ID PSB5_RAT Reviewed; 263 AA. AC P28075; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 3. DT 27-MAR-2024, entry version 162. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yokota K.Y., Tanaka K.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; 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 [3] RP PROTEIN SEQUENCE OF 60-77. RX PubMed=2335214; DOI=10.1016/0014-5793(90)80220-d; RA Lilley K.S., Davison M.D., Rivett A.J.; RT "N-terminal sequence similarities between components of the multicatalytic RT proteinase complex."; RL FEBS Lett. 262:327-329(1990). RN [4] RP INDUCTION BY THP AND DNB. RX PubMed=16988215; DOI=10.1095/biolreprod.106.053173; RA Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.; RT "Differential expression of genes encoding constitutive and inducible 20S RT proteasomal core subunits in the testis and epididymis of theophylline- or RT 1,3-dinitrobenzene-exposed rats."; RL Biol. Reprod. 76:149-163(2007). 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:0000250|UniProtKB:P28074}. 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 Directly interacts with POMP. Interacts with ABCB1 and TAP1. CC {ECO:0000250|UniProtKB:P28074}. 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 -!- INDUCTION: Down-regulated by theophylline (THP) and up-regulated by CC 1,3-dinitrobenzene (DNB), two reprotoxic agents thought to induce CC infertility. {ECO:0000269|PubMed:16988215}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA08204.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA08204.1; Type=Miscellaneous discrepancy; Note=Sequencing error.; Evidence={ECO:0000305}; 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; D45247; BAA08204.1; ALT_SEQ; mRNA. DR EMBL; CH474049; EDM14180.1; -; Genomic_DNA. DR PIR; S09087; S09087. DR RefSeq; NP_001099197.2; NM_001105727.2. DR PDB; 6EPC; EM; 12.30 A; 5=1-263. DR PDB; 6EPD; EM; 15.40 A; 5=1-263. DR PDB; 6EPE; EM; 12.80 A; 5=1-263. DR PDB; 6EPF; EM; 11.80 A; 5=1-263. DR PDB; 6TU3; EM; 2.70 A; L/Z=1-263. DR PDBsum; 6EPC; -. DR PDBsum; 6EPD; -. DR PDBsum; 6EPE; -. DR PDBsum; 6EPF; -. DR PDBsum; 6TU3; -. DR AlphaFoldDB; P28075; -. DR SMR; P28075; -. DR BioGRID; 248073; 4. DR IntAct; P28075; 1. DR STRING; 10116.ENSRNOP00000018005; -. DR BindingDB; P28075; -. DR ChEMBL; CHEMBL4523208; -. DR MEROPS; T01.012; -. DR PhosphoSitePlus; P28075; -. DR SwissPalm; P28075; -. DR jPOST; P28075; -. DR PaxDb; 10116-ENSRNOP00000018005; -. DR GeneID; 29425; -. DR KEGG; rno:29425; -. DR UCSC; RGD:61879; rat. DR AGR; RGD:61879; -. DR CTD; 5693; -. DR RGD; 61879; Psmb5. DR eggNOG; KOG0175; Eukaryota. DR InParanoid; P28075; -. DR OrthoDB; 4492251at2759; -. DR PhylomeDB; P28075; -. DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-RNO-174113; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-RNO-2467813; Separation of Sister Chromatids. DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-RNO-382556; ABC-family proteins mediated transport. DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-RNO-4641257; Degradation of AXIN. DR Reactome; R-RNO-4641258; Degradation of DVL. DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis. DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-RNO-5632684; Hedgehog 'on' state. DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs. DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-RNO-5689603; UCH proteinases. DR Reactome; R-RNO-5689880; Ub-specific processing proteases. DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex. DR Reactome; R-RNO-68949; Orc1 removal from chromatin. DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-RNO-69481; G2/M Checkpoints. DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity. DR Reactome; R-RNO-8951664; Neddylation. DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR PRO; PR:P28075; -. DR Proteomes; UP000002494; Unplaced. DR Proteomes; UP000234681; Chromosome 15. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0000502; C:proteasome complex; ISO:RGD. DR GO; GO:0005839; C:proteasome core complex; ISS: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; ISO:RGD. 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; ISO:RGD. DR GO; GO:0006508; P:proteolysis; ISO:RGD. DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD. 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:SF10; 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:0000269|PubMed:2335214" FT /id="PRO_0000026593" FT CHAIN 60..263 FT /note="Proteasome subunit beta type-5" FT /id="PRO_0000026594" 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 62 FT /note="T -> I (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="H -> E (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="V -> L (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="P -> A (in Ref. 2; EDM14180)" FT /evidence="ECO:0000305" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 108..129 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 135..147 FT /evidence="ECO:0007829|PDB:6TU3" FT TURN 148..151 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 183..190 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 191..201 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 208..225 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 251..255 FT /evidence="ECO:0007829|PDB:6TU3" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:6TU3" SQ SEQUENCE 263 AA; 28585 MW; 317FC0C827FE65CA CRC64; MALASVLQRP MPVNQHGFFG LGGRADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT TTLAFKFQHG VIVAADSRAT AGPYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGTAFSVGSG SVYAFGVMDR GYSYDLQVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN VADLHDKYTS SIP //