ID   SPOPL_XENLA             Reviewed;         392 AA.
AC   Q6GR09;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Speckle-type POZ protein-like;
GN   Name=spopl;
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC071125; AAH71125.1; -; mRNA.
DR   RefSeq; NP_001085358.1; NM_001091889.1.
DR   AlphaFoldDB; Q6GR09; -.
DR   SMR; Q6GR09; -.
DR   PRIDE; Q6GR09; -.
DR   DNASU; 443784; -.
DR   GeneID; 443784; -.
DR   KEGG; xla:443784; -.
DR   CTD; 443784; -.
DR   Xenbase; XB-GENE-5871534; spopl.L.
DR   OMA; GAVMQSD; -.
DR   OrthoDB; 864323at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 443784; Expressed in blastula and 19 other tissues.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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"
FT                   /id="PRO_0000274592"
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"
SQ   SEQUENCE   392 AA;  44643 MW;  18E8ED5BFE2F232B CRC64;
     MHEVATTVSS AEMSSPPVAE SWCYTQVKVV KFSYMWTINN FSFCREETGE VLKSSSFSSG
     PNDKLKWCLR VNPKGLDDES KDYLSLYLLL VSCPKNEVRA KFKFSLLNSK NEETKAMESQ
     RAYRFVQGKD WGFKKYIRRD FLLDEANGLL PDDKLTLYCE VSVVQDSINI SGQSSSNNLK
     VPECRLAEDM GYLWENRRFT DCSLFVEGKE FKAHKSILAA RSPVFSAMFE HPMQESRKNR
     VYIRDVDPEV FKEMMRFIYT GGTPHVDKMA DKLLAAADKY ALERLKVMCE ESLCNNLTVE
     NVADVLILAD LHSAEQLKAQ AIDFINRCSV LGQLGCKDRK NCNSNQTMDI METAGWKSMI
     KSHPHLVAEA FRALASAQCP PFGIPRKRLK QS