ID F6W3M9_CALJA Unreviewed; 2908 AA.
AC F6W3M9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 77.
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:ENSCJAP00000001123.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001123.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000001123.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000001123.4}
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 Ensembl; ENSCJAT00000001193.4; ENSCJAP00000001123.4; ENSCJAG00000000613.6.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000155810; -.
DR HOGENOM; CLU_000076_5_0_1; -.
DR OMA; KFEACHH; -.
DR TreeFam; TF300299; -.
DR Proteomes; UP000008225; Chromosome 9.
DR Bgee; ENSCJAG00000000613; Expressed in heart and 6 other cell types or tissues.
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; 5.
DR SMART; SM00215; VWC_out; 2.
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:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002495}.
FT DOMAIN 128..296
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 481..655
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 960..1127
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1372..1548
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1593..1760
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1786..1966
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2043..2219
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 2350..2423
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2524..2590
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2675..2740
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 2819..2907
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 862..903
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 871..899
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 905..916
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 962..1091
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 984..1126
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 993..1088
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1009..1016
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1155..1179
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1166..1206
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1184..1186
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1221..1225
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1244..1264
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1248..1260
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1291..1294
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1329..1332
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1367..1553
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1764..1765
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1781..1967
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1974..1999
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 1994..2035
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2022..2183
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2045..2180
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2067..2218
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2088..2096
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50"
FT DISULFID 2819..2869
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2834..2883
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2845..2899
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
FT DISULFID 2849..2901
FT /evidence="ECO:0000256|PIRSR:PIRSR002495-50,
FT ECO:0000256|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 2908 AA; 319671 MW; DF6E2B4FB495D7FE CRC64;
MEGRVFHLSW CWDCCLCKGS HRSQHTAIVI LGPGTGHELL GGQKAMFKGE EGVTEINLFF
CFEEMFLLLH ALTVASPAAS YLGNTDQLTF LASLQMIPAR FARVLLALAL TLPGILCAEG
TRGRSSMARC SLFGSDVINT FDGSMYSFAG YCSYLLAGDC QKHSFSIIGD FQNGKRVSLS
VYLGEFFDIH LFVNGTVTQG DQRVSMPYAS KGLYLETEAG YYKLSGEAYG FVARIDGSGN
FQVLLSDRYF NKTCGLCGNL NIFAEDDFMT QEGTLTSDPY DFANSWALSS GEQWCERASP
PSGSCNISSG EMQKGLWEQC QLLKSTSVFA RCHPLVDPEP FVALCEKTLC ECTEGLECVC
PTFLEYARTC AQEGMVLYGW TNHGACSPVC PAGMEYKQCV PPCTRTCQSL HINEVCQQQC
VDGCSCPEGQ LLDEGLCVES TKCPCMHSGK RYPPGTNLSQ DCNTCICRNS QWVCSNEDCP
GECLVTGQSH FKSFDNKYFT FSGICQYLLA RDCQDHSFSI VIETVQCADD PDAVCTRSVT
IRLPGLHNSL VKLKHGGGVA MDGQDVQLPL LKGDLRIQHT VTTSVHVSYG EDLQMDWDGR
GRLLVKLSPV YSGKTCGLCG NYNGNQGDDF LTPSGLAEPR VEDFGNAWKL HGDCQDLQKQ
HSDPCALNPR MTRFAEEACA VLTSPTFEAC HRAVSPLPYL RNCRYDVCSC SDGRECLCGA
LASYAAACAG RGVRIAWREP GRCELNCPKG QVYLQCGTPC NLTCRSLSYP DEECSEDCLE
GCFCPPGLYM DEMGNCVPKA QCPCYYDGEI FQPEDIFSDH HTVCYCEGGF MHCTMSEVPG
SLLPDAVLSS PLSHRSKRSL SCRPPMVKLV CPADNPRAEG LECAKTCQNY DLECMSMGCV
SGCLCPPGMV RHENRCVALE RCPCFHQGQE YAPGETVKID CNTCVCRDRK WNCTDHMCDA
TCSTIGMAHY LTFDGLKYMF PGECQYVLVQ DYCDSNPGTF RILVGNEGCS YPSVKCKKRV
TILVEGGEIE LFDGEVNVQR PMKDETHFEV VESGRYIILL LGKALSVVWD RHLSISVVLK
QTYQEQVCGL CGNFDGIQNN DLTSSNLQVE EDAVNFGNSW KVSSQCADTR RVPLDSSPAT
CRNNIMKQTM VDSSCRILTS DVFQDCNKLV DPEPYLDACI YDTCSCESIG DCTCFCDTVA
AYAHMCAQHG KVVTWRTTTL CPQSCEERNL RESGYECEWR YNSCAPACRI TCQHPEPLAC
PVQCVEGCHA HCPPGKILDE LLQTCVNPED CPVCEVAGRR LASGKKVTLN PSDPEHCQIC
HCDGVNLTCE ACQEPEGLVM PPTDAPVSPT TPYVEDVSEA PLHDFYCSKL LDLVFLLDGS
SRLSEAEFEV LKAFVVDMME RLRISQKWVR VAVVEYHDGS HAYIGLKDRK RPSELRRIAS
QVKYAGSQVA STSEVLKYTL FQIFGKIDRP EASRIILLLM ASQEPQRMSR NFVRYVQGLK
KKKVIVIPVG IGPHANLKQI RLIEKQAPEN KAFVLSGVDE LEQQRDEIVS YLCDLAPEAP
PPTMPPHMAQ VTVGPGLLGV SPLGPKRKSM VLDVAFVLEG SDKIGEADFN RTKEFMAEVI
QRMDVGQDGI HVTVLQYSYM VTVEYPFSEA QTKGDILQRV RDIRYQGGNR TNTGLALQHL
SEHSFLVSQG DREQAPNLVY MVTGNPASDE IKRLPGDIQV VPIGVGPHAN VQELETIGWP
NAPILIQDFE TLPREAPDLV LQRCCSGEGL QMPKLAPDPD CSQPLDVVLL LDGSSSSPAS
YFDEMKSFAK AFISKAKLGP HLTQVSVLQY GSITTIDVPW NAAMEKAHLL SLVDVMQREG
GPSQIGNALD FAVRYLTSEV HGARPGASKA VVILVTDVSV DSVGAAADAA RANRVTVFPI
GIGDRYDAAQ LRTLAGPAAD SNVVSLQRIE DLPTMVTLGN SFLHKLCSGF VRICMDEDGN
EKRPGDVWTL PDQCHTVTCQ PDGQTLLKSH RVNCDRGPRP SCPNSQSPLK VEETCGCRWT
CPCVCTGSST RHIVTFDGQN FKLTGSCSYV LFQNKEQDLE VILHNGACSP GARQGCMKSI
EVKHSALSVE LHSDMEVTVN GRLVSVPYVA GNVEVSIYGA IMHEVRFNHL GHIFTFTPQN
NEFQLQLSPK TFASKTYGLC GICDENGAND FMLRDGTVTT DWKTLVQEWT VQQSGQTCQP
ILEEQCLVSD SSQCQVLLST LFAECHKVLA PATFYAICQQ DSCHREQVCE VISSYAHLCR
SSGVCVDWRT PDFCAMSCPS SLVYNHCERG CPRHCDGNVS SCGDHPSEGC FCPPNQVMLE
GSCVPKEACT QCIGEDGVRH QFLEAWVPDH QPCQICTCLS GRKVNCTTQP CPTAKAPTCG
LCEVAHLRQN ADQCCPEYEC VCDPVSCDLP AVPHCEDGLQ PMLTNPGECR PNFTCACRKE
ECERVSPPSC PPHRFLTLRK TQCCDEYECA CNCVNSTVSC PLGYLASTAT NDCGCTTTTC
LPDKVCVHRG TIYPVGQFWE EGCDVCTCTD MEDAVMGLRV AQCSQKPCED SCRSGFTYVL
HEGECCGRCL PSACEVVTGS RRGDSQSSWK SVGSRWASLE NPCLINECVR VKEEVFVQQR
NVSCPQLEVP FCPPGFQLSC KTSECCPRCR CEPMEACMLN GTIIGPGKSV MVDVCTACHC
IVEAGAASGF QLECRKTTCK PCPLGYKEEN NPGECCGRCL PTACTIRLRG GQIMTLKRDE
MLQDGCDSHS CKVNEIGEYI WEKRVASCPP FDEHECLAEG GKIMKTPGTC CNRCEVPECK
DITARLQYVK VGSCKSEVEV DIHYCQGKCA SKAIYSIDIE DVQDQCSCCS PTRTEPMRVP
LHCTNGSVVY HEILNAMQCK CSPRKCSK
//
