ID   CRTC3_XENLA             Reviewed;         632 AA.
AC   Q52KS4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=CREB-regulated transcription coactivator 3;
DE   AltName: Full=Transducer of regulated cAMP response element-binding protein 3;
DE            Short=TORC-3;
DE            Short=Transducer of CREB protein 3;
GN   Name=crtc3; Synonyms=torc3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional coactivator for creb1 which activates
CC       transcription through both consensus and variant cAMP response element
CC       (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway,
CC       being active when dephosphorylated and acts independently of creb1
CC       'Ser-119' phosphorylation. Enhances the interaction of creb1 with taf4.
CC       Regulates the expression of specific CREB-activated genes such as the
CC       steroidogenic gene, StAR. Potent coactivator of ppargc1a and inducer of
CC       mitochondrial biogenesis in muscle cells (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binding, as a tetramer, through its N-terminal region, with
CC       the bZIP domain of creb1 enhances recruitment of taf4 to the promoter.
CC       'Arg-300' in the bZIP domain of creb1 is essential for this interaction
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Appears to be mainly nuclear. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH94209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC094209; AAH94209.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q52KS4; -.
DR   SMR; Q52KS4; -.
DR   IntAct; Q52KS4; 1.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008140; F:cAMP response element binding protein binding; IEA:InterPro.
DR   GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IEA:InterPro.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR   InterPro; IPR024786; TORC.
DR   InterPro; IPR024785; TORC_C.
DR   InterPro; IPR024784; TORC_M.
DR   InterPro; IPR024783; TORC_N.
DR   PANTHER; PTHR13589; PTHR13589; 1.
DR   Pfam; PF12886; TORC_C; 1.
DR   Pfam; PF12885; TORC_M; 1.
DR   Pfam; PF12884; TORC_N; 1.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..632
FT                   /note="CREB-regulated transcription coactivator 3"
FT                   /id="PRO_0000318533"
FT   REGION          105..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..428
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         145
FT                   /note="Phosphoserine; by SIK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   632 AA;  69349 MW;  AB68E6370F42165A CRC64;
     MTATPANSGS NPRKFSEKIA LHNQKQAEET RAFDELMSDL TVSRVQFQKL QQLRLAQTRA
     QYYGGSLPNV NQISSSPNDF QPSFHPMDNI RGMRHHGLVE RVSRNRLHSS HHRPVEKHGR
     QCDSSPYGSV YLSPPPDNNW RRTNSDSALH TSASSSKLQD AFMGGNQAML RAPKPPQRNP
     SLQDGEMNNF GEAFSYPTSM TEENMLNVTK PLPKQIWEAQ KVQCITSRPR SCEVPGIKVF
     PSSDSNASLS HYQGSLNTGG SLPDLTNLHF PSPLPTPLDP DDTVYANINA ENSSGLPAAM
     THLGISNSQG IQNTCSNPSI QATMNNNVNN HTPPGRNNPT LHPSLRLSSL SNPSLPTSAL
     GSSPRRRHTP VSPLTLTPGS ESNRSISNQF SPTSPMDMLP NSQGVSMDRC PLSLPPLEPP
     PPYPLYTDQP QPQLHHTQQQ MHESPESQNF QPPSPVPCPP LDLNLANSSL SGFFGDSFFD
     QQQPTKQGKY LWQQQEQYDM FGSPSSSLPN TNAFFDPNMN LQYSQASLMG LGGSHGSLQD
     SFHLRPNYLY SNYGGSVPNI ILTDDSSNSL SKDISNAVAG VSELGFDADN TFQFDDELKL
     GPLSLDGLSM LSDPDMVLPD PSIEDSFRSD KL