ID   ATF3_BOVIN              Reviewed;         181 AA.
AC   Q2KII1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-3;
DE            Short=cAMP-dependent transcription factor ATF-3;
DE   AltName: Full=Activating transcription factor 3;
GN   Name=ATF3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein binds the cAMP response element (CRE)
CC       (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral
CC       and cellular promoters. Represses transcription from promoters with ATF
CC       sites (By similarity). It may repress transcription by stabilizing the
CC       binding of inhibitory cofactors at the promoter (By similarity).
CC       {ECO:0000250|UniProtKB:P18847, ECO:0000250|UniProtKB:Q60765}.
CC   -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Interacts with
CC       KAT5; promoting KAT5 autoacetylation and KAT5 deubiquitination by USP7.
CC       {ECO:0000250|UniProtKB:P18847}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18847,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; BC112629; AAI12630.1; -; mRNA.
DR   RefSeq; NP_001039658.1; NM_001046193.2.
DR   RefSeq; XP_010811857.1; XM_010813555.2.
DR   AlphaFoldDB; Q2KII1; -.
DR   SMR; Q2KII1; -.
DR   STRING; 9913.ENSBTAP00000011265; -.
DR   PaxDb; Q2KII1; -.
DR   PRIDE; Q2KII1; -.
DR   GeneID; 515266; -.
DR   KEGG; bta:515266; -.
DR   CTD; 467; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_088612_0_2_1; -.
DR   InParanoid; Q2KII1; -.
DR   OrthoDB; 1457971at2759; -.
DR   TreeFam; TF326301; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR029812; ATF3.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF23; PTHR23351:SF23; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..181
FT                   /note="Cyclic AMP-dependent transcription factor ATF-3"
FT                   /id="PRO_0000285211"
FT   DOMAIN          86..149
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          76..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..110
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          114..142
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        79..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         162
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
FT   CROSSLNK        78
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
FT   CROSSLNK        175
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
SQ   SEQUENCE   181 AA;  20567 MW;  95A10B4CFA89AD88 CRC64;
     MMLQHPGQVS ASEVSASAFV PCLSPPGSLV FEDFANLTPF VKEELRLAIQ SKHLCHRMSS
     ALDSVTVSGR PLEMSVTKAE VAPEEDERKK RRRERNKIAA AKCRNKKKEK TECLQKESEK
     LESVNAELKA QIEELKNEKQ HLIYMLNLHR PTCIVRAQNG RTPEDERNLF IQQIKEGTLQ
     S