PSB5_RAT
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 03-AUG-2022, entry version 154.
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};
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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 SwissPalm; P28075; -.
DR jPOST; P28075; -.
DR PaxDb; P28075; -.
DR PRIDE; P28075; -.
DR GeneID; 29425; -.
DR KEGG; rno:29425; -.
DR UCSC; RGD:61879; rat.
DR CTD; 5693; -.
DR RGD; 61879; Psmb5.
DR eggNOG; KOG0175; Eukaryota.
DR InParanoid; P28075; -.
DR OrthoDB; 929961at2759; -.
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-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 Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR037558; Proteasome_beta_5.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF51; PTHR11599:SF51; 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; 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
