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DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA-damage-inducible protein GADD153)

 DDIT3_CRIGR             Reviewed;         168 AA.
P14607;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
30-AUG-2017, entry version 89.
RecName: Full=DNA damage-inducible transcript 3 protein;
Short=DDIT-3;
AltName: Full=C/EBP zeta;
AltName: Full=C/EBP-homologous protein;
Short=CHOP;
AltName: Full=C/EBP-homologous protein 10;
Short=CHOP-10;
AltName: Full=CCAAT/enhancer-binding protein homologous protein;
AltName: Full=Growth arrest and DNA-damage-inducible protein GADD153;
Name=DDIT3; Synonyms=CHOP, CHOP10, GADD153;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=2573827; DOI=10.1128/MCB.9.10.4196;
Fornace A.J. Jr., Nebert D.W., Hollander M.C., Luethy J.D.,
Papathanasiou M., Fargnoli J., Holbrook N.J.;
"Mammalian genes coordinately regulated by growth arrest signals and
DNA-damaging agents.";
Mol. Cell. Biol. 9:4196-4203(1989).
-!- FUNCTION: Multifunctional transcription factor in ER stress
response. Plays an essential role in the response to a wide
variety of cell stresses and induces cell cycle arrest and
apoptosis in response to ER stress. Plays a dual role both as an
inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and
as an activator of other genes. Acts as a dominant-negative
regulator of C/EBP-induced transcription: dimerizes with members
of the C/EBP family, impairs their association with C/EBP binding
sites in the promoter regions, and inhibits the expression of
C/EBP regulated genes. Positively regulates the transcription of
TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA,
BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2
and MYOD1, ATF4-dependent transcriptional activation of asparagine
synthetase (ASNS), CEBPA-dependent transcriptional activation of
hepcidin (HAMP) and CEBPB-mediated expression of peroxisome
proliferator-activated receptor gamma (PPARG). Inhibits the
canonical Wnt signaling pathway by binding to TCF7L2/TCF4,
impairing its DNA-binding properties and repressing its
transcriptional activity. Plays a regulatory role in the
inflammatory response through the induction of caspase-11
(CASP4/CASP11) which induces the activation of caspase-1 (CASP1)
and both these caspases increase the activation of pro-IL1B to
mature IL1B which is involved in the inflammatory response (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer (By similarity). Interacts with TCF7L2/TCF4,
EP300/P300, HDAC1, HDAC5 and HDAC6. Interacts with TRIB3 which
blocks its association with EP300/P300. Interacts with FOXO3,
CEBPB and ATF4 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Present in the
cytoplasm under non-stressed conditions and ER stress leads to its
nuclear accumulation. {ECO:0000250}.
-!- DOMAIN: The N-terminal region is necessary for its proteasomal
degradation, transcriptional activity and interaction with
EP300/P300. {ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
{ECO:0000250}.
-!- PTM: Phosphorylation at serine residues by MAPK14 enhances its
transcriptional activation activity while phosphorylation at
serine residues by CK2 inhibits its transcriptional activation
activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; M29238; AAA36982.1; -; mRNA.
HOVERGEN; HBG051328; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0001955; P:blood vessel maturation; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR016670; DNA_damage_induc_transcript_3.
PANTHER; PTHR16833; PTHR16833; 1.
PIRSF; PIRSF016571; C/EBPzeta_CHOP_DDIT3; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
2: Evidence at transcript level;
Activator; Apoptosis; Cell cycle; Cytoplasm; DNA-binding;
Growth arrest; Nucleus; Phosphoprotein; Repressor; Stress response;
Transcription; Transcription regulation; Ubl conjugation;
Unfolded protein response; Wnt signaling pathway.
CHAIN 1 168 DNA damage-inducible transcript 3
protein.
/FTId=PRO_0000076641.
DOMAIN 98 161 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 10 26 N-terminal. {ECO:0000250}.
REGION 10 18 Interaction with TRIB3. {ECO:0000250}.
REGION 101 129 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 133 147 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 92 95 Poly-Glu.
MOD_RES 14 14 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 15 15 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 30 30 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 31 31 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 78 78 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 81 81 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P35639}.
SEQUENCE 168 AA; 18831 MW; 5FD5A2A6C5228771 CRC64;
MAAESLPFTL ETVSSWELEA WYEDLQEVLS SDENGGPYSS SLGNEEGESK TFTTLDPASL
AWLTEEPGPA EVTSSSQSPR SPDSSQSCMA QEEEEDQGRT RKRKQSGQCP ARGTGKQRMK
EKEQENERKV AQLAEENERL KQEIERLTRE VEATRPGSDR PHVNLQQV


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