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Database: UniProt
Entry: A0A2K5KKG0_CERAT
LinkDB: A0A2K5KKG0_CERAT
Original site: A0A2K5KKG0_CERAT 
ID   A0A2K5KKG0_CERAT        Unreviewed;       447 AA.
AC   A0A2K5KKG0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-2 {ECO:0000256|PIRNR:PIRNR003153};
GN   Name=ATF2 {ECO:0000313|Ensembl:ENSCATP00000001175.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000001175.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000001175.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_011902451.1; XM_012047061.1.
DR   AlphaFoldDB; A0A2K5KKG0; -.
DR   SMR; A0A2K5KKG0; -.
DR   Ensembl; ENSCATT00000006223.1; ENSCATP00000001175.1; ENSCATG00000005694.1.
DR   GeneID; 105579833; -.
DR   CTD; 1386; -.
DR   GeneTree; ENSGT00940000156582; -.
DR   OMA; YQTADKD; -.
DR   OrthoDB; 1361169at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000005694; Expressed in cerebellum and 12 other cell types or tissues.
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   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR016378; TF_CRE-BP1-typ.
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; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|PIRNR:PIRNR003153};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR003153};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Transcription {ECO:0000256|PIRNR:PIRNR003153};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR003153}.
FT   DOMAIN          294..357
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          319..353
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        242..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  47987 MW;  804F54812C45B45F CRC64;
     MHCAWMWPDQ TPTPTRFLKN CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI
     IRSKIEEPSV VETTHQDSPL PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS LQVPNVLLTS
     SDSSVIIQQA VPSPTSSTVI TQAPSSNRPI VPVPGPFPLL LHLPNGQTMP VAIPASITSS
     NVHVPAAVPL VRPVTMVPSV PGIPGPSSPQ PVQSEAKMRL KAALTQQHPP VTNGDTVKGH
     GSGLVRTQSE ESRPQSLQQP ATSTTETPAS PAHTTPQTQS TSGRRRRAAN EDPDEKRRKF
     LERNRAAASR CRQKRKVWVQ SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC
     PVTAMQKKSG YHTADKDDSS EDISVPSSPH TEAIQHSSVS TSNGVSSTSK AEAVATSVLT
     QMADQSTEPA LSQIVMAPSS QSQPSGS
//
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