SPOP_DANRE
ID SPOP_DANRE Reviewed; 374 AA.
AC Q7T330;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Speckle-type POZ protein;
DE AltName: Full=HIB homolog 1;
DE AltName: Full=SPOP1;
GN Name=spop; ORFNames=zgc:64140;
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 MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 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; BC053276; AAH53276.1; -; mRNA.
DR RefSeq; NP_957424.1; NM_201130.1.
DR AlphaFoldDB; Q7T330; -.
DR SMR; Q7T330; -.
DR ELM; Q7T330; -.
DR STRING; 7955.ENSDARP00000127981; -.
DR PaxDb; Q7T330; -.
DR Ensembl; ENSDART00000159457; ENSDARP00000135804; ENSDARG00000100519.
DR Ensembl; ENSDART00000163473; ENSDARP00000130146; ENSDARG00000100519.
DR Ensembl; ENSDART00000193532; ENSDARP00000152225; ENSDARG00000100519.
DR GeneID; 100005514; -.
DR KEGG; dre:100005514; -.
DR CTD; 8405; -.
DR ZFIN; ZDB-GENE-040426-1378; spop.
DR eggNOG; KOG1987; Eukaryota.
DR GeneTree; ENSGT00940000154376; -.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q7T330; -.
DR OMA; IKFNYMW; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; Q7T330; -.
DR TreeFam; TF313419; -.
DR Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7T330; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000100519; Expressed in retina and 27 other tissues.
DR ExpressionAtlas; Q7T330; baseline.
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_0000274584"
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; 42134 MW; 687F6479802EEEC1 CRC64;
MSRVPSPPPP AEMTSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG
ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ
RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGQNTMNMVK
VPDCRLADEL GGLWEHSRFT DCSLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR
VEINDVEAEV FKEMMFFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCTSLSVE
NAAEILILAD LHSADQLKTQ AVDFINYHAS DVMETSGWKS MVASHPHLVA EAYRSLASAQ
CPFLGPPRKR LKQS
