CRBL2_RAT
ID CRBL2_RAT Reviewed; 123 AA.
AC Q5BJU6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=cAMP-responsive element-binding protein-like 2;
GN Name=Crebl2;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable regulator of CREB1 transcriptional activity which is
CC involved in adipose cells differentiation. May also play a regulatory
CC role in the cell cycle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CREB1; regulates CREB1 phosphorylation,
CC stability and transcriptional activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by AMPK. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; BC091323; AAH91323.1; -; mRNA.
DR RefSeq; NP_001015027.1; NM_001015027.1.
DR AlphaFoldDB; Q5BJU6; -.
DR SMR; Q5BJU6; -.
DR STRING; 10116.ENSRNOP00000009324; -.
DR PaxDb; Q5BJU6; -.
DR Ensembl; ENSRNOT00000119142; ENSRNOP00000094879; ENSRNOG00000067300.
DR GeneID; 362453; -.
DR KEGG; rno:362453; -.
DR UCSC; RGD:1309502; rat.
DR CTD; 1389; -.
DR RGD; 1309502; Crebl2.
DR eggNOG; KOG4515; Eukaryota.
DR GeneTree; ENSGT00390000005388; -.
DR InParanoid; Q5BJU6; -.
DR OrthoDB; 1551209at2759; -.
DR PhylomeDB; Q5BJU6; -.
DR TreeFam; TF323305; -.
DR PRO; PR:Q5BJU6; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR039250; CREBL2/REPTOR-BP.
DR PANTHER; PTHR21051; PTHR21051; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..123
FT /note="cAMP-responsive element-binding protein-like 2"
FT /id="PRO_0000318194"
FT DOMAIN 23..86
FT /note="bZIP"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..60
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT REGION 62..69
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT REGION 93..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 14019 MW; F1978A47A582D62C CRC64;
MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY LEELVSSRER
AICALREELE MYKQWCMAMD QGKIPSEIRA LLTGEEQNKS QQNSSRHPKA GKTDANTNSL
VGN