DDIT3_MOUSE
ID DDIT3_MOUSE Reviewed; 168 AA.
AC P35639; Q91YW9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA damage-inducible transcript 3 protein;
DE Short=DDIT-3;
DE AltName: Full=C/EBP zeta;
DE AltName: Full=C/EBP-homologous protein {ECO:0000303|PubMed:21285359};
DE Short=CHOP {ECO:0000303|PubMed:21285359};
DE AltName: Full=C/EBP-homologous protein 10;
DE Short=CHOP-10;
DE AltName: Full=CCAAT/enhancer-binding protein homologous protein;
DE AltName: Full=Growth arrest and DNA-damage-inducible protein GADD153;
GN Name=Ddit3; Synonyms=Chop {ECO:0000303|PubMed:21285359}, Chop10, Gadd153;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SWR/J;
RX PubMed=1547942; DOI=10.1101/gad.6.3.439;
RA Ron D., Habener J.F.;
RT "CHOP, a novel developmentally regulated nuclear protein that dimerizes
RT with transcription factors C/EBP and LAP and functions as a dominant-
RT negative inhibitor of gene transcription.";
RL Genes Dev. 6:439-453(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 PHOSPHORYLATION AT SER-78 AND SER-81.
RX PubMed=8650547; DOI=10.1126/science.272.5266.1347;
RA Wang X.Z., Ron D.;
RT "Stress-induced phosphorylation and activation of the transcription factor
RT CHOP (GADD153) by p38 MAP Kinase.";
RL Science 272:1347-1349(1996).
RN [4]
RP FUNCTION.
RX PubMed=12706815; DOI=10.1016/s0014-5793(03)00283-7;
RA Hattori T., Ohoka N., Hayashi H., Onozaki K.;
RT "C/EBP homologous protein (CHOP) up-regulates IL-6 transcription by
RT trapping negative regulating NF-IL6 isoform.";
RL FEBS Lett. 541:33-39(2003).
RN [5]
RP PHOSPHORYLATION AT SER-14; SER-15; SER-30 AND SER-31, AND MUTAGENESIS OF
RP SER-14; SER-15; SER-30 AND SER-31.
RX PubMed=12876286; DOI=10.1074/jbc.m306404200;
RA Ubeda M., Habener J.F.;
RT "CHOP transcription factor phosphorylation by casein kinase 2 inhibits
RT transcriptional activation.";
RL J. Biol. Chem. 278:40514-40520(2003).
RN [6]
RP FUNCTION.
RX PubMed=14684614; DOI=10.1210/en.2003-0868;
RA Pereira R.C., Delany A.M., Canalis E.;
RT "CCAAT/enhancer binding protein homologous protein (DDIT3) induces
RT osteoblastic cell differentiation.";
RL Endocrinology 145:1952-1960(2004).
RN [7]
RP FUNCTION.
RX PubMed=15601821; DOI=10.1101/gad.1250704;
RA Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R.,
RA Nagata K., Harding H.P., Ron D.;
RT "CHOP induces death by promoting protein synthesis and oxidation in the
RT stressed endoplasmic reticulum.";
RL Genes Dev. 18:3066-3077(2004).
RN [8]
RP FUNCTION.
RX PubMed=15775988; DOI=10.1038/sj.emboj.7600596;
RA Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.;
RT "TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway
RT and is involved in cell death.";
RL EMBO J. 24:1243-1255(2005).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=16670335; DOI=10.4049/jimmunol.176.10.6245;
RA Endo M., Mori M., Akira S., Gotoh T.;
RT "C/EBP homologous protein (CHOP) is crucial for the induction of caspase-11
RT and the pathogenesis of lipopolysaccharide-induced inflammation.";
RL J. Immunol. 176:6245-6253(2006).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=19752026; DOI=10.1083/jcb.200904060;
RA Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.;
RT "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate
RT receptor activity in endoplasmic reticulum stress-induced apoptosis.";
RL J. Cell Biol. 186:783-792(2009).
RN [11]
RP INDUCTION.
RX PubMed=19855386; DOI=10.1038/ncb1996;
RA Woo C.W., Cui D., Arellano J., Dorweiler B., Harding H., Fitzgerald K.A.,
RA Ron D., Tabas I.;
RT "Adaptive suppression of the ATF4-CHOP branch of the unfolded protein
RT response by toll-like receptor signalling.";
RL Nat. Cell Biol. 11:1473-1480(2009).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=19919955; DOI=10.1093/jb/mvp189;
RA Nakayama Y., Endo M., Tsukano H., Mori M., Oike Y., Gotoh T.;
RT "Molecular mechanisms of the LPS-induced non-apoptotic ER stress-CHOP
RT pathway.";
RL J. Biochem. 147:471-483(2010).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=21159964; DOI=10.1523/jneurosci.1598-10.2010;
RA Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S., Cregan S.P.;
RT "Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by
RT ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA.";
RL J. Neurosci. 30:16938-16948(2010).
RN [14]
RP INDUCTION.
RX PubMed=21285359; DOI=10.1074/jbc.m110.216093;
RA Palam L.R., Baird T.D., Wek R.C.;
RT "Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory
RT upstream ORF to enhance CHOP translation.";
RL J. Biol. Chem. 286:10939-10949(2011).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH HDAC1.
RX PubMed=22242125; DOI=10.1371/journal.pone.0029498;
RA Alter J., Bengal E.;
RT "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription
RT to delay myoblast differentiation.";
RL PLoS ONE 6:E29498-E29498(2011).
RN [16]
RP FUNCTION.
RX PubMed=22265908; DOI=10.1161/circulationaha.111.041830;
RA Loinard C., Zouggari Y., Rueda P., Ramkhelawon B., Cochain C., Vilar J.,
RA Recalde A., Richart A., Charue D., Duriez M., Mori M.,
RA Arenzana-Seisdedos F., Levy B.I., Heymes C., Silvestre J.S.;
RT "C/EBP homologous protein-10 (CHOP-10) limits postnatal neovascularization
RT through control of endothelial nitric oxide synthase gene expression.";
RL Circulation 125:1014-1026(2012).
RN [17]
RP FUNCTION, AND INTERACTION WITH ATF4.
RX PubMed=23624402; DOI=10.1038/ncb2738;
RA Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L.,
RA Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A.,
RA Kaufman R.J.;
RT "ER-stress-induced transcriptional regulation increases protein synthesis
RT leading to cell death.";
RL Nat. Cell Biol. 15:481-490(2013).
CC -!- FUNCTION: Multifunctional transcription factor in endoplasmic reticulum
CC (ER) stress response (PubMed:15601821, PubMed:19752026). Plays an
CC essential role in the response to a wide variety of cell stresses and
CC induces cell cycle arrest and apoptosis in response to ER stress
CC (PubMed:15601821, PubMed:19752026). Plays a dual role both as an
CC inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an
CC activator of other genes (PubMed:1547942). Acts as a dominant-negative
CC regulator of C/EBP-induced transcription: dimerizes with members of the
CC C/EBP family, impairs their association with C/EBP binding sites in the
CC promoter regions, and inhibits the expression of C/EBP regulated genes
CC (PubMed:1547942). Positively regulates the transcription of TRIB3, IL6,
CC IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and
CC ERO1L (PubMed:12706815, PubMed:15775988, PubMed:21159964,
CC PubMed:14684614, PubMed:19919955). Negatively regulates; expression of
CC BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine
CC synthetase (ASNS), CEBPA-dependent transcriptional activation of
CC hepcidin (HAMP) and CEBPB-mediated expression of peroxisome
CC proliferator-activated receptor gamma (PPARG) (By similarity). Together
CC with ATF4, mediates ER-mediated cell death by promoting expression of
CC genes involved in cellular amino acid metabolic processes, mRNA
CC translation and the unfolded protein response (UPR) in response to ER
CC stress (PubMed:22242125, PubMed:23624402). Inhibits the canonical Wnt
CC signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding
CC properties and repressing its transcriptional activity (By similarity).
CC Plays a regulatory role in the inflammatory response through the
CC induction of caspase-11 (CASP4/CASP11) which induces the activation of
CC caspase-1 (CASP1) and both these caspases increase the activation of
CC pro-IL1B to mature IL1B which is involved in the inflammatory response
CC (PubMed:16670335). Acts as a major regulator of postnatal
CC neovascularization through regulation of endothelial nitric oxide
CC synthase (NOS3)-related signaling (PubMed:22265908).
CC {ECO:0000250|UniProtKB:P35638, ECO:0000269|PubMed:12706815,
CC ECO:0000269|PubMed:14684614, ECO:0000269|PubMed:1547942,
CC ECO:0000269|PubMed:15601821, ECO:0000269|PubMed:15775988,
CC ECO:0000269|PubMed:16670335, ECO:0000269|PubMed:19752026,
CC ECO:0000269|PubMed:19919955, ECO:0000269|PubMed:21159964,
CC ECO:0000269|PubMed:22242125, ECO:0000269|PubMed:22265908,
CC ECO:0000269|PubMed:23624402}.
CC -!- SUBUNIT: Heterodimer. Interacts with TCF7L2/TCF4, EP300/P300, HDAC5 and
CC HDAC6 (By similarity). Interacts with TRIB3 which blocks its
CC association with EP300/P300 (By similarity). Interacts with FOXO3, and
CC CEBPB (By similarity). Interacts with ATF4 (PubMed:23624402). Interacts
CC with HDAC1 (PubMed:22242125). {ECO:0000250|UniProtKB:P35638,
CC ECO:0000269|PubMed:22242125, ECO:0000269|PubMed:23624402}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with isoform AltDDIT3 of DDIT3.
CC {ECO:0000250|UniProtKB:P35638}.
CC -!- INTERACTION:
CC P35639; Q06507: Atf4; NbExp=3; IntAct=EBI-10636142, EBI-77383;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1547942}. Nucleus
CC {ECO:0000269|PubMed:22242125}. Note=Present in the cytoplasm under non-
CC stressed conditions and ER stress leads to its nuclear accumulation.
CC {ECO:0000269|PubMed:22242125}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P35639-1; Sequence=Displayed;
CC Name=AltDDIT3;
CC IsoId=A0A2R8VHR8-1; Sequence=External;
CC -!- INDUCTION: [Isoform 1]: By various stress, such as oxidative stress,
CC amino-acid deprivation, hypoxia and ER stress (PubMed:16670335,
CC PubMed:19752026, PubMed:19855386, PubMed:19919955, PubMed:21159964,
CC PubMed:22242125). Specifically produced in response to stress: in
CC absence of stress, AltDDIT3, the upstream ORF of this bicistronic gene,
CC is translated, thereby preventing its translation (PubMed:21285359).
CC During ER stress, induced by a EIF2AK3/ATF4 pathway and/or ERN1/ATF6
CC pathway (PubMed:19855386, PubMed:21159964). Expression is suppressed by
CC TLR-TRIF signaling pathway during prolonged ER stress (PubMed:16670335,
CC PubMed:19752026, PubMed:19855386, PubMed:19919955, PubMed:21159964,
CC PubMed:22242125). {ECO:0000269|PubMed:16670335,
CC ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:19855386,
CC ECO:0000269|PubMed:19919955, ECO:0000269|PubMed:21159964,
CC ECO:0000269|PubMed:21285359, ECO:0000269|PubMed:22242125}.
CC -!- DOMAIN: The N-terminal region is necessary for its proteasomal
CC degradation, transcriptional activity and interaction with EP300/P300.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at serine residues by MAPK14 enhances its
CC transcriptional activation activity while phosphorylation at serine
CC residues by CK2 inhibits its transcriptional activation activity.
CC {ECO:0000269|PubMed:12876286, ECO:0000269|PubMed:8650547}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X67083; CAA47465.1; -; mRNA.
DR EMBL; BC013718; AAH13718.1; -; mRNA.
DR CCDS; CCDS24236.1; -. [P35639-1]
DR PIR; S26148; S26148.
DR RefSeq; NP_001277112.1; NM_001290183.1. [P35639-1]
DR RefSeq; NP_031863.3; NM_007837.4. [P35639-1]
DR RefSeq; XP_006513260.1; XM_006513197.3. [P35639-1]
DR AlphaFoldDB; P35639; -.
DR SMR; P35639; -.
DR BioGRID; 199078; 4.
DR ComplexPortal; CPX-65; bZIP transcription factor complex, Cebpa-Ddit3.
DR ComplexPortal; CPX-66; bZIP transcription factor complex, Cebpb-Ddit3.
DR DIP; DIP-60705N; -.
DR IntAct; P35639; 3.
DR STRING; 10090.ENSMUSP00000026475; -.
DR BindingDB; P35639; -.
DR ChEMBL; CHEMBL2146304; -.
DR iPTMnet; P35639; -.
DR PhosphoSitePlus; P35639; -.
DR MaxQB; P35639; -.
DR PaxDb; P35639; -.
DR PRIDE; P35639; -.
DR ProteomicsDB; 279512; -. [P35639-1]
DR Antibodypedia; 4408; 1040 antibodies from 43 providers.
DR DNASU; 13198; -.
DR Ensembl; ENSMUST00000026475; ENSMUSP00000026475; ENSMUSG00000025408. [P35639-1]
DR GeneID; 13198; -.
DR KEGG; mmu:13198; -.
DR UCSC; uc007hiy.2; mouse. [P35639-1]
DR CTD; 1649; -.
DR MGI; MGI:109247; Ddit3.
DR VEuPathDB; HostDB:ENSMUSG00000025408; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00390000006305; -.
DR InParanoid; P35639; -.
DR OMA; QCPARAG; -.
DR OrthoDB; 1338770at2759; -.
DR PhylomeDB; P35639; -.
DR TreeFam; TF105006; -.
DR BioGRID-ORCS; 13198; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Ddit3; mouse.
DR PRO; PR:P35639; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P35639; protein.
DR Bgee; ENSMUSG00000025408; Expressed in granulocyte and 259 other tissues.
DR ExpressionAtlas; P35639; baseline and differential.
DR Genevisible; P35639; MM.
DR GO; GO:1990622; C:CHOP-ATF3 complex; ISO:MGI.
DR GO; GO:1990617; C:CHOP-ATF4 complex; ISO:MGI.
DR GO; GO:0036488; C:CHOP-C/EBP complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
DR GO; GO:0009948; P:anterior/posterior axis specification; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0060840; P:artery development; IMP:MGI.
DR GO; GO:0001955; P:blood vessel maturation; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
DR GO; GO:0006983; P:ER overload response; IMP:MGI.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010467; P:gene expression; IGI:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:1990442; P:intrinsic apoptotic signaling pathway in response to nitrosative stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0032792; P:negative regulation of CREB transcription factor activity; ISO:MGI.
DR GO; GO:2000016; P:negative regulation of determination of dorsal identity; IDA:BHF-UCL.
DR GO; GO:0043392; P:negative regulation of DNA binding; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IGI:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:MGI.
DR GO; GO:0032713; P:negative regulation of interleukin-4 production; ISO:MGI.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:ParkinsonsUK-UCL.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0036119; P:response to platelet-derived growth factor; IMP:MGI.
DR GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IGI:MGI.
DR GO; GO:1904738; P:vascular associated smooth muscle cell migration; IMP:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016670; DNA_damage_induc_transcript_3.
DR PANTHER; PTHR16833; PTHR16833; 1.
DR PIRSF; PIRSF016571; C/EBPzeta_CHOP_DDIT3; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative initiation; Apoptosis; Cell cycle; Cytoplasm;
KW DNA-binding; Growth arrest; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Stress response; Transcription; Transcription regulation;
KW Ubl conjugation; Unfolded protein response; Wnt signaling pathway.
FT CHAIN 1..168
FT /note="DNA damage-inducible transcript 3 protein"
FT /id="PRO_0000076643"
FT DOMAIN 98..161
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 10..26
FT /note="N-terminal"
FT /evidence="ECO:0000250"
FT REGION 10..18
FT /note="Interaction with TRIB3"
FT /evidence="ECO:0000250"
FT REGION 34..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..129
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 133..147
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 34..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12876286"
FT MOD_RES 15
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12876286"
FT MOD_RES 30
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12876286"
FT MOD_RES 31
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12876286"
FT MOD_RES 78
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000269|PubMed:8650547"
FT MOD_RES 81
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000269|PubMed:8650547"
FT MUTAGEN 14
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12876286"
FT MUTAGEN 15
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12876286"
FT MUTAGEN 30
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12876286"
FT MUTAGEN 31
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12876286"
FT CONFLICT 34
FT /note="I -> N (in Ref. 2; AAH13718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 19189 MW; CA423B79512F33AB CRC64;
MAAESLPFTL ETVSSWELEA WYEDLQEVLS SDEIGGTYIS SPGNEEEESK TFTTLDPASL
AWLTEEPGPT EVTRTSQSPR SPDSSQSSMA QEEEEEEQGR TRKRKQSGQC PARPGKQRMK
EKEQENERKV AQLAEENERL KQEIERLTRE VETTRRALID RMVSLHQA
