CEBPG_BOVIN
ID CEBPG_BOVIN Reviewed; 149 AA.
AC Q3T0B9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=CCAAT/enhancer-binding protein gamma;
DE Short=C/EBP gamma;
GN Name=CEBPG;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that binds to the promoter and the
CC enhancer regions of target genes. Binds to the enhancer element PRE-I
CC (positive regulatory element-I) of the IL-4 gene. Binds to the promoter
CC and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a
CC cis-acting element in the G-CSF gene promoter.
CC {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53567,
CC ECO:0000250|UniProtKB:P53568}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with
CC CEBPA and CEBPB. Interacts with ZNF638; this interaction increases
CC transcriptional activation. {ECO:0000250|UniProtKB:P26801,
CC ECO:0000250|UniProtKB:P53568}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; BC102461; AAI02462.1; -; mRNA.
DR RefSeq; NP_001029973.1; NM_001034801.1.
DR RefSeq; XP_010813108.1; XM_010814806.2.
DR AlphaFoldDB; Q3T0B9; -.
DR SMR; Q3T0B9; -.
DR STRING; 9913.ENSBTAP00000023345; -.
DR PaxDb; Q3T0B9; -.
DR GeneID; 617530; -.
DR KEGG; bta:617530; -.
DR CTD; 1054; -.
DR eggNOG; KOG3119; Eukaryota.
DR HOGENOM; CLU_146813_0_0_1; -.
DR InParanoid; Q3T0B9; -.
DR OrthoDB; 1532157at2759; -.
DR TreeFam; TF105009; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..149
FT /note="CCAAT/enhancer-binding protein gamma"
FT /id="PRO_0000247011"
FT DOMAIN 62..125
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..92
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 REGION 128..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar 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 149 AA; 16386 MW; F31B3F730F45A552 CRC64;
MSKVSQQNST PGVNGISVIH TQAHASGLQQ VPQLVPAGPG GGGKAVPPSK QSKKSSPMDR
NSDEYRQRRE RNNMAVKKSR LKSKQKAQDT LQRVNQLKEE NERLEAKIKL LTKELSVLKD
LFLEHAHNLA DNVQPSSTEN TTNPDKAGQ
