ID G3N4G8_GASAC Unreviewed; 216 AA.
AC G3N4G8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000188.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000000188.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000000188.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC complex which is characterized by its ability to cleave peptides with
CC Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. {ECO:0000256|RuleBase:RU004203}.
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. {ECO:0000256|ARBA:ARBA00025456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC -!- SUBUNIT: Component of the proteasome complex.
CC {ECO:0000256|RuleBase:RU004203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC Nucleus {ECO:0000256|RuleBase:RU004203}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC {ECO:0000256|RuleBase:RU004203}.
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DR STRING; 69293.ENSGACP00000000180; -.
DR MEROPS; T01.013; -.
DR Ensembl; ENSGACT00000000180.1; ENSGACP00000000180.1; ENSGACG00000000137.1.
DR Ensembl; ENSGACT00000000188.1; ENSGACP00000000188.1; ENSGACG00000000143.1.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000159897; -.
DR OMA; SAGXMEL; -.
DR TreeFam; TF106221; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000000137; Expressed in spleen and 6 other cell types or tissues.
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; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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 CDD; cd03762; proteasome_beta_type_6; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF8; PROTEASOME SUBUNIT BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT ACT_SITE 18
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 216 AA; 23254 MW; F7539AFCA1A6ECBB CRC64;
MLQETGTEWL SQEVKTGTTI IAVEFDGGVV LGSDSRVSAG ASVVNRVMNK LSPLHDKIYC
ALSGSAADAQ TIAEVVHYQL DVHSIEIDED PQVRSAATLV RNISYKYKEE LSAHLIVAGW
DRRDGGQVFA TLSGLLTRQP FAVGGSGSSY VYGFVDAEFR GGMSKEECQQ FVVNTLSLAI
NRDGSSGGVA YIVSIDEHGT EEKVVLGNDL PTFFDQ
//
