Q28295 (VWF_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
von Willebrand factor
Short name=vWF

Gene names

Name:	VWF
Synonyms:	F8VWF

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	2813 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › extracellular space › extracellular 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 process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-substrate adhesion 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_component	Weibel-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_function	chaperone 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Propeptide	23 – 763	741	By similarity		PRO_0000022680
	Chain	764 – 2813	2050	von Willebrand factor		PRO_0000022681
Regions
	Domain	34 – 240	207	VWFD 1
	Domain	295 – 348	54	TIL 1
	Domain	387 – 598	212	VWFD 2
	Domain	652 – 707	56	TIL 2
	Domain	776 – 827	52	TIL 3
	Domain	866 – 1074	209	VWFD 3
	Domain	1146 – 1196	51	TIL 4
	Domain	1277 – 1453	177	VWFA 1
	Domain	1498 – 1665	168	VWFA 2
	Domain	1691 – 1871	181	VWFA 3
	Domain	1949 – 2153	205	VWFD 4
	Domain	2255 – 2328	74	VWFC 1
	Domain	2429 – 2495	67	VWFC 2
	Domain	2580 – 2645	66	VWFC 3
	Domain	2724 – 2812	89	CTCK
	Region	764 – 787	24	Amino-terminal
	Region	788 – 833	46	E1
	Region	826 – 853	28	CX
	Region	2216 – 2261	46	E2
	Motif	531 – 533	3	Cell attachment site Potential
	Motif	698 – 700	3	Cell attachment site Potential
	Motif	2507 – 2509	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	156	1	N-linked (GlcNAc...) Potential
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
	Glycosylation	666	1	N-linked (GlcNAc...) Potential
	Glycosylation	857	1	N-linked (GlcNAc...) Potential
	Glycosylation	1231	1	N-linked (GlcNAc...) Potential
	Glycosylation	1515	1	N-linked (GlcNAc...) Potential
	Glycosylation	1574	1	N-linked (GlcNAc...) Potential
	Glycosylation	2223	1	N-linked (GlcNAc...) Potential
	Glycosylation	2290	1	N-linked (GlcNAc...) Potential
	Glycosylation	2357	1	N-linked (GlcNAc...) Potential
	Glycosylation	2400	1	N-linked (GlcNAc...) Potential
	Glycosylation	2546	1	N-linked (GlcNAc...) Potential
	Glycosylation	2585	1	N-linked (GlcNAc...) Potential
	Glycosylation	2790	1	N-linked (GlcNAc...) Potential
	Disulfide bond	767 ↔ 808		By similarity
	Disulfide bond	776 ↔ 804		By similarity
	Disulfide bond	810 ↔ 821		By similarity
	Disulfide bond	867 ↔ 996		By similarity
	Disulfide bond	889 ↔ 1031		By similarity
	Disulfide bond	898 ↔ 993		By similarity
	Disulfide bond	914 ↔ 921		By similarity
	Disulfide bond	1060 ↔ 1084		By similarity
	Disulfide bond	1071 ↔ 1111		By similarity
	Disulfide bond	1089 ↔ 1091		By similarity
	Disulfide bond	1126 ↔ 1130		By similarity
	Disulfide bond	1149 ↔ 1169		By similarity
	Disulfide bond	1153 ↔ 1165		By similarity
	Disulfide bond	1196 ↔ 1199		By similarity
	Disulfide bond	1234 ↔ 1237		By similarity
	Disulfide bond	1272 ↔ 1458		By similarity
	Disulfide bond	1669 ↔ 1670		By similarity
	Disulfide bond	1686 ↔ 1872		By similarity
	Disulfide bond	1879 ↔ 1904		By similarity
	Disulfide bond	1899 ↔ 1940		Or C-1899 with C-1942 By similarity
	Disulfide bond	1927 ↔ 2088		By similarity
	Disulfide bond	1950 ↔ 2085		By similarity
	Disulfide bond	1972 ↔ 2123		By similarity
	Disulfide bond	1993 ↔ 2001		By similarity
	Disulfide bond	2724 ↔ 2774		By similarity
	Disulfide bond	2739 ↔ 2788		By similarity
	Disulfide bond	2750 ↔ 2804		By similarity
	Disulfide bond	2754 ↔ 2806		By similarity
	Disulfide bond	? ↔ 2811		By similarity
Experimental info
	Sequence conflict	70	1	V → I in AAD04919. Ref.4
	Sequence conflict	266	1	A → G in AAB93766. Ref.2
	Sequence conflict	280	1	I → V in AAB93766. Ref.2
	Sequence conflict	409 – 411	3	VCH → ICQ in AAB93766. Ref.2
	Sequence conflict	994	1	G → A in AAB05549. Ref.1
	Sequence conflict	1021	1	F → L in AAB93766. Ref.2
	Sequence conflict	2381	1	L → P in AAB93766. Ref.2
	Sequence conflict	2406	1	P → L in AAB93766. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q28295 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 5DF93E1E5E72F80C	FASTA	2,813	309,719
	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

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.
RefSeq	NP_001002932.1. NM_001002932.1.
UniGene	Cfa.111.
3D structure databases
ProteinModelPortal	Q28295.
SMR	Q28295. Positions 1261-1468, 1684-1873.
ModBase	Search...
Protein family/group databases
MEROPS	I08.950.
Proteomic databases
PaxDb	Q28295.
PRIDE	Q28295.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399544.
KEGG	cfa:399544.
Organism-specific databases
CTD	7450.
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000169747.
HOVERGEN	HBG004380.
InParanoid	Q28295.
KO	K03900.
OrthoDB	EOG44TP6X.
Family and domain databases
InterPro	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]
Pfam	PF08742. C8. 4 hits. PF01826. TIL. 5 hits. PF00092. VWA. 3 hits. PF00093. VWC. 2 hits. PF00094. VWD. 4 hits. [Graphical view]
PIRSF	PIRSF002495. VWF. 1 hit.
SMART	SM00832. C8. 4 hits. SM00041. CT. 1 hit. SM00327. VWA. 3 hits. SM00214. VWC. 5 hits. SM00216. VWD. 4 hits. [Graphical view]
SUPFAM	SSF57567. Cysrich_TIL. 5 hits.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	20816602.

Entry information

Entry name

VWF_CANFA

Accession

Primary (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:	April 3, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program