ID   CRBL2_BOVIN             Reviewed;         120 AA.
AC   Q0VD32;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=cAMP-responsive element-binding protein-like 2;
GN   Name=CREBL2;
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=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH BICP22, AND SUBCELLULAR LOCATION.
RX   PubMed=16352405; DOI=10.1016/j.vetmic.2005.11.046;
RA   Saydam O., Steiner F., Vogt B., Schwyzer M.;
RT   "Host cell targets of immediate-early protein BICP22 of bovine herpesvirus
RT   1.";
RL   Vet. Microbiol. 113:185-192(2006).
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.
CC   -!- SUBUNIT: Interacts with CREB1; regulates CREB1 phosphorylation,
CC       stability and transcriptional activity (By similarity). Interacts with
CC       immediate-early (IE) protein BICP22 of bovine herpesvirus-1 (BHV-1).
CC       {ECO:0000250, ECO:0000269|PubMed:16352405}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16352405}.
CC   -!- PTM: Phosphorylated by AMPK. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; BC119861; AAI19862.1; -; mRNA.
DR   RefSeq; NP_001069556.1; NM_001076088.1.
DR   AlphaFoldDB; Q0VD32; -.
DR   SMR; Q0VD32; -.
DR   IntAct; Q0VD32; 1.
DR   STRING; 9913.ENSBTAP00000040624; -.
DR   PaxDb; Q0VD32; -.
DR   PRIDE; Q0VD32; -.
DR   Ensembl; ENSBTAT00000043028; ENSBTAP00000040624; ENSBTAG00000011957.
DR   GeneID; 537195; -.
DR   KEGG; bta:537195; -.
DR   CTD; 1389; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011957; -.
DR   VGNC; VGNC:27699; CREBL2.
DR   eggNOG; KOG4515; Eukaryota.
DR   GeneTree; ENSGT00390000005388; -.
DR   HOGENOM; CLU_134161_0_0_1; -.
DR   InParanoid; Q0VD32; -.
DR   OMA; DQGRMPE; -.
DR   OrthoDB; 1551209at2759; -.
DR   TreeFam; TF323305; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000011957; Expressed in adenohypophysis and 104 other tissues.
DR   GO; GO:0016604; C:nuclear body; IDA:AgBase.
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   1: Evidence at protein level;
KW   Activator; Differentiation; DNA-binding; Host-virus interaction; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..120
FT                   /note="cAMP-responsive element-binding protein-like 2"
FT                   /id="PRO_0000318191"
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..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  13787 MW;  CC91B2D226D0B4A1 CRC64;
     MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY LEELVSSRER
     AICALREELE MYKQWCMAMD QGKIPSEIKA LLTGEEQSKS QQNSSRHMKA GKTDANSNSW