ID   PSB9_ORYLA              Reviewed;         217 AA.
AC   Q8UW64; Q8UWC6;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
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   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hd-rR, and HNI;
RX   PubMed=11862394; DOI=10.1007/s00251-001-0427-3;
RA   Matsuo M.Y., Asakawa S., Shimizu N., Kimura H., Nonaka M.;
RT   "Nucleotide sequence of the MHC class I genomic region of a teleost, the
RT   medaka (Oryzias latipes).";
RL   Immunogenetics 53:930-940(2002).
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; BA000027; BAB83845.1; -; Genomic_DNA.
DR   EMBL; AB073378; BAB84548.1; -; Genomic_DNA.
DR   RefSeq; NP_001265756.1; NM_001278827.1.
DR   AlphaFoldDB; Q8UW64; -.
DR   SMR; Q8UW64; -.
DR   STRING; 8090.ENSORLP00000008342; -.
DR   MEROPS; T01.013; -.
DR   GeneID; 100049434; -.
DR   KEGG; ola:100049434; -.
DR   CTD; 30665; -.
DR   eggNOG; KOG0174; Eukaryota.
DR   InParanoid; Q8UW64; -.
DR   OrthoDB; 1172133at2759; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW   Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..18
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026633"
FT   CHAIN           19..217
FT                   /note="Proteasome subunit beta type-9"
FT                   /id="PRO_0000026634"
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"
FT   VARIANT         5
FT                   /note="Missing (in strain: HD-RR)"
SQ   SEQUENCE   217 AA;  23547 MW;  A9AB1C04E57EB4C9 CRC64;
     MLGEEAEPQW ISEEVKTGTT IIAIEFNGGV VLGSDSRVSA GDSVVNRVMN KLSPLHDKIY
     CALSGSAADA QTIAEMVNYQ LDVHSLEIDE DPQVRSAATL VKNISYKYKE ELSAHLIVAG
     WDRRDGGQVF ATLGGLLTRQ PFAIGGSGSS YVYGFVDAEY RRGMTKEECQ KFVVNTLALA
     MNRDGSSGGV AYIVTIDEHS TDEKVILGND LPTFFDQ