SPOPL_MOUSE
ID SPOPL_MOUSE Reviewed; 392 AA.
AC Q2M2N2; A2AL52; Q3TSH4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Speckle-type POZ protein-like;
DE AltName: Full=HIB homolog 2;
GN Name=Spopl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 and
CC subsequent proteasomal degradation of target proteins, but with
CC relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complexes containing homodimeric SPOPL or the
CC heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin
CC ligase complexes containing only SPOP. May function to down-regulate
CC the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-
CC protein ligase complexes that contain SPOP (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Heterodimer with SPOP. Component of cullin-RING-
CC based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC containing homodimeric SPOPL or the heterodimer formed by SPOP and
CC SPOPL. Interacts with CUL3 and MACROH2A1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2M2N2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M2N2-2; Sequence=VSP_022824;
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI11868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE36701.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK162056; BAE36701.1; ALT_FRAME; mRNA.
DR EMBL; AL773534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08155.1; -; Genomic_DNA.
DR EMBL; BC111867; AAI11868.1; ALT_INIT; mRNA.
DR CCDS; CCDS15730.1; -. [Q2M2N2-1]
DR RefSeq; NP_001159469.1; NM_001165997.1. [Q2M2N2-2]
DR RefSeq; NP_001159470.1; NM_001165998.1. [Q2M2N2-2]
DR RefSeq; NP_084049.2; NM_029773.2. [Q2M2N2-1]
DR RefSeq; XP_006498477.1; XM_006498414.2. [Q2M2N2-1]
DR RefSeq; XP_017174813.1; XM_017319324.1. [Q2M2N2-2]
DR AlphaFoldDB; Q2M2N2; -.
DR SMR; Q2M2N2; -.
DR BioGRID; 218353; 23.
DR STRING; 10090.ENSMUSP00000114974; -.
DR PhosphoSitePlus; Q2M2N2; -.
DR MaxQB; Q2M2N2; -.
DR PaxDb; Q2M2N2; -.
DR PRIDE; Q2M2N2; -.
DR ProteomicsDB; 261576; -. [Q2M2N2-1]
DR Antibodypedia; 33596; 139 antibodies from 21 providers.
DR DNASU; 76857; -.
DR Ensembl; ENSMUST00000132484; ENSMUSP00000114974; ENSMUSG00000026771. [Q2M2N2-1]
DR GeneID; 76857; -.
DR KEGG; mmu:76857; -.
DR UCSC; uc008ioh.2; mouse. [Q2M2N2-1]
DR UCSC; uc008ioi.2; mouse. [Q2M2N2-2]
DR CTD; 339745; -.
DR MGI; MGI:1924107; Spopl.
DR VEuPathDB; HostDB:ENSMUSG00000026771; -.
DR eggNOG; KOG1987; Eukaryota.
DR GeneTree; ENSGT00940000155953; -.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q2M2N2; -.
DR OMA; GAVMQSD; -.
DR PhylomeDB; Q2M2N2; -.
DR TreeFam; TF313419; -.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76857; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Spopl; mouse.
DR PRO; PR:Q2M2N2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q2M2N2; protein.
DR Bgee; ENSMUSG00000026771; Expressed in otolith organ and 218 other tissues.
DR ExpressionAtlas; Q2M2N2; baseline and differential.
DR Genevisible; Q2M2N2; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; 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 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 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..392
FT /note="Speckle-type POZ protein-like"
FT /id="PRO_0000274589"
FT DOMAIN 31..161
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 200..267
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT VAR_SEQ 1..160
FT /note="MSREPTPPLPGDMSTSPVAESWCYTQVKVVKFSYMWTINNFSFCREEMGEVL
FT KSSTFSSGPNDKMKWCLRVNPKGLDDESKDYLSLYLLLVSCPKSEVRAKFKFSLLNDKR
FT EETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCE -> MIKGKK
FT QKQWKAKEHIDLYRGRTGDLKNSLEGIFCLMKLMVSFQMTSLRYSVSISNTACRRGGSI
FT ALPSLKNWHLPLHCKWCCRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022824"
FT CONFLICT 202
FT /note="C -> G (in Ref. 1; BAE36701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 44699 MW; 22471681536252CA CRC64;
MSREPTPPLP GDMSTSPVAE SWCYTQVKVV KFSYMWTINN FSFCREEMGE VLKSSTFSSG
PNDKMKWCLR VNPKGLDDES KDYLSLYLLL VSCPKSEVRA KFKFSLLNDK REETKAMESQ
RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNV SGHTSTNTLK
VPECRLAEDL GNLWENTRFT DCCFFVRGKE FKAHKSVLAA RSPVFNAMFE HEMEECTKNR
VEINDLDPEV FKEMMRFVYT GKAPNLDKMA DNLLAAADKY ALERLKVMCE EALCSNLSVE
NVADTLVLAD LHSAEQLKAQ AIDFINRCSV LRQLGCKDGK NWNNNQATDI METSGWKSMI
QSHPHLVAEA FRALASSQCP QFGIPRKRLK QS
