CRTC3_XENTR
ID CRTC3_XENTR Reviewed; 637 AA.
AC Q0IHT3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) 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}.
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DR EMBL; BC122981; AAI22982.1; -; mRNA.
DR RefSeq; NP_001072163.1; NM_001078695.1.
DR AlphaFoldDB; Q0IHT3; -.
DR SMR; Q0IHT3; -.
DR STRING; 8364.ENSXETP00000060646; -.
DR PaxDb; Q0IHT3; -.
DR PRIDE; Q0IHT3; -.
DR DNASU; 496857; -.
DR Ensembl; ENSXETT00000062847; ENSXETP00000060646; ENSXETG00000001294.
DR GeneID; 496857; -.
DR KEGG; xtr:496857; -.
DR CTD; 64784; -.
DR Xenbase; XB-GENE-5787077; crtc3.
DR eggNOG; ENOG502QV9G; Eukaryota.
DR HOGENOM; CLU_019357_2_0_1; -.
DR InParanoid; Q0IHT3; -.
DR OrthoDB; 1118500at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000001294; Expressed in gastrula and 16 other tissues.
DR ExpressionAtlas; Q0IHT3; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IBA:GO_Central.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..637
FT /note="CREB-regulated transcription coactivator 3"
FT /id="PRO_0000318534"
FT REGION 105..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..456
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 143
FT /note="Phosphothreonine"
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 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 69484 MW; 5717B5116FBE125F CRC64;
MAATPAASGS NPRKFSEKIA LHNQKQAEET RAFDELMSDL TVSRVQFQKL QQLRLAQSRA
QYYGGSLPNV NQISSSPTDF QPSFHPTDNI RGMRHHGLVE RVSRNRLHSS HHRPIEKHGR
QCDSSPYGSV YLSPPPDNNW RRTNSDSALH TSASSTKSQD PFMGGAQAML RAPKPPQRNT
SLQDGEIDNF GEVFSFPNAM TEENMLNVTK PLPKQIWEAQ KVQCITSRPR SCEVPNIKVF
PSSDSNASLS HFQGSLNTGG SLPDLTNLHF PSPLPTPLDP DDTAYANISA ENSSGLPAAM
THLGISGSPG MQNTRSNPSI QATMNNNSLA SNVNSHTPPG RNNPALHPSL RLSSLSNPSL
PTSALGTSPR RRHTPVSPLT LTPGSESNRS ISNQFSPTSP MNMPPNSQGV SMDRSPLSLP
PLEPPPPYPL YSDQPQPHLH HTQQQMHESL DSQNYQPPSP VPCPPLDLNL ANSSLSGFFG
DSFFDQQQPT KQGKYLWQQQ EQYDMFGSPS SSLPNTNAFF DPNMNLQYSQ ASLMGLGGSH
GSLQDSFHLR PNYLYSNCGG SVPNIILTDD SSNSLSKDIS NAVAGVSELG FDADNTFQLD
DELKLGPLSL DGLSMLSDPD MVLPDPSIED SFRSDKL
