ID   PSB5_PONAB              Reviewed;         263 AA.
AC   Q5R8S2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 3.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Proteasome subunit beta type-5;
DE            EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
DE   Flags: Precursor;
GN   Name=PSMB5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859678; CAH91838.1; -; mRNA.
DR   RefSeq; NP_001126063.1; NM_001132591.2.
DR   AlphaFoldDB; Q5R8S2; -.
DR   SMR; Q5R8S2; -.
DR   STRING; 9601.ENSPPYP00000006427; -.
DR   MEROPS; T01.012; -.
DR   Ensembl; ENSPPYT00000047037.1; ENSPPYP00000036656.1; ENSPPYG00000041109.1.
DR   GeneID; 100173015; -.
DR   KEGG; pon:100173015; -.
DR   CTD; 5693; -.
DR   eggNOG; KOG0175; Eukaryota.
DR   GeneTree; ENSGT00940000157841; -.
DR   HOGENOM; CLU_035750_7_3_1; -.
DR   InParanoid; Q5R8S2; -.
DR   OMA; NLGMAMQ; -.
DR   OrthoDB; 4492251at2759; -.
DR   TreeFam; TF106223; -.
DR   Proteomes; UP000001595; Chromosome 14.
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:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Threonine protease; Zymogen.
FT   PROPEP          1..59
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000276766"
FT   CHAIN           60..263
FT                   /note="Proteasome subunit beta type-5"
FT                   /id="PRO_0000276767"
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"
SQ   SEQUENCE   263 AA;  28480 MW;  AED4A73DF41AA6EF CRC64;
     MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT
     TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
     QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
     SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE
     DGWIRVSSDN VADLHEKYSG STP
//