ID   ZB183_XENLA             Reviewed;         519 AA.
AC   Q6NRM8;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 18.3;
DE   AltName: Full=Zinc finger protein 238.3;
GN   Name=zbtb18.3; Synonyms=znf238.3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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; BC070718; AAH70718.1; -; mRNA.
DR   RefSeq; NP_001084919.1; NM_001091450.1.
DR   RefSeq; XP_018119831.1; XM_018264342.1.
DR   RefSeq; XP_018119832.1; XM_018264343.1.
DR   AlphaFoldDB; Q6NRM8; -.
DR   SMR; Q6NRM8; -.
DR   DNASU; 431971; -.
DR   GeneID; 431971; -.
DR   KEGG; xla:431971; -.
DR   CTD; 431971; -.
DR   OMA; AGYEDIM; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 431971; Expressed in brain and 19 other tissues.
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   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..519
FT                   /note="Zinc finger and BTB domain-containing protein 18.3"
FT                   /id="PRO_0000391928"
FT   DOMAIN          24..91
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         367..389
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         407..429
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         435..457
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         463..486
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          189..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  58490 MW;  8E8C4FCB4FD473AE CRC64;
     MEFPEHSRHL LQCLSEQRHQ GFLCDCTVLV GDAHFRAHRA VLASCSMYFH LFYKDQLDKK
     NIVYLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
     ATTEADSTKK EEDTLSCSDK IECLSDGSSH MAGDLPSDED DVEEEKINSK TDLATESGNM
     WIRLSSDSAS IPQTGGEVDT HTTAAGKTAD SPCSSTGSLS HRSATSMGDS TDVDCVLDLS
     VKSSLSGTET LNNSYLSSQE ILRNSLVQVK IEREASCEDN DIHTSEYDIE RNTVKENVSS
     NIRAPYEPVH LAPIREDSVL RELDHDDKAI NDDMITPENE RVQMEANIDN SLLPYVQNIL
     SPAGQIFMCP LCNKVFPSPH ILQIHLSTHF REQEGIRSKP TNDVHVPTCS LCGKTFSCMY
     TLKRHERTHS GEKPFTCTQC GKSFQYSHNL SRHAVVHTRE KPHACKWCER RFTQSGDLYR
     HIRKFHCELV NSLSVKSETL GLPAVRDWTL EDSSQELWK