SPOP_CAEEL
ID SPOP_CAEEL Reviewed; 451 AA.
AC P34568; Q5CZ49;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Speckle-type POZ protein homolog {ECO:0000305};
DE AltName: Full=BTB and MATH domain-containing protein 43 {ECO:0000305};
DE AltName: Full=HIB homolog {ECO:0000305};
GN Name=spop-1 {ECO:0000312|WormBase:T16H12.5a};
GN Synonyms=bath-43 {ECO:0000312|WormBase:T16H12.5a};
GN ORFNames=T16H12.5 {ECO:0000312|WormBase:T16H12.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 187-TYR--TYR-451; TRP-195 AND PHE-197.
RX PubMed=34593637; DOI=10.1073/pnas.2104664118;
RA Snoznik C., Medvedeva V., Mojsilovic-Petrovic J., Rudich P., Oosten J.,
RA Kalb R.G., Lamitina T.;
RT "The nuclear ubiquitin ligase adaptor SPOP is a conserved regulator of
RT C9orf72 dipeptide toxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Mediates ubiquitination and proteasomal degradation of target
CC proteins, most likely in complex with cul-3 (PubMed:16740475). May
CC promote the degradation of bromodomain-containing proteins such as bet-
CC 1 (PubMed:34593637). {ECO:0000269|PubMed:16740475,
CC ECO:0000269|PubMed:34593637}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34593637}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O43791}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T16H12.5a};
CC IsoId=P34568-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T16H12.5b};
CC IsoId=P34568-2; Sequence=VSP_014361;
CC -!- DOMAIN: The BTB (POZ) domain mediates dimerization and interaction with
CC a cullin. {ECO:0000250|UniProtKB:O43791}.
CC -!- DOMAIN: The MATH domain mediates interaction with protein-ubiquitin
CC ligase substrates. {ECO:0000250|UniProtKB:O43791}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses the age-
CC dependent paralysis and growth arrest induced by exogenous dipeptide
CC repeat proteins PR50 and GR50. {ECO:0000269|PubMed:34593637}.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; BX284603; CAA83138.2; -; Genomic_DNA.
DR EMBL; BX284603; CAI58651.1; -; Genomic_DNA.
DR PIR; S42384; S42384.
DR RefSeq; NP_001022764.1; NM_001027593.1. [P34568-1]
DR RefSeq; NP_001022765.1; NM_001027594.3. [P34568-2]
DR AlphaFoldDB; P34568; -.
DR SMR; P34568; -.
DR BioGRID; 41616; 3.
DR IntAct; P34568; 2.
DR STRING; 6239.T16H12.5a; -.
DR EPD; P34568; -.
DR PaxDb; P34568; -.
DR EnsemblMetazoa; T16H12.5a.1; T16H12.5a.1; WBGene00011815. [P34568-1]
DR EnsemblMetazoa; T16H12.5b.1; T16H12.5b.1; WBGene00011815. [P34568-2]
DR GeneID; 176422; -.
DR KEGG; cel:CELE_T16H12.5; -.
DR UCSC; T16H12.5b.2; c. elegans. [P34568-1]
DR CTD; 176422; -.
DR WormBase; T16H12.5a; CE29054; WBGene00011815; spop-1. [P34568-1]
DR WormBase; T16H12.5b; CE00510; WBGene00011815; spop-1. [P34568-2]
DR eggNOG; KOG1987; Eukaryota.
DR GeneTree; ENSGT00940000155953; -.
DR InParanoid; P34568; -.
DR OMA; IKFNYMW; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; P34568; -.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR UniPathway; UPA00143; -.
DR PRO; PR:P34568; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011815; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..451
FT /note="Speckle-type POZ protein homolog"
FT /id="PRO_0000065467"
FT DOMAIN 95..225
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 265..338
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014361"
FT MUTAGEN 187..451
FT /note="Missing: In gk630214; suppresses the age-dependent
FT paralysis and growth arrest induced by exogenous dipeptide
FT repeat proteins PR50 and GR50. The age-dependent paralysis
FT phenotype is further suppressed in a bet-1 RNAi
FT background."
FT /evidence="ECO:0000269|PubMed:34593637"
FT MUTAGEN 195
FT /note="W->G: In dr95; suppresses the age-dependent
FT paralysis and growth arrest induced by exogenous dipeptide
FT repeat protein PR50. The age-dependent paralysis phenotype
FT is further suppressed in a bet-1 RNAi background."
FT /evidence="ECO:0000269|PubMed:34593637"
FT MUTAGEN 197
FT /note="F->V: In dr100; suppresses the age-dependent
FT paralysis and growth arrest induced by exogenous dipeptide
FT repeat protein PR50. Decreases spop-1 protein levels."
FT /evidence="ECO:0000269|PubMed:34593637"
SQ SEQUENCE 451 AA; 51062 MW; B36B1C618FBBB3A3 CRC64;
MILLAKFRNL YSKSRANDTI SEGDKPEKAT GDLEAGRNRL VSMEVGMGND EVVSSGSGNS
AHGRSISPSP SSASHGDPLL PVAENWCHTQ VKVVKFNYMW TINNFSFCRE EMGEVLKSST
FSAGCNDKLK WCLRINPKGL DEESRDYLSL YLLLVQCNKS EVRAKFKFSI LNAKREETKA
MESQRAYRFV QGKDWGFKKF IRRDFLLDEA NGLLPGDRLS IFCEVSVVAE TVNVTGQTNV
SQLFKVPPCR LADDMYGLFD NKQFSDFTLV CKSDLGSPTQ TFHIHKAILA ARSRVFSAMF
EHHMQESDTN MTTVDDIEPE VMRELLVYMY TGQTKYIEQM AQSLIAAADK YQLDRLKVMC
EQALCYQLTT DNASLTLMLA DMYSASQLRA HSINFINVNA NEVMDTEGWE DLVRDHPKLL
EEVFRALATQ QTPPVVLVQP PKKRPKHNCP Y
