ZBT18_XENTR
ID ZBT18_XENTR Reviewed; 521 AA.
AC Q0IJ29; Q28FU6;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE AltName: Full=Zinc finger protein 238;
GN Name=zbtb18; Synonyms=znf238; ORFNames=TGas069c09.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316.
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor that plays a role in various
CC developmental processes. Specifically binds the consensus DNA sequence
CC 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by
CC recruiting chromatin remodeling multiprotein complexes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZBTB18 subfamily. {ECO:0000305}.
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DR EMBL; BC121215; AAI21216.1; -; mRNA.
DR EMBL; CR761742; CAJ83468.1; -; mRNA.
DR RefSeq; NP_001016948.2; NM_001016948.3.
DR AlphaFoldDB; Q0IJ29; -.
DR SMR; Q0IJ29; -.
DR STRING; 8364.ENSXETP00000031817; -.
DR PaxDb; Q0IJ29; -.
DR GeneID; 549702; -.
DR KEGG; xtr:549702; -.
DR CTD; 10472; -.
DR Xenbase; XB-GENE-1003542; zbtb18.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_034521_0_0_1; -.
DR InParanoid; Q0IJ29; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..521
FT /note="Zinc finger and BTB domain-containing protein 18"
FT /id="PRO_0000391929"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 369..391
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..488
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 190..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 316
FT /note="P -> I (in Ref. 2; CAJ83468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58450 MW; ECC5C9EDC63B24F2 CRC64;
MEFPEHSRHL LQCLSEQRHQ GFLCDCTVLV GDAHFRAHRA VLASCSMYFH LFYKDQLDKR
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
ATTEADSTKK EEDASSCSDK IECLSDGSSH MAGDLPSDED DVEEEKINIL PGKTDLATES
GNMWIRLPSD SASIPQTGGE AETHTAAAGK TADSPCSSTG SLSHRSATSM RDSADVDCVL
DLSVKSSLSG AETLNNSYLS SQEILRNSLV QVKVEKEASC DENDIDTTEY DIERNTVKES
SSSNIRAPYE PVHLAPIRED SVLRELDHDD KASDDDITPE NERVQMETNM DSSLLPYVPN
ILSPAGQIFM CPLCNKVFPS PHILQIHLST HFREQEGIRS KPANDVHVPT CSLCGKTFSC
MYTLKRHERT HSGEKPFTCT QCGKSFQYSH NLSRHAVVHT REKPHACKWC ERRFTQSGDL
YRHIRKFHCE LVNSLSVKSE TLGLPAVRDW TLEDSSQELW K