CEBPG_RAT
ID CEBPG_RAT Reviewed; 150 AA.
AC P26801;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=CCAAT/enhancer-binding protein gamma;
DE Short=C/EBP gamma;
GN Name=Cebpg;
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, AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1377818; DOI=10.1093/nar/20.12.3091;
RA Thomassin H., Hamel D., Bernier D., Guertin M., Belanger L.;
RT "Molecular cloning of two C/EBP-related proteins that bind to the promoter
RT and the enhancer of the alpha 1-fetoprotein gene. Further analysis of C/EBP
RT beta and C/EBP gamma.";
RL Nucleic Acids Res. 20:3091-3098(1992).
CC -!- FUNCTION: Transcription factor that binds to the promoter and the
CC enhancer regions of target genes. Binds to the promoter and the
CC enhancer of the alpha-1-fetoprotein gene (PubMed:1377818). Binds to the
CC enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene
CC (By similarity). Binds to the promoter and the enhancer of the
CC immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the
CC G-CSF gene promoter (By similarity). {ECO:0000250|UniProtKB:P53567,
CC ECO:0000250|UniProtKB:P53568, ECO:0000269|PubMed:1377818}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with
CC CEBPA and CEBPB (PubMed:1377818). Interacts with ZNF638; this
CC interaction increases transcriptional activation (By similarity).
CC {ECO:0000250|UniProtKB:P53568, ECO:0000269|PubMed:1377818}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:1377818}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45745.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X64403; CAA45745.1; ALT_INIT; mRNA.
DR PIR; S26300; S26300.
DR RefSeq; NP_036963.1; NM_012831.1.
DR AlphaFoldDB; P26801; -.
DR SMR; P26801; -.
DR BioGRID; 247340; 3.
DR STRING; 10116.ENSRNOP00000028703; -.
DR iPTMnet; P26801; -.
DR PhosphoSitePlus; P26801; -.
DR PaxDb; P26801; -.
DR PRIDE; P26801; -.
DR GeneID; 25301; -.
DR KEGG; rno:25301; -.
DR UCSC; RGD:2330; rat.
DR CTD; 1054; -.
DR RGD; 2330; Cebpg.
DR VEuPathDB; HostDB:ENSRNOG00000021144; -.
DR eggNOG; KOG3119; Eukaryota.
DR HOGENOM; CLU_146813_0_0_1; -.
DR InParanoid; P26801; -.
DR OMA; HAHNFAD; -.
DR OrthoDB; 1532157at2759; -.
DR PhylomeDB; P26801; -.
DR TreeFam; TF105009; -.
DR PRO; PR:P26801; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021144; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; P26801; baseline and differential.
DR Genevisible; P26801; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0044377; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding, bending; IDA:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IEP:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; ISO:RGD.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEP:RGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..150
FT /note="CCAAT/enhancer-binding protein gamma"
FT /id="PRO_0000076630"
FT DOMAIN 62..125
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 27..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..93
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 97..118
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 56..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P53567"
SQ SEQUENCE 150 AA; 16388 MW; B7B1686652E52326 CRC64;
MSKLSQPAST AGVNGISVIH TQAHASGLQQ VPQLVPAGPG GGGKAVPPSK QSKKSSPMDR
NSDEYRQRRE RNNMAVKKSR LKSKQKAQDT LQRVNQLKEE NERLEAKIKL LTKELSVLKD
LFLEHAHNLA DNVQPISTET TVANSDNTGQ
