ZBT18_DANRE
ID ZBT18_DANRE Reviewed; 537 AA.
AC Q1L8W0; Q4JEX7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc finger and BTB domain-containing protein 18;
DE AltName: Full=Zinc finger protein 238;
GN Name=zbtb18; Synonyms=znf238; ORFNames=si:ch211-221n23.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fernandes M., Dahmane N.;
RT "The BTB/POZ protein ZF238 (RP58) is essential for dorso-ventral CNS
RT patterning and for interpreting SHH signaling.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; AY562553; AAT68457.1; -; mRNA.
DR EMBL; CR589882; CAK04546.1; -; Genomic_DNA.
DR RefSeq; NP_001076421.1; NM_001082952.1.
DR AlphaFoldDB; Q1L8W0; -.
DR SMR; Q1L8W0; -.
DR STRING; 7955.ENSDARP00000118751; -.
DR PaxDb; Q1L8W0; -.
DR Ensembl; ENSDART00000169895; ENSDARP00000141791; ENSDARG00000028228.
DR Ensembl; ENSDART00000186463; ENSDARP00000144804; ENSDARG00000028228.
DR GeneID; 100003157; -.
DR KEGG; dre:100003157; -.
DR CTD; 10472; -.
DR ZFIN; ZDB-GENE-050419-73; zbtb18.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155092; -.
DR HOGENOM; CLU_004253_11_3_1; -.
DR InParanoid; Q1L8W0; -.
DR OMA; GASDYDM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q1L8W0; -.
DR TreeFam; TF337437; -.
DR PRO; PR:Q1L8W0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000028228; Expressed in tail bud paraxial mesoderm and 72 other tissues.
DR ExpressionAtlas; Q1L8W0; baseline.
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..537
FT /note="Zinc finger and BTB domain-containing protein 18"
FT /id="PRO_0000391925"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 385..407
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 453..475
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 481..504
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 122..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 217
FT /note="S -> T (in Ref. 1; AAT68457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 59193 MW; 442AC175C44C34BF CRC64;
MEFPDHSRHL LQCLSEQRHQ GFLCDSTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
DIVHLNSDIV TAPAFALLLE FMYEGKLQFK SLPVEDVLAA ASYLHMYDIV KVCKKKLKQK
ATAEADSTKR EEDTSSCSDK VESFSEGGST GRPATADLLQ SDDEDMENKR DSPQEPGSMW
MRLPSDRTTS PTTSPREAET HGPDAGKSPA GSPSSSSGSL SRRSAASRRV SADTDCVLDL
SVKSSLGGGP GENIAGNPYF CSSVTPDSLQ SALVQVKVEK DTGSDDDELV SGDYEMEHSG
VKEPPSTNGT HLSLVAQRRL GLEAHLSALR EASLASELER DDKGGDDDTD VLGGDSDRVQ
EAAGVESSLL PYVSSMLGAP HTQIFMCPLC NKVFPSPHIL QIHLSTHFRE QEGVRAKPAG
DVNVPTCSIC GKTFSCMYTL KRHERTHSGE KPYTCTTCGK SFQYSHNLSR HAVVHTREKP
HACKWCERRF TQSGDLYRHI RKFHCELVNS LSVKSEALNL PTVRDWALED SSQELWK
