ID   PSB9_ONCMY              Reviewed;         217 AA.
AC   Q9PT26;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Proteasome subunit beta type-9;
DE            EC=3.4.25.1;
DE   AltName: Full=Low molecular mass protein 2;
DE   Flags: Precursor;
GN   Name=psmb9; Synonyms=lmp2;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Shasta; TISSUE=Thymocyte;
RX   PubMed=10395670;
RA   Hansen J.D., Strassburger P., Thorgaard G.H., Young W.P., Du Pasquier L.;
RT   "Expression, linkage, and polymorphism of MHC-related genes in rainbow
RT   trout, Oncorhynchus mykiss.";
RL   J. Immunol. 163:774-786(1999).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity. This
CC       subunit is involved in antigen processing to generate class I binding
CC       peptides (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1;
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is composed of 28
CC       subunits that are arranged in four stacked rings, resulting in a
CC       barrel-shaped structure. The two end rings are each formed by seven
CC       alpha subunits, and the two central rings are each formed by seven beta
CC       subunits. The catalytic chamber with the active sites is on the inside
CC       of the barrel. Component of the immunoproteasome, where it displaces
CC       the equivalent housekeeping subunit PSMB6 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC       subunit is responsible for the nucleophile proteolytic activity.
CC       {ECO:0000250|UniProtKB:O35955}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; AF115541; AAD53038.1; -; mRNA.
DR   AlphaFoldDB; Q9PT26; -.
DR   SMR; Q9PT26; -.
DR   MEROPS; T01.013; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR034383; Proteasome_beta9.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF50; PTHR11599:SF50; 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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW   Threonine protease; Zymogen.
FT   PROPEP          1..18
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026635"
FT   CHAIN           19..217
FT                   /note="Proteasome subunit beta type-9"
FT                   /id="PRO_0000026636"
FT   ACT_SITE        19
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            18..19
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:O35955"
SQ   SEQUENCE   217 AA;  23406 MW;  69E680F35464B671 CRC64;
     MLDESLEPGW LSEEVKTGTT IIAIEFDGGV VLGSDSRVSA GETVVNRVMN KLSLLHDKIY
     CALSGSAADA QTIAEMVNYQ LDVHSIEVGE DPQVRSAATL VKNISYKYKE DLSAHLIVAG
     WDKRGGGQVY VTLNGLLSRQ PFAVGGSGSS YVYGFVDAEY RKAMSKEDCQ QFVVNTLSLA
     MSRDGSSGGV AYLVTIDEKG AEEKCILGNE LPTFYDQ