ID   SPOLB_DANRE             Reviewed;         392 AA.
AC   A0JMG1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Speckle-type POZ protein-like B;
DE   AltName: Full=HIB homolog 3;
GN   Name=spoplb; ORFNames=zgc:153365;
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 [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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=16740475; DOI=10.1016/j.devcel.2006.05.004;
RA   Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.;
RT   "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading
RT   Ci/Gli transcription factor.";
RL   Dev. Cell 10:719-729(2006).
CC   -!- FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin-protein ligase complex that mediates the ubiquitination and
CC       subsequent proteasomal degradation of target proteins, but with
CC       relatively low efficiency. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer. Heterodimer with SPOP. Component of cullin-RING-
CC       based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC       containing homodimeric SPOPL or the heterodimer formed by SPOP and
CC       SPOPL (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI25866.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BX323597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125865; AAI25866.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001073438.1; NM_001079969.1.
DR   AlphaFoldDB; A0JMG1; -.
DR   SMR; A0JMG1; -.
DR   STRING; 7955.ENSDARP00000103804; -.
DR   PaxDb; A0JMG1; -.
DR   Ensembl; ENSDART00000109418; ENSDARP00000103804; ENSDARG00000003974.
DR   GeneID; 558170; -.
DR   KEGG; dre:558170; -.
DR   CTD; 558170; -.
DR   ZFIN; ZDB-GENE-061103-277; spoplb.
DR   eggNOG; KOG1987; Eukaryota.
DR   GeneTree; ENSGT00940000155953; -.
DR   HOGENOM; CLU_004253_2_0_1; -.
DR   InParanoid; A0JMG1; -.
DR   OMA; VRSTIEC; -.
DR   OrthoDB; 864323at2759; -.
DR   PhylomeDB; A0JMG1; -.
DR   TreeFam; TF313419; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:A0JMG1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 11.
DR   Bgee; ENSDARG00000003974; Expressed in testis and 27 other tissues.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR   Gene3D; 2.60.210.10; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR008974; TRAF-like.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00917; MATH; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..392
FT                   /note="Speckle-type POZ protein-like B"
FT                   /id="PRO_0000274591"
FT   DOMAIN          31..161
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   DOMAIN          200..267
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   CONFLICT        9
FT                   /note="P -> S (in Ref. 2; AAI25866)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  44248 MW;  89D181AEF6222753 CRC64;
     MSRVPTPPPP GEMTSGPVAE SWCYTQVKVV KFSYMWTINN FSFCREEMGE VVRSSTFSSG
     PNDKMKWCLR VNPKGLDDES KDYLSLYLLL VSCPKSEVRA KFKFSLLNAK REETKAMESQ
     RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGQSNTNMLK
     VPECQLSDDL GNLWEGSRFT DCSLFVGGQE FKAHKSILAA RSPVFNAMFE HKMEESKKNR
     VDISDVEPDV FREMMVFIYT GKAPNLEKMA DNLLAAADKY ALERLKVLCE EALCNSLSVE
     NVADVLILAD LHSAEQLKAQ AIDFINRCSV LRQLGCKDGK NWNSNHAADI METAGWKAMI
     QSHPHLVAEA FRALASAQCT PFGLPRKRLK QS