Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q28833

- VWF_PIG

UniProt

Q28833 - VWF_PIG

Protein

von Willebrand factor

Gene

VWF

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. extracellular matrix Source: UniProtKB
    3. extracellular region Source: UniProtKB
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    5. Weibel-Palade body Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei‹1 – 437›437By similarityPRO_0000022686Add
    BLAST
    Chaini438 – 24822045von Willebrand factorPRO_0000022687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi? ↔ 2480By similarity
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi905 – 9051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi908 ↔ 911By similarity
    Disulfide bondi942 ↔ 1128By similarity
    Glycosylationi1184 – 11841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1243 – 12431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1338 ↔ 1339By similarity
    Disulfide bondi1355 ↔ 1541By similarity
    Cross-linki1389 – 1389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Disulfide bondi1548 ↔ 1573By similarity
    Disulfide bondi1568 ↔ 1609Or C-1568 with C-1611PROSITE-ProRule annotation
    Disulfide bondi1596 ↔ 1757By similarity
    Disulfide bondi1619 ↔ 1754By similarity
    Glycosylationi1640 – 16401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1641 ↔ 1792By similarity
    Disulfide bondi1662 ↔ 1670By similarity
    Glycosylationi1892 – 18921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1959 – 19591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2026 – 20261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2069 – 20691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2215 – 22151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2254 – 22541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2393 ↔ 2443By similarity
    Disulfide bondi2408 ↔ 2457By similarity
    Disulfide bondi2419 ↔ 2473By similarity
    Disulfide bondi2423 ↔ 2475By similarity
    Glycosylationi2459 – 24591N-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, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiQ28833.
    PRIDEiQ28833.

    Expressioni

    Tissue specificityi

    Plasma.

    Interactioni

    Subunit structurei

    Multimeric. Interacts with F8 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ28833.
    SMRiQ28833. Positions 931-1138, 1353-1542.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 272212VWFD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini326 – 38156TIL 1Add
    BLAST
    Domaini450 – 50152TIL 2Add
    BLAST
    Domaini540 – 748209VWFD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini820 – 87051TIL 3Add
    BLAST
    Domaini947 – 1127181VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1167 – 1334168VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1360 – 1540181VWFA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1618 – 1822205VWFD 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1924 – 199774VWFC 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2098 – 216467VWFC 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2249 – 231466VWFC 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2393 – 248189CTCKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni438 – 46124Amino-terminalAdd
    BLAST
    Regioni462 – 50746E1Add
    BLAST
    Regioni500 – 52728CXAdd
    BLAST
    Regioni1885 – 193046E2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2176 – 21783Cell attachment siteSequence Analysis

    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

    eggNOGiNOG12793.
    HOVERGENiHBG004380.

    Family and domain databases

    Gene3Di3.40.50.410. 3 hits.
    InterProiIPR006207. 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]
    PfamiPF08742. C8. 3 hits.
    PF01826. TIL. 4 hits.
    PF00092. VWA. 3 hits.
    PF00093. VWC. 2 hits.
    PF00094. VWD. 3 hits.
    [Graphical view]
    SMARTiSM00832. 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]
    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

    DGCSCPEGQL LDDGRCVESA ECSCVHSGKR YPPGASLSRD CNTCICRNSL     50
    WVCSNEDCPG ECLVTGQSHF KSFDNRHFTF SGVCQYLLAR DCQDHTFSVI 100
    IETVQCADDP DAVCTRSVTV RLPSPHNSLV KLKHGGGVAM DGWDVQIPFL 150
    QGDLRIQHTV MASVHLSYGE DLQIDWDGRG RLLVKLSPVY AGRTCGLCGN 200
    YNGNQGDDFL TPAGLVEPLV EHFGNAWKLH GDCEDLRKQP TDPCSFNPRL 250
    TRFAEEACAI LTSPKFQACH DAVGPLPYLQ NCHYDVCSCS DGRDCLCDAV 300
    ATYAAACARR GVHIGWREPG FCALSCPPGQ VYLQCGTPCN LTCRSLSYPD 350
    EECAEDCLEG CFCPPGLYLD GSGDCVPKAQ CPCYHDGEIF QPEDIFSDHH 400
    TMCYCEDGFM HCSRAGAPGS LQPEVVLSSP LSHRSKRSLS CRPPMVKLVC 450
    PADNPRAEGL ECAKTCQNYD LECVSTGCVS GCLCPPGMVR HENRCVALQR 500
    CPCFHQGREY APGETVKVDC NTCVCRDRKW SCTDHVCDAS CSALGLAHYL 550
    TFDGLKYLFP GECQYVLVQD YCGSNPGTFR ILLGNEGCGY PSLKCRKRVT 600
    ILVDGGEIEL FDGEVMVKKP LKDETHFEVV ESGRFITVLL GSGLSVVWDR 650
    HLGISVFLKQ TYQEQVCGLC GNFDGVQNND LTGSSLQVEE DPVDFGNSWK 700
    VSPQCADTRK VPLDTSPATC HNNVMKQTMV DSSCRILTSD IFQDCNKLVD 750
    PEPYLDVCIY DTCSCESIGD CACFCDTIAA YARVCAQHGK VVTWRTATLC 800
    PQNCEERNLR EDGYQCEWRY NSCAPACPVT CQHPEPLACP VSCVEGCHAH 850
    CPPGKILDEL LQTCVSPEDC PVCEAAGRRL APGKKIILNP RDPAHCQICH 900
    CDGVNLTCEA CAEPVPPTEG PVSPTTPYEE DTPEPPLHDF FCSKLLDLVF 950
    LLDGSDKLSE ADFEALKVFV VGMMEHLHIS QKHIRVAVVE YHDGPHAYIS 1000
    LQDRKRPSEL RRIASQVKYA GSEVASISEV LKYTLFQIFG RVDRPEASRI 1050
    ALLLMASQEP RRLAQNLARY LQGLKKKKVT VIPVGIGPHV SLKQIRLIEK 1100
    QAPENKAFVV SGVDELEQRK NEIISYLCDL APEVPAPTRR PLVAQVTVAP 1150
    ELPGVSTLEP KKRMALDVVF VLEGSDKVGE ANFNRSTEFV EEVIRRMDVG 1200
    RDSVHVTVLQ YSYVVAVEHS FREAQSKGEV LQRVREIRFQ GGNRTNTGLA 1250
    LQYLSEHSFS ASQGDREEAP NLVYMVTGNP ASDEIKRMPG DIQVVPIGVG 1300
    PDVDMQELER LSWPNAPIFI QDFETLPREA PDLVLQRCCS GEGPHLPTQA 1350
    PVPDCSQPLG VVLLLDGSSS LPASYFDEMK SFTKAFISKA NIGPQLTQVS 1400
    VLQYGSITTI DLPWNMPLEK AHLRGLVDLM QREGGPSQIG DALGFAVRYV 1450
    MSQVHGARPE ASKAVVIVVT DTSTDSVDAA AAAARSNRVA VFPIGIGDRY 1500
    DEAQLRTLAG PGASSNVVKL QRIEDLPTLV TLGNSFLHKL CSGFVRVCID 1550
    EDGSERKPGD VWTLPDQCHT VTCLPDGQTL LKSHRVNCDQ GLQPSCPSNQ 1600
    PPIRVEEACG CRWTCPCVCT GSSTRHIVTF DGQNFKLMGN CSYVLFHNKE 1650
    QDLEVILHNG ACGAGARQAC MKSIEVKHNG LSVELHRDME VVVNGRQVSV 1700
    PYVGGNMEVG IYGTIMYEVR FNHLGHILTF TPQNNEFQLQ LSPKTFASKM 1750
    YGLCGICDEN GANDFMLRDG TVTTDWKTMV QEWAVQQPGQ MCQPVPKEQC 1800
    PVSGGYQCQV LLSALFAECH KVLAPAAYFA ICQQDSCHQE QVCEAVASYA 1850
    HLCRTKGVCV DWRTPDFCAV SCPPSLVYNH CEHGCPRHCE GNSSSCGDHP 1900
    SEGCFCPPHQ VMLGSSCVPE EACTQCVDDD GIRHQFLETW VPDHQPCQIC 1950
    TCLSGRRVNC TLQPCPTARA PACGLCEVAR LRQEAHQCCP EYECVCDLVS 2000
    CDLPPVPHCE GGLQPTLTNP GECRPNFTCA CRKEECPRGP LPSCPPHRTP 2050
    ALRKTQCCDE YECACNCVNT TLSCPLGYLA STVTNDCGCT TTTCLPDKVC 2100
    VHRGTVYPVG QFWEEGCDVC TCTDLEDAVM GLRVAQCAQK PCEDSCRPGF 2150
    TYVLHEGECC GKCLPSACKV VIGSFRGDSV SYWKSVGSHW ASPENPCLIN 2200
    ECVRVKEEVF VQQRNVSCPM LDVPTCPVGF QLSCKTSGCC PTCRCEPVEA 2250
    CLLNGTIIGA GESLMIDVCT TCRCMLQEGV VFGFKLECKK TTCEACPLGY 2300
    KEEKMPGECC GRCLPTACTI QLRGGQIMTL KRDETLQDGC DSHFCRVNER 2350
    GEYIWEKRIT GCPPFDQHKC LAAGGKIMKI PGTCCDTCEE PECKDMTARL 2400
    QYVKVGNCRS EEEVDIHYCQ GKCTSKAVYS IDTEDVEDQC ACCSPTRTEP 2450
    MQVPLRCTNG STIYHEVLNA IQCKCSPRKC SK 2482
    Length:2,482
    Mass (Da):272,397
    Last modified:May 1, 1999 - v2
    Checksum:iD499B7DDFBBCAEDD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052036 mRNA. Translation: AAC06229.1.
    S64541 mRNA. Translation: AAB27829.2.
    PIRiPN0563.
    UniGeneiSsc.978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052036 mRNA. Translation: AAC06229.1 .
    S64541 mRNA. Translation: AAB27829.2 .
    PIRi PN0563.
    UniGenei Ssc.978.

    3D structure databases

    ProteinModelPortali Q28833.
    SMRi Q28833. Positions 931-1138, 1353-1542.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi I08.954.

    Proteomic databases

    PaxDbi Q28833.
    PRIDEi Q28833.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004380.

    Family and domain databases

    Gene3Di 3.40.50.410. 3 hits.
    InterProi IPR006207. 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 ]
    Pfami PF08742. C8. 3 hits.
    PF01826. TIL. 4 hits.
    PF00092. VWA. 3 hits.
    PF00093. VWC. 2 hits.
    PF00094. VWD. 3 hits.
    [Graphical view ]
    SMARTi SM00832. 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 ]
    SUPFAMi SSF53300. SSF53300. 3 hits.
    SSF57567. SSF57567. 4 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. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 111 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