ID   PSB5_MOUSE              Reviewed;         264 AA.
AC   O55234; Q3UZI1; Q91X53; Q9CWR4; Q9R1P2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 3.
DT   24-JAN-2024, entry version 186.
DE   RecName: Full=Proteasome subunit beta type-5;
DE            EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
DE   AltName: Full=Macropain epsilon chain;
DE   AltName: Full=Multicatalytic endopeptidase complex epsilon chain;
DE   AltName: Full=Proteasome chain 6;
DE   AltName: Full=Proteasome epsilon chain;
DE   AltName: Full=Proteasome subunit X;
DE   Flags: Precursor;
GN   Name=Psmb5;
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 C57BL/6J;
RX   PubMed=9382924; DOI=10.1007/s002510050329;
RA   Kohda K., Matsuda Y., Ishibashi T., Tanaka K., Kasahara M.;
RT   "Structural analysis and chromosomal localization of the mouse Psmb5 gene
RT   coding for the constitutively expressed beta-type proteasome subunit.";
RL   Immunogenetics 47:77-87(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B10.A; TISSUE=Macrophage;
RX   PubMed=10436176; DOI=10.1007/s002510050562;
RA   Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA   Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT   "The complete primary structure of mouse 20S proteasomes.";
RL   Immunogenetics 49:835-842(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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   PROTEIN SEQUENCE OF 79-91; 141-150 AND 167-179, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INDUCTION BY ANTIOXIDANTS.
RX   PubMed=14612418; DOI=10.1128/mcb.23.23.8786-8794.2003;
RA   Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W.;
RT   "Antioxidants enhance mammalian proteasome expression through the Keap1-
RT   Nrf2 signaling pathway.";
RL   Mol. Cell. Biol. 23:8786-8794(2003).
RN   [7]
RP   INDUCTION BY ANTIOXIDANTS.
RX   PubMed=16723119; DOI=10.1016/j.bbrc.2006.05.043;
RA   Kwak M.K., Kensler T.W.;
RT   "Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer 3-
RT   methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE,
RT   pathway.";
RL   Biochem. Biophys. Res. Commun. 345:1350-1357(2006).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16434403; DOI=10.1074/jbc.m511512200;
RA   Ma X.H., Hu S.J., Ni H., Zhao Y.C., Tian Z., Liu J.L., Ren G., Liang X.H.,
RA   Yu H., Wan P., Yang Z.M.;
RT   "Serial analysis of gene expression in mouse uterus at the implantation
RT   site.";
RL   J. Biol. Chem. 281:9351-9360(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA   Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA   Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA   Sleckman B.P.;
RT   "Proteasome activator PA200 is required for normal spermatogenesis.";
RL   Mol. Cell. Biol. 26:2999-3007(2006).
RN   [10]
RP   INDUCTION BY DITHIOLETHIONE.
RX   PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
RA   Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
RT   "Tissue specific increase of the catalytic subunits of the 26S proteasome
RT   by indirect antioxidant dithiolethione in mice: enhanced activity for
RT   degradation of abnormal protein.";
RL   Life Sci. 80:2411-2420(2007).
RN   [11]
RP   INDUCTION BY LITHIUM.
RX   PubMed=18349697; DOI=10.1097/ypg.0b013e3282fb0051;
RA   Chetcuti A., Adams L.J., Mitchell P.B., Schofield P.R.;
RT   "Microarray gene expression profiling of mouse brain mRNA in a model of
RT   lithium treatment.";
RL   Psychiatr. Genet. 18:64-72(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=19183883; DOI=10.1007/s12272-009-1124-2;
RA   Park H.M., Kim J.A., Kwak M.K.;
RT   "Protection against amyloid beta cytotoxicity by sulforaphane: role of the
RT   proteasome.";
RL   Arch. Pharm. Res. 32:109-115(2009).
RN   [13]
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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and 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   [15]
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: Component of the 20S core proteasome complex involved in the
CC       proteolytic degradation of most intracellular proteins. This complex
CC       plays numerous essential roles within the cell by associating with
CC       different regulatory particles. Associated with two 19S regulatory
CC       particles, forms the 26S proteasome and thus participates in the ATP-
CC       dependent degradation of ubiquitinated proteins. The 26S proteasome
CC       plays a key role in the maintenance of protein homeostasis by removing
CC       misfolded or damaged proteins that could impair cellular functions, and
CC       by removing proteins whose functions are no longer required. Associated
CC       with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC       independent protein degradation. This type of proteolysis is required
CC       in several pathways including spermatogenesis (20S-PA200 complex) or
CC       generation of a subset of MHC class I-presented antigenic peptides
CC       (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a
CC       chymotrypsin-like activity. {ECO:0000269|PubMed:16581775,
CC       ECO:0000269|PubMed:19183883, ECO:0000269|PubMed:22341445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28074};
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7
CC       (PubMed:16857966, PubMed:22341445). Directly interacts with POMP (By
CC       similarity). Interacts with ABCB1 and TAP1 (By similarity).
CC       {ECO:0000250|UniProtKB:P28074, ECO:0000269|PubMed:16857966,
CC       ECO:0000269|PubMed:22341445}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}. Nucleus
CC       {ECO:0000250|UniProtKB:P28074}. Note=Translocated from the cytoplasm
CC       into the nucleus following interaction with AKIRIN2, which bridges the
CC       proteasome with the nuclear import receptor IPO9.
CC       {ECO:0000250|UniProtKB:P28074}.
CC   -!- TISSUE SPECIFICITY: Expressed in uterus at the embryo implantation
CC       site. {ECO:0000269|PubMed:16434403, ECO:0000269|PubMed:22341445}.
CC   -!- INDUCTION: Up-regulated in embryonic fibroblasts and neuroblastoma
CC       cells by antioxidants through the Nrf2-ARE pathway (at protein level).
CC       Up-regulated by the antioxidant dithiolethione (D3T) in liver, small
CC       intestine and brain (at protein level). Down-regulated under lithium
CC       treatment. {ECO:0000269|PubMed:14612418, ECO:0000269|PubMed:16723119,
CC       ECO:0000269|PubMed:17521679, ECO:0000269|PubMed:18349697}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB003304; BAA24916.1; -; mRNA.
DR   EMBL; AB003306; BAA24917.1; -; Genomic_DNA.
DR   EMBL; AF060091; AAD50536.1; -; mRNA.
DR   EMBL; AK010441; BAB26942.1; -; mRNA.
DR   EMBL; AK133839; BAE21876.1; -; mRNA.
DR   EMBL; BC012246; AAH12246.1; -; mRNA.
DR   EMBL; BC106144; AAI06145.1; -; mRNA.
DR   CCDS; CCDS27095.1; -.
DR   RefSeq; NP_035316.1; NM_011186.1.
DR   PDB; 3UNB; X-ray; 2.90 A; 1/K/Y/m=60-264.
DR   PDB; 3UNE; X-ray; 3.20 A; 1/K/Y/m=60-264.
DR   PDBsum; 3UNB; -.
DR   PDBsum; 3UNE; -.
DR   AlphaFoldDB; O55234; -.
DR   SMR; O55234; -.
DR   BioGRID; 202421; 109.
DR   CORUM; O55234; -.
DR   IntAct; O55234; 67.
DR   STRING; 10090.ENSMUSP00000022803; -.
DR   BindingDB; O55234; -.
DR   ChEMBL; CHEMBL1944494; -.
DR   MEROPS; T01.012; -.
DR   iPTMnet; O55234; -.
DR   MetOSite; O55234; -.
DR   PhosphoSitePlus; O55234; -.
DR   SwissPalm; O55234; -.
DR   EPD; O55234; -.
DR   jPOST; O55234; -.
DR   MaxQB; O55234; -.
DR   PaxDb; 10090-ENSMUSP00000022803; -.
DR   PeptideAtlas; O55234; -.
DR   ProteomicsDB; 291762; -.
DR   Pumba; O55234; -.
DR   Antibodypedia; 22368; 264 antibodies from 34 providers.
DR   DNASU; 19173; -.
DR   Ensembl; ENSMUST00000022803.6; ENSMUSP00000022803.5; ENSMUSG00000022193.8.
DR   GeneID; 19173; -.
DR   KEGG; mmu:19173; -.
DR   UCSC; uc007twl.1; mouse.
DR   AGR; MGI:1194513; -.
DR   CTD; 5693; -.
DR   MGI; MGI:1194513; Psmb5.
DR   VEuPathDB; HostDB:ENSMUSG00000022193; -.
DR   eggNOG; KOG0175; Eukaryota.
DR   GeneTree; ENSGT00940000157841; -.
DR   HOGENOM; CLU_035750_7_3_1; -.
DR   InParanoid; O55234; -.
DR   OMA; NLGMAMQ; -.
DR   OrthoDB; 4492251at2759; -.
DR   PhylomeDB; O55234; -.
DR   TreeFam; TF106223; -.
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; 19173; 22 hits in 73 CRISPR screens.
DR   ChiTaRS; Psmb5; mouse.
DR   PRO; PR:O55234; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; O55234; Protein.
DR   Bgee; ENSMUSG00000022193; Expressed in proximal tubule and 69 other cell types or tissues.
DR   ExpressionAtlas; O55234; baseline and differential.
DR   Genevisible; O55234; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
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:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR   CDD; cd03761; proteasome_beta_type_5; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF3; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW   Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..59
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026591"
FT   CHAIN           60..264
FT                   /note="Proteasome subunit beta type-5"
FT                   /id="PRO_0000026592"
FT   ACT_SITE        60
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P28074"
FT   BINDING         108
FT                   /ligand="bortezomib"
FT                   /ligand_id="ChEBI:CHEBI:52717"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        110
FT                   /note="D -> N (in Ref. 3; BAB26942)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="S -> N (in Ref. 4; AAH12246)"
FT                   /evidence="ECO:0000305"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   HELIX           108..129
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   HELIX           135..147
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   TURN            148..153
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          156..164
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   HELIX           191..200
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   HELIX           208..225
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:3UNE"
FT   STRAND          231..239
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   STRAND          242..250
FT                   /evidence="ECO:0007829|PDB:3UNB"
FT   HELIX           251..258
FT                   /evidence="ECO:0007829|PDB:3UNB"
SQ   SEQUENCE   264 AA;  28532 MW;  FCCD619734EF3C57 CRC64;
     MALASVLQRP MPVNQHGFFG LGGGADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT
     TTLAFKFLHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
     QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
     SGTAFSVGSG SVYAYGVMDR GYSYDLKVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE
     DGWIRVSSDN VADLHDKYSS VSVP
//