ATBP_DROVI
ID ATBP_DROVI Reviewed; 376 AA.
AC B4M7J1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=AT-rich binding protein {ECO:0000250|UniProtKB:Q86P48};
GN Name=ATbp {ECO:0000250|UniProtKB:Q86P48}; ORFNames=GJ16440;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW62758.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW62758.1};
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}.
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DR EMBL; CH940653; EDW62758.1; -; Genomic_DNA.
DR RefSeq; XP_002057272.2; XM_002057236.2.
DR AlphaFoldDB; B4M7J1; -.
DR STRING; 7244.FBpp0230857; -.
DR EnsemblMetazoa; FBtr0442801; FBpp0399249; FBgn0203624.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_712250_0_0_1; -.
DR InParanoid; B4M7J1; -.
DR OMA; ERWYICD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; B4M7J1; -.
DR Proteomes; UP000008792; 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..376
FT /note="AT-rich binding protein"
FT /id="PRO_0000378617"
FT ZN_FING 29..52
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..333
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 339..362
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 143..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 40123 MW; D128B3FA6B77A1BD CRC64;
MGFPRILSKN NKIYTKLGEF CLSGDSFWIV CHTCQEELQT QDAFWKHIQD EHNFLHGLAK
QEHGRNSSYC LPDVDAATAP ANQTALPVPL ALYHCAKYSE EEQREVAAAV ELHEAQQQQQ
QQQQQQQQQQ QLQQQQQQRD SAELQAVTAA AESSARSNNS GSGIDIKVEP TSLTLTSEIQ
VAAAAAAAAA AAGAAAAGAV TANTTIYHLS QVVPGPPPPP PPTPCFVTTP TAGGVSTTPP
HPALAGPVGA GGNGGNGANA TVMQQACGTL GMPLLGVAAG QAELVAKESN STTASASSAV
SSDDGERWYI CDYGACGLKF KYKSRMELHR VVHSKERRFN CDMCSASFKQ SCNLSTHRKK
KHSLRGIKSE LLPQRF