PSB9_MUSPL
ID PSB9_MUSPL Reviewed; 219 AA.
AC O35523;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 platythrix (Flat-haired mouse) (Pyromys platythrix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Pyromys.
OX NCBI_TaxID=10101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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; D44459; BAA22580.1; -; mRNA.
DR AlphaFoldDB; O35523; -.
DR SMR; O35523; -.
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:0005839; C:proteasome core complex; ISS:UniProtKB.
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: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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW Threonine protease; Zymogen.
FT PROPEP 1..20
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026627"
FT CHAIN 21..219
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000026628"
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; 23442 MW; 820E9AE4B73BB376 CRC64;
MLRAGAPTAG SFRTKEVHTG TTIMAVEFDG GVVVGSDSRV SAGEAVVNRV FDKLSPLHQR
IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV
AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTSEE CRRFTTNAIT
LAMNRDGSSG GVIYLVTITV AGVDHRVILG DELPKFYDE