ZB182_XENLA
ID ZB182_XENLA Reviewed; 472 AA.
AC Q7ZWZ4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18.2;
DE AltName: Full=Zinc finger protein 238.2;
GN Name=zbtb18.2; Synonyms=znf238.2;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC046572; AAH46572.1; ALT_INIT; mRNA.
DR RefSeq; NP_001079635.1; NM_001086166.1.
DR AlphaFoldDB; Q7ZWZ4; -.
DR SMR; Q7ZWZ4; -.
DR DNASU; 379322; -.
DR GeneID; 379322; -.
DR KEGG; xla:379322; -.
DR CTD; 379322; -.
DR Xenbase; XB-GENE-1219070; znf238.2.L.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379322; Expressed in blastula 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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
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..472
FT /note="Zinc finger and BTB domain-containing protein 18.2"
FT /id="PRO_0000391927"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 344..366
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..463
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 127..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 52691 MW; 2BD665BDDFA4C21B CRC64;
MEFPDHSRQL LQCLSQQRHQ GFLCDCTVLV GEAQFRAHRA VLASCSMYFH LFYRDQLDKR
DIVHLNSDIV TAPAFSLLLQ FMYEGKLEFS NLPVEDVLAA ASYLHMYDIV KVCKGKLKDK
ELNSGEKIID DGEKDDKPVD SEEHHEHSFD ASQQKISTLD SVKPIWKEKV SGLSGLSSDL
IGVNSVPAEA VMCKRAAGKT KANDSSPSSP LSQRSANHTH PPSDRDGALD LSFKPMPGRD
SFHPSYVFGQ LVSDSQQQGS LPLVKHEQDL LSEQEDSQAK SPKSQQVGNP AKSLVTGLGH
MFTGNGNSHT REDDLYQDRD ESEDEMDSSD LSTSGVLVSP GQICICPLCS KVFPSPHILQ
LHLSSHFKDK DNSRIKMSPD GSVPTCTICG KTFSCMYTLK RHERTHSGEK PFTCGQCGKS
FQYSHNLSRH AVVHTREKPH ACKWCERRFT QSGDLYRHIR KFHCGLVKSL VV