CREST_RAT
ID CREST_RAT Reviewed; 401 AA.
AC Q91XJ0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Calcium-responsive transcription coactivator;
DE AltName: Full=SS18-like protein 1;
GN Name=Ss18l1; Synonyms=Crest;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH CREBBP AND EP300, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=14716005; DOI=10.1126/science.1089845;
RA Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
RA Cowan M., Ghosh A.;
RT "Dendrite development regulated by CREST, a calcium-regulated
RT transcriptional activator.";
RL Science 303:197-202(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=15488321; DOI=10.1016/j.neulet.2004.08.062;
RA Pradhan A., Liu Y.;
RT "The calcium-responsive transactivator recruits CREB binding protein to
RT nuclear bodies.";
RL Neurosci. Lett. 370:191-195(2004).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MFD DOMAIN.
RX PubMed=15866867; DOI=10.1074/jbc.m504018200;
RA Pradhan A., Liu Y.;
RT "A multifunctional domain of the calcium-responsive transactivator (CREST)
RT that inhibits dendritic growth in cultured neurons.";
RL J. Biol. Chem. 280:24738-24743(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH SMARCA4/BRG1.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
CC -!- FUNCTION: Transcriptional activator which is required for calcium-
CC dependent dendritic growth and branching in cortical neurons. Recruits
CC CREB-binding protein (CREBBP) to nuclear bodies. Component of the
CC CREST-BRG1 complex, a multiprotein complex that regulates promoter
CC activation by orchestrating a calcium-dependent release of a repressor
CC complex and a recruitment of an activator complex. In resting neurons,
CC transcription of the c-FOS promoter is inhibited by BRG1-dependent
CC recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium
CC influx, RB1 is dephosphorylated by calcineurin, which leads to release
CC of the repressor complex. At the same time, there is increased
CC recruitment of CREBBP to the promoter by a CREST-dependent mechanism,
CC which leads to transcriptional activation. The CREST-BRG1 complex also
CC binds to the NR2B promoter, and activity-dependent induction of NR2B
CC expression involves a release of HDAC1 and recruitment of CREBBP.
CC {ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:15866867,
CC ECO:0000269|PubMed:19081374}.
CC -!- SUBUNIT: Homodimer. Dimerization may be necessary for its function in
CC neuronal dendritic development. Interacts (via C-terminus) with CREBBP
CC (via N-terminus), EP300 and SMARCA4/BRG1. Interacts with the nBAF
CC complex (By similarity). Association with CREBBP facilitates
CC transcription while the association with SMARCA4/BRG1 suppresses CREST-
CC mediated transcription in resting neurons. {ECO:0000250,
CC ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:15866867,
CC ECO:0000269|PubMed:19081374}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14716005,
CC ECO:0000269|PubMed:15488321, ECO:0000269|PubMed:15866867}. Chromosome,
CC centromere, kinetochore {ECO:0000250}. Note=Localizes to nuclear
CC bodies. Colocalizes with SGO1 at kinetochore (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain (at protein level). Also found in the heart,
CC liver, kidney and testis. {ECO:0000269|PubMed:14716005}.
CC -!- DEVELOPMENTAL STAGE: Detected as early as E18 in the developing
CC cerebral cortex, and expression reaches its peak at P1, declines after
CC P10, and remains at a relatively low level throughout adulthood. At
CC E18, expressed in the forebrain, midbrain, and hindbrain. Within the
CC forebrain, it is expressed in postmitotic cells of the cortical plate.
CC At this stage, it can also be detected in other structures of central
CC and peripheral nervous systems, including the trigeminal ganglion,
CC superior cervical ganglion, retina and olfactory epithelium. Expression
CC in the cortex is high at birth and declines substantially by P20. At
CC P7, expressed in all cortical layers, and in the hippocampus,
CC expression is high in the cell body layers of all subdivisions. Within
CC the brain, expression decreases through development but continues to be
CC expressed at high levels in the olfactory bulb, hippocampus, and
CC cerebellum into adulthood. {ECO:0000269|PubMed:14716005}.
CC -!- DOMAIN: The MFD (multi-functional domain) domain is involved in
CC transcription transactivation, nuclear body targeting and dimerization.
CC Inhibits dendritic growth in cultured neurons.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
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DR EMBL; AY034073; AAK53461.1; -; mRNA.
DR RefSeq; NP_620273.1; NM_138918.1.
DR AlphaFoldDB; Q91XJ0; -.
DR SMR; Q91XJ0; -.
DR STRING; 10116.ENSRNOP00000011306; -.
DR PaxDb; Q91XJ0; -.
DR PRIDE; Q91XJ0; -.
DR GeneID; 192352; -.
DR KEGG; rno:192352; -.
DR CTD; 26039; -.
DR RGD; 621847; Ss18l1.
DR VEuPathDB; HostDB:ENSRNOG00000060010; -.
DR eggNOG; KOG3227; Eukaryota.
DR HOGENOM; CLU_054580_1_0_1; -.
DR InParanoid; Q91XJ0; -.
DR OMA; SAQQYMG; -.
DR OrthoDB; 1442230at2759; -.
DR PRO; PR:Q91XJ0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000060010; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q91XJ0; RN.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0071565; C:nBAF complex; ISO:RGD.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IDA:UniProtKB.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 1: Evidence at protein level;
KW Activator; Calcium; Centromere; Chromatin regulator; Chromosome;
KW Kinetochore; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..401
FT /note="Calcium-responsive transcription coactivator"
FT /id="PRO_0000391347"
FT REGION 1..148
FT /note="N-terminal auto-inhibitory domain; necessary for
FT interaction with SMARCA4/BRG1"
FT REGION 72..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..237
FT /note="Methionine-rich intra-molecular domain"
FT REGION 214..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..322
FT /note="MFD domain"
FT REGION 339..401
FT /note="Necessary for nuclear localization"
FT REGION 392..401
FT /note="Necessary for interaction with CREBBP and for the
FT recruitment of CREBBP to the nuclear bodies"
FT /evidence="ECO:0000269|PubMed:14716005"
FT MOTIF 50..53
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 358..361
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 376..384
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 396..399
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 240..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43999 MW; 2B1805EC74EEC12F CRC64;
MSVAFASARP RGKGEVTQQT IQKMLDENHH LIQCILDYQS KGKTAECTQY QQILHRNLVY
LATIADSNQN MQSLLPAPPT QNMNLGPGAL SQSGSSQGLH PQGSLSDTVS TGLPPASLMQ
GQIGNGPNHV SMQQTAQSTL PTTSMSMSGS GHGTGPGYSH SGPTSQSVPM QGQGAISNYV
SRTNINMQSN PVSMMHQQAA RPTTTQRRVE ASITRARRPL HDGPGWQGGS MMGQRPMAPY
RPSQQGSSQQ YLGQEEYYSE QYSHSQGSAE PMSQQYYPDG HSDYAYQQSS YTEQSYDRSF
EDPTQHYYEG GNSQYSQQQA GYQQGTAQQQ TYSQQQYPNQ QSYPGQQQGY GPAQGAPSQY
SGYQQGQGQQ YGSYRTSQTG PSAQQQRPYG YEQGQYGNYQ Q
