ID A0A2K6MK04_RHIBE Unreviewed; 429 AA.
AC A0A2K6MK04;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-2 {ECO:0000256|PIRNR:PIRNR003153};
GN Name=ATF2 {ECO:0000313|Ensembl:ENSRBIP00000036128.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000036128.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000036128.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000036128.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6MK04; -.
DR STRING; 61621.ENSRBIP00000036128; -.
DR Ensembl; ENSRBIT00000060131.1; ENSRBIP00000036128.1; ENSRBIG00000041657.1.
DR GeneTree; ENSGT00940000156582; -.
DR OMA; YQTADKD; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:1902562; C:H4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0044013; F:histone H2B acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:1990253; P:cellular response to leucine starvation; IEA:Ensembl.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
DR CDD; cd14687; bZIP_ATF2; 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|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:UP000233180};
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 25..49
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 276..339
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 183..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..335
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 224..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 46076 MW; 3FCC6163C76FF54B CRC64;
MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE MTLKFGPARN
DSVIVKVGLF NELEVPLAQT AQPTSAIVRP ASLQVPNVLL TSSDSSVIIQ QAVPSPTSST
VITQAPSSNR PIVPVPGPFP LLLHLPNGQT MPVAIPASIT SSNVHVPAAV PLVRPVTMVP
SVPGIPGPSS PQPVQSEAKM RLKAALTQQH PPVTNGDTVK GHGSGLVRTQ SEESRPQSLQ
QPATSTTETP ASPAHTTPQT QSTSGRRRRA ANEDPDEKRR KFLERNRAAA SRCRQKRKVW
VQSLEKKAED LSSLNGQLQS EVTLLRNEVA QLKQLLLAHK DCPVTAMQKK SGYHTADKDD
SSEDISVPSS PHTEAIQHSS VSTSNGVSST SKAEAIATSV LTQMADQSTE PALSQIVMAP
SSQSQPSGS
//
