CRTC1_RAT
ID CRTC1_RAT Reviewed; 630 AA.
AC Q157S1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=CREB-regulated transcription coactivator 1;
DE AltName: Full=Mucoepidermoid carcinoma translocated protein 1 homolog;
DE AltName: Full=Transducer of regulated cAMP response element-binding protein 1;
DE Short=TORC-1;
DE Short=Transducer of CREB protein 1;
GN Name=Crtc1; Synonyms=Mect1, Torc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Hao W., Hong S., Zhiqi X.;
RT "TORC1 in the central nervous system.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-151.
RX PubMed=19244510; DOI=10.1523/jneurosci.2296-08.2009;
RA Li S., Zhang C., Takemori H., Zhou Y., Xiong Z.Q.;
RT "TORC1 regulates activity-dependent CREB-target gene transcription and
RT dendritic growth of developing cortical neurons.";
RL J. Neurosci. 29:2334-2343(2009).
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-133' 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 PGC1alpha and inducer
CC of mitochondrial biogenesis in muscle cells (By similarity). In the
CC hippocampus, involved in late-phase long-term potentiation (L-LTP)
CC maintenance at the Schaffer collateral-CA1 synapses. May be required
CC for dendritic growth of developing cortical neurons. In concert with
CC SIK1, regulates the light-induced entrainment of the circadian clock.
CC In response to light stimulus, coactivates the CREB-mediated
CC transcription of PER1 which plays an important role in the photic
CC entrainment of the circadian clock (By similarity).
CC {ECO:0000250|UniProtKB:Q68ED7, ECO:0000250|UniProtKB:Q6UUV9,
CC ECO:0000269|PubMed:19244510}.
CC -!- SUBUNIT: Binds, as a tetramer, through its N-terminal region, with the
CC bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is
CC essential for this interaction. Interaction, via its C-terminal, with
CC TAF4, enhances recruitment of TAF4 to CREB1. Interacts with 14-3-3
CC proteins, including YWHAE/14-3-3 epsilon. Interacts with calmodulin-
CC dependent catalytic subunit PPP3CA/calcineurin A.
CC {ECO:0000250|UniProtKB:Q6UUV9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68ED7}. Nucleus
CC {ECO:0000250|UniProtKB:Q68ED7}. Note=Cytoplasmic when phosphorylated by
CC SIK or AMPK and when sequestered by 14-3-3 proteins. Translocated to
CC the nucleus on Ser-151 dephosphorylation, instigated by a number of
CC factors including calcium ion and cAMP levels. Light stimulation
CC triggers a nuclear accumulation in the suprachiasmatic nucleus (SCN) of
CC the brain. {ECO:0000250|UniProtKB:Q68ED7,
CC ECO:0000250|UniProtKB:Q6UUV9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing cortical neurons,
CC peaking during dendrite development. {ECO:0000269|PubMed:19244510}.
CC -!- PTM: Phosphorylation/dephosphorylation states of Ser-151 are required
CC for regulating transduction of CREB activity. TORCs are inactive when
CC phosphorylated, and active when dephosphorylated at this site. This
CC primary site of phosphorylation is mediated by SIKs (SIK1 and SIK2), is
CC regulated by cAMP and calcium levels and is dependent on the
CC phosphorylation of SIKs by LKB1. {ECO:0000269|PubMed:19244510}.
CC -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
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DR EMBL; DQ538521; ABG23027.1; -; mRNA.
DR RefSeq; NP_001040580.1; NM_001047115.1.
DR AlphaFoldDB; Q157S1; -.
DR SMR; Q157S1; -.
DR BioGRID; 599406; 1.
DR IntAct; Q157S1; 1.
DR STRING; 10116.ENSRNOP00000030925; -.
DR iPTMnet; Q157S1; -.
DR PhosphoSitePlus; Q157S1; -.
DR jPOST; Q157S1; -.
DR PaxDb; Q157S1; -.
DR PRIDE; Q157S1; -.
DR GeneID; 684527; -.
DR KEGG; rno:684527; -.
DR CTD; 23373; -.
DR RGD; 1589158; Crtc1.
DR VEuPathDB; HostDB:ENSRNOG00000022421; -.
DR eggNOG; ENOG502QU41; Eukaryota.
DR HOGENOM; CLU_019357_2_0_1; -.
DR InParanoid; Q157S1; -.
DR OMA; FNMVEGA; -.
DR OrthoDB; 1118500at2759; -.
DR PhylomeDB; Q157S1; -.
DR PRO; PR:Q157S1; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000022421; Expressed in frontal cortex and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0008140; F:cAMP response element binding protein binding; ISO:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:1902631; P:negative regulation of membrane hyperpolarization; ISO:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Activator; Biological rhythms; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..630
FT /note="CREB-regulated transcription coactivator 1"
FT /id="PRO_0000413636"
FT REGION 142..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..258
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 142..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 571
FT /note="Required for ubiquitination and degradation"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68ED7"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UUV9"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68ED7"
FT MOD_RES 151
FT /note="Phosphoserine; by SIK1 and SIK2"
FT /evidence="ECO:0000269|PubMed:19244510"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6UUV9"
SQ SEQUENCE 630 AA; 66924 MW; 2ABD42BE1F0D1095 CRC64;
MATSNNPRKF SEKIALHNQK QAEETAAFEE VMKDLSLTRA ARLQLQKSQY LQLGPSRGQY
YGGSLPNVNQ IGSSSMDLSF QTPFQSSGLD TSRTTRHHGL VDRVYRERGR LGSPHRRPLS
VDKHGRQADS CPYGTVYLSP PADTSWRRTN SDSALHQSTM TPTQAESFTG GPQDAHQKRV
LLLTVPGMEE TGSETDKTLS KQSWDSKKAG SRPKSCEVPG INIFPSADQE NTAALIPATH
NTGGSLPDLS TIHFPSPLPT PLDPEEPPFP ALTSSGSTGS LAHLGVGGTG QGMNTPSSSP
QRRPAVVSPL SLSTEARRQQ AQQVPPTLSP LSPITQAVAM DALSLEQQLP YAFFTQAGSQ
QPPPQPQPPP PPPPVSQQQP PPPQVSVGLP QGGPLLPSAS LTRGPQLPPL AVTVPSTLPQ
SPTESPGQPP MGIDVTSAPA LQYRTGAGSP ATQSPTSPVS NQGFSPGSSP QHTSTLGSVF
GDAYYEQQMT ARQANALSRQ LEQFNMMENA ISSSSLYNPG STLNYSQAAM MGLSGSHGGL
QDPQQLGYAG HGGIPNIILT VTGESPPSLS KELSSTLAGV SDVSFDSDHQ FPLDELKIDP
LTLDGLHMLN DPDMVLADPA TEDTFRMDRL
