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Q28833 (VWF_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length2482 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Secreted By similarity. Secretedextracellular spaceextracellular matrix By similarity. Note: Localized to storage granules By similarity.

Tissue specificity

Plasma.

Domain

The propeptide 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.

N- and O-glycosylated By similarity.

Sequence similarities

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

Contains 3 TIL (trypsin inhibitory-like) domains.

Contains 3 VWFA domains.

Contains 3 VWFC domains.

Contains 3 VWFD domains.

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
Hemostasis
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   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

Propeptide‹1 – 437›437 By similarity
PRO_0000022686
Chain438 – 24822045von Willebrand factor
PRO_0000022687

Regions

Domain61 – 272212VWFD 1
Domain326 – 38156TIL 1
Domain450 – 50152TIL 2
Domain540 – 748209VWFD 2
Domain820 – 87051TIL 3
Domain947 – 1127181VWFA 1
Domain1167 – 1334168VWFA 2
Domain1360 – 1540181VWFA 3
Domain1618 – 1822205VWFD 3
Domain1924 – 199774VWFC 1
Domain2098 – 216467VWFC 2
Domain2249 – 231466VWFC 3
Domain2393 – 248189CTCK
Region438 – 46124Amino-terminal
Region462 – 50746E1
Region500 – 52728CX
Region1885 – 193046E2
Motif2176 – 21783Cell attachment site Potential

Amino acid modifications

Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation9051N-linked (GlcNAc...) Potential
Glycosylation11841N-linked (GlcNAc...) Potential
Glycosylation12431N-linked (GlcNAc...) Potential
Glycosylation16401N-linked (GlcNAc...) Potential
Glycosylation18921N-linked (GlcNAc...) Potential
Glycosylation19591N-linked (GlcNAc...) Potential
Glycosylation20261N-linked (GlcNAc...) Potential
Glycosylation20691N-linked (GlcNAc...) Potential
Glycosylation22151N-linked (GlcNAc...) Potential
Glycosylation22541N-linked (GlcNAc...) Potential
Glycosylation24591N-linked (GlcNAc...) Potential
Disulfide bond441 ↔ 482 By similarity
Disulfide bond450 ↔ 478 By similarity
Disulfide bond484 ↔ 495 By similarity
Disulfide bond541 ↔ 670 By similarity
Disulfide bond563 ↔ 705 By similarity
Disulfide bond572 ↔ 667 By similarity
Disulfide bond588 ↔ 595 By similarity
Disulfide bond734 ↔ 758 By similarity
Disulfide bond745 ↔ 785 By similarity
Disulfide bond763 ↔ 765 By similarity
Disulfide bond800 ↔ 804 By similarity
Disulfide bond823 ↔ 843 By similarity
Disulfide bond827 ↔ 839 By similarity
Disulfide bond870 ↔ 873 By similarity
Disulfide bond908 ↔ 911 By similarity
Disulfide bond942 ↔ 1128 By similarity
Disulfide bond1338 ↔ 1339 By similarity
Disulfide bond1355 ↔ 1541 By similarity
Disulfide bond1548 ↔ 1573 By similarity
Disulfide bond1568 ↔ 1609Or C-1568 with C-1611 By similarity
Disulfide bond1596 ↔ 1757 By similarity
Disulfide bond1619 ↔ 1754 By similarity
Disulfide bond1641 ↔ 1792 By similarity
Disulfide bond1662 ↔ 1670 By similarity
Disulfide bond2393 ↔ 2443 By similarity
Disulfide bond2408 ↔ 2457 By similarity
Disulfide bond2419 ↔ 2473 By similarity
Disulfide bond2423 ↔ 2475 By similarity
Disulfide bond? ↔ 2480 By similarity
Cross-link1389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q28833 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: D499B7DDFBBCAEDD

FASTA2,482272,397
        10         20         30         40         50         60 
DGCSCPEGQL LDDGRCVESA ECSCVHSGKR YPPGASLSRD CNTCICRNSL WVCSNEDCPG 

        70         80         90        100        110        120 
ECLVTGQSHF KSFDNRHFTF SGVCQYLLAR DCQDHTFSVI IETVQCADDP DAVCTRSVTV 

       130        140        150        160        170        180 
RLPSPHNSLV KLKHGGGVAM DGWDVQIPFL QGDLRIQHTV MASVHLSYGE DLQIDWDGRG 

       190        200        210        220        230        240 
RLLVKLSPVY AGRTCGLCGN YNGNQGDDFL TPAGLVEPLV EHFGNAWKLH GDCEDLRKQP 

       250        260        270        280        290        300 
TDPCSFNPRL TRFAEEACAI LTSPKFQACH DAVGPLPYLQ NCHYDVCSCS DGRDCLCDAV 

       310        320        330        340        350        360 
ATYAAACARR GVHIGWREPG FCALSCPPGQ VYLQCGTPCN LTCRSLSYPD EECAEDCLEG 

       370        380        390        400        410        420 
CFCPPGLYLD GSGDCVPKAQ CPCYHDGEIF QPEDIFSDHH TMCYCEDGFM HCSRAGAPGS 

       430        440        450        460        470        480 
LQPEVVLSSP LSHRSKRSLS CRPPMVKLVC PADNPRAEGL ECAKTCQNYD LECVSTGCVS 

       490        500        510        520        530        540 
GCLCPPGMVR HENRCVALQR CPCFHQGREY APGETVKVDC NTCVCRDRKW SCTDHVCDAS 

       550        560        570        580        590        600 
CSALGLAHYL TFDGLKYLFP GECQYVLVQD YCGSNPGTFR ILLGNEGCGY PSLKCRKRVT 

       610        620        630        640        650        660 
ILVDGGEIEL FDGEVMVKKP LKDETHFEVV ESGRFITVLL GSGLSVVWDR HLGISVFLKQ 

       670        680        690        700        710        720 
TYQEQVCGLC GNFDGVQNND LTGSSLQVEE DPVDFGNSWK VSPQCADTRK VPLDTSPATC 

       730        740        750        760        770        780 
HNNVMKQTMV DSSCRILTSD IFQDCNKLVD PEPYLDVCIY DTCSCESIGD CACFCDTIAA 

       790        800        810        820        830        840 
YARVCAQHGK VVTWRTATLC PQNCEERNLR EDGYQCEWRY NSCAPACPVT CQHPEPLACP 

       850        860        870        880        890        900 
VSCVEGCHAH CPPGKILDEL LQTCVSPEDC PVCEAAGRRL APGKKIILNP RDPAHCQICH 

       910        920        930        940        950        960 
CDGVNLTCEA CAEPVPPTEG PVSPTTPYEE DTPEPPLHDF FCSKLLDLVF LLDGSDKLSE 

       970        980        990       1000       1010       1020 
ADFEALKVFV VGMMEHLHIS QKHIRVAVVE YHDGPHAYIS LQDRKRPSEL RRIASQVKYA 

      1030       1040       1050       1060       1070       1080 
GSEVASISEV LKYTLFQIFG RVDRPEASRI ALLLMASQEP RRLAQNLARY LQGLKKKKVT 

      1090       1100       1110       1120       1130       1140 
VIPVGIGPHV SLKQIRLIEK QAPENKAFVV SGVDELEQRK NEIISYLCDL APEVPAPTRR 

      1150       1160       1170       1180       1190       1200 
PLVAQVTVAP ELPGVSTLEP KKRMALDVVF VLEGSDKVGE ANFNRSTEFV EEVIRRMDVG 

      1210       1220       1230       1240       1250       1260 
RDSVHVTVLQ YSYVVAVEHS FREAQSKGEV LQRVREIRFQ GGNRTNTGLA LQYLSEHSFS 

      1270       1280       1290       1300       1310       1320 
ASQGDREEAP NLVYMVTGNP ASDEIKRMPG DIQVVPIGVG PDVDMQELER LSWPNAPIFI 

      1330       1340       1350       1360       1370       1380 
QDFETLPREA PDLVLQRCCS GEGPHLPTQA PVPDCSQPLG VVLLLDGSSS LPASYFDEMK 

      1390       1400       1410       1420       1430       1440 
SFTKAFISKA NIGPQLTQVS VLQYGSITTI DLPWNMPLEK AHLRGLVDLM QREGGPSQIG 

      1450       1460       1470       1480       1490       1500 
DALGFAVRYV MSQVHGARPE ASKAVVIVVT DTSTDSVDAA AAAARSNRVA VFPIGIGDRY 

      1510       1520       1530       1540       1550       1560 
DEAQLRTLAG PGASSNVVKL QRIEDLPTLV TLGNSFLHKL CSGFVRVCID EDGSERKPGD 

      1570       1580       1590       1600       1610       1620 
VWTLPDQCHT VTCLPDGQTL LKSHRVNCDQ GLQPSCPSNQ PPIRVEEACG CRWTCPCVCT 

      1630       1640       1650       1660       1670       1680 
GSSTRHIVTF DGQNFKLMGN CSYVLFHNKE QDLEVILHNG ACGAGARQAC MKSIEVKHNG 

      1690       1700       1710       1720       1730       1740 
LSVELHRDME VVVNGRQVSV PYVGGNMEVG IYGTIMYEVR FNHLGHILTF TPQNNEFQLQ 

      1750       1760       1770       1780       1790       1800 
LSPKTFASKM YGLCGICDEN GANDFMLRDG TVTTDWKTMV QEWAVQQPGQ MCQPVPKEQC 

      1810       1820       1830       1840       1850       1860 
PVSGGYQCQV LLSALFAECH KVLAPAAYFA ICQQDSCHQE QVCEAVASYA HLCRTKGVCV 

      1870       1880       1890       1900       1910       1920 
DWRTPDFCAV SCPPSLVYNH CEHGCPRHCE GNSSSCGDHP SEGCFCPPHQ VMLGSSCVPE 

      1930       1940       1950       1960       1970       1980 
EACTQCVDDD GIRHQFLETW VPDHQPCQIC TCLSGRRVNC TLQPCPTARA PACGLCEVAR 

      1990       2000       2010       2020       2030       2040 
LRQEAHQCCP EYECVCDLVS CDLPPVPHCE GGLQPTLTNP GECRPNFTCA CRKEECPRGP 

      2050       2060       2070       2080       2090       2100 
LPSCPPHRTP ALRKTQCCDE YECACNCVNT TLSCPLGYLA STVTNDCGCT TTTCLPDKVC 

      2110       2120       2130       2140       2150       2160 
VHRGTVYPVG QFWEEGCDVC TCTDLEDAVM GLRVAQCAQK PCEDSCRPGF TYVLHEGECC 

      2170       2180       2190       2200       2210       2220 
GKCLPSACKV VIGSFRGDSV SYWKSVGSHW ASPENPCLIN ECVRVKEEVF VQQRNVSCPM 

      2230       2240       2250       2260       2270       2280 
LDVPTCPVGF QLSCKTSGCC PTCRCEPVEA CLLNGTIIGA GESLMIDVCT TCRCMLQEGV 

      2290       2300       2310       2320       2330       2340 
VFGFKLECKK TTCEACPLGY KEEKMPGECC GRCLPTACTI QLRGGQIMTL KRDETLQDGC 

      2350       2360       2370       2380       2390       2400 
DSHFCRVNER GEYIWEKRIT GCPPFDQHKC LAAGGKIMKI PGTCCDTCEE PECKDMTARL 

      2410       2420       2430       2440       2450       2460 
QYVKVGNCRS EEEVDIHYCQ GKCTSKAVYS IDTEDVEDQC ACCSPTRTEP MQVPLRCTNG 

      2470       2480 
STIYHEVLNA IQCKCSPRKC SK 

« Hide

References

[1]Seaman W.T., Read M.S., Bellinger D.A., Nichols T.C.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of the factor VIII binding domain of human, porcine and rabbit von Willebrand factor."
Lavergne J.-M., Piao Y.C., Ferreira V., Kerbiriou-Nabias D., Bahnak B.R., Meyer D.
Biochem. Biophys. Res. Commun. 194:1019-1024(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 397-553.
[3]"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
AF052036 mRNA. Translation: AAC06229.1.
S64541 mRNA. Translation: AAB27829.2.
PIRPN0563.
UniGeneSsc.978.

3D structure databases

ProteinModelPortalQ28833.
SMRQ28833. Positions 931-1138, 1353-1542.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI08.954.

Proteomic databases

PaxDbQ28833.
PRIDEQ28833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004380.

Family and domain databases

Gene3D3.40.50.410. 3 hits.
InterProIPR006207. Cys_knot_C.
IPR000742. EG-like_dom.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR002035. VWF_A.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]
PfamPF08742. C8. 3 hits.
PF01826. TIL. 4 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 3 hits.
[Graphical view]
SMARTSM00832. C8. 3 hits.
SM00041. CT. 1 hit.
SM00181. EGF. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 4 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. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVWF_PIG
AccessionPrimary (citable) accession number: Q28833
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 110 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