PSB9_MOUSE
ID PSB9_MOUSE Reviewed; 219 AA.
AC P28076; O09085; O09151; Q07704; Q60827; Q64278;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Proteasome subunit beta type-9;
DE EC=3.4.25.1;
DE AltName: Full=LMP-2d;
DE AltName: Full=Low molecular mass protein 2;
DE AltName: Full=Macropain chain 7;
DE AltName: Full=Multicatalytic endopeptidase complex chain 7;
DE AltName: Full=Proteasome chain 7;
DE AltName: Full=Proteasome subunit beta-1i;
DE AltName: Full=Really interesting new gene 12 protein;
DE Flags: Precursor;
GN Name=Psmb9; Synonyms=Lmp2, Ring12;
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 [MRNA].
RC STRAIN=Various strains;
RX PubMed=1681432; DOI=10.1038/353664a0;
RA Martinez C.K., Monaco J.J.;
RT "Homology of proteasome subunits to a major histocompatibility complex-
RT linked LMP gene.";
RL Nature 353:664-667(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NOD;
RX PubMed=7901128; DOI=10.1016/0378-1119(93)90646-K;
RA Kishi F., Suminami Y., Monaco J.J.;
RT "Genomic organization of the mouse Lmp-2 gene and characteristic structure
RT of its promoter.";
RL Gene 133:243-248(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LMP-2B AND LMP-2Q.
RX PubMed=7681985; DOI=10.1073/pnas.90.7.2681;
RA Zhou P., Cao H., Smart M., David C.;
RT "Molecular basis of genetic polymorphism in major histocompatibility
RT complex-linked proteasome gene (Lmp-2).";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2681-2684(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=8325639; DOI=10.1006/geno.1993.1245;
RA Zhou P., Zanelli E., Smart M., David C.;
RT "Genomic organization and tissue expression of mouse proteasome gene Lmp-
RT 2.";
RL Genomics 16:664-668(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.RIII, C57BL/6J, and R37;
RX PubMed=8854085;
RA Nandi D., Iyer M.N., Monaco J.J.;
RT "Molecular and serological analysis of polymorphisms in the murine major
RT histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7.";
RL Exp. Clin. Immunogenet. 13:20-29(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=8575819; DOI=10.1007/bf00587301;
RA Peleraux A., Karlsson L., Chambers J., Peterson P.A.;
RT "Genomic organization of a mouse MHC class II region including the H2-M and
RT Lmp2 loci.";
RL Immunogenetics 43:204-214(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Various strains; TISSUE=Spleen;
RA Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10.MOL-SGR;
RX PubMed=8672125; DOI=10.1007/s003359900149;
RA Mizuno K., Koide T., Sagai T., Moriwaki K., Shiroishi T.;
RT "Molecular analysis of a recombinational hotspot adjacent to Lmp2 gene in
RT the mouse MHC: fine location and chromatin structure.";
RL Mamm. Genome 7:490-496(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [11]
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16222703; DOI=10.1002/jcp.20508;
RA Wang H.X., Wang H.M., Lin H.Y., Yang Q., Zhang H., Tsang B.K., Zhu C.;
RT "Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9
RT expression and activities in human invasive extravillous trophoblast cell
RT line.";
RL J. Cell. Physiol. 206:616-623(2006).
RN [13]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
RA Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
RT "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
RT immunoproteasome-dependent epitopes.";
RL J. Immunol. 177:8393-8399(2006).
RN [14]
RP INDUCTION BY EGR1.
RX PubMed=16452686; DOI=10.1523/jneurosci.4199-05.2006;
RA James A.B., Conway A.M., Morris B.J.;
RT "Regulation of the neuronal proteasome by Zif268 (Egr1).";
RL J. Neurosci. 26:1624-1634(2006).
RN [15]
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 [16]
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 [17]
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).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
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).
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. Contributes to NFKBIA degradation and subsequently NFKB1
CC generation. {ECO:0000269|PubMed:16222703, 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 PSMB6. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Interacts with NCOA1, NCOA2 and NCOA3.
CC {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). Expressed at
CC high levels in the thymus, spleen, lung, heart and liver. Expressed at
CC moderate levels in the kidney. {ECO:0000269|PubMed:22341445,
CC ECO:0000269|PubMed:8325639}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Up-
CC regulated by IRF1. Up-regulated by heat shock treatment. Down-regulated
CC by EGR1 in neuronal cells. {ECO:0000269|PubMed:15907481,
CC ECO:0000269|PubMed:16452686, ECO:0000269|PubMed:17142736}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- DISRUPTION PHENOTYPE: Depletion of LMP2 by RNAi suppresses expression
CC and activities of the matrix metalloproteinase MMP2 and MMP9 by
CC blocking the transfer of active NF-kappa-B heterodimers into the
CC nucleus. {ECO:0000269|PubMed:16222703}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39439.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S59862; AAB20105.1; -; mRNA.
DR EMBL; U22448; AAA75305.1; -; mRNA.
DR EMBL; U22447; AAA75304.1; -; mRNA.
DR EMBL; S58203; AAP13903.1; -; mRNA.
DR EMBL; L11613; AAA39439.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U22919; AAA75306.1; -; mRNA.
DR EMBL; U22920; AAA75307.1; -; mRNA.
DR EMBL; U35323; AAA98932.1; -; Genomic_DNA.
DR EMBL; D14566; BAA40680.1; -; Genomic_DNA.
DR EMBL; D44454; BAA22575.1; -; mRNA.
DR EMBL; D44457; BAA22578.1; -; mRNA.
DR EMBL; D44458; BAA22579.1; -; mRNA.
DR EMBL; D44460; BAA22581.1; -; mRNA.
DR EMBL; D44461; BAA22582.1; -; mRNA.
DR EMBL; D44462; BAA22583.1; -; mRNA.
DR EMBL; D43620; BAA19855.1; -; Genomic_DNA.
DR EMBL; AF027865; AAB81528.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69911.1; -; Genomic_DNA.
DR EMBL; AK008429; BAB25664.1; -; mRNA.
DR CCDS; CCDS28642.1; -.
DR PIR; JC2019; JC2019.
DR RefSeq; NP_038613.1; NM_013585.2.
DR PDB; 3UNF; X-ray; 2.90 A; N/b=21-219.
DR PDB; 3UNH; X-ray; 3.20 A; N/b=21-219.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; P28076; -.
DR SMR; P28076; -.
DR BioGRID; 201181; 20.
DR CORUM; P28076; -.
DR IntAct; P28076; 5.
DR STRING; 10090.ENSMUSP00000133499; -.
DR BindingDB; P28076; -.
DR ChEMBL; CHEMBL1944491; -.
DR GuidetoPHARMACOLOGY; 2409; -.
DR MEROPS; T01.013; -.
DR iPTMnet; P28076; -.
DR PhosphoSitePlus; P28076; -.
DR EPD; P28076; -.
DR jPOST; P28076; -.
DR MaxQB; P28076; -.
DR PaxDb; P28076; -.
DR PeptideAtlas; P28076; -.
DR PRIDE; P28076; -.
DR ProteomicsDB; 291609; -.
DR DNASU; 16912; -.
DR GeneID; 16912; -.
DR KEGG; mmu:16912; -.
DR CTD; 5698; -.
DR MGI; MGI:1346526; Psmb9.
DR eggNOG; KOG0174; Eukaryota.
DR InParanoid; P28076; -.
DR OrthoDB; 1172133at2759; -.
DR PhylomeDB; P28076; -.
DR TreeFam; TF106221; -.
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; 16912; 8 hits in 77 CRISPR screens.
DR ChiTaRS; Psmb9; mouse.
DR PRO; PR:P28076; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P28076; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
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:0070628; F:proteasome binding; ISO:MGI.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034383; Proteasome_beta9.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF50; PTHR11599:SF50; 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; Immunity; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..20
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026621"
FT CHAIN 21..219
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000026622"
FT ACT_SITE 21
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 20..21
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28065"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28065"
FT VARIANT 60
FT /note="R -> H (in LMP-2b)"
FT VARIANT 126
FT /note="R -> C (in LMP-2b)"
FT VARIANT 177
FT /note="N -> D (in LMP-2b and LMP-2q)"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3UNF"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3UNF"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3UNF"
SQ SEQUENCE 219 AA; 23397 MW; 036BC558E770BD3E CRC64;
MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV FDKLSPLHQR
IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV
AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT
LAMNRDGSSG GVIYLVTITA AGVDHRVILG DELPKFYDE
