ATF2_CHICK
ID ATF2_CHICK Reviewed; 487 AA.
AC O93602;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-2;
DE Short=cAMP-dependent transcription factor ATF-2;
DE AltName: Full=Activating transcription factor 2;
GN Name=ATF2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9819389; DOI=10.1128/mcb.18.12.7020;
RA Huguier S., Baguet J., Perez S., van Dam H., Castellazzi M.;
RT "Transcription factor ATF2 cooperates with v-Jun to promote growth factor-
RT independent proliferation in vitro and tumor formation in vivo.";
RL Mol. Cell. Biol. 18:7020-7029(1998).
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') (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form a homodimer in the absence
CC of DNA. Can form a heterodimer with JUN. Heterodimerization is
CC essential for its transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Mitochondrion
CC outer membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; Y17724; CAA76838.1; -; mRNA.
DR RefSeq; NP_990235.1; NM_204904.1.
DR AlphaFoldDB; O93602; -.
DR BMRB; O93602; -.
DR SMR; O93602; -.
DR STRING; 9031.ENSGALP00000032623; -.
DR PaxDb; O93602; -.
DR GeneID; 395727; -.
DR KEGG; gga:395727; -.
DR CTD; 1386; -.
DR VEuPathDB; HostDB:geneid_395727; -.
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; O93602; -.
DR OrthoDB; 978850at2759; -.
DR PhylomeDB; O93602; -.
DR PRO; PR:O93602; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR029836; ATF2.
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; PTHR19304:SF9; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57959; SSF57959; 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 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA damage; DNA-binding; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..487
FT /note="Cyclic AMP-dependent transcription factor ATF-2"
FT /id="PRO_0000076580"
FT DOMAIN 334..397
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT ZN_FING 7..31
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..356
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 362..390
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 407..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 387..396
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 288..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 52407 MW; A1F42734D9C6A146 CRC64;
MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRNKIEEPSV VETTHQDSPL
PHPESTTNDE KEVSLQQTAQ PTSTIVRPAS LQVPNVLLTS SDSSVIIQQA IPSPTSSTVI
TQAPSSNRPI VPVPGPFPLL LHLPNGQTMP VAIPASITNS NVHVPAAVPL VRPVTMVPSI
PGIPGPSSPQ PVQSEAKLRL KAALTQQHPQ VTNGDTAKGH PSGLVRTQSE EPRPQSLQQP
ATSTTETPAS PAQPTQQTPN TGGRRRRAAN EDPDEKRRKF LERNRAAASR CRQKRKVWVQ
SLEKKAEDLS SLNGQLQNEV TLLRNEVAQL KQLLLAHKDC PVTAMQKKSG YHTADKDDSS
EDISVPSSPH TEAIQHSSVS TSNGVSSTSK AEAVATSVLT QLADQSSEPG LPQVGVVPPS
QAQPSGS
