WNT5_DROME
ID WNT5_DROME Reviewed; 1004 AA.
AC P28466; Q01535; Q9VWT4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein Wnt-5;
DE AltName: Full=dWnt-3;
DE AltName: Full=dWnt-5;
DE Flags: Precursor;
GN Name=Wnt5; Synonyms=Wnt-3, WNT-5; ORFNames=CG6407;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=1425336; DOI=10.1242/dev.115.2.475;
RA Russell J., Gennissen A., Nusse R.;
RT "Isolation and expression of two novel Wnt/wingless gene homologues in
RT Drosophila.";
RL Development 115:475-485(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=1358729; DOI=10.1016/0012-1606(92)90049-m;
RA Eisenberg L.M., Ingham P.W., Brown A.M.C.;
RT "Cloning and characterization of a novel Drosophila Wnt gene, Dwnt-5, a
RT putative downstream target of the homeobox gene distal-less.";
RL Dev. Biol. 154:73-83(1992).
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;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION BY PORCUPINE, AND INTERACTION WITH PORCUPINE.
RX PubMed=11821428; DOI=10.1074/jbc.m200187200;
RA Tanaka K., Kitagawa Y., Kadowaki T.;
RT "Drosophila segment polarity gene product porcupine stimulates the
RT posttranslational N-glycosylation of wingless in the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 277:12816-12823(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. Probable
CC developmental protein. May be a signaling molecule which affects the
CC development of discrete regions of tissues. Is likely to signal over
CC only few cell diameters. May have a role in limb and CNS development;
CC may be a downstream target of Dll that acts in the specification of
CC these primordia. {ECO:0000269|PubMed:1358729,
CC ECO:0000269|PubMed:1425336}.
CC -!- SUBUNIT: Interacts with porcupine (por). {ECO:0000269|PubMed:11821428}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Dynamic expression pattern during embryogenesis.
CC Expression is seen in the limb primordia of the head and thoracic
CC segments, mesodermal and neurogenic regions.
CC {ECO:0000269|PubMed:1358729, ECO:0000269|PubMed:1425336}.
CC -!- PTM: Glycosylated, glycosylation is stimulated by porcupine at the ER.
CC {ECO:0000269|PubMed:11821428}.
CC -!- PTM: Palmitoleoylated by porcupine. The lipid group functions as a
CC sorting signal, targeting the ligand to polarized vesicles that
CC transport Wnt5 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; X64736; CAA46002.1; -; mRNA.
DR EMBL; M97450; AAA29020.1; -; mRNA.
DR EMBL; AE014298; AAF48853.1; -; Genomic_DNA.
DR EMBL; BT010268; AAQ23586.1; -; mRNA.
DR PIR; A48821; A48821.
DR RefSeq; NP_001285407.1; NM_001298478.1.
DR RefSeq; NP_476924.1; NM_057576.5.
DR AlphaFoldDB; P28466; -.
DR BioGRID; 59151; 17.
DR DIP; DIP-22455N; -.
DR IntAct; P28466; 5.
DR MINT; P28466; -.
DR STRING; 7227.FBpp0074394; -.
DR GlyGen; P28466; 13 sites.
DR PaxDb; P28466; -.
DR DNASU; 32838; -.
DR EnsemblMetazoa; FBtr0074623; FBpp0074394; FBgn0010194.
DR EnsemblMetazoa; FBtr0343046; FBpp0309792; FBgn0010194.
DR GeneID; 32838; -.
DR KEGG; dme:Dmel_CG6407; -.
DR CTD; 32838; -.
DR FlyBase; FBgn0010194; Wnt5.
DR VEuPathDB; VectorBase:FBgn0010194; -.
DR eggNOG; KOG3913; Eukaryota.
DR HOGENOM; CLU_303411_0_0_1; -.
DR InParanoid; P28466; -.
DR OMA; RFEPIIQ; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; P28466; -.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
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 Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P28466; -.
DR BioGRID-ORCS; 32838; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32838; -.
DR PRO; PR:P28466; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010194; Expressed in antennal lobe (Drosophila) and 29 other tissues.
DR ExpressionAtlas; P28466; baseline and differential.
DR Genevisible; P28466; DM.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IMP:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP: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:0061643; P:chemorepulsion of axon; IMP:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0016204; P:determination of muscle attachment site; IMP:FlyBase.
DR GO; GO:0050919; P:negative chemotaxis; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:FlyBase.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; 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; 2.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1004
FT /note="Protein Wnt-5"
FT /id="PRO_0000041479"
FT REGION 238..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 868
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 583..594
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 633..641
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 643..661
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 862..876
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 864..871
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 933..964
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 949..959
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 963..1003
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 979..994
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 981..991
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 986..987
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 282
FT /note="G -> GGGG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="D -> E (in Ref. 1; CAA46002)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="S -> SSSS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="S -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 112459 MW; 4E2BB4DC7165CAA5 CRC64;
MSCYRKRHFL LWLLRAVCML HLTARGAYAT VGLQGVPTWI YLGLKSPFIE FGNQVEQLAN
SSIPLNMTKD EQANMHQEGL RKLGTFIKPV DLRDSETGFV KADLTKRLVF DRPNNITSRP
IHPIQEEMDQ KQIILLDEDT DENGLPASLT DEDRKFIVPM ALKNISPDPR WAATTPSPSA
LQPNAKAIST IVPSPLAQVE GDPTSNIDDL KKHILFLHNM TKTNSNFESK FVKFPSLQKD
KAKTSGAGGS PPNPKRPQRP IHQYSAPIAP PTPKVPAPDG GGVGGAAYNP GEQPIGGYYQ
NEELANNQSL LKPTDTDSHP AAGGSSHGQK NPSEPQVILL NETLSTETSI EADRSPSINQ
PKAGSPARTT KRPPCLRNPE SPKCIRQRRR EEQQRQRERD EWFRGQSQYM QPRFEPIIQT
INNTKRFAVS IEIPDSFKVS SEGSDGELLS RVERSQPSIS SSSSSSSSSS RKIMPDYIKV
SMENNTSVTD YFKHDVVMTS ADVASDREFL IKNMEEHGGA GSANSHHNDT TPTADAYSET
IDLNPNNCYS AIGLSNSQKK QCVKHTSVMP AISRGARAAI QECQFQFKNR RWNCSTTNDE
TVFGPMTSLA APEMAFIHAL AAATVTSFIA RACRDGQLAS CSCSRGSRPK QLHDDWKWGG
CGDNLEFAYK FATDFIDSRE KETNRETRGV KRKREEINKN RMHSDDTNAF NIGIKRNKNV
DAKNDTSLVV RNVRKSTEAE NSHILNENFD QHLLELEQRI TKEILTSKID EEEMIKLQEK
IKQEIVNTKF FKGEQQPRKK KRKNQRAAAD APAYPRNGIK ESYKDGGILP RSTATVKARS
LMNLHNNEAG RRAVIKKARI TCKCHGVSGS CSLITCWQQL SSIREIGDYL REKYEGATKV
KINKRGRLQI KDLQFKVPTA HDLIYLDESP DWCRNSYALH WPGTHGRVCH KNSSGLESCA
ILCCGRGYNT KNIIVNERCN CKFHWCCQVK CEVCTKVLEE HTCK
