ATF3_RAT
ID ATF3_RAT Reviewed; 181 AA.
AC P29596;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-3;
DE Short=cAMP-dependent transcription factor ATF-3;
DE AltName: Full=Activating transcription factor 3;
DE AltName: Full=Liver regeneration factor 1 {ECO:0000303|PubMed:1902565};
DE Short=LRF-1 {ECO:0000303|PubMed:1902565};
GN Name=Atf3; Synonyms=Lrf1 {ECO:0000303|PubMed:1902565};
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=1902565; DOI=10.1073/pnas.88.9.3511;
RA Hsu J.-C., Laz T., Mohn K.L., Taub R.;
RT "Identification of LRF-1, a leucine-zipper protein that is rapidly and
RT highly induced in regenerating liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3511-3515(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19913522; DOI=10.1016/j.brainres.2009.11.011;
RA Reid A.J., Welin D., Wiberg M., Terenghi G., Novikov L.N.;
RT "Peripherin and ATF3 genes are differentially regulated in regenerating and
RT non-regenerating primary sensory neurons.";
RL Brain Res. 1310:1-7(2010).
CC -!- FUNCTION: This protein binds the cAMP response element (CRE)
CC (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral
CC and cellular promoters. Represses transcription from promoters with ATF
CC sites (By similarity). It may repress transcription by stabilizing the
CC binding of inhibitory cofactors at the promoter (By similarity).
CC {ECO:0000250|UniProtKB:P18847, ECO:0000250|UniProtKB:Q60765}.
CC -!- SUBUNIT: ATF3 alone can bind DNA, but it preferentially forms
CC heteromeric complexes with JUN and JUNB and does not interact with FOS.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Expressed in tissues containing skeletal muscle or
CC smooth muscle (PubMed:1902565). Expressed in cutaneous and muscular
CC sensory neurons (PubMed:19913522). {ECO:0000269|PubMed:1902565,
CC ECO:0000269|PubMed:19913522}.
CC -!- INDUCTION: Up-regulated in regenerating neurons after nerve injury
CC (PubMed:19913522). Rapidly and highly induced in regenerating liver and
CC mitogen-stimulated cells (PubMed:1902565). {ECO:0000269|PubMed:1902565,
CC ECO:0000269|PubMed:19913522}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; M63282; AAA41542.1; -; mRNA.
DR EMBL; BC078903; AAH78903.1; -; mRNA.
DR PIR; A39382; A39382.
DR RefSeq; NP_037044.1; NM_012912.2.
DR AlphaFoldDB; P29596; -.
DR SMR; P29596; -.
DR CORUM; P29596; -.
DR STRING; 10116.ENSRNOP00000005085; -.
DR PaxDb; P29596; -.
DR Ensembl; ENSRNOT00000005085; ENSRNOP00000005085; ENSRNOG00000003745.
DR GeneID; 25389; -.
DR KEGG; rno:25389; -.
DR CTD; 467; -.
DR RGD; 2165; Atf3.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000156376; -.
DR InParanoid; P29596; -.
DR OMA; PLEMSVM; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; P29596; -.
DR TreeFam; TF326301; -.
DR PRO; PR:P29596; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003745; Expressed in jejunum and 19 other tissues.
DR Genevisible; P29596; RN.
DR GO; GO:1990622; C:CHOP-ATF3 complex; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001709; P:cell fate determination; TAS:RGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029812; ATF3.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF23; PTHR23351:SF23; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..181
FT /note="Cyclic AMP-dependent transcription factor ATF-3"
FT /id="PRO_0000076583"
FT DOMAIN 86..149
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 76..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..110
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 114..142
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18847"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18847"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18847"
SQ SEQUENCE 181 AA; 20764 MW; E36971E1A96F262B CRC64;
MMLQHPGQVS ASEVSATAIV PCLSPPGSLV FEDFANLTPF VKEELRFAIQ NKHLCHRMSS
ALESVTINNR PLEMSVTKSE VAPEEDERKR RRRERNKIAA AKCRNKKKEK TECLQKESEK
LESVNAELKA QIEELKNEKQ HLIYMLNLHR PTCIVRAQNG RTPEDERNLF IQQIKEGTLQ
S
