ATBP_SARPE
ID ATBP_SARPE Reviewed; 354 AA.
AC Q26635;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=AT-rich binding protein {ECO:0000312|EMBL:BAA07349.1};
DE AltName: Full=A/T-stretch binding protein {ECO:0000312|EMBL:BAA07349.1};
OS Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Sarcophagidae; Sarcophaga; Boettcherisca.
OX NCBI_TaxID=7386;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA07349.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7607207; DOI=10.1111/j.1432-1033.1995.0396h.x;
RA Nakanishi-Matsui M., Kubo T., Natori S.;
RT "Molecular cloning and nuclear localization of ATBP, a novel (A+T)-stretch-
RT binding protein of Sarcophaga peregrina (flesh fly).";
RL Eur. J. Biochem. 230:396-400(1995).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8307011; DOI=10.1111/j.1432-1033.1994.tb19958.x;
RA Matsui M., Kobayashi A., Kubo T., Natori S.;
RT "Purification and characterization of ATBP, a novel protein that binds to
RT A/T stretches in three segments of the Sarcophaga lectin gene.";
RL Eur. J. Biochem. 219:449-454(1994).
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. {ECO:0000269|PubMed:8307011}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:8307011}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7607207,
CC ECO:0000269|PubMed:8307011}.
CC -!- TISSUE SPECIFICITY: Fat body. {ECO:0000269|PubMed:7607207}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38160; BAA07349.1; -; mRNA.
DR PIR; S65687; S65687.
DR AlphaFoldDB; Q26635; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
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 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..354
FT /note="AT-rich binding protein"
FT /id="PRO_0000378619"
FT ZN_FING 31..54
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..309
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..338
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 84..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 40195 MW; E1E80D6E17CAAC3E CRC64;
MGFPRIISKN NKIYTKLGAF CLSGDGQQFW IVCHTCQEEL QTQDKFWKHI QDEHNFMHGP
KQEQGRTAAQ AYMEAAEAAA MTPLPLYRKV SENDQQRDDV VSTEDEDMQK EPKDYTEMRA
HDDQQQTAAV AIDIKLEPSS LSQQSAVQAQ QQQQQQQQQQ QQQQQQQQQQ EQLQQQQQQQ
QTQQIEITTP LMYQIPQVHP PVSAYAALVQ APAINTLNMS VAAAAAAVAS NQVPSTMANL
LPQELQYKQE LQYKQEVQQH KESTNNSTTA SASSAMSSDD GERFYICDFE NCGLKFKYHS
RLELHRSVHS KVRRFACEIC GASFKQSCNL STHRKKKHAL KGTTKATLVP SQSF
