SPOP_PONAB
ID SPOP_PONAB Reviewed; 374 AA.
AC Q5NVK7; Q5R4U6; Q5R7J5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Speckle-type POZ protein;
GN Name=SPOP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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 of
CC target proteins, leading most often to their proteasomal degradation.
CC In complex with CUL3, involved in ubiquitination and proteasomal
CC degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with
CC CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not
CC lead to their proteasomal degradation. Inhibits transcriptional
CC activation of PDX1/IPF1 targets, such as insulin, by promoting
CC PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex containing homodimeric SPOP has higher
CC ubiquitin ligase activity than the complex that contains the
CC heterodimer formed by SPOP and SPOPL. Involved in the regulation of
CC bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4
CC stability. {ECO:0000250|UniProtKB:O43791}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O43791}.
CC -!- SUBUNIT: Interacts with GLI2 and GLI3 (By similarity). Homodimer and
CC homooligomer. Heterodimer with SPOPL. Each dimer interacts with two
CC CUL3 molecules. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complexes that contain CUL3 and homodimeric
CC SPOP, or the heterodimer formed by SPOP and SPOPL, plus a target
CC protein, such as MACROH2A1, PDX1/IPF1, BMI1, BRMS1 and DAXX (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O43791}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43791}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O43791}.
CC -!- DOMAIN: The BTB (POZ) domain mediates dimerization and interaction with
CC CUL3. {ECO:0000250|UniProtKB:O43791}.
CC -!- DOMAIN: The MATH domain mediates interaction with protein-ubiquitin
CC ligase substrates, such as MACROH2A1 and BMI1.
CC {ECO:0000250|UniProtKB:O43791}.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; CR860120; CAH92265.1; -; mRNA.
DR EMBL; CR861145; CAH93220.1; -; mRNA.
DR EMBL; CR926019; CAI29656.1; -; mRNA.
DR RefSeq; NP_001126893.1; NM_001133421.1.
DR AlphaFoldDB; Q5NVK7; -.
DR SMR; Q5NVK7; -.
DR STRING; 9601.ENSPPYP00000010012; -.
DR Ensembl; ENSPPYT00000010412; ENSPPYP00000010012; ENSPPYG00000008923.
DR GeneID; 100173908; -.
DR KEGG; pon:100173908; -.
DR CTD; 8405; -.
DR eggNOG; KOG1987; Eukaryota.
DR GeneTree; ENSGT00940000154376; -.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q5NVK7; -.
DR OMA; IKFNYMW; -.
DR OrthoDB; 864323at2759; -.
DR TreeFam; TF313419; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q5NVK7; -.
DR Proteomes; UP000001595; Chromosome 17.
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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
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_0000274583"
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 123..133
FT /note="Important for binding substrate proteins"
FT /evidence="ECO:0000250"
FT REGION 186..217
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250"
FT REGION 297..355
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250"
FT CONFLICT 98
FT /note="V -> I (in Ref. 1; CAH93220)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="F -> V (in Ref. 1; CAH92265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 42132 MW; EE5F4C5CF6FD09DC 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
VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE
NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ
CPFLGPPRKR LKQS
