EBI_DROME
ID EBI_DROME Reviewed; 700 AA.
AC Q95RJ9; Q9XZK1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=F-box-like/WD repeat-containing protein ebi;
GN Name=ebi; ORFNames=CG4063;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTANT EBI4.
RX PubMed=10215623; DOI=10.1101/gad.13.8.954;
RA Dong X., Tsuda L., Zavitz K.H., Lin M., Li S., Carthew R.W., Zipursky S.L.;
RT "ebi regulates epidermal growth factor receptor signaling pathways in
RT Drosophila.";
RL Genes Dev. 13:954-965(1999).
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.
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 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).
RN [5]
RP FUNCTION, INTERACTION WITH PHYL AND SINA, AND MUTANTS EBICC1 AND EBICC3.
RX PubMed=11032805; DOI=10.1093/emboj/19.20.5376;
RA Boulton S.J., Brook A., Staehling-Hampton K., Heitzler P., Dyson N.;
RT "A role for Ebi in neuronal cell cycle control.";
RL EMBO J. 19:5376-5386(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH SNO; SMR AND SU(H).
RX PubMed=12230979; DOI=10.1016/s0092-8674(02)00875-9;
RA Tsuda L., Nagaraj R., Zipursky S.L., Banerjee U.;
RT "An EGFR/Ebi/Sno pathway promotes delta expression by inactivating
RT Su(H)/SMRTER repression during inductive notch signaling.";
RL Cell 110:625-637(2002).
CC -!- FUNCTION: F-box-like component of E3 ubiquitin ligase complexes;
CC involved in R7 photoreceptor cell differentiation, cone cell
CC development and neuronal cell cycle control. E3 ubiquitin ligase
CC complexes mediate ubiquitination and subsequent proteasomal degradation
CC of target proteins. Required for specification of R7 photoreceptor cell
CC fate in the eye by participating in the ubiquitination and subsequent
CC proteasomal degradation of Tramtrack (ttk), a general inhibitor of
CC photoreceptor differentiation. Required to block the S phase entry in
CC the peripheral nervous system and central nervous system in a process
CC that does not involve the degradation of ttk. Involved in cone cell
CC development by preventing the transcriptional repression mediated by
CC Su(H) on Dl, probably by participating in a E3 complex that contains
CC sno and mediates the ubiquitination and subsequent proteasomal
CC degradation of some component of the Su(H) repressor complex.
CC {ECO:0000269|PubMed:10215623, ECO:0000269|PubMed:11032805,
CC ECO:0000269|PubMed:12230979}.
CC -!- SUBUNIT: Component of some E3 complex at least composed of sina, ebi
CC and phyl, required for the degradation of ttk. Probably forms a E3
CC complex with sno, required for the degradation of some component of the
CC Su(H) repressor complex. Interacts with sno and Su(H) and Smr.
CC {ECO:0000269|PubMed:11032805, ECO:0000269|PubMed:12230979}.
CC -!- INTERACTION:
CC Q95RJ9; Q9VNC2: HDAC3; NbExp=2; IntAct=EBI-421390, EBI-128090;
CC Q95RJ9; Q27934: phyl; NbExp=4; IntAct=EBI-421390, EBI-77033;
CC Q95RJ9; P21461: sina; NbExp=3; IntAct=EBI-421390, EBI-77019;
CC Q95RJ9; P08044: sna; NbExp=2; IntAct=EBI-421390, EBI-152305;
CC Q95RJ9; P42282: ttk; NbExp=2; IntAct=EBI-421390, EBI-77008;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10215623}.
CC -!- TISSUE SPECIFICITY: Widely expressed both in embryos and larvae.
CC {ECO:0000269|PubMed:10215623}.
CC -!- DOMAIN: The F-box-like domain is related to the F-box domain, and
CC apparently displays the same function as component of ubiquitin E3
CC ligase complexes.
CC -!- MISCELLANEOUS: 'Ebi' means 'shrimp' in Japanese.
CC -!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28874.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF146345; AAD35017.1; -; mRNA.
DR EMBL; AE014134; AAF51501.1; -; Genomic_DNA.
DR EMBL; AY061326; AAL28874.1; ALT_FRAME; mRNA.
DR RefSeq; NP_477329.1; NM_057981.4.
DR AlphaFoldDB; Q95RJ9; -.
DR SMR; Q95RJ9; -.
DR BioGRID; 59468; 70.
DR IntAct; Q95RJ9; 7.
DR MINT; Q95RJ9; -.
DR STRING; 7227.FBpp0077715; -.
DR PaxDb; Q95RJ9; -.
DR EnsemblMetazoa; FBtr0078055; FBpp0077715; FBgn0263933.
DR GeneID; 33212; -.
DR KEGG; dme:Dmel_CG4063; -.
DR CTD; 33212; -.
DR FlyBase; FBgn0263933; ebi.
DR VEuPathDB; VectorBase:FBgn0263933; -.
DR eggNOG; KOG0273; Eukaryota.
DR GeneTree; ENSGT00940000153421; -.
DR HOGENOM; CLU_007609_2_0_1; -.
DR InParanoid; Q95RJ9; -.
DR OMA; KWNKCGN; -.
DR OrthoDB; 1463197at2759; -.
DR PhylomeDB; Q95RJ9; -.
DR Reactome; R-DME-350054; Notch-HLH transcription pathway.
DR Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DME-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q95RJ9; -.
DR BioGRID-ORCS; 33212; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 33212; -.
DR PRO; PR:Q95RJ9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0263933; Expressed in thoracico-abdominal ganglion (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q95RJ9; baseline and differential.
DR Genevisible; Q95RJ9; DM.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0017053; C:transcription repressor complex; IGI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:FlyBase.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045183; Ebi-like.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR PANTHER; PTHR22846; PTHR22846; 2.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Reference proteome; Repeat; Sensory transduction;
KW Ubl conjugation pathway; Vision; WD repeat.
FT CHAIN 1..700
FT /note="F-box-like/WD repeat-containing protein ebi"
FT /id="PRO_0000050960"
FT DOMAIN 4..36
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 41..84
FT /note="F-box-like"
FT REPEAT 353..392
FT /note="WD 1"
FT REPEAT 408..447
FT /note="WD 2"
FT REPEAT 449..488
FT /note="WD 3"
FT REPEAT 491..531
FT /note="WD 4"
FT REPEAT 532..571
FT /note="WD 5"
FT REPEAT 574..622
FT /note="WD 6"
FT REPEAT 625..664
FT /note="WD 7"
FT REPEAT 666..700
FT /note="WD 8"
FT REGION 93..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 16
FT /note="L->Q: In ebiCC1; induces ectopic S phases within the
FT peripheral and central nervous system."
FT MUTAGEN 510
FT /note="C->Y: In ebi4; induces defects in R7 cell
FT development in the eye."
FT MUTAGEN 602
FT /note="S->L: In ebiCC3; induces ectopic S phases within the
FT peripheral and central nervous system."
SQ SEQUENCE 700 AA; 72387 MW; 28C6D8D07BB79FB7 CRC64;
MSFSSDEVNF LVYRYLQESG FLHSAYVFGI ESHISQSNIN GALVPPAALL TILQKGLLYT
EVEWSVGEDG EVARPIEGLS LIDAVMPEVK PLKPIVKTEP GKPGAVDSSA PAGGNQNNNA
KPEIKIEPGT GVAGSAGGNK IAGSTTGTST PTDQSASEVD SSGNAANNAG GTYAGNNGAG
GNQASTGGSN STSTPAGGDL AAPGASQKKS QNSNEAGSSS SGNAGNANAT STDDAASSTS
TNGNSSTSSS VEQPTSGLTP AGGTVSTSNP DAAASGGAST ATGSKAPSGA VTIRVGAQGN
NVQSGSSNAQ SSAPSGTISS STSGGAGTPA ALVPMDIDEN IEIPESKARV LRGHESEVFI
CAWNPSRDLL ASGSGDSTAR IWDMSDANTN SNQLVLRHCI QKGGAEVPSN KDVTSLDWNC
DGSLLATGSY DGYARIWKTD GRLASTLGQH KGPIFALKWN KCGNYILSAG VDKTTIIWDA
STGQCTQQFA FHSAPALDVD WQTNQAFASC STDQRIHVCR LGVNEPIKTF KGHTNEVNAI
KWCPQGQLLA SCSDDMTLKI WSMNRDRCCH DLQAHSKEIY TIKWSPTGPG TNNPNTNLIL
ASASFDSTVR LWDVERGSCI HTLTKHTEPV YSVAFSPDGK HLASGSFDKC VHIWSTQTGQ
LVHSYKGTGG IFEVCWNSKG TKVGASASDG SVFVLDLRKF
