PSB5_BOVIN
ID PSB5_BOVIN Reviewed; 263 AA.
AC Q32KL2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Proteasome subunit beta type-5;
DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
DE Flags: Precursor;
GN Name=PSMB5 {ECO:0000312|EMBL:AAI10040.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAI10040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI10040.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI10040.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC110039; AAI10040.1; -; mRNA.
DR RefSeq; NP_001032701.1; NM_001037612.2.
DR PDB; 1IRU; X-ray; 2.75 A; L/Z=60-262.
DR PDBsum; 1IRU; -.
DR AlphaFoldDB; Q32KL2; -.
DR SMR; Q32KL2; -.
DR IntAct; Q32KL2; 1.
DR STRING; 9913.ENSBTAP00000016918; -.
DR MEROPS; T01.012; -.
DR PaxDb; Q32KL2; -.
DR PRIDE; Q32KL2; -.
DR Ensembl; ENSBTAT00000016918; ENSBTAP00000016918; ENSBTAG00000012726.
DR GeneID; 534640; -.
DR KEGG; bta:534640; -.
DR CTD; 5693; -.
DR VEuPathDB; HostDB:ENSBTAG00000012726; -.
DR VGNC; VGNC:33449; PSMB5.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000157841; -.
DR HOGENOM; CLU_035750_7_3_1; -.
DR InParanoid; Q32KL2; -.
DR OMA; NLGMAMQ; -.
DR OrthoDB; 929961at2759; -.
DR TreeFam; TF106223; -.
DR EvolutionaryTrace; Q32KL2; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000012726; Expressed in tongue muscle and 106 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
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; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..59
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000331491"
FT CHAIN 60..263
FT /note="Proteasome subunit beta type-5"
FT /evidence="ECO:0000250|UniProtKB:P28074"
FT /id="PRO_0000331492"
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 STRAND 62..67
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 108..129
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 263 AA; 28609 MW; 63FB47F28EE677BF CRC64;
MALASVLERP LSVNRRGFFG LGGRADLLDL GPGSPSDGLS LAAPSWGVPE EPRIEILHGT
TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
SGATFSVGSG SVYAYGVMDR GYSYDLEVEE AYDLARRAIY QATYRDAYSG GSVSLYHVRE
DGWIRVSSDN VADLHDKYSG STH
