ID   AP2E_DANRE              Reviewed;         423 AA.
AC   Q6P0E7; Q6PBA7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Transcription factor AP-2-epsilon;
DE            Short=AP-2-epsilon;
GN   Name=tfap2e {ECO:0000312|ZFIN:ZDB-GENE-040426-1455}; ORFNames=zgc:65882;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAH65649.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH65649.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC       inducible viral and cellular enhancer elements to regulate
CC       transcription of selected genes. AP-2 factors bind to the consensus
CC       sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC       spectrum of important biological functions. {ECO:0000305}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC       other AP-2 family members (By similarity).
CC       {ECO:0000250|UniProtKB:Q6VUP9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6VUP9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P0E7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P0E7-2; Sequence=VSP_052605;
CC   -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC059800; AAH59800.1; ALT_INIT; mRNA.
DR   EMBL; BC065649; AAH65649.1; -; mRNA.
DR   RefSeq; NP_957115.2; NM_200821.2. [Q6P0E7-2]
DR   AlphaFoldDB; Q6P0E7; -.
DR   STRING; 7955.ENSDARP00000007990; -.
DR   PaxDb; Q6P0E7; -.
DR   Ensembl; ENSDART00000190005; ENSDARP00000153493; ENSDARG00000008861. [Q6P0E7-2]
DR   GeneID; 393794; -.
DR   KEGG; dre:393794; -.
DR   CTD; 339488; -.
DR   ZFIN; ZDB-GENE-040426-1455; tfap2e.
DR   eggNOG; KOG3811; Eukaryota.
DR   GeneTree; ENSGT00950000182848; -.
DR   InParanoid; Q6P0E7; -.
DR   PhylomeDB; Q6P0E7; -.
DR   Reactome; R-DRE-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR   Reactome; R-DRE-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR   PRO; PR:Q6P0E7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 19.
DR   Bgee; ENSDARG00000008861; Expressed in larva and 22 other tissues.
DR   ExpressionAtlas; Q6P0E7; baseline.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0030318; P:melanocyte differentiation; IGI:ZFIN.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004979; TF_AP2.
DR   InterPro; IPR013854; TF_AP2_C.
DR   PANTHER; PTHR10812; PTHR10812; 1.
DR   Pfam; PF03299; TF_AP-2; 1.
DR   PRINTS; PR01748; AP2TNSCPFCT.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..423
FT                   /note="Transcription factor AP-2-epsilon"
FT                   /id="PRO_0000309518"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..405
FT                   /note="H-S-H (helix-span-helix), dimerization"
FT                   /evidence="ECO:0000255"
FT   MOTIF           50..55
FT                   /note="PPxY motif"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        10..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         24
FT                   /note="L -> LSQL (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052605"
SQ   SEQUENCE   423 AA;  45514 MW;  4A336882609C1DAE CRC64;
     MLVHSYSSME RADGLSSSSP GGRLSQLNQA AYSSAPPLCH TPASDFQPPY FPPPYPQSSL
     SYSQSQDGGY PHLPEPYPSL NSLHQHQQAA WHSQRSRSED AGLLSQPHRA LSLDPRREYP
     GVPRLLTHGL GDGAAALGDG PLGMHAVHHG LDDIQGLEEA SALGILDHSV IKKVPLPSKL
     NGSTISALSL SKEGLGLGGV SNPAEVFCSV PGRLSLLSST SKYKVTVGEV QRRLAPPECL
     NASLLGGVLR RAKSKNGGRC LRERLEKIGL NLPAGRRKAA NVTLLTALVE GEAVHLARDF
     GYVCETEFPA RATAEYLCRQ TEPDQLPTRR SMLLATKEIC KEFVDLMSQD RSPLGASRPT
     PCLEPGVQSS LTHFSLLTHG FGTPALCAAL SAFQSYLLEA LKLLDKGENG GKNHHDKELK
     HRK