CREST_BOVIN
ID CREST_BOVIN Reviewed; 402 AA.
AC Q08E31;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Calcium-responsive transactivator;
DE AltName: Full=SS18-like protein 1;
GN Name=SS18L1; Synonyms=CREST;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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. Association with CREBBP facilitates transcription while the
CC association with SMARCA4/BRG1 suppresses CREST-mediated transcription
CC in resting neurons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies.
CC Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The MFD (multi-functional domain) domain is involved in
CC transcription transactivation, nuclear body targeting and dimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
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DR EMBL; BC123448; AAI23449.1; -; mRNA.
DR RefSeq; NP_001071563.1; NM_001078095.1.
DR AlphaFoldDB; Q08E31; -.
DR SMR; Q08E31; -.
DR STRING; 9913.ENSBTAP00000019202; -.
DR PaxDb; Q08E31; -.
DR Ensembl; ENSBTAT00000019202; ENSBTAP00000019202; ENSBTAG00000014438.
DR GeneID; 768207; -.
DR KEGG; bta:768207; -.
DR CTD; 26039; -.
DR VEuPathDB; HostDB:ENSBTAG00000014438; -.
DR VGNC; VGNC:35306; SS18L1.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000159853; -.
DR HOGENOM; CLU_054580_1_0_1; -.
DR InParanoid; Q08E31; -.
DR OMA; SAQQYMG; -.
DR OrthoDB; 1442230at2759; -.
DR TreeFam; TF330999; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000014438; Expressed in retina and 105 other tissues.
DR ExpressionAtlas; Q08E31; baseline.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0071565; C:nBAF complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS: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; IEA:Ensembl.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IBA:GO_Central.
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; ISS:UniProtKB.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 2: Evidence at transcript level;
KW Activator; Calcium; Centromere; Chromatin regulator; Chromosome;
KW Kinetochore; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..402
FT /note="Calcium-responsive transactivator"
FT /id="PRO_0000391345"
FT REGION 1..148
FT /note="N-terminal auto-inhibitory domain; necessary for
FT interaction with SMARCA4/BRG1"
FT /evidence="ECO:0000250"
FT REGION 72..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..237
FT /note="Methionine-rich intra-molecular domain"
FT /evidence="ECO:0000250"
FT REGION 195..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..323
FT /note="MFD domain"
FT /evidence="ECO:0000250"
FT REGION 262..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..402
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 393..402
FT /note="Necessary for interaction with CREBBP and for the
FT recruitment of CREBBP to the nuclear bodies"
FT /evidence="ECO:0000250"
FT MOTIF 50..53
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 359..362
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 377..385
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 397..400
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 43329 MW; B26C099261ABF431 CRC64;
MSVAFASARP RGKGEVTQQT IQKMLDENHH LIQCILDYQS KGKTAECTQY QQILHRNLVY
LATIADSNQN MQSLLPAPPT QSMTLGPGGL SQSGSAQGLH SQGSLSDAIG AGLPPSSLMQ
AQIGNGPNHV SLQQTAQSTL PTTSMSMSGS GHGSGPGYSH SGPASQSVPL QSQGAISNYV
SRANINMQSN PVSMMHQQAA SSHYSAAQGG SQHYQGQSMA MMGQSGQGGG VMGQRPMAPY
RPSQQGSSQQ YLGQEEYYGG EQYGHGQAAS EPMSQQYYPD GHGDYAYQPA SYTDQSYDRS
FEDSTQHYYE GGNSQYSQQQ TGYQQGTAQQ QTYSQQQYPN QQSYPGQQQG YGPAQGAPSQ
YSSYQQGQGQ QYGSYRASQT GPSTQQQRPY GYEQGQYGNY QQ
