CRBL2_MOUSE
ID CRBL2_MOUSE Reviewed; 123 AA.
AC Q32M00; Q8BR67;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=cAMP-responsive element-binding protein-like 2;
GN Name=Crebl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREB1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21728997; DOI=10.1042/bj20101475;
RA Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.;
RT "CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1
RT adipocytes.";
RL Biochem. J. 439:27-38(2011).
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. {ECO:0000269|PubMed:21728997}.
CC -!- SUBUNIT: Interacts with CREB1; regulates CREB1 phosphorylation,
CC stability and transcriptional activity. {ECO:0000269|PubMed:21728997}.
CC -!- INTERACTION:
CC Q32M00; Q01147: Creb1; NbExp=4; IntAct=EBI-5314489, EBI-2291098;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21728997}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in adipose
CC tissue, skeletal muscle, and liver (at protein level).
CC {ECO:0000269|PubMed:21728997}.
CC -!- INDUCTION: Up-regulated during preadipocyte differentiation (at protein
CC level). {ECO:0000269|PubMed:21728997}.
CC -!- PTM: Phosphorylated by AMPK. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AK045467; BAC32383.1; -; mRNA.
DR EMBL; BC109358; AAI09359.1; -; mRNA.
DR EMBL; BC109359; AAI09360.1; -; mRNA.
DR CCDS; CCDS20640.1; -.
DR RefSeq; NP_808355.1; NM_177687.3.
DR RefSeq; XP_011239631.1; XM_011241329.2.
DR AlphaFoldDB; Q32M00; -.
DR SMR; Q32M00; -.
DR IntAct; Q32M00; 1.
DR STRING; 10090.ENSMUSP00000035304; -.
DR PaxDb; Q32M00; -.
DR PRIDE; Q32M00; -.
DR DNASU; 232430; -.
DR GeneID; 232430; -.
DR KEGG; mmu:232430; -.
DR UCSC; uc009ekt.1; mouse.
DR CTD; 1389; -.
DR MGI; MGI:1889385; Crebl2.
DR eggNOG; KOG4515; Eukaryota.
DR InParanoid; Q32M00; -.
DR OrthoDB; 1551209at2759; -.
DR PhylomeDB; Q32M00; -.
DR TreeFam; TF323305; -.
DR BioGRID-ORCS; 232430; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Crebl2; mouse.
DR PRO; PR:Q32M00; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q32M00; protein.
DR GO; GO:0005634; C:nucleus; IDA: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; IMP:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP: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 1: Evidence at protein 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_0000318193"
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 92..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 103
FT /note="N -> S (in Ref. 1; BAC32383)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="N -> D (in Ref. 1; BAC32383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 14002 MW; A1B85B8AA582D62E CRC64;
MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY LEELVSSRER
AICALREELE MYKQWCMAMD QGKIPSEIRA LLTGEEQSKP QQNSSRHPKA GKTDANTNSL
VGN
