ID   ATBP_DROWI              Reviewed;         379 AA.
AC   B4NEU8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=AT-rich binding protein {ECO:0000250|UniProtKB:Q86P48};
GN   Name=ATbp {ECO:0000250|UniProtKB:Q86P48}; ORFNames=GK25708;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1] {ECO:0000312|EMBL:EDW82267.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW82267.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: May be a transcription factor for genes having (A+T)
CC       stretches in their promoter and/or enhancer regions. Binds to AT rich
CC       DNA (By similarity). {ECO:0000250|UniProtKB:Q86P48}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86P48}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW82267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH964239; EDW82267.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002071281.2; XM_002071245.2.
DR   AlphaFoldDB; B4NEU8; -.
DR   SMR; B4NEU8; -.
DR   STRING; 7260.FBpp0254851; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; B4NEU8; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..379
FT                   /note="AT-rich binding protein"
FT                   /id="PRO_0000378618"
FT   ZN_FING         29..52
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         312..336
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         342..365
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          114..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  41027 MW;  72754ECB0F350CDC CRC64;
     MGFPRILSKN NKIYTKLGEF CLSGDSFWIV CHTCQEELQT QDQFWKHIQD EHNFLHGVAK
     EHSRTSSYCL TDVEAAAAAT TPGATASSQG AGSVTAVTVP LALYHCSAKY SDDEQREVEL
     HEAHQQQQQQ QQQQLHQQQQ QQQRDAAKEL AELHANAVAA AAAVAAASDG SARSSSGIDI
     KVEPATLALP PDMQAAAAAA AAANATIYHL PQLVPAPAPP PTASFVSASG GSTSTTVSTT
     PPSHQPIMQQ QQHQQQQQQQ QQTSTTLAMS VNQSTAIAAA ALLTGPDLPK DSNSTTASAG
     SAVSSDDGER WYICDYESCG LKFKYKSRME LHRVVHSKER RFNCDLCSAS FKQSCNLSTH
     RKKKHAMRGI KSELLPQRF