DLISH_DROME
ID DLISH_DROME Reviewed; 355 AA.
AC A1ZAY1;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=SH3 domain-containing protein Dlish {ECO:0000305};
DE AltName: Full=Dachs ligand with SH3 domains {ECO:0000303|PubMed:27692068};
GN Name=Dlish {ECO:0000303|PubMed:27692068};
GN ORFNames=CG10933 {ECO:0000312|FlyBase:FBgn0034264};
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|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|EMBL:ACX47665.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACX47665.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH APP; CUL1; DACHS; DCO; FBXL7; FT AND SLMB,
RP SUBCELLULAR LOCATION, PALMITOYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27692068; DOI=10.7554/elife.16624;
RA Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
RT "The novel SH3 domain protein Dlish/CG10933 mediates fat signaling in
RT Drosophila by binding and regulating Dachs.";
RL Elife 5:E16624-E16624(2016).
RN [5]
RP ERRATUM OF PUBMED:27692068.
RX PubMed=27824307; DOI=10.7554/elife.22672;
RA Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
RL Elife 5:E22672-E22672(2016).
CC -!- FUNCTION: Required for the apical cell cortex localization, total
CC cellular level and full activity of dachs.
CC {ECO:0000269|PubMed:27692068}.
CC -!- SUBUNIT: Interacts with dachs (via C-terminus); the interaction is
CC direct. Interacts (via N-terminus including SH3 domain 1) with
CC palmitoyltransferase app; this leads to palmitoylation of Dlish by app.
CC Also interacts with dco, ft, ft-regulated E3 ubiquitin ligase Fbxl7, F-
CC box protein slmb and SCF E3 ubiquitin-protein ligase complex component
CC Cul1. {ECO:0000269|PubMed:27692068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27692068}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:27692068}. Note=Low levels
CC are found diffusely in the cytoplasm with high levels concentrated at
CC the subapical cell cortex. {ECO:0000269|PubMed:27692068}.
CC -!- PTM: Palmitoylated by app. {ECO:0000269|PubMed:27692068}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC spacing between the anterior and posterior crossveins of the wing,
CC reduced levels of subapical cortical dachs, increased levels of dachs
CC throughout the cytoplasm, increased total cellular levels of dachs and
CC suppression of the overgrowth and dachs up-regulation seen in ft
CC mutants. {ECO:0000269|PubMed:27692068}.
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DR EMBL; AE013599; AAF57808.2; -; Genomic_DNA.
DR EMBL; BT099964; ACX47665.1; -; mRNA.
DR RefSeq; NP_611251.2; NM_137407.3.
DR AlphaFoldDB; A1ZAY1; -.
DR SMR; A1ZAY1; -.
DR IntAct; A1ZAY1; 1.
DR STRING; 7227.FBpp0086020; -.
DR SwissPalm; A1ZAY1; -.
DR PaxDb; A1ZAY1; -.
DR DNASU; 37014; -.
DR EnsemblMetazoa; FBtr0086860; FBpp0086020; FBgn0034264.
DR GeneID; 37014; -.
DR KEGG; dme:Dmel_CG10933; -.
DR UCSC; CG10933-RA; d. melanogaster.
DR CTD; 37014; -.
DR FlyBase; FBgn0034264; Dlish.
DR VEuPathDB; VectorBase:FBgn0034264; -.
DR eggNOG; ENOG502QPX9; Eukaryota.
DR GeneTree; ENSGT00940000171466; -.
DR HOGENOM; CLU_039664_1_0_1; -.
DR InParanoid; A1ZAY1; -.
DR OMA; HHANLTG; -.
DR OrthoDB; 1518001at2759; -.
DR PhylomeDB; A1ZAY1; -.
DR SignaLink; A1ZAY1; -.
DR BioGRID-ORCS; 37014; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37014; -.
DR PRO; PR:A1ZAY1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034264; Expressed in eye disc (Drosophila) and 11 other tissues.
DR ExpressionAtlas; A1ZAY1; baseline and differential.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0120219; C:subapical part of cell; IDA:FlyBase.
DR GO; GO:0045296; F:cadherin binding; IPI:FlyBase.
DR GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:FlyBase.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR InterPro; IPR039687; NPHP1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15176:SF1; PTHR15176:SF1; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipoprotein; Palmitate; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..355
FT /note="SH3 domain-containing protein Dlish"
FT /id="PRO_0000438853"
FT DOMAIN 57..117
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 183..243
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 287..352
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 355 AA; 40131 MW; C500D56CD93F467B CRC64;
MAFLCPVRMR RDKKKATNAS IERDLPAVGV LGMGRITGSS SIETLVRVGI EKEHGLSPDS
KMVVLHDFTP CVDDELEVKR GQLVNILYRE NDWVYVIGQD SRQEGFIPFS YCAPCNTQLA
DLAVKKKLPR EQCPEQPIEE NIPLLGTDNK LDVLCDETLN PGSANSIENT LLVEPECTPF
VKEPSGRCIV LYTFIARDEN DLSVERGEFV TVLNREDPDW FWIMRSDGQE GFVPASFIYP
ADSVRVLQQQ KATLNAMETI LQQGQQGQQS QQQQQPQLGL GTDDLRYHGT ELVMLYDYKA
QAPDDLYLSV RRGDWIYADL TNQTVDGWLW AYAPKTRKYG FIPKAYARPP AMTSL
