WNT8_DROME
ID WNT8_DROME Reviewed; 309 AA.
AC Q9VFX1;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Wnt inhibitor of Dorsal protein;
DE AltName: Full=Protein Wnt-8;
DE AltName: Full=dWnt-8;
DE Flags: Precursor;
GN Name=wntD; Synonyms=Wnt8; ORFNames=CG8458;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF54924.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP PRELIMINARY PALMITOYLATION.
RX PubMed=12717451; DOI=10.1038/nature01611;
RA Willert K., Brown J.D., Danenberg E., Duncan A.W., Weissman I.L., Reya T.,
RA Yates J.R. III, Nusse R.;
RT "Wnt proteins are lipid-modified and can act as stem cell growth factors.";
RL Nature 423:448-452(2003).
RN [5]
RP LACK OF PALMITOYLATION.
RX PubMed=18430724; DOI=10.1074/jbc.m802059200;
RA Ching W., Hang H.C., Nusse R.;
RT "Lipid-independent secretion of a Drosophila Wnt protein.";
RL J. Biol. Chem. 283:17092-17098(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 31-240, AND DISULFIDE BONDS.
RX PubMed=23791946; DOI=10.1016/j.str.2013.05.006;
RA Chu M.L., Ahn V.E., Choi H.J., Daniels D.L., Nusse R., Weis W.I.;
RT "structural Studies of Wnts and identification of an LRP6 binding site.";
RL Structure 21:1235-1242(2013).
CC -!- FUNCTION: Binds as a ligand to a family of frizzled seven-transmembrane
CC receptors and acts through a cascade of genes on the nucleus.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it is not
CC lipidated. {ECO:0000269|PubMed:18430724}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014297; AAF54924.2; -; Genomic_DNA.
DR EMBL; AY071538; AAL49160.1; -; mRNA.
DR RefSeq; NP_650272.1; NM_142015.2.
DR PDB; 4KRR; X-ray; 2.12 A; A=31-240.
DR PDBsum; 4KRR; -.
DR AlphaFoldDB; Q9VFX1; -.
DR SMR; Q9VFX1; -.
DR BioGRID; 66717; 9.
DR IntAct; Q9VFX1; 2.
DR STRING; 7227.FBpp0082243; -.
DR PaxDb; Q9VFX1; -.
DR DNASU; 41633; -.
DR EnsemblMetazoa; FBtr0082775; FBpp0082243; FBgn0038134.
DR GeneID; 41633; -.
DR KEGG; dme:Dmel_CG8458; -.
DR CTD; 41633; -.
DR FlyBase; FBgn0038134; wntD.
DR VEuPathDB; VectorBase:FBgn0038134; -.
DR eggNOG; KOG3913; Eukaryota.
DR HOGENOM; CLU_901006_0_0_1; -.
DR InParanoid; Q9VFX1; -.
DR OMA; ERRCNCK; -.
DR OrthoDB; 618621at2759; -.
DR PhylomeDB; Q9VFX1; -.
DR Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; Q9VFX1; -.
DR BioGRID-ORCS; 41633; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41633; -.
DR PRO; PR:Q9VFX1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038134; Expressed in mesectoderm and 24 other tissues.
DR Genevisible; Q9VFX1; DM.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IPI:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; IMP:FlyBase.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR026540; WntD.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF81; PTHR12027:SF81; 1.
DR Pfam; PF00110; wnt; 2.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Disulfide bond; Extracellular matrix;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..309
FT /note="Wnt inhibitor of Dorsal protein"
FT /id="PRO_0000041480"
FT DISULFID 51..62
FT /evidence="ECO:0000269|PubMed:23791946,
FT ECO:0007744|PDB:4KRR"
FT DISULFID 102..110
FT /evidence="ECO:0000269|PubMed:23791946,
FT ECO:0007744|PDB:4KRR"
FT DISULFID 112..121
FT /evidence="ECO:0000269|PubMed:23791946,
FT ECO:0007744|PDB:4KRR"
FT DISULFID 162..179
FT /evidence="ECO:0000269|PubMed:23791946,
FT ECO:0007744|PDB:4KRR"
FT DISULFID 164..174
FT /evidence="ECO:0000269|PubMed:23791946,
FT ECO:0007744|PDB:4KRR"
FT DISULFID 232..269
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 248..262
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 266..308
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 284..299
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 286..296
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:4KRR"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4KRR"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:4KRR"
FT HELIX 81..103
FT /evidence="ECO:0007829|PDB:4KRR"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:4KRR"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:4KRR"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:4KRR"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4KRR"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:4KRR"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:4KRR"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4KRR"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4KRR"
SQ SEQUENCE 309 AA; 34777 MW; BA6AC2F3198B4DAD CRC64;
MIFAITFFMG ITSTLAAVLE PMSYYQYTQF QAPLSWEDIT GKGLKQALDS CQQSFQWQRW
NCPSQDFVQK NSKPEENSPN REDVYVAAIS MAAIVHTLTK DCANGVIAGC GCTENALNVP
CAHEPTKALE QYEKHFGSGS GAIGHNRRVV GALLQRSLEQ ECRCKQPGAV QGECQEEECV
AVLKPFEAIA QDLLQMYDDA IQLEGASSNL KIMWQNIPLD SLVFMQDSPN YCERDATGLW
KGTRGRQCSK DGSGSLEERL SCQQLCRVCG YRVRSQHVRT ERRCNCKLVW GFRLQCDVCV
QLERQYSCY
