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Protein

von Willebrand factor

Gene

VWF

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Cell adhesion, Hemostasis

Protein family/group databases

MEROPSiI08.954.

Names & Taxonomyi

Protein namesi
Recommended name:
von Willebrand factor
Short name:
vWF
Gene namesi
Name:VWF
Synonyms:F8VWF
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000022686‹1 – 437By similarityAdd BLAST›437
ChainiPRO_0000022687438 – 2482von Willebrand factorAdd BLAST2045

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi? ↔ 2480By similarity
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi441 ↔ 482By similarity
Disulfide bondi450 ↔ 478By similarity
Disulfide bondi484 ↔ 495By similarity
Disulfide bondi541 ↔ 670By similarity
Disulfide bondi563 ↔ 705By similarity
Disulfide bondi572 ↔ 667By similarity
Disulfide bondi588 ↔ 595By similarity
Disulfide bondi734 ↔ 758By similarity
Disulfide bondi745 ↔ 785By similarity
Disulfide bondi763 ↔ 765By similarity
Disulfide bondi800 ↔ 804By similarity
Disulfide bondi823 ↔ 843By similarity
Disulfide bondi827 ↔ 839By similarity
Disulfide bondi870 ↔ 873By similarity
Glycosylationi905N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi908 ↔ 911By similarity
Disulfide bondi942 ↔ 1128By similarity
Glycosylationi1184N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1243N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1338 ↔ 1339By similarity
Disulfide bondi1355 ↔ 1541By similarity
Disulfide bondi1548 ↔ 1573By similarity
Disulfide bondi1568 ↔ 1609Or C-1568 with C-1611PROSITE-ProRule annotation
Disulfide bondi1596 ↔ 1757By similarity
Disulfide bondi1619 ↔ 1754By similarity
Glycosylationi1640N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1641 ↔ 1792By similarity
Disulfide bondi1662 ↔ 1670By similarity
Glycosylationi1892N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1959N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2026N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2069N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2215N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2254N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2393 ↔ 2443By similarity
Disulfide bondi2408 ↔ 2457By similarity
Disulfide bondi2419 ↔ 2473By similarity
Disulfide bondi2423 ↔ 2475By similarity
Glycosylationi2459N-linked (GlcNAc...)Sequence analysis1

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

PaxDbiQ28833.
PeptideAtlasiQ28833.
PRIDEiQ28833.

Expressioni

Tissue specificityi

Plasma.

Interactioni

Subunit structurei

Multimeric. Interacts with F8 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000759.

Structurei

3D structure databases

ProteinModelPortaliQ28833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 272VWFD 1PROSITE-ProRule annotationAdd BLAST212
Domaini326 – 381TIL 1Add BLAST56
Domaini450 – 501TIL 2Add BLAST52
Domaini540 – 748VWFD 2PROSITE-ProRule annotationAdd BLAST209
Domaini820 – 870TIL 3Add BLAST51
Domaini947 – 1127VWFA 1PROSITE-ProRule annotationAdd BLAST181
Domaini1167 – 1334VWFA 2PROSITE-ProRule annotationAdd BLAST168
Domaini1360 – 1540VWFA 3PROSITE-ProRule annotationAdd BLAST181
Domaini1618 – 1822VWFD 3PROSITE-ProRule annotationAdd BLAST205
Domaini1924 – 1997VWFC 1PROSITE-ProRule annotationAdd BLAST74
Domaini2098 – 2164VWFC 2PROSITE-ProRule annotationAdd BLAST67
Domaini2249 – 2314VWFC 3PROSITE-ProRule annotationAdd BLAST66
Domaini2393 – 2481CTCKPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni438 – 461Amino-terminalAdd BLAST24
Regioni462 – 507E1Add BLAST46
Regioni500 – 527CXAdd BLAST28
Regioni1885 – 1930E2Add BLAST46

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2176 – 2178Cell attachment siteSequence analysis3

Domaini

The propeptide 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 3 VWFD domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1216. Eukaryota.
ENOG410XNSK. LUCA.
HOVERGENiHBG004380.
InParanoidiQ28833.

Family and domain databases

Gene3Di3.40.50.410. 3 hits.
InterProiIPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR032361. VWA_N2.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PANTHERiPTHR11339:SF259. PTHR11339:SF259. 4 hits.
PfamiPF08742. C8. 3 hits.
PF01826. TIL. 4 hits.
PF00092. VWA. 3 hits.
PF16164. VWA_N2. 1 hit.
PF00093. VWC. 2 hits.
PF00094. VWD. 3 hits.
[Graphical view]
SMARTiSM00832. C8. 3 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00215. VWC_out. 2 hits.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 4 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. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

Q28833-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DGCSCPEGQL LDDGRCVESA ECSCVHSGKR YPPGASLSRD CNTCICRNSL
60 70 80 90 100
WVCSNEDCPG ECLVTGQSHF KSFDNRHFTF SGVCQYLLAR DCQDHTFSVI
110 120 130 140 150
IETVQCADDP DAVCTRSVTV RLPSPHNSLV KLKHGGGVAM DGWDVQIPFL
160 170 180 190 200
QGDLRIQHTV MASVHLSYGE DLQIDWDGRG RLLVKLSPVY AGRTCGLCGN
210 220 230 240 250
YNGNQGDDFL TPAGLVEPLV EHFGNAWKLH GDCEDLRKQP TDPCSFNPRL
260 270 280 290 300
TRFAEEACAI LTSPKFQACH DAVGPLPYLQ NCHYDVCSCS DGRDCLCDAV
310 320 330 340 350
ATYAAACARR GVHIGWREPG FCALSCPPGQ VYLQCGTPCN LTCRSLSYPD
360 370 380 390 400
EECAEDCLEG CFCPPGLYLD GSGDCVPKAQ CPCYHDGEIF QPEDIFSDHH
410 420 430 440 450
TMCYCEDGFM HCSRAGAPGS LQPEVVLSSP LSHRSKRSLS CRPPMVKLVC
460 470 480 490 500
PADNPRAEGL ECAKTCQNYD LECVSTGCVS GCLCPPGMVR HENRCVALQR
510 520 530 540 550
CPCFHQGREY APGETVKVDC NTCVCRDRKW SCTDHVCDAS CSALGLAHYL
560 570 580 590 600
TFDGLKYLFP GECQYVLVQD YCGSNPGTFR ILLGNEGCGY PSLKCRKRVT
610 620 630 640 650
ILVDGGEIEL FDGEVMVKKP LKDETHFEVV ESGRFITVLL GSGLSVVWDR
660 670 680 690 700
HLGISVFLKQ TYQEQVCGLC GNFDGVQNND LTGSSLQVEE DPVDFGNSWK
710 720 730 740 750
VSPQCADTRK VPLDTSPATC HNNVMKQTMV DSSCRILTSD IFQDCNKLVD
760 770 780 790 800
PEPYLDVCIY DTCSCESIGD CACFCDTIAA YARVCAQHGK VVTWRTATLC
810 820 830 840 850
PQNCEERNLR EDGYQCEWRY NSCAPACPVT CQHPEPLACP VSCVEGCHAH
860 870 880 890 900
CPPGKILDEL LQTCVSPEDC PVCEAAGRRL APGKKIILNP RDPAHCQICH
910 920 930 940 950
CDGVNLTCEA CAEPVPPTEG PVSPTTPYEE DTPEPPLHDF FCSKLLDLVF
960 970 980 990 1000
LLDGSDKLSE ADFEALKVFV VGMMEHLHIS QKHIRVAVVE YHDGPHAYIS
1010 1020 1030 1040 1050
LQDRKRPSEL RRIASQVKYA GSEVASISEV LKYTLFQIFG RVDRPEASRI
1060 1070 1080 1090 1100
ALLLMASQEP RRLAQNLARY LQGLKKKKVT VIPVGIGPHV SLKQIRLIEK
1110 1120 1130 1140 1150
QAPENKAFVV SGVDELEQRK NEIISYLCDL APEVPAPTRR PLVAQVTVAP
1160 1170 1180 1190 1200
ELPGVSTLEP KKRMALDVVF VLEGSDKVGE ANFNRSTEFV EEVIRRMDVG
1210 1220 1230 1240 1250
RDSVHVTVLQ YSYVVAVEHS FREAQSKGEV LQRVREIRFQ GGNRTNTGLA
1260 1270 1280 1290 1300
LQYLSEHSFS ASQGDREEAP NLVYMVTGNP ASDEIKRMPG DIQVVPIGVG
1310 1320 1330 1340 1350
PDVDMQELER LSWPNAPIFI QDFETLPREA PDLVLQRCCS GEGPHLPTQA
1360 1370 1380 1390 1400
PVPDCSQPLG VVLLLDGSSS LPASYFDEMK SFTKAFISKA NIGPQLTQVS
1410 1420 1430 1440 1450
VLQYGSITTI DLPWNMPLEK AHLRGLVDLM QREGGPSQIG DALGFAVRYV
1460 1470 1480 1490 1500
MSQVHGARPE ASKAVVIVVT DTSTDSVDAA AAAARSNRVA VFPIGIGDRY
1510 1520 1530 1540 1550
DEAQLRTLAG PGASSNVVKL QRIEDLPTLV TLGNSFLHKL CSGFVRVCID
1560 1570 1580 1590 1600
EDGSERKPGD VWTLPDQCHT VTCLPDGQTL LKSHRVNCDQ GLQPSCPSNQ
1610 1620 1630 1640 1650
PPIRVEEACG CRWTCPCVCT GSSTRHIVTF DGQNFKLMGN CSYVLFHNKE
1660 1670 1680 1690 1700
QDLEVILHNG ACGAGARQAC MKSIEVKHNG LSVELHRDME VVVNGRQVSV
1710 1720 1730 1740 1750
PYVGGNMEVG IYGTIMYEVR FNHLGHILTF TPQNNEFQLQ LSPKTFASKM
1760 1770 1780 1790 1800
YGLCGICDEN GANDFMLRDG TVTTDWKTMV QEWAVQQPGQ MCQPVPKEQC
1810 1820 1830 1840 1850
PVSGGYQCQV LLSALFAECH KVLAPAAYFA ICQQDSCHQE QVCEAVASYA
1860 1870 1880 1890 1900
HLCRTKGVCV DWRTPDFCAV SCPPSLVYNH CEHGCPRHCE GNSSSCGDHP
1910 1920 1930 1940 1950
SEGCFCPPHQ VMLGSSCVPE EACTQCVDDD GIRHQFLETW VPDHQPCQIC
1960 1970 1980 1990 2000
TCLSGRRVNC TLQPCPTARA PACGLCEVAR LRQEAHQCCP EYECVCDLVS
2010 2020 2030 2040 2050
CDLPPVPHCE GGLQPTLTNP GECRPNFTCA CRKEECPRGP LPSCPPHRTP
2060 2070 2080 2090 2100
ALRKTQCCDE YECACNCVNT TLSCPLGYLA STVTNDCGCT TTTCLPDKVC
2110 2120 2130 2140 2150
VHRGTVYPVG QFWEEGCDVC TCTDLEDAVM GLRVAQCAQK PCEDSCRPGF
2160 2170 2180 2190 2200
TYVLHEGECC GKCLPSACKV VIGSFRGDSV SYWKSVGSHW ASPENPCLIN
2210 2220 2230 2240 2250
ECVRVKEEVF VQQRNVSCPM LDVPTCPVGF QLSCKTSGCC PTCRCEPVEA
2260 2270 2280 2290 2300
CLLNGTIIGA GESLMIDVCT TCRCMLQEGV VFGFKLECKK TTCEACPLGY
2310 2320 2330 2340 2350
KEEKMPGECC GRCLPTACTI QLRGGQIMTL KRDETLQDGC DSHFCRVNER
2360 2370 2380 2390 2400
GEYIWEKRIT GCPPFDQHKC LAAGGKIMKI PGTCCDTCEE PECKDMTARL
2410 2420 2430 2440 2450
QYVKVGNCRS EEEVDIHYCQ GKCTSKAVYS IDTEDVEDQC ACCSPTRTEP
2460 2470 2480
MQVPLRCTNG STIYHEVLNA IQCKCSPRKC SK
Length:2,482
Mass (Da):272,397
Last modified:May 1, 1999 - v2
Checksum:iD499B7DDFBBCAEDD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052036 mRNA. Translation: AAC06229.1.
S64541 mRNA. Translation: AAB27829.2.
PIRiPN0563.
UniGeneiSsc.978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052036 mRNA. Translation: AAC06229.1.
S64541 mRNA. Translation: AAB27829.2.
PIRiPN0563.
UniGeneiSsc.978.

3D structure databases

ProteinModelPortaliQ28833.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000759.

Protein family/group databases

MEROPSiI08.954.

Proteomic databases

PaxDbiQ28833.
PeptideAtlasiQ28833.
PRIDEiQ28833.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1216. Eukaryota.
ENOG410XNSK. LUCA.
HOVERGENiHBG004380.
InParanoidiQ28833.

Family and domain databases

Gene3Di3.40.50.410. 3 hits.
InterProiIPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR032361. VWA_N2.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PANTHERiPTHR11339:SF259. PTHR11339:SF259. 4 hits.
PfamiPF08742. C8. 3 hits.
PF01826. TIL. 4 hits.
PF00092. VWA. 3 hits.
PF16164. VWA_N2. 1 hit.
PF00093. VWC. 2 hits.
PF00094. VWD. 3 hits.
[Graphical view]
SMARTiSM00832. C8. 3 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00215. VWC_out. 2 hits.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 4 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. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVWF_PIG
AccessioniPrimary (citable) accession number: Q28833
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.