WNT4_DROME
ID WNT4_DROME Reviewed; 539 AA.
AC P40589; Q8MPQ1; Q8SWU3; Q9VM29;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein Wnt-4;
DE AltName: Full=dWnt-4;
DE Flags: Precursor;
GN Name=Wnt4; Synonyms=Wnt-4; ORFNames=CG4698;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE, SEQUENCE REVISION TO 171, AND FUNCTION.
RX PubMed=11970894; DOI=10.1016/s1534-5807(02)00142-9;
RA Cohen E.D., Mariol M.-C., Wallace R.M.H., Weyers J., Kamberov Y.G.,
RA Pradel J., Wilder E.L.;
RT "DWnt4 regulates cell movement and focal adhesion kinase during Drosophila
RT ovarian morphogenesis.";
RL Dev. Cell 2:437-448(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 151-539.
RX PubMed=7867502; DOI=10.1242/dev.121.1.209;
RA Graba Y., Gieseler K., Aragnol D., Laurenti P., Mariol M.-C., Berenger H.,
RA Sagnier T., Pradel J.;
RT "DWnt-4, a novel Drosophila Wnt gene acts downstream of homeotic complex
RT genes in the visceral mesoderm.";
RL Development 121:209-218(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
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. Acts
CC downstream of homeotic complex genes in the visceral mesoderm and is
CC required for embryonic segmentation. Also required for cell movement
CC and FAK regulation during ovarian morphogenesis.
CC {ECO:0000269|PubMed:11970894}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: Palmitoleoylated by porcupine. The lipid group functions as a
CC sorting signal, targeting the ligand to polarized vesicles that
CC transport Wnt4 to unique sites at the cell surface. Depalmitoleoylated
CC by notum, leading to inhibit Wnt signaling pathway.
CC {ECO:0000250|UniProtKB:P09615}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; AF533773; AAN04479.1; -; mRNA.
DR EMBL; AE014134; AAF52499.2; -; Genomic_DNA.
DR EMBL; AY095078; AAM11406.1; -; mRNA.
DR RefSeq; NP_001260187.1; NM_001273258.2.
DR RefSeq; NP_476972.2; NM_057624.4.
DR AlphaFoldDB; P40589; -.
DR SMR; P40589; -.
DR BioGRID; 60153; 13.
DR IntAct; P40589; 3.
DR MINT; P40589; -.
DR STRING; 7227.FBpp0088345; -.
DR GlyGen; P40589; 3 sites.
DR PaxDb; P40589; -.
DR DNASU; 34007; -.
DR EnsemblMetazoa; FBtr0089291; FBpp0088345; FBgn0010453.
DR EnsemblMetazoa; FBtr0334799; FBpp0306845; FBgn0010453.
DR GeneID; 34007; -.
DR KEGG; dme:Dmel_CG4698; -.
DR CTD; 54361; -.
DR FlyBase; FBgn0010453; Wnt4.
DR VEuPathDB; VectorBase:FBgn0010453; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000157480; -.
DR HOGENOM; CLU_505559_0_0_1; -.
DR InParanoid; P40589; -.
DR OMA; QGLYNEH; -.
DR OrthoDB; 624528at2759; -.
DR PhylomeDB; P40589; -.
DR Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-4086400; PCP/CE pathway.
DR SignaLink; P40589; -.
DR BioGRID-ORCS; 34007; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34007; -.
DR PRO; PR:P40589; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010453; Expressed in embryonic optic lobe primordium and 79 other tissues.
DR ExpressionAtlas; P40589; baseline and differential.
DR Genevisible; P40589; DM.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; ISS: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:0005102; F:signaling receptor binding; ISS: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:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IGI:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; 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:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:FlyBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..539
FT /note="Protein Wnt-4"
FT /id="PRO_0000041478"
FT REGION 34..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 403
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 274..285
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 322..330
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 332..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 397..411
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 399..406
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 478..497
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 486..492
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 496..538
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 512..529
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 514..526
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 521..522
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 18
FT /note="F -> L (in Ref. 1; AAN04479)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> R (in Ref. 1; AAN04479)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="F -> L (in Ref. 5; AAM11406)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="R -> A (in Ref. 1; AAN04479)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="L -> V (in Ref. 1; AAN04479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58685 MW; 6682C8B3D729D067 CRC64;
MPSPTGVFVL MILTHLSFGL GQVRNEDQLL MVGQNGDLDS SNPAIHHQQH QQHQQHQQHQ
QHQSNHNLNN GNMNSTILNT LMGNNAGQVV NSSPGGGGSM INQLGSSTSS VPSVIGGGVG
SVGNPWHSAV GLGVPGNGMG LPSSHGLGGN MGSHPHGHAL AGLAKLGIIV PGGQGLPGNL
GYGGTMLNGG GVGGAAGMGL GIGSNTNNMD MQQGLYNEHF ISEHTVMAVF TSQGQVGGPC
RYMPATRRQN HQCRKETGLP GTLSEARRLA TTHCEEQFRY DRWNCSIETR GKRNIFKKLY
KETAFVHALT AAAMTHSIAR ACAEGRMTKC SCGPKKHNRE AQDFQWGGCN DNLKHGKRVT
RSFLDLRGGD GDEVSEILRH DSEVGIEAVS SQMMDKCKCH GVSGSCSMKT CWKKMADFNA
TATLLRQKYN EAIRKAPNQR SMRQVSSSRM KKPKQRRKKP QQSQYTTLYY LETSPSYCAV
TKDRQCLHPD NCGTLCCGRG YTTQVVKQVE KCRCRFNNGR CCQLICDYCQ RLENKYFCK
