RTBP_DROME
ID RTBP_DROME Reviewed; 118 AA.
AC Q9VL14; Q8IPC6; Q8IPC7; Q8MYS1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=REPTOR-binding partner {ECO:0000303|PubMed:25920570};
GN Name=REPTOR-BP {ECO:0000303|PubMed:25920570,
GN ECO:0000312|FlyBase:FBgn0032202};
GN ORFNames=CG18619 {ECO:0000312|FlyBase:FBgn0032202};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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:AAM29644.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29644.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM29644.1};
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 [4] {ECO:0000312|EMBL:ACY38293.1, ECO:0000312|EMBL:ACY38294.1, ECO:0000312|EMBL:ANY27448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B; C AND D).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACY38293.1, ECO:0000312|EMBL:ACY38294.1,
RC ECO:0000312|EMBL:ANY27448.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ACY38293.1, ECO:0000312|EMBL:ACY38294.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.,
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH REPTOR, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25920570; DOI=10.1016/j.devcel.2015.03.013;
RA Tiebe M., Lutz M., De La Garza A., Buechling T., Boutros M., Teleman A.A.;
RT "REPTOR and REPTOR-BP regulate organismal metabolism and transcription
RT downstream of TORC1.";
RL Dev. Cell 33:272-284(2015).
CC -!- FUNCTION: Transcriptional regulator that acts in the TORC1 signaling
CC pathway to regulate energy homeostasis and promote survival during
CC nutrient deprivation. Interacts with REPTOR to form a transcriptional
CC activator complex that functions downstream of TORC1 to up-regulate the
CC expression of most target genes induced by TORC1 inhibition. In the
CC complex, acts to enhance the binding of the transcriptional activator
CC REPTOR to the regulatory sequences of target genes. Under normal
CC conditions TORC1 is active, inhibiting the formation of the
CC REPTOR/REPTOR-BP complex by phosphorylating REPTOR and mediates its
CC cytoplasmic retention by forming a docking site for 14-3-3 proteins.
CC Upon TORC1 inhibition resulting from nutrient stress, REPTOR is
CC recruited into the nucleus where it interacts with REPTOR-BP and
CC together they maintain organismal metabolism by activating the
CC expression of target stress response genes including those involved in
CC glycogenesis and triglyceride biosynthesis. The complex also appears to
CC negatively regulate some aspects of TORC1-dependent larval growth.
CC {ECO:0000269|PubMed:25920570}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with REPTOR (via C-
CC terminus). {ECO:0000269|PubMed:25920570}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25920570}. Chromosome
CC {ECO:0000269|PubMed:25920570}. Note=Binds chromatin.
CC {ECO:0000269|PubMed:25920570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A {ECO:0000312|FlyBase:FBgn0032202};
CC IsoId=Q9VL14-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0032202};
CC IsoId=Q9VL14-2; Sequence=VSP_059825;
CC Name=C {ECO:0000312|FlyBase:FBgn0032202};
CC IsoId=Q9VL14-3; Sequence=VSP_059825, VSP_059826, VSP_059827;
CC Name=D {ECO:0000312|FlyBase:FBgn0032202};
CC IsoId=Q9VL14-4; Sequence=VSP_059826, VSP_059827;
CC -!- DISRUPTION PHENOTYPE: Sensitive to nutrient stress. Larvae display no
CC obvious phenotype under normal feeding conditions; larval growth and
CC development is normal, and there is no effect on triglyceride and
CC glycogen levels. However when mutants pupate and become adults they
CC display reduced triglyceride and glycogen stores leading to adults
CC dying within 18 hours of starvation whereas controls survive 2.5 days
CC without food. Larvae are also sensitive to nutrient stress displaying
CC 50% lethality when fed a low nutrient diet.
CC {ECO:0000269|PubMed:25920570}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AE014134; AAF52891.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10733.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10734.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10735.1; -; Genomic_DNA.
DR EMBL; AY113639; AAM29644.1; -; mRNA.
DR EMBL; BT100178; ACY38293.1; -; mRNA.
DR EMBL; BT100179; ACY38294.1; -; mRNA.
DR EMBL; KX531638; ANY27448.1; -; mRNA.
DR RefSeq; NP_609363.1; NM_135519.3. [Q9VL14-1]
DR RefSeq; NP_723546.1; NM_164903.2. [Q9VL14-2]
DR RefSeq; NP_723547.1; NM_164904.2. [Q9VL14-4]
DR RefSeq; NP_723548.1; NM_164905.3. [Q9VL14-3]
DR AlphaFoldDB; Q9VL14; -.
DR SMR; Q9VL14; -.
DR IntAct; Q9VL14; 17.
DR STRING; 7227.FBpp0088679; -.
DR PaxDb; Q9VL14; -.
DR DNASU; 34371; -.
DR EnsemblMetazoa; FBtr0089735; FBpp0088676; FBgn0032202. [Q9VL14-4]
DR EnsemblMetazoa; FBtr0089736; FBpp0088677; FBgn0032202. [Q9VL14-3]
DR EnsemblMetazoa; FBtr0089737; FBpp0088678; FBgn0032202. [Q9VL14-2]
DR EnsemblMetazoa; FBtr0089738; FBpp0088679; FBgn0032202. [Q9VL14-1]
DR GeneID; 34371; -.
DR KEGG; dme:Dmel_CG18619; -.
DR UCSC; CG18619-RA; d. melanogaster. [Q9VL14-1]
DR UCSC; CG18619-RB; d. melanogaster.
DR UCSC; CG18619-RC; d. melanogaster.
DR UCSC; CG18619-RD; d. melanogaster.
DR CTD; 34371; -.
DR FlyBase; FBgn0032202; REPTOR-BP.
DR VEuPathDB; VectorBase:FBgn0032202; -.
DR eggNOG; KOG4515; Eukaryota.
DR GeneTree; ENSGT00390000005388; -.
DR HOGENOM; CLU_134161_2_0_1; -.
DR InParanoid; Q9VL14; -.
DR OMA; DQGRMPE; -.
DR OrthoDB; 1551209at2759; -.
DR PhylomeDB; Q9VL14; -.
DR SignaLink; Q9VL14; -.
DR BioGRID-ORCS; 34371; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34371; -.
DR PRO; PR:Q9VL14; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032202; Expressed in spermathecum and 34 other tissues.
DR ExpressionAtlas; Q9VL14; baseline and differential.
DR Genevisible; Q9VL14; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0038202; P:TORC1 signaling; IMP:FlyBase.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR039250; CREBL2/REPTOR-BP.
DR PANTHER; PTHR21051; PTHR21051; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosome; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..118
FT /note="REPTOR-binding partner"
FT /id="PRO_0000445230"
FT DOMAIN 40..90
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..77
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 82..89
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 20..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 20
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_059825"
FT VAR_SEQ 89..94
FT /note="LIQWNN -> VVNSME (in isoform C and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_059826"
FT VAR_SEQ 95..118
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_059827"
SQ SEQUENCE 118 AA; 13852 MW; 764AE068724BD897 CRC64;
MADMEIQSNK MSITEETQVQ TRKECGKRGR KPGRKTSTEK LDMKAKLERS RQSARECRAR
KKLRYQYLEE LVADREKAVV ALRTELERLI QWNNQLSESN TPTNNDQLLQ ELGILKQE