ID G1QTE2_NOMLE Unreviewed; 2790 AA.
AC G1QTE2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
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:ENSNLEP00000004210.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000004210.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000004210.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000004210.2}
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 EMBL; ADFV01078401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000004210; -.
DR Ensembl; ENSNLET00000004430.2; ENSNLEP00000004210.2; ENSNLEG00000003335.2.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000155810; -.
DR HOGENOM; CLU_000076_5_0_1; -.
DR InParanoid; G1QTE2; -.
DR OMA; KFEACHH; -.
DR TreeFam; TF300299; -.
DR Proteomes; UP000001073; Chromosome 23.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0031589; P:cell-substrate adhesion; IEA:UniProtKB-UniRule.
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:SF361; VON WILLEBRAND FACTOR; 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; 4.
DR SMART; SM00215; VWC_out; 1.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF57603; FnI-like domain; 1.
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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000001073};
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..2790
FT /note="von Willebrand factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014179853"
FT DOMAIN 33..201
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 363..537
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 842..1009
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1254..1430
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1475..1642
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1668..1848
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1925..2101
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 2232..2305
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2406..2472
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2557..2622
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2701..2789
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 744..785
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 753..781
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 787..798
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 844..973
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 866..1008
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 875..970
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 891..898
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1037..1061
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1048..1088
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1066..1068
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1103..1107
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1126..1146
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1130..1142
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1173..1176
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1211..1214
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1249..1435
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1646..1647
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1663..1849
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1856..1881
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1876..1917
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1904..2065
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1927..2062
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1949..2100
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1970..1978
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2701..2751
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2716..2765
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2727..2781
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2731..2783
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 2790 AA; 306330 MW; D099632F0F08E19B CRC64;
MIPARFAGVL LALALILPGT LCAEGTRGRS SMARCSLFGS DFINTFDGSM YSFAGYCSYL
LAGDCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG TVTQGDQRVS MPYASKGLYL
ETEAGYSKLS GETYGFVARI DGSGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFTTQEGTL
TSDPYDFANS WALSSGEQWC ERASPPSSSC NISSGEMQKD LWEQCQLLRA PRCLPAPFVA
LCEKTLCECA GGLECTCPAF LEYARTCAQE GMVLYGWTDH SACSPVCPAG MEYKQCVSPC
ARTCQSLHIN EVCQERCVDG CSCPEGQLLD EGLCVESTEC PCMHSGKRYP PGTCPGDWGG
KLGECLVTGQ SHFKSFDNRY FTFSGICQYL LARDCQDHSF SIVIETVQCA DDPDAVCTRS
VTIRLPGLHN SLVKLKHGGG VAMDGQDVQL PLLKGDLRIQ HTVTASVHLS HGEDLQLDWD
GRGRLLVKLS PVYAGKTCGL CGNYNGNQGD DFITPSGLAE PRVEDFGNAW KLHGNCQDLQ
KQHSDPCALN PRMTRFSEEA CAVLTSPTFE ACHRAVSPLP YLRNCRYDVC SCSDGRECLC
GALASYAAAC AGRGVRVAWR QPDRCELNCP KGQVYLQCGT PCNLTCRSLS YPDEECNEAC
LEGCFCPPGL YMDERGDCVP KAQCPCYYDG EIFQPEDIFS DHHTMCYCED GFMHCTMSGV
PGSLLPDAVL SSPLSHRSKR SLSCRPPMVK LVCPADNPRA EGLECAKTCQ NYDLECMSMG
CVSGCLCPPG MVRHENRCVA LERCPCFHQG KEYAPGETVK IGCNTCVCRD RKWNCTDHVC
DATCSTIGMA HYLTFDGLKY MFPGECQYVL VQDYCGSNPG TFRVLVGNEG CSHPSVKCKK
RVTILVEGGE IELFDGEANV KRPMKDETHF EVVESGRYII LLLGKALSVV WDRHLSISVV
LKQTYQEKVC GLCGNFDGIQ NNDLTSSNLQ VEEDPVDFGN SWKVSSQCAD TRKVPLDSSP
ATCHNNIMKQ TMVDSSCRIL TSDVFQDCNK LVDPEPYLDV CIYDTCSCES IGDCACFCDT
IAAYAHVCAQ HGKVVTWRTA TLCPQSCEER NLRENGYECE WRYNSCAPAC RVTCQHPEPL
ACPVQCVEGC HAHCPPGKIL DELLQTCVSP EDCPVCEVAG RRFAPGKKVT LNPSDPEHCQ
ICHCDGVNLT CEACQEPGGL VVPPTDAPVS PTTPYVEDTW EPPLHDFYCS RLLDLVFLLD
GSSRLSEAEF EVLKAFVVDM MERLRISQKW VRVAVVEYHD GSHAYIGLKD RKRPSELRRI
ASQVKYAGSQ VASTSEVLKY TLFQIFGKID RPEASRIALL LMASQEPQRM SRNFVRYVQG
LKKKKVIVIP VGIGPHANLK QIRLVEKQAP ENKAFVLSGV DELEQQRDEI VSYLCDLAPE
APPPTLPPNM AQVTVGPGLL GVSTLGPKRN SMVLDVAFVL EGSDKIGEAD FNRSKEFMEE
VIQRMDVGQD SIHVTVLQYS YMVTVEYPFS EAQSKGDILQ RVREIRYQGG NRTNTGLALQ
YLSDHSFLVS QGDREQAPNL VYMVTGNPAS DEIKRLPGDI QVVPIGVGPN ANVQELERIG
WPNAPILIQD FETLPREAPD LVLQRCCSGE GLQIPTLSPA SDCSQPLDVI FLLDGSSSFP
ASYFDEMKSF AKAFISKANI GPHLTQVSVL QYGSITTIDV PWNVAPEKAH LLSLVDVMQR
EGGPSQIGDA LGFAVRYLTS EMHGARPGAS KAVVILVTDV SVDSVDAAAD AARSNRVTVF
PIGIGDRYDA AQLRILAGPA GDSNMVKLQR IEDLPTMVTL GNSFLHKLCS GFVRICMDED
GNEKRPGDVW TLPDQCHTVT CQPDGQTLLK SHRVNCDRGP RPSCPNSQSP VKVEETCGCR
WTCPCVCTGS STRHIVTFDG QNFKLTGSCS YVLFQNKEQD LEVILHNGAC SPGARQGCMK
SIEVKHSALS VELHSDMEVT VNGRLVSVPY VGGNMEVNVY GTIMHEVRFN HLGHIFTFTP
QNNEFQLQLS PKTFASKTYG LCGICDENGA NDFMLRDGTV TTDWKTLVQE WTVQQPGHTC
HPIPEEQCLV PDSSHCQILL LPLFAECHKV LAPATFYAIC QQDSCHQEQV CGVIASYAHL
CRTNGVCVDW RTPDFCAMSC PPSLVYNHCE HGCPRHCDGN VSSCGDHPSE GCFCPPNKVM
LEGSCVPEEA CTQCIGEDGV QHQFLEAWVP DHQPCQICTC LSGRKVNCTT QPCPTAKAPT
CGLCEVARLR QNADQCCPEY ECVCDPVSCD LPPVPHCEGG LQPTLTNPGE CRPNFTCACR
KEECERVSPP SCPPHRLPTL RKTQCCDEYE CACNCVNSTV SCPLGYLAST ATNDCGCTTT
TCLPDKVCVH RSTIYPVGQF WEEGCDVCTC TDMEDAVMGL RVAQCSQKPC EDSCRSGFTY
VLHEGECCGR CLPSACEVVT GSPRGDSQSF WKSVGSQWAS PENPCLINEC VRVKEEVFVQ
QRNVSCPQLE VPACPSGFQL SCKTSVCCPS CRCERVEACM LNGTIIGPGK SVMIDVCTTC
RCMVQVGVIS GFKLECRKTT CNPCPLGYKE ENNTGECCGR CLPTACTIQL RGGQIMTLKR
DETLQDGCDT HFCKVNERGE YFWEKRVTGC PPFDEHKCLA EGGKIMKIPG TCCDTCEEPE
CNDITARLQY VKVGSCKSEV EVDIHYCQGK CASKAMYSID INDVQDQCSC CSPTRTEPMQ
VPLHCTNGSV VYHEVLNAME CKCSPRKCSK
//
