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Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4)

 ATF4_BOVIN              Reviewed;         348 AA.
Q3ZCH6;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
25-OCT-2017, entry version 92.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-4;
Short=cAMP-dependent transcription factor ATF-4;
AltName: Full=Activating transcription factor 4;
Name=ATF4 {ECO:0000250|UniProtKB:P18848};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1] {ECO:0000312|EMBL:AAI02237.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford {ECO:0000312|EMBL:AAI02237.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAI02237.1};
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305}
INTERACTION WITH CEP290.
PubMed=16682973; DOI=10.1038/ng1786;
Sayer J.A., Otto E.A., O'toole J.F., Nurnberg G., Kennedy M.A.,
Becker C., Hennies H.C., Helou J., Attanasio M., Fausett B.V.,
Utsch B., Khanna H., Liu Y., Drummond I., Kawakami I., Kusakabe T.,
Tsuda M., Ma L., Lee H., Larson R.G., Allen S.J., Wilkinson C.J.,
Nigg E.A., Shou C., Lillo C., Williams D.S., Hoppe B., Kemper M.J.,
Neuhaus T., Parisi M.A., Glass I.A., Petry M., Kispert A., Gloy J.,
Ganner A., Walz G., Zhu X., Goldman D., Nurnberg P., Swaroop A.,
Leroux M.R., Hildebrandt F.;
"The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome
and activates transcription factor ATF4.";
Nat. Genet. 38:674-681(2006).
-!- FUNCTION: Transcriptional activator. Binds the cAMP response
element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence
present in many viral and cellular promoters. Cooperates with
FOXO1 in osteoblasts to regulate glucose homeostasis through
suppression of beta-cell production and decrease in insulin
production. Regulates the induction of DDIT3/CHOP and asparagine
synthetase (ASNS) in response to endoplasmic reticulum (ER)
stress. In concert with DDIT3/CHOP, activates the transcription of
TRIB3 and promotes ER stress-induced neuronal apoptosis by
regulating the transcriptional induction of BBC3/PUMA. Activates
transcription of SIRT4. Regulates the circadian expression of the
core clock component PER2 and the serotonin transporter SLC6A4.
Binds in a circadian time-dependent manner to the cAMP response
elements (CRE) in the SLC6A4 and PER2 promoters and periodically
activates the transcription of these genes. During ER stress
response, activates the transcription of NLRP1, possibly in
concert with other factors. {ECO:0000250|UniProtKB:P18848}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Interacts
with CEBPB and binds DNA as a heterodimer with CEBPB. Interacts
with NEK6, DAPK2 and ZIPK/DAPK3. Interacts (via its leucine zipper
domain) with GABBR1 and GABBR2 (via their C-termini). Forms a
heterodimer with TXLNG in osteoblasts. Interacts (via its DNA
binding domain) with FOXO1 (C-terminal half); the interaction
occurs in osteoblasts and regulates glucose homeostasis through
suppression of beta-cell proliferation and a decrease in insulin
production. Interacts with SATB2; the interaction results in
enhanced DNA binding and transactivation by these transcription
factors (By similarity). Interacts with CEP290 (via an N-terminal
region) (PubMed:16682973). Interacts with DDIT3/CHOP (By
similarity). {ECO:0000250|UniProtKB:P18848,
ECO:0000250|UniProtKB:Q06507, ECO:0000250|UniProtKB:Q9ES19,
ECO:0000269|PubMed:16682973}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES19}.
Cell membrane {ECO:0000250|UniProtKB:Q9ES19}. Nucleus
{ECO:0000250|UniProtKB:P18848, ECO:0000250|UniProtKB:Q9ES19,
ECO:0000255|PROSITE-ProRule:PRU00978}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P18848}. Note=Colocalizes with GABBR1 in
hippocampal neuron dendritic membranes. Colocalizes with NEK6 in
the centrosome (By similarity). {ECO:0000250|UniProtKB:P18848,
ECO:0000250|UniProtKB:Q9ES19}.
-!- DOMAIN: The BetaTrCP degron motif promotes binding to BTRC when
phosphorylated. {ECO:0000250}.
-!- PTM: Ubiquitinated by SCF(BTRC) in response to mTORC1 signal,
followed by proteasomal degradation and leading to down-regulate
expression of SIRT4. {ECO:0000250}.
-!- PTM: Phosphorylated by NEK6 (By similarity). Phosphorylated on the
betaTrCP degron motif at Ser-215, followed by phosphorylation at
Ser-220, Ser-227, Ser-231 and Ser-245, promoting interaction with
BTRC and ubiquitination. Phosphorylation is promoted by mTORC1 (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000255}.
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EMBL; BC102236; AAI02237.1; -; mRNA.
RefSeq; NP_001029514.1; NM_001034342.2.
UniGene; Bt.49442; -.
ProteinModelPortal; Q3ZCH6; -.
SMR; Q3ZCH6; -.
STRING; 9913.ENSBTAP00000023213; -.
PaxDb; Q3ZCH6; -.
PRIDE; Q3ZCH6; -.
GeneID; 509107; -.
KEGG; bta:509107; -.
CTD; 468; -.
eggNOG; KOG4571; Eukaryota.
eggNOG; ENOG4111ZXT; LUCA.
HOGENOM; HOG000004844; -.
HOVERGEN; HBG004301; -.
InParanoid; Q3ZCH6; -.
KO; K04374; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IBA:GO_Central.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
InterPro; IPR029811; ATF4.
InterPro; IPR004827; bZIP.
PANTHER; PTHR13044:SF2; PTHR13044:SF2; 1.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Biological rhythms; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 348 Cyclic AMP-dependent transcription factor
ATF-4.
/FTId=PRO_0000258021.
DOMAIN 275 338 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 277 297 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 302 338 Interaction with GABBR1.
{ECO:0000250|UniProtKB:Q9ES19}.
REGION 303 331 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 211 220 BetaTrCP degron motif.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
CROSSLNK 53 53 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18848}.
CROSSLNK 256 256 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18848}.
CROSSLNK 264 264 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18848}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P18848}.
SEQUENCE 348 AA; 38245 MW; 84C13618325BB27E CRC64;
MAEMSFLSSE VLGGDFVSPF DQLGLGAEES LGLLDDNLEV AKHFKHHGFS CDKAKAGSSE
WLAVDWLVSD NSKEDAFSGT DWMVEKMDLK EFDFDILFSK DDLETMPDEL LATLDDTCDL
FQPLVQETNK EPPQIVNPIG HLPEGLPTID QGAPFTFFQP LPPSPGTLSS TPDHSFSLEL
CSEVVIPEGD SKPDSTTTGF PQCIKEEDAP SDNDSGICMS PDSSLGSPQD SPSTSRGSPN
KSLLSPGALS GSSRPKPYDP PGEKMVAAKV KGEKLDKKLK KMEQNKTAAT RYRQKKRAEQ
EALTGECKEL EKKNEALKEK ADSLAKEIQY LKDQIEEVRK AREKKRVL


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