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Cyclic AMP-dependent transcription factor ATF-7 (cAMP-dependent transcription factor ATF-7) (Activating transcription factor 7) (Transcription factor ATF-A)

 ATF7_PONAB              Reviewed;         483 AA.
Q5R9C9;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
25-OCT-2017, entry version 81.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-7;
Short=cAMP-dependent transcription factor ATF-7;
AltName: Full=Activating transcription factor 7;
AltName: Full=Transcription factor ATF-A;
Name=ATF7;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays important functions in early cell signaling. Binds
the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-
3'), a sequence present in many viral and cellular promoters.
Activator of the NF-ELAM1/delta-A site of the E-selectin promoter.
Has no intrinsic transcriptional activity, but activates
transcription on formation of JUN or FOS heterodimers. Also can
bind TRE promoter sequences when heterodimerized with members of
the JUN family (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer; binds DNA as homodimer (By similarity).
Heterodimer; heterodimerizes with other members of ATF family and
with JUN family members (By similarity). Interacts with JNK2; the
interaction does not phosphorylate ATF7 but acts as a docking site
for other ATF-associated partners such as JUN family members.
Interacts (via its transactivation domain) with TAF12 the
interaction potentiates the transactivation activity and is
inhibited by ATF7 sumoylation. Interacts with TAF4; the
interaction inhibits the TAF12-dependent transactivation.
Interacts with MAPK9; the interaction does not phosphorylate ATF7
but acts as a docking site for ATF7-associated partners such as
JUN (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000250}. Note=Mainly
nucleoplasmic. Restricted distribution to the perinuculear region.
The sumoylated form locates to the nuclear peiphery (By
similarity). {ECO:0000250}.
-!- PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing
subsequent phosphorylation on Thr-51. This latter phosphorylation
prevents sumoylation, increases binding to TAF12 and enhances
transcriptional activity (By similarity). {ECO:0000250}.
-!- PTM: Sumoylation delays nuclear localization and inhibits
transactivation activity through preventing binding to TAF12.
RANBP2 appears to be the specific E3 ligase (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; CR859460; CAH91631.1; -; mRNA.
RefSeq; NP_001125959.1; NM_001132487.1.
UniGene; Pab.13121; -.
ProteinModelPortal; Q5R9C9; -.
SMR; Q5R9C9; -.
STRING; 9601.ENSPPYP00000005229; -.
PRIDE; Q5R9C9; -.
GeneID; 100172894; -.
KEGG; pon:100172894; -.
CTD; 11016; -.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
HOVERGEN; HBG004300; -.
InParanoid; Q5R9C9; -.
KO; K09045; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR016378; TF_CRE-BP1-typ.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00170; bZIP_1; 1.
PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
SMART; SM00338; BRLZ; 1.
SMART; SM00355; ZnF_C2H2; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
2: Evidence at transcript level;
Activator; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 483 Cyclic AMP-dependent transcription factor
ATF-7.
/FTId=PRO_0000076594.
DOMAIN 332 395 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
ZN_FING 7 31 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1 285 Transactivation domain. {ECO:0000250}.
REGION 334 354 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 360 388 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 118 253 Pro-rich.
COMPBIAS 322 325 Poly-Arg.
MOD_RES 51 51 Phosphothreonine; by MAPK11.
{ECO:0000250|UniProtKB:P17544}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000250|UniProtKB:P17544}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:P17544}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000250|UniProtKB:P17544}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:P17544}.
CROSSLNK 107 107 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P17544}.
SEQUENCE 483 AA; 51743 MW; D05D084FC73330D6 CRC64;
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD
SPASSPCSPP LKEKEVTPKP VLISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP
PSNRQMGSPT GSLPLVMHLA NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN
SSGSISPSGH PIPSEAKMRL KATLTHQVSS INGGCGMVVG SASTMVTARP EQSQILIQHP
DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL
EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP
TGSPAPVIQH SSATAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS
AGR


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