PSB10_MOUSE
ID PSB10_MOUSE Reviewed; 273 AA.
AC O35955; O08687; Q99KC5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Proteasome subunit beta type-10;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 10;
DE AltName: Full=Macropain subunit MECl-1;
DE AltName: Full=Multicatalytic endopeptidase complex subunit MECl-1;
DE AltName: Full=Proteasome MECl-1;
DE AltName: Full=Proteasome subunit beta-2i;
DE Flags: Precursor;
GN Name=Psmb10; Synonyms=Lmp10, Mecl1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and BALB/cJ; TISSUE=Liver;
RX PubMed=9367687; DOI=10.1006/geno.1997.4977;
RA Cruz M., Elenich L.A., Smolarek T.A., Menon A.G., Monaco J.J.;
RT "DNA sequence, chromosomal localization, and tissue expression of the mouse
RT proteasome subunit lmp10 (Psmb10) gene.";
RL Genomics 45:618-622(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RX PubMed=9300697;
RA Hayashi M., Ishibashi T., Tanaka K., Kasahara M.;
RT "The mouse genes encoding the third pair of beta-type proteasome subunits
RT regulated reciprocally by IFN-gamma: structural comparison, chromosomal
RT localization, and analysis of the promoter.";
RL J. Immunol. 159:2760-2770(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.;
RT "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1:
RT reciprocally regulated tissue expression of interferon-gamma-modulated
RT proteasome subunits.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MUTAGENESIS OF THR-40, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=10413086; DOI=10.1016/s0014-5793(99)00768-1;
RA Salzmann U., Kral S., Braun B., Standera S., Schmidt M., Kloetzel P.M.,
RA Sijts A.;
RT "Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation
RT of cleavage specificity between yeast and mammalian proteasomes.";
RL FEBS Lett. 454:11-15(1999).
RN [6]
RP INDUCTION BY INTERFERON GAMMA AND IRF1.
RX PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
RA Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K.,
RA Okamoto R., Kanai T., Watanabe M.;
RT "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression
RT of immunosubunits of the proteasome.";
RL FEBS Lett. 579:2781-2787(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=16709825; DOI=10.4049/jimmunol.176.11.6665;
RA Basler M., Moebius J., Elenich L., Groettrup M., Monaco J.J.;
RT "An altered T cell repertoire in MECL-1-deficient mice.";
RL J. Immunol. 176:6665-6672(2006).
RN [8]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP IDENTIFICATION IN THE SPERMATOPROTEASOME.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides. Plays a role in determining the T-cell repertoire for an
CC antiviral T-cell response. {ECO:0000269|PubMed:22341445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB7. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445,
CC ECO:0000269|PubMed:23706739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Up-
CC regulated by IRF1. {ECO:0000269|PubMed:15907481}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000305|PubMed:10413086}.
CC -!- DISRUPTION PHENOTYPE: Impaired response of cytotoxic T-lymphocyte (CTL)
CC to dominant epitopes of lymphocytic choriomeningitis virus (LCMV).
CC {ECO:0000269|PubMed:16709825}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; U77784; AAB86994.1; -; mRNA.
DR EMBL; U77785; AAB87637.1; -; Genomic_DNA.
DR EMBL; D85561; BAA22855.1; -; mRNA.
DR EMBL; D85562; BAA22856.1; -; Genomic_DNA.
DR EMBL; Y10875; CAA71825.1; -; mRNA.
DR EMBL; BC004730; AAH04730.1; -; mRNA.
DR CCDS; CCDS22621.1; -.
DR RefSeq; NP_038668.2; NM_013640.3.
DR PDB; 3UNF; X-ray; 2.90 A; H/V=40-273.
DR PDB; 3UNH; X-ray; 3.20 A; H/V=40-273.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; O35955; -.
DR SMR; O35955; -.
DR BioGRID; 202419; 20.
DR CORUM; O35955; -.
DR IntAct; O35955; 4.
DR STRING; 10090.ENSMUSP00000034369; -.
DR BindingDB; O35955; -.
DR ChEMBL; CHEMBL4523133; -.
DR MEROPS; T01.014; -.
DR iPTMnet; O35955; -.
DR PhosphoSitePlus; O35955; -.
DR CPTAC; non-CPTAC-3611; -.
DR EPD; O35955; -.
DR MaxQB; O35955; -.
DR PaxDb; O35955; -.
DR PeptideAtlas; O35955; -.
DR PRIDE; O35955; -.
DR ProteomicsDB; 291655; -.
DR Antibodypedia; 29677; 235 antibodies from 35 providers.
DR DNASU; 19171; -.
DR Ensembl; ENSMUST00000034369; ENSMUSP00000034369; ENSMUSG00000031897.
DR GeneID; 19171; -.
DR KEGG; mmu:19171; -.
DR UCSC; uc009nep.2; mouse.
DR CTD; 5699; -.
DR MGI; MGI:1096380; Psmb10.
DR VEuPathDB; HostDB:ENSMUSG00000031897; -.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000161047; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; O35955; -.
DR OMA; RVSYGFY; -.
DR OrthoDB; 977476at2759; -.
DR PhylomeDB; O35955; -.
DR TreeFam; TF106222; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19171; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Psmb10; mouse.
DR PRO; PR:O35955; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35955; protein.
DR Bgee; ENSMUSG00000031897; Expressed in small intestine Peyer's patch and 240 other tissues.
DR Genevisible; O35955; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034384; Proteasome_beta2/10.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF41; PTHR11599:SF41; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..39
FT /note="Removed in mature form"
FT /id="PRO_0000026653"
FT CHAIN 40..273
FT /note="Proteasome subunit beta type-10"
FT /id="PRO_0000026654"
FT ACT_SITE 40
FT /note="Nucleophile"
FT SITE 39..40
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:10413086"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P40306"
FT MUTAGEN 40
FT /note="T->A: Prevents the correct removal of the
FT propeptide."
FT /evidence="ECO:0000269|PubMed:10413086"
FT CONFLICT 4
FT /note="Q -> E (in Ref. 4; AAH04730)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="T -> R (in Ref. 4; AAH04730)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> L (in Ref. 3; CAA71825)"
FT /evidence="ECO:0000305"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 88..109
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3UNF"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3UNH"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:3UNF"
SQ SEQUENCE 273 AA; 29063 MW; 9A1AAE55888FA905 CRC64;
MLKQAVEPTG GFSFENCQRN ASLEHVLPGL RVPHARKTGT TIAGLVFRDG VILGADTRAT
NDSVVADKSC EKIHFIAPKI YCCGAGVAAD TEMTTRMAAS KMELHALSTG REPRVATVTR
ILRQTLFRYQ GHVGASLVVG GVDLNGPQLY EVHPHGSYSR LPFTALGSGQ GAAVALLEDR
FQPNMTLEAA QELLVEAITA GILSDLGSGG NVDACVITAG GAKLQRALST PTEPVQRAGR
YRFAPGTTPV LTREVRPLTL ELLEETVQAM EVE
