ID   PSB9_MUSSI              Reviewed;         219 AA.
AC   O35524;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Proteasome subunit beta type-9;
DE            EC=3.4.25.1;
DE   AltName: Full=Low molecular mass protein 2;
DE   AltName: Full=Macropain chain 7;
DE   AltName: Full=Multicatalytic endopeptidase complex chain 7;
DE   AltName: Full=Proteasome chain 7;
DE   AltName: Full=Proteasome subunit beta-1i;
DE   AltName: Full=Really interesting new gene 12 protein;
DE   Flags: Precursor;
GN   Name=Psmb9; Synonyms=Lmp2, Ring12;
OS   Mus spicilegus (Steppe mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ZBN; TISSUE=Spleen;
RA   Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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.
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. Component of the
CC       spermatoproteasome, a form of the proteasome specifically found in
CC       testis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by interferon gamma (at protein level).
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   -!- MISCELLANEOUS: Encoded in the MHC class II region.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; D44463; BAA22584.1; -; mRNA.
DR   AlphaFoldDB; O35524; -.
DR   SMR; O35524; -.
DR   MEROPS; T01.013; -.
DR   MGI; MGI:1346526; Psmb9.
DR   Proteomes; UP000694415; Unplaced.
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:1990111; C:spermatoproteasome 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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW   Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..20
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026629"
FT   CHAIN           21..219
FT                   /note="Proteasome subunit beta type-9"
FT                   /id="PRO_0000026630"
FT   ACT_SITE        21
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            20..21
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:O35955"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P28065"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P28065"
SQ   SEQUENCE   219 AA;  23425 MW;  036BC558F040BD3E CRC64;
     MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV FDKLSPLHQR
     IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV
     AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT
     LAMNRDGSSG GVIYLVTITA AGVDHRVILG DELPRFYDE