ID A0A287D5M7_ICTTR Unreviewed; 390 AA.
AC A0A287D5M7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-2 {ECO:0000256|PIRNR:PIRNR003153};
GN Name=ATF2 {ECO:0000313|Ensembl:ENSSTOP00000028848.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000028848.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000028848.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Transcriptional activator which regulates the transcription
CC of various genes, including those involved in anti-apoptosis, cell
CC growth, and DNA damage response. Dependent on its binding partner,
CC binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-
CC 3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-
CC 3'). {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form a homodimer in the absence
CC of DNA. {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SIMILARITY: Belongs to the bZIP family.
CC {ECO:0000256|PIRNR:PIRNR003153}.
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DR EMBL; AGTP01035590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287D5M7; -.
DR Ensembl; ENSSTOT00000033122.1; ENSSTOP00000028848.1; ENSSTOG00000014079.3.
DR GeneTree; ENSGT00940000156582; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14687; bZIP_ATF2; 1.
DR CDD; cd12192; GCN4_cent; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016378; TF_CRE-BP1-typ.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19304:SF9; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-2; 1.
DR PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PIRSF; PIRSF003153; ATF2_CRE-BP1; 2.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|PIRNR:PIRNR003153};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR003153};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003153};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transcription {ECO:0000256|PIRNR:PIRNR003153};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003153};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 7..31
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 237..300
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 112..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 262..296
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 42524 MW; 0D42AEA71A1C7217 CRC64;
MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRSKIEEPSI VETTHQDSPL
PHPESTTSDE KLVRPVTMVP SVPGIPGPSS PQPVQQSEAK MRLKAALTQQ HPPVTNGDTV
KGHGSGLVRT QSEESRPQSL QQPATSTTET PASPAHTTPQ TQNTSGRRRR AANEDPDEKR
RKFLERNRAA ASRCRQKRKV WVQSLEKKAE DLSSLNGQLQ SEVTLLRNEV AQLKQLLLAH
KDCPVTAMQK KSGYHTADKD DSSEDLSVPS SPHTEAIQHS SVSTSNGVSS TSKAEAVATS
VLTQMADQSM EPALSQIVMA PSSQSQPSGS
//