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Cyclic AMP-dependent transcription factor ATF-5 (cAMP-dependent transcription factor ATF-5) (Activating transcription factor 5) (Transcription factor ATFx)

 ATF5_RAT                Reviewed;         281 AA.
Q6P788; Q8CIT6;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-5;
Short=cAMP-dependent transcription factor ATF-5;
AltName: Full=Activating transcription factor 5;
AltName: Full=Transcription factor ATFx;
Name=Atf5; Synonyms=Atfx;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, INDUCTION, AND
FUNCTION.
STRAIN=New England Deaconess Hospital;
PubMed=12805299;
Angelastro J.M., Ignatova T.N., Kukekov V.G., Steindler D.A.,
Stengren G.B., Mendelsohn C., Greene L.A.;
"Regulated expression of ATF5 is required for the progression of
neural progenitor cells to neurons.";
J. Neurosci. 23:4590-4600(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND DNA-BINDING.
PubMed=19531563; DOI=10.1158/1541-7786.MCR-08-0365;
Li G., Li W., Angelastro J.M., Greene L.A., Liu D.X.;
"Identification of a novel DNA binding site and a transcriptional
target for activating transcription factor 5 in c6 glioma and mcf-7
breast cancer cells.";
Mol. Cancer Res. 7:933-943(2009).
[4]
FUNCTION, AND INDUCTION BY PRO-APOPTOTIC STIMULI.
PubMed=21212266; DOI=10.1074/jbc.M110.207639;
Dluzen D., Li G., Tacelosky D., Moreau M., Liu D.X.;
"BCL-2 is a downstream target of ATF5 that mediates the prosurvival
function of ATF5 in a cell type-dependent manner.";
J. Biol. Chem. 286:7705-7713(2011).
[5]
FUNCTION, INTERACTION WITH EP300, ACETYLATION AT LYS-29, AND
MUTAGENESIS OF LYS-29.
PubMed=21791614; DOI=10.1128/MCB.05887-11;
Liu D.X., Qian D., Wang B., Yang J.M., Lu Z.;
"p300-Dependent ATF5 acetylation is essential for Egr-1 gene
activation and cell proliferation and survival.";
Mol. Cell. Biol. 31:3906-3916(2011).
-!- FUNCTION: Transcription factor that either stimulates or represses
gene transcription through binding of different DNA regulatory
elements such as cAMP response element (CRE) (consensus: 5'-
GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE)
(consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid
response element (AARE), present in many viral and cellular
promoters. Critically involved, often in a cell type-dependent
manner, in cell survival, proliferation, and differentiation. Its
transcriptional activity is enhanced by CCND3 and slightly
inhibited by CDK4 (By similarity) (PubMed:19531563,
PubMed:21212266). Important regulator of the cerebral cortex
formation, functions in cerebral cortical neuroprogenitor cells to
maintain proliferation and to block differentiation into neurons.
Must be down-regulated in order for such cells to exit the cycle
and differentiate (By similarity) (PubMed:12805299). Participates
in the pathways by which SHH promotes cerebellar granule neuron
progenitor cells proliferation. Critical for survival of mature
olfactory sensory neurons (OSN), directs expression of OSN-
specific genes (By similarity). May be involved in osteogenic
differentiation. Promotes cell proliferation and survival by
inducing the expression of EGR1 sinergistically with ELK1. Once
acetylated by EP300, binds to ARE sequences on target genes
promoters, such as BCL2 and EGR1 (By similarity)
(PubMed:21791614). Plays an anti-apoptotic role through the
transcriptional regulation of BCL2, this function seems to be cell
type-dependent (By similarity). Cooperates with NR1I3/CAR in the
transcriptional activation of CYP2B6 in liver. In hepatic cells,
represses CRE-dependent transcription and inhibits proliferation
by blocking at G2/M phase. May act as a negative regulator of IL1B
transduction pathway in liver. Upon IL1B stimulus, cooperates with
NLK to activate the transactivation activity of C/EBP subfamily
members. Besides its function of transcription factor, acts as a
cofactor of CEBPB to activate CEBPA and promote adipocyte
differentiation. Regulates centrosome dynamics in a cell-
cycle- and centriole-age-dependent manner. Forms 9-foci
symmetrical ring scaffold around the mother centriole to control
centrosome function and the interaction between centrioles and
pericentriolar material (By similarity).
{ECO:0000250|UniProtKB:O70191, ECO:0000250|UniProtKB:Q6P788,
ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000269|PubMed:12805299,
ECO:0000269|PubMed:19531563, ECO:0000269|PubMed:21212266,
ECO:0000269|PubMed:21791614}.
-!- SUBUNIT: Binds DNA as a dimer. Interacts with PTP4A1/PRL-1 (By
similarity). Interacts with CCND3, but not with CCND1 or CCND2.
Interacts with HSPA1A or HSPA1B; the interaction protects ATF5
from degradation via proteasome-dependent and caspase-dependent
processes. Interacts (via C-terminal region) with NPM1 (via C-
terminal region); the interaction leads to loss of association
between HSPA1A or HSPA1B and ATF5 and promotes ATF5 degradation
via proteasome-dependent and caspase-dependent processes.
Interacts with NLK; the interaction stabilizes ATF5 at the protein
level in a kinase-independent manner. Interacts with alpha-
tubulin, gamma-tubulin members TUBGCP2 and TUBGCP4, PCNT; the
ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the
mother centriole and the pericentriolar material (PCM) in the
centrosome (By similarity). Interacts with CEBPB and EP300; EP300
is required for ATF5 and CEBPB interaction and DNA binding (By
similarity) (PubMed:21791614). {ECO:0000250|UniProtKB:O70191,
ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000269|PubMed:21791614}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2D1}.
Nucleus {ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000255|PROSITE-
ProRule:PRU00978}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000250|UniProtKB:Q9Y2D1}. Note=Actively
transported to the centrosome and accumulated in the
pericentriolar material (PCM) during G1 to M phase via a
microtubule-dependent mechanism. During late telophase and
cytokinesis, translocates from the centrosome to the midbody.
{ECO:0000250|UniProtKB:Q9Y2D1}.
-!- DEVELOPMENTAL STAGE: Expressed in embryonic nasal epithelium,
dorsal root, trigeminal ganglia, brain and liver. Within the
brain, expression is highest in the ventricular zone and decreased
in structures containing migrating and postmitotic neurons (at
protein level). {ECO:0000269|PubMed:12805299}.
-!- INDUCTION: Down-regulated during neuronal differentiation. Down-
regulated by pro-apoptotic stimuli (PubMed:21212266).
{ECO:0000269|PubMed:12805299, ECO:0000269|PubMed:21212266}.
-!- PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by
the proteasome. {ECO:0000250}.
-!- PTM: Acetylated at Lys-29 by EP300, the acetylation enhances the
interaction with CEBPB, DNA-binding and transactivation activity.
{ECO:0000269|PubMed:21791614}.
-!- PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by
the proteasome. Cisplatin inhibits ubiquitination and proteasome-
mediated degradation by inhibiting the interaction with CDC34.
Ubiquitination and degradation by the proteasome are inhibited by
NLK in a kinase-independent manner.
{ECO:0000250|UniProtKB:Q9Y2D1}.
-!- PTM: Phosphorylated by NLK, probably at Ser-92 and Ser-126.
{ECO:0000250|UniProtKB:Q9Y2D1}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; AY123225; AAM92263.1; -; mRNA.
EMBL; BC061786; AAH61786.1; -; mRNA.
RefSeq; NP_758839.3; NM_172336.3.
RefSeq; XP_006229042.1; XM_006228980.2.
RefSeq; XP_017444334.1; XM_017588845.1.
UniGene; Rn.229186; -.
ProteinModelPortal; Q6P788; -.
SMR; Q6P788; -.
BioGrid; 251873; 1.
STRING; 10116.ENSRNOP00000027260; -.
iPTMnet; Q6P788; -.
PhosphoSitePlus; Q6P788; -.
PaxDb; Q6P788; -.
GeneID; 282840; -.
KEGG; rno:282840; -.
UCSC; RGD:628902; rat.
CTD; 22809; -.
RGD; 628902; Atf5.
eggNOG; KOG4571; Eukaryota.
eggNOG; ENOG4111ZXT; LUCA.
HOGENOM; HOG000004844; -.
HOVERGEN; HBG003535; -.
InParanoid; Q6P788; -.
KO; K09044; -.
PhylomeDB; Q6P788; -.
TreeFam; TF316136; -.
PRO; PR:Q6P788; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:RGD.
GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; IDA:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0046605; P:regulation of centrosome cycle; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR029855; ATF-5.
InterPro; IPR004827; bZIP.
PANTHER; PTHR13044:SF3; PTHR13044:SF3; 2.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; Cytoskeleton;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 281 Cyclic AMP-dependent transcription factor
ATF-5.
/FTId=PRO_0000076588.
DOMAIN 207 270 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 21 Required for protein stabilization
induced by IL1B.
{ECO:0000250|UniProtKB:Q9Y2D1}.
REGION 119 216 Interaction with PTP4A1.
{ECO:0000250|UniProtKB:O70191}.
REGION 209 229 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 235 249 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 123 135 Poly-Pro.
MOD_RES 29 29 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:21791614}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D1}.
MUTAGEN 29 29 K->R: Not acetylated by EP300.
{ECO:0000269|PubMed:21791614}.
CONFLICT 193 193 L -> P (in Ref. 1; AAM92263).
{ECO:0000305}.
SEQUENCE 281 AA; 30205 MW; FBBF68FB44F9C601 CRC64;
MSLLATLGLE LDRALLPASG LGWLVDYGKL PLAPAPLGPY EVLGGALEGG LPGGGEPLAG
DGFSDWMTER VDFTALLPLE APLPPGTLPP PSPAPPDLEA MASLLKKELE QMEDFFLDAP
LLPPPSPPPP PPPAPSLPLP LPLPTFDLPQ PPTLDTLDLL AVYCRSEAGP GDSGLTTLPV
PQQPPPLAPL PSLSRPAPYP SPASTRGDRK QKKRDQNKSA ALRYRQRKRA EGEALEGECQ
GLEARNRELR ERAESVEREI QYVKDLLIEV YKARSQRTRS A


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