ID   SPOP_XENTR              Reviewed;         374 AA.
AC   Q6P8B3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Speckle-type POZ protein;
GN   Name=spop;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) 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; BC061316; AAH61316.1; -; mRNA.
DR   RefSeq; NP_989003.1; NM_203672.1.
DR   RefSeq; XP_012827047.1; XM_012971593.2.
DR   RefSeq; XP_012827048.1; XM_012971594.2.
DR   RefSeq; XP_012827050.1; XM_012971596.2.
DR   RefSeq; XP_017953174.1; XM_018097685.1.
DR   AlphaFoldDB; Q6P8B3; -.
DR   SMR; Q6P8B3; -.
DR   STRING; 8364.ENSXETP00000057841; -.
DR   PaxDb; Q6P8B3; -.
DR   DNASU; 394599; -.
DR   Ensembl; ENSXETT00000057841; ENSXETP00000057841; ENSXETG00000027799.
DR   GeneID; 394599; -.
DR   KEGG; xtr:394599; -.
DR   CTD; 8405; -.
DR   Xenbase; XB-GENE-1003310; spop.
DR   eggNOG; KOG1987; Eukaryota.
DR   HOGENOM; CLU_004253_2_0_1; -.
DR   InParanoid; Q6P8B3; -.
DR   OrthoDB; 864323at2759; -.
DR   PhylomeDB; Q6P8B3; -.
DR   Reactome; R-XTR-5632684; Hedgehog 'on' state.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000027799; Expressed in skeletal muscle tissue and 13 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:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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   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"
FT                   /id="PRO_0000274587"
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;  42154 MW;  2DC5738E57025BF7 CRC64;
     MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG
     ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ
     RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGQNTMNMVK
     VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR
     VEIKDVEPDV FKEMMCFIYT GKASNLDKMA DDLLAAADKY ALERLKVMCE EALCSNLSVE
     NAAEILILAD LHSADQLKTQ AVDFINYHAS DVMETSGWKS MVVSHPHLVA EAYRSLASAQ
     CPFLGPPRKR LKQS