPortalQ28295.
SMRQ28295. Positions 1261-1468, 1684-1873.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI08.950.

Proteomic databases

PaxDbQ28295.
PRIDEQ28295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399544.
KEGGcfa:399544.

Organism-specific databases

CTD7450.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000169747.
HOVERGENHBG004380.
InParanoidQ28295.
KOK03900.

Family and domain databases

Gene3D3.40.50.410. 3 hits.
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]
SUPFAMSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 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

NextBio20816602.

Entry information

Entry nameVWF_CANFA
AccessionPrimary (citable) accession number: Q28295
Secondary accession number(s): Q28311, Q9TSI4
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families