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   27-MAR-2024, entry version 160.
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}.
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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; 7227-FBpp0082243; -.
DR   DNASU; 41633; -.
DR   EnsemblMetazoa; FBtr0082775; FBpp0082243; FBgn0038134.
DR   GeneID; 41633; -.
DR   KEGG; dme:Dmel_CG8458; -.
DR   AGR; FB:FBgn0038134; -.
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; 2874082at2759; -.
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 cell types or tissues.
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   CDD; cd19340; Wnt_Wnt8; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR043158; Wnt_C.
DR   PANTHER; PTHR12027:SF112; PROTEIN WNT-2-RELATED; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   Genevisible; Q9VFX1; DM.
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
//