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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
 
 
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