PSB9_BOVIN
ID PSB9_BOVIN Reviewed; 219 AA.
AC Q3SZC2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Proteasome subunit beta type-9;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit beta-1i;
DE Flags: Precursor;
GN Name=PSMB9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x;
RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., Muzney D.M.,
RA Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., Skow L.C.;
RT "Comparative analysis of the bovine MHC class IIb sequence identifies
RT inversion breakpoints and three unexpected genes.";
RL Anim. Genet. 37:121-129(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 (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. 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; AY957499; AAY34699.1; -; Genomic_DNA.
DR EMBL; BC102963; AAI02964.1; -; mRNA.
DR RefSeq; NP_001029560.1; NM_001034388.2.
DR PDB; 7DR6; EM; 4.10 A; W/Z=1-219.
DR PDB; 7DR7; EM; 3.30 A; W/Z=1-219.
DR PDB; 7DRW; EM; 4.20 A; W/Z=1-219.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3SZC2; -.
DR SMR; Q3SZC2; -.
DR IntAct; Q3SZC2; 1.
DR STRING; 9913.ENSBTAP00000011789; -.
DR MEROPS; T01.013; -.
DR PaxDb; Q3SZC2; -.
DR PRIDE; Q3SZC2; -.
DR Ensembl; ENSBTAT00000011789; ENSBTAP00000011789; ENSBTAG00000008954.
DR GeneID; 510593; -.
DR KEGG; bta:510593; -.
DR CTD; 5698; -.
DR VEuPathDB; HostDB:ENSBTAG00000008954; -.
DR VGNC; VGNC:33453; PSMB9.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000159897; -.
DR HOGENOM; CLU_035750_5_2_1; -.
DR InParanoid; Q3SZC2; -.
DR OMA; LPWAGEV; -.
DR OrthoDB; 1172133at2759; -.
DR TreeFam; TF106221; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000008954; Expressed in blood and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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: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 GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; IEA:Ensembl.
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 3D-structure; Acetylation; Cytoplasm; Hydrolase; Immunity; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..20
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239860"
FT CHAIN 21..219
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000239861"
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"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 69..90
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:7DR7"
SQ SEQUENCE 219 AA; 23404 MW; 16388C96B02E28C1 CRC64;
MLRTGAPNGD LPRAGEVHTG TTIMAVEFDG GVVVGSDSRV SAGEAVVNRV FDKLSPLHQH
IYCALSGSAA DAQAIADMAA YQLELHGMEL EEPPLVLAAA NVVRNITYKY REDLSAHLMV
AGWDQREGGQ VYGTMSGMLI RQPFAIGGSG STYIYGYVDA AYKPGMSPEE CRRFTTNAIA
LAMKRDGSSG GVIYLATITG AGVDHRVILG DELPRFYDE
