VWF_PIG
ID VWF_PIG Reviewed; 2482 AA.
AC Q28833;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=von Willebrand factor;
DE Short=vWF;
DE Flags: Precursor; Fragment;
GN Name=VWF; Synonyms=F8VWF;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seaman W.T., Read M.S., Bellinger D.A., Nichols T.C.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 397-553.
RX PubMed=8352759; DOI=10.1006/bbrc.1993.1923;
RA Lavergne J.-M., Piao Y.C., Ferreira V., Kerbiriou-Nabias D., Bahnak B.R.,
RA Meyer D.;
RT "Primary structure of the factor VIII binding domain of human, porcine and
RT rabbit von Willebrand factor.";
RL Biochem. Biophys. Res. Commun. 194:1019-1024(1993).
RN [3]
RP REVIEW.
RX PubMed=12871266; DOI=10.1046/j.1538-7836.2003.00260.x;
RA Ruggeri Z.M.;
RT "von Willebrand factor, platelets and endothelial cell interactions.";
RL J. Thromb. Haemost. 1:1335-1342(2003).
CC -!- FUNCTION: Important in the maintenance of hemostasis, it promotes
CC adhesion of platelets to the sites of vascular injury by forming a
CC molecular bridge between sub-endothelial collagen matrix and platelet-
CC surface receptor complex, glycoprotein Ibalpha/IX/V. Also acts as a
CC chaperone for coagulation factor VIII, delivering it to the site of
CC injury, stabilizing its heterodimeric structure and protecting it from
CC premature clearance from plasma (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Multimeric. Interacts with F8 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular
CC space, extracellular matrix {ECO:0000250}. Note=Localized to storage
CC granules. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DOMAIN: The propeptide is required for multimerization of vWF and for
CC its targeting to storage granules. {ECO:0000250}.
CC -!- PTM: All cysteine residues are involved in intrachain or interchain
CC disulfide bonds. {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; AF052036; AAC06229.1; -; mRNA.
DR EMBL; S64541; AAB27829.2; -; mRNA.
DR PIR; PN0563; PN0563.
DR AlphaFoldDB; Q28833; -.
DR SMR; Q28833; -.
DR STRING; 9823.ENSSSCP00000000759; -.
DR MEROPS; I08.954; -.
DR PaxDb; Q28833; -.
DR PeptideAtlas; Q28833; -.
DR PRIDE; Q28833; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q28833; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0033093; C:Weibel-Palade body; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019865; F:immunoglobulin binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0007599; P:hemostasis; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR037578; Von_Willebrand_factor.
DR InterPro; IPR032361; VWA_N2.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR11339:SF361; PTHR11339:SF361; 2.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF01826; TIL; 2.
DR Pfam; PF00092; VWA; 3.
DR Pfam; PF16164; VWA_N2; 1.
DR Pfam; PF00093; VWC; 2.
DR Pfam; PF00094; VWD; 3.
DR SMART; SM00832; C8; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00327; VWA; 3.
DR SMART; SM00214; VWC; 5.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR SUPFAM; SSF57567; SSF57567; 4.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS50234; VWFA; 3.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 3.
DR PROSITE; PS51233; VWFD; 3.
PE 2: Evidence at transcript level;
KW Blood coagulation; Cell adhesion; Cleavage on pair of basic residues;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hemostasis;
KW Reference proteome; Repeat; Secreted.
FT PROPEP <1..437
FT /evidence="ECO:0000250"
FT /id="PRO_0000022686"
FT CHAIN 438..2482
FT /note="von Willebrand factor"
FT /id="PRO_0000022687"
FT DOMAIN 60..234
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 326..381
FT /note="TIL 1"
FT DOMAIN 450..501
FT /note="TIL 2"
FT DOMAIN 539..706
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 820..870
FT /note="TIL 3"
FT DOMAIN 947..1127
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1167..1334
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1360..1540
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1617..1793
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1924..1997
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2098..2164
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2249..2314
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2393..2481
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 438..461
FT /note="Amino-terminal"
FT REGION 462..507
FT /note="E1"
FT REGION 500..527
FT /note="CX"
FT REGION 1885..1930
FT /note="E2"
FT MOTIF 2176..2178
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 84..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 106..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 441..482
FT /evidence="ECO:0000250"
FT DISULFID 450..478
FT /evidence="ECO:0000250"
FT DISULFID 484..495
FT /evidence="ECO:0000250"
FT DISULFID 541..670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 563..705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 572..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 588..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 734..758
FT /evidence="ECO:0000250"
FT DISULFID 745..785
FT /evidence="ECO:0000250"
FT DISULFID 763..765
FT /evidence="ECO:0000250"
FT DISULFID 800..804
FT /evidence="ECO:0000250"
FT DISULFID 823..843
FT /evidence="ECO:0000250"
FT DISULFID 827..839
FT /evidence="ECO:0000250"
FT DISULFID 870..873
FT /evidence="ECO:0000250"
FT DISULFID 908..911
FT /evidence="ECO:0000250"
FT DISULFID 942..1128
FT /evidence="ECO:0000250"
FT DISULFID 1338..1339
FT /evidence="ECO:0000250"
FT DISULFID 1355..1541
FT /evidence="ECO:0000250"
FT DISULFID 1548..1573
FT /evidence="ECO:0000250"
FT DISULFID 1568..1609
FT /note="Or C-1568 with C-1611"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039,
FT ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1596..1757
FT /evidence="ECO:0000250"
FT DISULFID 1619..1754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1641..1792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1662..1670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2393..2443
FT /evidence="ECO:0000250"
FT DISULFID 2408..2457
FT /evidence="ECO:0000250"
FT DISULFID 2419..2473
FT /evidence="ECO:0000250"
FT DISULFID 2423..2475
FT /evidence="ECO:0000250"
FT DISULFID ?..2480
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 2482 AA; 272397 MW; D499B7DDFBBCAEDD CRC64;
DGCSCPEGQL LDDGRCVESA ECSCVHSGKR YPPGASLSRD CNTCICRNSL WVCSNEDCPG
ECLVTGQSHF KSFDNRHFTF SGVCQYLLAR DCQDHTFSVI IETVQCADDP DAVCTRSVTV
RLPSPHNSLV KLKHGGGVAM DGWDVQIPFL QGDLRIQHTV MASVHLSYGE DLQIDWDGRG
RLLVKLSPVY AGRTCGLCGN YNGNQGDDFL TPAGLVEPLV EHFGNAWKLH GDCEDLRKQP
TDPCSFNPRL TRFAEEACAI LTSPKFQACH DAVGPLPYLQ NCHYDVCSCS DGRDCLCDAV
ATYAAACARR GVHIGWREPG FCALSCPPGQ VYLQCGTPCN LTCRSLSYPD EECAEDCLEG
CFCPPGLYLD GSGDCVPKAQ CPCYHDGEIF QPEDIFSDHH TMCYCEDGFM HCSRAGAPGS
LQPEVVLSSP LSHRSKRSLS CRPPMVKLVC PADNPRAEGL ECAKTCQNYD LECVSTGCVS
GCLCPPGMVR HENRCVALQR CPCFHQGREY APGETVKVDC NTCVCRDRKW SCTDHVCDAS
CSALGLAHYL TFDGLKYLFP GECQYVLVQD YCGSNPGTFR ILLGNEGCGY PSLKCRKRVT
ILVDGGEIEL FDGEVMVKKP LKDETHFEVV ESGRFITVLL GSGLSVVWDR HLGISVFLKQ
TYQEQVCGLC GNFDGVQNND LTGSSLQVEE DPVDFGNSWK VSPQCADTRK VPLDTSPATC
HNNVMKQTMV DSSCRILTSD IFQDCNKLVD PEPYLDVCIY DTCSCESIGD CACFCDTIAA
YARVCAQHGK VVTWRTATLC PQNCEERNLR EDGYQCEWRY NSCAPACPVT CQHPEPLACP
VSCVEGCHAH CPPGKILDEL LQTCVSPEDC PVCEAAGRRL APGKKIILNP RDPAHCQICH
CDGVNLTCEA CAEPVPPTEG PVSPTTPYEE DTPEPPLHDF FCSKLLDLVF LLDGSDKLSE
ADFEALKVFV VGMMEHLHIS QKHIRVAVVE YHDGPHAYIS LQDRKRPSEL RRIASQVKYA
GSEVASISEV LKYTLFQIFG RVDRPEASRI ALLLMASQEP RRLAQNLARY LQGLKKKKVT
VIPVGIGPHV SLKQIRLIEK QAPENKAFVV SGVDELEQRK NEIISYLCDL APEVPAPTRR
PLVAQVTVAP ELPGVSTLEP KKRMALDVVF VLEGSDKVGE ANFNRSTEFV EEVIRRMDVG
RDSVHVTVLQ YSYVVAVEHS FREAQSKGEV LQRVREIRFQ GGNRTNTGLA LQYLSEHSFS
ASQGDREEAP NLVYMVTGNP ASDEIKRMPG DIQVVPIGVG PDVDMQELER LSWPNAPIFI
QDFETLPREA PDLVLQRCCS GEGPHLPTQA PVPDCSQPLG VVLLLDGSSS LPASYFDEMK
SFTKAFISKA NIGPQLTQVS VLQYGSITTI DLPWNMPLEK AHLRGLVDLM QREGGPSQIG
DALGFAVRYV MSQVHGARPE ASKAVVIVVT DTSTDSVDAA AAAARSNRVA VFPIGIGDRY
DEAQLRTLAG PGASSNVVKL QRIEDLPTLV TLGNSFLHKL CSGFVRVCID EDGSERKPGD
VWTLPDQCHT VTCLPDGQTL LKSHRVNCDQ GLQPSCPSNQ PPIRVEEACG CRWTCPCVCT
GSSTRHIVTF DGQNFKLMGN CSYVLFHNKE QDLEVILHNG ACGAGARQAC MKSIEVKHNG
LSVELHRDME VVVNGRQVSV PYVGGNMEVG IYGTIMYEVR FNHLGHILTF TPQNNEFQLQ
LSPKTFASKM YGLCGICDEN GANDFMLRDG TVTTDWKTMV QEWAVQQPGQ MCQPVPKEQC
PVSGGYQCQV LLSALFAECH KVLAPAAYFA ICQQDSCHQE QVCEAVASYA HLCRTKGVCV
DWRTPDFCAV SCPPSLVYNH CEHGCPRHCE GNSSSCGDHP SEGCFCPPHQ VMLGSSCVPE
EACTQCVDDD GIRHQFLETW VPDHQPCQIC TCLSGRRVNC TLQPCPTARA PACGLCEVAR
LRQEAHQCCP EYECVCDLVS CDLPPVPHCE GGLQPTLTNP GECRPNFTCA CRKEECPRGP
LPSCPPHRTP ALRKTQCCDE YECACNCVNT TLSCPLGYLA STVTNDCGCT TTTCLPDKVC
VHRGTVYPVG QFWEEGCDVC TCTDLEDAVM GLRVAQCAQK PCEDSCRPGF TYVLHEGECC
GKCLPSACKV VIGSFRGDSV SYWKSVGSHW ASPENPCLIN ECVRVKEEVF VQQRNVSCPM
LDVPTCPVGF QLSCKTSGCC PTCRCEPVEA CLLNGTIIGA GESLMIDVCT TCRCMLQEGV
VFGFKLECKK TTCEACPLGY KEEKMPGECC GRCLPTACTI QLRGGQIMTL KRDETLQDGC
DSHFCRVNER GEYIWEKRIT GCPPFDQHKC LAAGGKIMKI PGTCCDTCEE PECKDMTARL
QYVKVGNCRS EEEVDIHYCQ GKCTSKAVYS IDTEDVEDQC ACCSPTRTEP MQVPLRCTNG
STIYHEVLNA IQCKCSPRKC SK
