1433E_DROME
ID 1433E_DROME Reviewed; 262 AA.
AC P92177; Q8IN86; Q8IN87; Q9VEA8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=14-3-3 protein epsilon;
DE AltName: Full=Suppressor of Ras1 3-9;
GN Name=14-3-3epsilon; Synonyms=14-3-3e, SR3-9; ORFNames=CG31196;
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 [GENOMIC DNA / MRNA] (ISOFORM D), AND MUTAGENESIS OF
RP GLU-183; PHE-199 AND TYR-214.
RX PubMed=9159394; DOI=10.1101/gad.11.9.1132;
RA Chang H.C., Rubin G.M.;
RT "14-3-3 epsilon positively regulates Ras-mediated signaling in
RT Drosophila.";
RL Genes Dev. 11:1132-1139(1997).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP INTERACTION WITH YKI.
RX PubMed=18256197; DOI=10.1242/dev.015255;
RA Oh H., Irvine K.D.;
RT "In vivo regulation of Yorkie phosphorylation and localization.";
RL Development 135:1081-1088(2008).
RN [6]
RP FUNCTION, AND INTERACTION WITH YKI.
RX PubMed=19900439; DOI=10.1016/j.ydbio.2009.10.046;
RA Ren F., Zhang L., Jiang J.;
RT "Hippo signaling regulates Yorkie nuclear localization and activity through
RT 14-3-3 dependent and independent mechanisms.";
RL Dev. Biol. 337:303-312(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH PAV AND MICROTUBULES.
RX PubMed=32022690; DOI=10.7554/elife.52009;
RA Norkett R., Del Castillo U., Lu W., Gelfand V.I.;
RT "Ser/Thr kinase Trc controls neurite outgrowth in Drosophila by modulating
RT microtubule-microtubule sliding.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Positively regulates Ras-mediated pathways. Acts downstream
CC or parallel to Raf, but upstream of nuclear factors in Ras signaling.
CC Three mutants have been isolated, that suppress the rough eye phenotype
CC caused by mutated Ras1 (sev-Ras1 v12). Inhibits yki activity by
CC restricting its nuclear localization. Together with pav, has a role in
CC the inhibition of microtubule sliding during neurite outgrowth
CC (PubMed:32022690). {ECO:0000269|PubMed:19900439,
CC ECO:0000269|PubMed:32022690}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with phosphorylated yki
CC (PubMed:18256197, PubMed:19900439). Interacts with pav (when serine
CC phosphorylated); the interaction is necessary for association of the
CC complex pav-14-3-3epsilon complex to the microtubules, thereby
CC inhibiting microtubule sliding (PubMed:32022690).
CC {ECO:0000250|UniProtKB:P29310, ECO:0000269|PubMed:18256197,
CC ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:32022690}.
CC -!- INTERACTION:
CC P92177; Q9VX75: baz; NbExp=5; IntAct=EBI-204478, EBI-2295779;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist.;
CC Name=A;
CC IsoId=P92177-3; Sequence=Displayed;
CC Name=B;
CC IsoId=P92177-2; Sequence=VSP_008203;
CC Name=C;
CC IsoId=P92177-4; Sequence=VSP_026086;
CC Name=D;
CC IsoId=P92177-1; Sequence=VSP_008204;
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; U84898; AAC47520.1; -; Genomic_DNA.
DR EMBL; U84897; AAC47519.1; -; mRNA.
DR EMBL; AE014297; AAF55519.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13764.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13765.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13766.1; -; Genomic_DNA.
DR RefSeq; NP_732309.1; NM_169796.2. [P92177-3]
DR RefSeq; NP_732310.1; NM_169797.3. [P92177-2]
DR RefSeq; NP_732311.1; NM_169798.3. [P92177-1]
DR RefSeq; NP_732312.1; NM_169799.2. [P92177-4]
DR AlphaFoldDB; P92177; -.
DR SMR; P92177; -.
DR BioGRID; 67207; 61.
DR DIP; DIP-18498N; -.
DR IntAct; P92177; 235.
DR MINT; P92177; -.
DR STRING; 7227.FBpp0082987; -.
DR iPTMnet; P92177; -.
DR PaxDb; P92177; -.
DR PRIDE; P92177; -.
DR DNASU; 42186; -.
DR EnsemblMetazoa; FBtr0083565; FBpp0082987; FBgn0020238. [P92177-3]
DR EnsemblMetazoa; FBtr0083566; FBpp0082988; FBgn0020238. [P92177-2]
DR EnsemblMetazoa; FBtr0083567; FBpp0082989; FBgn0020238. [P92177-4]
DR EnsemblMetazoa; FBtr0083568; FBpp0082990; FBgn0020238. [P92177-1]
DR GeneID; 42186; -.
DR KEGG; dme:Dmel_CG31196; -.
DR CTD; 42186; -.
DR FlyBase; FBgn0020238; 14-3-3epsilon.
DR VEuPathDB; VectorBase:FBgn0020238; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR InParanoid; P92177; -.
DR OMA; IPCATTG; -.
DR PhylomeDB; P92177; -.
DR Reactome; R-DME-2028269; Signaling by Hippo.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-3371511; HSF1 activation.
DR Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P92177; -.
DR BioGRID-ORCS; 42186; 0 hits in 3 CRISPR screens.
DR ChiTaRS; 14-3-3epsilon; fly.
DR GenomeRNAi; 42186; -.
DR PRO; PR:P92177; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0020238; Expressed in eye disc (Drosophila) and 22 other tissues.
DR ExpressionAtlas; P92177; baseline and differential.
DR Genevisible; P92177; DM.
DR GO; GO:0005813; C:centrosome; HDA:FlyBase.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0050815; F:phosphoserine residue binding; IPI:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0051012; P:microtubule sliding; IMP:UniProtKB.
DR GO; GO:0150013; P:negative regulation of neuron projection arborization; IMP:UniProtKB.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; IMP:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; HGI:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IGI:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR GO; GO:0009411; P:response to UV; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..262
FT /note="14-3-3 protein epsilon"
FT /id="PRO_0000058650"
FT REGION 236..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 239..244
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_026086"
FT VAR_SEQ 239..240
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:9159394"
FT /id="VSP_008204"
FT VAR_SEQ 239
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_008203"
FT MUTAGEN 183
FT /note="E->K: Suppressor of sev-Ras1 V12; subviable."
FT /evidence="ECO:0000269|PubMed:9159394"
FT MUTAGEN 199
FT /note="F->Y: Suppressor of sev-Ras1 V12."
FT /evidence="ECO:0000269|PubMed:9159394"
FT MUTAGEN 214
FT /note="Y->F: Suppressor of sev-Ras1 V12."
FT /evidence="ECO:0000269|PubMed:9159394"
SQ SEQUENCE 262 AA; 29799 MW; 2C1562208547DA9C CRC64;
MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW
RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF
YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV
DPNAGDGEPK EQIQDVEDQD VS
