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Q28295

- VWF_CANFA

UniProt

Q28295 - VWF_CANFA

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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

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
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 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-KW
  5. Weibel-Palade body Source: UniProtKB
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 – 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

« Hide

        10         20         30         40         50
MSPTRLVRVL LALALILPGK LCTKGTVGRS SMARCSLFGG DFINTFDESM
60 70 80 90 100
YSFAGDCSYL LAGDCQEHSV SLIGGFQNGK RVSLSVYLGE FFDIHLFVNG
110 120 130 140 150
TMLQGTQSIS MPYASNGLYL EAEAGYYKLS SEAYGFVARI DGNGNFQVLL
160 170 180 190 200
SDRYFNKTCG LCGNFNIFAE DDFRTQEGTL TSDPYDFANS WALSSGEQRC
210 220 230 240 250
KRVSPPSSPC NVSSDEVQQV LWEQCQLLKS ASVFARCHPL VDPEPFVALC
260 270 280 290 300
ERTLCTCVQG MECPCAVLLE YARACAQQGI VLYGWTDHSV CRPACPAGME
310 320 330 340 350
YKECVSPCTR TCQSLHVKEV CQEQCVDGCS CPEGQLLDEG HCVGSAECSC
360 370 380 390 400
VHAGQRYPPG ASLLQDCHTC ICRNSLWICS NEECPGECLV TGQSHFKSFD
410 420 430 440 450
NRYFTFSGVC HYLLAQDCQD HTFSVVIETV QCADDLDAVC TRSVTVRLPG
460 470 480 490 500
HHNSLVKLKH GGGVSMDGQD IQIPLLQGDL RIQHTVMASV RLSYGEDLQM
510 520 530 540 550
DWDGRGRLLV TLSPAYAGKT CGLCGNYNGN RGDDFVTPAG LAEPLVEDFG
560 570 580 590 600
NAWKLLGACE NLQKQHRDPC SLNPRQARFA EEACALLTSS KFEPCHRAVG
610 620 630 640 650
PQPYVQNCRY DVCSCSDGRD CLCSAVANYA AACARRGVHI AWREPGFCAL
660 670 680 690 700
SCPQGQVYLQ CGTPCNMTCR SLSYPEEDCN EVCLEGCFCP PGLYLDERGD
710 720 730 740 750
CVPKAQCPCY YDGEIFQPED IFSDHHTMCY CEDGFMHCTT SGGLGSLLPN
760 770 780 790 800
PVLSSPRSHR SKRSLSCRPP MVKLVCPADN PRAEGLECAK TCQNYDLQCM
810 820 830 840 850
STGCVSGCLC PQGMVRHENR CVALERCPCF HQGQEYAPGE TVKIDCNTCV
860 870 880 890 900
CRDRKWNCTD HVCDATCSAI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS
910 920 930 940 950
NPGTFRILVG NEGCSYPSVK CKKRVTILVE GGEIELFDGE VNVKKPMKDE
960 970 980 990 1000
THFEVVESGQ YVILLLGKAL SVVWDHRLSI SVTLKRTYQE QVCGLCGNFD
1010 1020 1030 1040 1050
GIQNNDFTSS SLQIEEDPVD FGNSWKVNPQ CADTKKVPLD SSPAVCHNNI
1060 1070 1080 1090 1100
MKQTMVDSSC RILTSDIFQD CNRLVDPEPF LDICIYDTCS CESIGDCTCF
1110 1120 1130 1140 1150
CDTIAAYAHV CAQHGKVVAW RTATFCPQNC EERNLHENGY ECEWRYNSCA
1160 1170 1180 1190 1200
PACPITCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC IDPEDCPVCE
1210 1220 1230 1240 1250
VAGRRLAPGK KIILNPSDPE HCQICHCDGV NFTCQACREP GSLVVPPTEG
1260 1270 1280 1290 1300
PIGSTTSYVE DTPEPPLHDF HCSRLLDLVF LLDGSSKLSE DEFEVLKVFV
1310 1320 1330 1340 1350
VGMMEHLHIS QKRIRVAVVE YHDGSHAYIE LKDRKRPSEL RRITSQVKYA
1360 1370 1380 1390 1400
GSEVASTSEV LKYTLFQIFG KIDRPEASRI ALLLMASQEP SRLARNLVRY
1410 1420 1430 1440 1450
VQGLKKKKVI VIPVGIGPHA SLKQIHLIEK QAPENKAFVF SGVDELEQRR
1460 1470 1480 1490 1500
DEIINYLCDL APEAPAPTQH PPMAQVTVGS ELLGVSSPGP KRNSMVLDVV
1510 1520 1530 1540 1550
FVLEGSDKIG EANFNKSREF MEEVIQRMDV GQDRIHVTVL QYSYMVTVEY
1560 1570 1580 1590 1600
TFSEAQSKGE VLQQVRDIRY RGGNRTNTGL ALQYLSEHSF SVSQGDREQV
1610 1620 1630 1640 1650
PNLVYMVTGN PASDEIKRMP GDIQVVPIGV GPHANVQELE KIGWPNAPIL
1660 1670 1680 1690 1700
IHDFEMLPRE APDLVLQRCC SGEGLQIPTL SPTPDCSQPL DVVLLLDGSS
1710 1720 1730 1740 1750
SIPASYFDEM KSFTKAFISR ANIGPRLTQV SVLQYGSITT IDVPWNVAYE
1760 1770 1780 1790 1800
KVHLLSLVDL MQQEGGPSQI GDALSFAVRY VTSEVHGARP GASKAVVILV
1810 1820 1830 1840 1850
TDVSVDSVDA AAEAARSNRV TVFPIGIGDR YSEAQLSSLA GPKAGSNMVR
1860 1870 1880 1890 1900
LQRIEDLPTV ATLGNSFFHK LCSGFDRVCV DEDGNEKRPG DVWTLPDQCH
1910 1920 1930 1940 1950
TVTCLPDGQT LLKSHRVNCD RGPRPSCPNG QPPLRVEETC GCRWTCPCVC
1960 1970 1980 1990 2000
MGSSTRHIVT FDGQNFKLTG SCSYVLFQNK EQDLEVILHN GACSPGAKET
2010 2020 2030 2040 2050
CMKSIEVKHD GLSVELHSDM QMTVNGRLVS IPYVGGDMEV NVYGTIMYEV
2060 2070 2080 2090 2100
RFNHLGHIFT FTPQNNEFQL QLSPRTFASK TYGLCGICDE NGANDFILRD
2110 2120 2130 2140 2150
GTVTTDWKAL IQEWTVQQLG KTCQPVPEEQ CPVSSSSHCQ VLLSELFAEC
2160 2170 2180 2190 2200
HKVLAPATFY AMCQPDSCHP KKVCEAIALY AHLCRTKGVC VDWRRANFCA
2210 2220 2230 2240 2250
MSCPPSLVYN HCEHGCPRLC EGNTSSCGDQ PSEGCFCPPN QVMLEGSCVP
2260 2270 2280 2290 2300
EEACTQCISE DGVRHQFLET WVPAHQPCQI CTCLSGRKVN CTLQPCPTAR
2310 2320 2330 2340 2350
APTCGPCEVA RLRQNAEQCC PEYECVCDLV SCDLPPVPPC EDGLQMTLTN
2360 2370 2380 2390 2400
PGECRPNFTC ACRKDECRRE SPPSCPPHRT LALRKTQCCD EYECACNCVN
2410 2420 2430 2440 2450
STVSCPLGYL ASAVTNDCGC TTTTCFPDKV CVHRGTIYPV GQFWEEACDV
2460 2470 2480 2490 2500
CTCTDLEDSV MGLRVAQCSQ KPCEDNCLSG FTYVLHEGEC CGRCLPSACE
2510 2520 2530 2540 2550
VVIGSPRGDA QSHWKNVGSH WASPDNPCLI NECVRVKEEV FVQQRNVSCP
2560 2570 2580 2590 2600
QLNVPTCPTG FQLSCKTSEC CPTCHCEPLE ACLLNGTIIG PGKSLMIDVC
2610 2620 2630 2640 2650
TTCRCTVQVG VISGFKLECR KTTCEACPLG YKEEKNQGEC CGRCLPIACT
2660 2670 2680 2690 2700
IQLRGGQIMT LKRDETIQDG CDSHFCKVNE RGEYIWEKRV TGCPPFDEHK
2710 2720 2730 2740 2750
CLAEGGKIMK IPGTCCDTCE EPECKDIIAK LQRVKVGDCK SEEEVDIHYC
2760 2770 2780 2790 2800
EGKCASKAVY SIHMEDVQDQ CSCCSPTQTE PMQVPLRCTN GSLIYHEILN
2810
AMQCRCSPRK CSK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 117 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