CRTC1_CAEEL
ID CRTC1_CAEEL Reviewed; 486 AA.
AC Q95XA8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 4.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CREB-regulated transcription coactivator 1 homolog {ECO:0000312|WormBase:Y20F4.2};
GN Name=crtc-1 {ECO:0000312|WormBase:Y20F4.2};
GN ORFNames=Y20F4.2 {ECO:0000312|WormBase:Y20F4.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CRH-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT SER-76 AND SER-179, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-76; SER-179 AND 423-PRO--THR-428.
RX PubMed=21331044; DOI=10.1038/nature09706;
RA Mair W., Morantte I., Rodrigues A.P., Manning G., Montminy M., Shaw R.J.,
RA Dillin A.;
RT "Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1
RT and CREB.";
RL Nature 470:404-408(2011).
RN [3] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25723162; DOI=10.1016/j.cell.2015.02.004;
RA Burkewitz K., Morantte I., Weir H.J., Yeo R., Zhang Y., Huynh F.K.,
RA Ilkayeva O.R., Hirschey M.D., Grant A.R., Mair W.B.;
RT "Neuronal CRTC-1 governs systemic mitochondrial metabolism and lifespan via
RT a catecholamine signal.";
RL Cell 160:842-855(2015).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=26232604; DOI=10.1016/j.jmb.2015.07.017;
RA Li W., Bell H.W., Ahnn J., Lee S.K.;
RT "Regulator of calcineurin (rcan-1) regulates thermotaxis behavior in
RT Caenorhabditis elegans.";
RL J. Mol. Biol. 427:3457-3468(2015).
CC -!- FUNCTION: Transcriptional coactivator for crh-1, the homolog of
CC vertebrate transcription factor CREB1 (PubMed:21331044). Regulates the
CC transcription of metabolic genes and may have a role in mitochondrial
CC dynamics and metabolism (PubMed:25723162). Through crh-1, counteracts
CC the pro-lifespan-extension signals of AMPK both cell autonomously and,
CC when expressed in neurons, at a systemic level, possibly using the
CC catecholamine analog, octopamine, as a messenger (PubMed:21331044,
CC PubMed:25723162). {ECO:0000269|PubMed:21331044,
CC ECO:0000269|PubMed:25723162}.
CC -!- SUBUNIT: Interacts with crh-1. {ECO:0000269|PubMed:21331044}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21331044,
CC ECO:0000269|PubMed:26232604}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21331044}. Note=Localization is phosphorylation-
CC dependent with the phosphorylated form translocating to the cytosol
CC (PubMed:21331044). Cytosolic sequestration requires 14-3-3 proteins
CC fft-1 and fft-2 (PubMed:21331044). Nuclear localization may in part
CC depend on activity of the calcineurin subunit tax-6 and its regulator
CC rcan-1 in response to changes in intracellular calcium levels
CC (PubMed:26232604). {ECO:0000269|PubMed:21331044,
CC ECO:0000269|PubMed:26232604}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the intestine and in head and
CC tail neurons (PubMed:21331044). Expressed in octopaminergic RIC neurons
CC (PubMed:25723162). {ECO:0000269|PubMed:21331044,
CC ECO:0000269|PubMed:25723162}.
CC -!- PTM: Phosphorylated by AMPK at Ser-76 and Ser-179. Dephosphorylated by
CC tax-6, the catalytic subunit of calcineurin.
CC {ECO:0000269|PubMed:21331044}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down results in increased
CC lifespan. {ECO:0000269|PubMed:21331044}.
CC -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
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DR EMBL; FO081781; CCD73417.2; -; Genomic_DNA.
DR RefSeq; NP_490917.4; NM_058516.5.
DR AlphaFoldDB; Q95XA8; -.
DR SMR; Q95XA8; -.
DR DIP; DIP-59883N; -.
DR IntAct; Q95XA8; 3.
DR STRING; 6239.Y20F4.2; -.
DR iPTMnet; Q95XA8; -.
DR PaxDb; Q95XA8; -.
DR EnsemblMetazoa; Y20F4.2.1; Y20F4.2.1; WBGene00021237.
DR GeneID; 259368; -.
DR KEGG; cel:CELE_Y20F4.2; -.
DR UCSC; Y20F4.2; c. elegans.
DR CTD; 259368; -.
DR WormBase; Y20F4.2; CE47164; WBGene00021237; crtc-1.
DR eggNOG; ENOG502SAC7; Eukaryota.
DR GeneTree; ENSGT00390000010652; -.
DR HOGENOM; CLU_594810_0_0_1; -.
DR InParanoid; Q95XA8; -.
DR OMA; QVQSITH; -.
DR OrthoDB; 1583510at2759; -.
DR PRO; PR:Q95XA8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021237; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IPI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
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; IPR024783; TORC_N.
DR PANTHER; PTHR13589; PTHR13589; 2.
DR Pfam; PF12884; TORC_N; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..486
FT /note="CREB-regulated transcription coactivator 1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433354"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:21331044"
FT MOD_RES 179
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:21331044"
FT MUTAGEN 76
FT /note="S->A: Loss of phosphorylation. Leads to nuclear
FT sequestration; when associated with A-179."
FT /evidence="ECO:0000269|PubMed:21331044"
FT MUTAGEN 179
FT /note="S->A: Loss of phosphorylation. Leads to nuclear
FT sequestration; when associated with A-76."
FT /evidence="ECO:0000269|PubMed:21331044"
FT MUTAGEN 423..428
FT /note="PKLTIT->AKATAA: Calcineurin binding site mutation.
FT Loss of nuclear translocation in response to increased
FT calcium influx."
FT /evidence="ECO:0000269|PubMed:21331044"
SQ SEQUENCE 486 AA; 53172 MW; F8B572680FEB9FE8 CRC64;
MSNSNTPRKF SEKIAILERK QNEENTTFED IMRQVQSITH HPTDSSGSST ATAPMPIPQQ
GLLPPQQPWG HNLGGSLPNV HQMPSYSPPQ WPPNWQHEIQ HRPIQGHRSR SPEDHMIGSA
SGSPSHHYHP YGMRSNGLSR SPDRTPPQHP QYTPYGPPYN QPGQLVPPES WNQINRARSD
PAIHNMGGMV PMHPHHHQQQ QMAFHQMPHY LQNSMPGPSG MMAPNSQSQQ HSPQLTPQGS
QQGSPVQMHH QIPPPLQMGN NQQMGGGNNG MSPLQSPNHM MTPMYGYHNG SPLHSPMDSP
HASTLMLDGS GTPSPYMEVS PPGMHDFNQD AGSLPNLQNV QQQQQQQQEI YTNGGAPGGG
YYHAPIGPRH STGACGPRLV PGPALTPESQ SAPTSPHNQL DPNQPPMWPT RTFSNSPEAL
DIPKLTITNA EGAPGHHVDS YNDFNDLGLD SLDSVLCNGA PPQTISNHQT PNNSFHDPGG
TQMLQN
