ID   SPOPB_XENLA             Reviewed;         374 AA.
AC   Q0IHH9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Speckle-type POZ protein B;
GN   Name=spop-b;
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 (SEP-2006) 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 of
CC       target proteins, leading most often to their proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin-protein ligase complexes that contain CUL3 and SPOP, plus a
CC       target protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}.
CC   -!- DOMAIN: The BTB (POZ) domain mediates dimerization and interaction with
CC       CUL3. {ECO:0000250}.
CC   -!- DOMAIN: The MATH domain mediates interaction with protein-ubiquitin
CC       ligase substrates. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR   EMBL; BC123148; AAI23149.1; -; mRNA.
DR   RefSeq; NP_001090478.1; NM_001097009.1.
DR   RefSeq; XP_018093133.1; XM_018237644.1.
DR   AlphaFoldDB; Q0IHH9; -.
DR   SMR; Q0IHH9; -.
DR   DNASU; 779391; -.
DR   GeneID; 779391; -.
DR   KEGG; xla:779391; -.
DR   CTD; 779391; -.
DR   Xenbase; XB-GENE-1003315; spop.S.
DR   OMA; VRSTIEC; -.
DR   OrthoDB; 864323at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 779391; Expressed in testis and 19 other tissues.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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   CDD; cd18518; BACK_SPOP; 1.
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; IPR034089; SPOP_C.
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..374
FT                   /note="Speckle-type POZ protein B"
FT                   /id="PRO_0000274586"
FT   DOMAIN          31..161
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   DOMAIN          173..297
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          71..191
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000250"
FT   REGION          297..355
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  42170 MW;  6FA56BE42508239D CRC64;
     MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG
     ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ
     RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGQNTMNMVK
     VPECRLSDEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR
     VEIKDVEPDV FKEMMCFIYT GKASNLDKMA DDLLAAADKY ALERLKVMCE EALCSNLSVE
     NAAEILILAD LHSADQLKTQ AVDFINYHAS DVMETSGWKS MVVSHPHLVA EAYRSLASAQ
     CPFLGPPRKR LKQS