ID   AP2D_DANRE              Reviewed;         450 AA.
AC   Q5RJ20; Q4V8R1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transcription factor AP-2-delta;
DE            Short=AP-2-delta;
GN   Name=tfap2d {ECO:0000250|UniProtKB:Q7Z6R9};
GN   ORFNames=si:dkey-5e16.2, zgc:114196;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000312|EMBL:CAI21171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larva {ECO:0000312|EMBL:AAH97244.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) 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 (By similarity).
CC       {ECO:0000250}.
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:Q91ZK0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000255}.
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DR   EMBL; BX005121; CAI21171.1; -; Genomic_DNA.
DR   EMBL; BC097244; AAH97244.1; -; mRNA.
DR   RefSeq; NP_001020717.1; NM_001025546.1.
DR   AlphaFoldDB; Q5RJ20; -.
DR   STRING; 7955.ENSDARP00000028710; -.
DR   PaxDb; Q5RJ20; -.
DR   Ensembl; ENSDART00000193975; ENSDARP00000153448; ENSDARG00000023272.
DR   GeneID; 566838; -.
DR   KEGG; dre:566838; -.
DR   CTD; 83741; -.
DR   ZFIN; ZDB-GENE-050913-99; tfap2d.
DR   eggNOG; KOG3811; Eukaryota.
DR   GeneTree; ENSGT00950000182848; -.
DR   HOGENOM; CLU_035175_5_0_1; -.
DR   InParanoid; Q5RJ20; -.
DR   OMA; GHTNSEK; -.
DR   OrthoDB; 641707at2759; -.
DR   PhylomeDB; Q5RJ20; -.
DR   TreeFam; TF313718; -.
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:Q5RJ20; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000023272; Expressed in camera-type eye and 12 other tissues.
DR   ExpressionAtlas; Q5RJ20; 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: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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..450
FT                   /note="Transcription factor AP-2-delta"
FT                   /id="PRO_0000309515"
FT   REGION          280..410
FT                   /note="H-S-H (helix-span-helix), dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          414..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        255
FT                   /note="R -> K (in Ref. 2; AAH97244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  49509 MW;  86BB27BF98A17167 CRC64;
     MSATFPGLVH DAEIRHDGSN SYRLMQLGCL ESVANSSVAY SSSSPLTYPA TGTEFASPYF
     PTNHQYTPLH HQSFHYEFQH SHPAVNPDAY SLNSLHHSQQ YYQQLHHGEP ADFINLHNAR
     ALKSSCLDEQ RRELGCLDAY RRHDLSIMSH GSQYGMHPEQ RLLPGAGLGL PPPGADDLQG
     SVDAQCGLVL NGQGGVIRRG GTCVVNPTDL FCSVPGRLSL LSSTSKYKVT IAEVKRRLSP
     PECLNASLLG GILRRAKSKN GGRCLREKLD RLGLNLPAGR RKAANVTLLT SLVEGEALHL
     ARDFGYTCET EFPTKAVGEH LARQHTEPKE QNARKKMVLA TKQICKEFQD LLSQDRSPLG
     SSRPTPILDL DIQRHLTHFS LITHGFGTPA ICAALSTFQT ILSEMLNYLE KHSANKSTGT
     PDTNQINSNS DKTLRKTEAP TKDGKIEKTE