ID F1SL22_PIG Unreviewed; 2940 AA.
AC F1SL22;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=von Willebrand factor {ECO:0000256|ARBA:ARBA00016619, ECO:0000256|PIRNR:PIRNR002495};
DE Short=vWF {ECO:0000256|PIRNR:PIRNR002495};
GN Name=VWF {ECO:0000313|Ensembl:ENSSSCP00000000759.3,
GN ECO:0000313|VGNC:VGNC:104094};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000000759.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000000759.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000000759.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000000759.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 GPIb-IX-V. Also acts as a chaperone for
CC coagulation factor VIII, delivering it to the site of injury,
CC stabilizing its heterodimeric structure and protecting it from
CC premature clearance from plasma. {ECO:0000256|PIRNR:PIRNR002495}.
CC -!- SUBUNIT: Multimeric. Interacts with F8.
CC {ECO:0000256|ARBA:ARBA00025858}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR002495}.
CC Secreted {ECO:0000256|PIRNR:PIRNR002495}. Note=Localized to storage
CC granules. {ECO:0000256|PIRNR:PIRNR002495}.
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DR SMR; F1SL22; -.
DR PeptideAtlas; F1SL22; -.
DR Ensembl; ENSSSCT00000000775.5; ENSSSCP00000000759.3; ENSSSCG00000000712.6.
DR VGNC; VGNC:104094; VWF.
DR GeneTree; ENSGT00940000155810; -.
DR HOGENOM; CLU_248604_0_0_1; -.
DR InParanoid; F1SL22; -.
DR OMA; KFEACHH; -.
DR TreeFam; TF300299; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Reactome; R-SSC-216083; Integrin cell surface interactions.
DR Reactome; R-SSC-354192; Integrin signaling.
DR Reactome; R-SSC-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-SSC-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-SSC-430116; GP1b-IX-V activation signalling.
DR Reactome; R-SSC-5674135; MAP2K and MAPK activation.
DR Reactome; R-SSC-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-SSC-76009; Platelet Aggregation (Plug Formation).
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000712; Expressed in endocardial endothelium and 40 other cell types or tissues.
DR ExpressionAtlas; F1SL22; baseline and differential.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0033093; C:Weibel-Palade body; IEA:UniProtKB-UniRule.
DR GO; GO:0005518; F:collagen binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019865; F:immunoglobulin binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IEA:UniProtKB-UniRule.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:Ensembl.
DR CDD; cd19941; TIL; 5.
DR CDD; cd01450; vWFA_subfamily_ECM; 3.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR037578; Von_Willebrand_factor.
DR InterPro; IPR032361; VWA_N2.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
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; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR PANTHER; PTHR11339:SF398; MUCIN-2-LIKE-RELATED; 1.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF00092; VWA; 3.
DR Pfam; PF16164; VWA_N2; 1.
DR Pfam; PF00093; VWC; 2.
DR Pfam; PF00094; VWD; 4.
DR PIRSF; PIRSF002495; VWF; 1.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00832; C8; 4.
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; 4.
DR SUPFAM; SSF57603; FnI-like domain; 2.
DR SUPFAM; SSF57567; Serine protease inhibitors; 5.
DR SUPFAM; SSF53300; vWA-like; 3.
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; 4.
PE 1: Evidence at protein level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR002495};
KW Cell adhesion {ECO:0000256|PIRNR:PIRNR002495};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002495-50};
KW Extracellular matrix {ECO:0000256|PIRNR:PIRNR002495};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR002495};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SL22};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002495};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2940
FT /note="von Willebrand factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012067781"
FT DOMAIN 33..201
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 385..559
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 864..1031
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1272..1452
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1492..1659
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1685..1865
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1942..2118
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 2249..2322
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2423..2489
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2574..2639
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2718..2806
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT REGION 2816..2855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2879..2940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2827..2850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 766..807
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 775..803
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 809..820
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 866..995
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 888..1030
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 897..992
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 913..920
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1059..1083
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1070..1110
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1088..1090
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1125..1129
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1148..1168
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1152..1164
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1195..1198
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1233..1236
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1267..1453
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1663..1664
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1680..1866
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1873..1898
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1893..1934
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1921..2082
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1944..2079
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1966..2117
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1987..1995
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2718..2768
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2733..2782
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2744..2798
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2748..2800
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 2940 AA; 321996 MW; EF8CD6136FD7DE99 CRC64;
MVPVRLARVL LALALTLPGA LCGEETLGKS SMARCSLFGS NFINTFDQSM YSFAGSCSYL
LAGDCQKHSF SIIGDFQDGK RVGLSVYLGE FFDIHVFVNG TVLQGDQSIS TPYASKGLYL
ESQAGYHTLS SEAYGFVARI DGSGNFQVLL SDRYFNKTCG LCGDFNIFSE DDFKTQEGTL
TSDPYSFANS WALSSGEQHC QRAAPPSISC NISSEMQKGL WEQCQLLKSA SVFARCHPLV
DPEPFVALCE KMLCPCAQGL QCPCPALLEY ARACAQQGML LYGWMDHSLC RPDCPAGMEY
RECVSPCTRT CQSLHINEVC QEQCVDGCSC PEGQLLDDGR CVESAECSCV HSGKRYPPGA
SLSRDCNTCI CRNSLWVCSN EDCPGECLVT GQSHFKSFDN RHFTFSGVCQ YLLARDCQDH
TFSVIIETVQ CADDPDAVCT RSVTVRLPSP HNSLVKLKHG GGVAMDGWDV QIPFLQGDLR
IQHTVMASVH LSYGEDLQID WDGRGRLLVK LSPVYAGRTC GLCGNYNGNQ GDDFLTPAGL
VEPLVEHFGN AWKLHGDCED LRKQPTDPCS LNPRLTRFAE EACAILTSPK FQACHDAVGP
LPYLQNCHYD VCSCSDGRDC LCDAVATYAA ACARRGVHIG WREPGFCALS CPPGQVYLQC
GTPCNLTCRS LSYPDEECAE DCLEGCFCPP GLYLDGSGDC VPKAQCPCYH DGEIFQPEDI
FSDHHTMCYC EDGFMHCSRA GAPGSLQPEV VLSSPLSHRS KRSLSCRPPM VKLVCPADNP
RAEGLECAKT CQNYDLECVS TGCVSGCLCP PGMVRHENRC VALQRCPCFH QGREYAPGET
VKVDCNTCVC RDRKWSCTDH VCDASCSALG LAHYLTFDGL KYLFPGECQY VLVQDYCGSN
PGTFRILLGN EGCGYPSLKC RKRVTILVDG GEIELFDGEV MVKKPLKDET HFEVVESGRF
ITVLLGSGLS VVWDRHLGIS VFLKQTYQEQ VCGLCGNFDG VQNNDLTGSS LQVEEDPVDF
GNSWKVSPQC ADTRKVPLDT SPATCHNNVM KQTMVDSSCR ILTSDIFQDC NKLVDPEPYL
DVCIYDTCSC ESIGDCACFC DTIAAYARVC AQHGKVVTWR TATLCPQNCE ERNLREDGYQ
CEWRYNSCAP ACPVTCQHPE PLACPVSCVE GCHAHCPPGK ILDELLQTCV SPEDCPVCEA
AGRRLAPGKK ITLNPRDPAH CQICHCDGVN LTCEACAEPV PPTEGPVSPT TPYEEDTPEP
PLHDFFCSKL LDLVFLLDGS DKLSEADFEA LKVFVVGMME HLHISQKHIR VAVVEYHDGS
HAYISLQDRK RPSELRRIAS QVKYAGSEVA SISEVLKYTL FQIFGRVDRP EASRIALLLM
ASQEPRRLAQ NLARYLQGLK KKKVTVIPVG IGPHVSLKQI RLIEKQAPEN KAFVVSGVDE
LEQRKNEIIS YLCDLAPEVP APTRRPLVAQ VTVAPELPGV STLEPKKRMV LDVVFVLEGS
DKVGEANFNR STEFVEEVIR RMDVGRDSVH VTVLQYSYVV AVEHSFREAQ SKGEVLQRVR
EIRFQGGNRT NTGLALQYLS EHSFSASQGD REEAPNLVYM VTGNPASDEI KRMPGDIQVV
PIGVGPDVDM QELERLSWPN APIFIQDFET LPREAPDLVL QRCCSGEGPH LPTQAPVPDC
SQPLDVVLLL DGSSSLPASY FDEMKSFTKA FISKANIGPQ LTQVSVLQYG SITTIDLPWN
MPLEKAHLRG LVDLMQREGG PSQIGDALGF AVRYVMSQVH GARPEASKAV VIMVTDTSTD
SVDAAAAAAR SNRVAVFPIG IGDRYDEAQL RTLAGPGASS NVVKLQRIED LPTLVTLGNS
FLHKLCSGFV RVCIDEDGSE RKPGDVWTLP DQCHTVTCLP DGQTLLKSHR VNCDQGLQPS
CPSNQPPIRV EEACGCRWTC PCVCTGSSTR HIVTFDGQNF KLMGNCSYVL FHNKEQDLEV
ILHNGACGAG ARQACMKSIE VKHNGLSVEL HRDMEVVVNG RQVSVPYVGG NMEVGIYGTI
MYEVRFNHLG HILTFTPQNN EFQLQLSPKT FASKMYGLCG ICDENGANDF MLRDGTVTTD
WKTMVQEWAV QQPGQMCQPV PKEQCPVSGG YQCQVLLSAL FAECHKVLAP AAYFAICQQD
SCHQEQVCEA VASYAHLCQT KGVCVDWRTP DFCAVSCPPS LVYNHCEHGC PRHCEGNSSS
CGDHPSEGCF CPPHQVMLGS SCVPEEACTQ CVDDDGIRHQ FLETWVPDHQ PCQICTCLSG
RRVNCTLQPC PTARAPACGL CEVARLRQGA HQCCPEYECV CDLVSCDLPP VPHCEGGLQP
TLTNPGECRP NFTCACRKEE CPRGPLPSCP PHRTPALRKT QCCDEYECAC NCVNTTLSCP
LGYLASTVTN DCGCTTTTCL PDKVCVHRGT VYPVGQFWEE GCDVCTCTDL EDAVMGLRVA
QCAQKPCEDS CRPGFTYVLH EGECCGKCLP SACKVVIGSF RGDSVSYWKS VGSHWASPEN
PCLINECVRV KEEVFVQQRN VSCPMLDVPT CPVGFQLSCK TSGCCPTCRC EPVEACLLNG
TIIGAGESLM IDVCTTCRCM LQEGVVFGFK LECKKTTCEA CPLGYKEEKM PGECCGRCLP
TACTIQLRGG QIMTLKRDET LQDGCDSHFC RVNERGEYIW EKRITGCPPF DQHKCLAAGG
KIMKIPGTCC DTCEEPECKD MTARLQYVKV GNCRSEEEVD IHYCQGKCTS KAVYSIDTED
VEDQCACCSP TRTEPMQVPL RCTNGSTIYH EVLNAIQCKC SPRKCSKYPA APWLPTSAEP
TDGGQRGPGP QTWTAVPQGA GSQSPGPAGQ LPSSFRPATW WRELPQQLCH QQLPGCQRAG
VLGGPSEPHA LPRQPEEGRL RARLPLPETR GAPGPRLPGP LAGHRLQWGD RQGPPRGGSQ
//
