PSB9_SALSA
ID PSB9_SALSA Reviewed; 217 AA.
AC Q9DD33; A7KE02;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
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-a; Synonyms=lmp2-a;
GN and
GN Name=psmb9-b; Synonyms=lmp2-b;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Grimholt U.;
RT "Proteasome genes in Atlantic salmon.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17651474; DOI=10.1186/1471-2164-8-251;
RA Lukacs M.F., Harstad H., Grimholt U., Beetz-Sargent M., Cooper G.A.,
RA Reid L., Bakke H.G., Phillips R.B., Miller K.M., Davidson W.S., Koop B.F.;
RT "Genomic organization of duplicated major histocompatibility complex class
RT I regions in Atlantic salmon (Salmo salar).";
RL BMC Genomics 8:251-251(2007).
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; AF184932; AAG43434.1; -; mRNA.
DR EMBL; AF184933; AAG43435.1; -; mRNA.
DR EMBL; AF184934; AAG43436.1; -; mRNA.
DR EMBL; AF184935; AAG43437.1; -; mRNA.
DR EMBL; AF184936; AAG43438.1; -; mRNA.
DR EMBL; EF210363; ABQ01991.1; -; Genomic_DNA.
DR EMBL; EF427379; ABQ59649.1; -; Genomic_DNA.
DR EMBL; EF427384; ABQ59682.1; -; Genomic_DNA.
DR RefSeq; NP_001117174.1; NM_001123702.2.
DR RefSeq; NP_001117186.1; NM_001123714.1.
DR RefSeq; XP_014032547.1; XM_014177072.1.
DR RefSeq; XP_014032548.1; XM_014177073.1.
DR RefSeq; XP_014032549.1; XM_014177074.1.
DR AlphaFoldDB; Q9DD33; -.
DR SMR; Q9DD33; -.
DR STRING; 8030.ENSSSAP00000035410; -.
DR MEROPS; T01.013; -.
DR GeneID; 100136936; -.
DR GeneID; 100137045; -.
DR KEGG; sasa:100136936; -.
DR KEGG; sasa:100137045; -.
DR CTD; 100136936; -.
DR CTD; 30665; -.
DR OrthoDB; 1172133at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR Proteomes; UP000087266; Chromosome ssa27.
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 Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..18
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026637"
FT CHAIN 19..217
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000026638"
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; 23392 MW; E3543052F7AEA800 CRC64;
MLEESSEPGW LSEEVKTGTT IIAIEFDGGV VLGSDSRVSA GETVVNRVMN KLSLLHDKIY
CALSGSAADA QTIAEMVNYQ LDVHSIEVGE DPQVRSAATL VKNISYKYKE ELSAHLIVAG
WDKRGGGQVY VTLNGLLSRQ PFAVGGSGSA YVYGFVDAEY RKAMSKEDCQ QFVVNTLSLA
MSRDGSSGGV AYLVTIDEKG AEEKCILGNE LPTFYDQ
