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Database: UniProt
Entry: A0A287D5M7_ICTTR
LinkDB: A0A287D5M7_ICTTR
Original site: A0A287D5M7_ICTTR 
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
//
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