ID Q68EX4_XENLA Unreviewed; 277 AA.
AC Q68EX4;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN Name=psmb7.S {ECO:0000313|RefSeq:NP_001087535.1,
GN ECO:0000313|Xenbase:XB-GENE-946045};
GN Synonyms=MGC84123 {ECO:0000313|EMBL:AAH80076.1}, psmb7
GN {ECO:0000313|RefSeq:NP_001087535.1,
GN ECO:0000313|Xenbase:XB-GENE-946045};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH80076.1};
RN [1] {ECO:0000313|RefSeq:NP_001087535.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH80076.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000313|EMBL:AAH80076.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001087535.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- 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 EMBL; BC080076; AAH80076.1; -; mRNA.
DR RefSeq; NP_001087535.1; NM_001094066.1.
DR STRING; 8355.Q68EX4; -.
DR MEROPS; T01.A02; -.
DR PaxDb; 8355-Q68EX4; -.
DR DNASU; 447359; -.
DR GeneID; 447359; -.
DR KEGG; xla:447359; -.
DR AGR; Xenbase:XB-GENE-946045; -.
DR CTD; 447359; -.
DR Xenbase; XB-GENE-946045; psmb7.S.
DR OMA; VEKEFNC; -.
DR OrthoDB; 5485745at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 447359; Expressed in testis and 19 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:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03763; proteasome_beta_type_7; 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; IPR024689; Proteasome_bsu_C.
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:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR Pfam; PF12465; Pr_beta_C; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU004203};
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:UP000186698}.
FT DOMAIN 235..271
FT /note="Proteasome beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12465"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 277 AA; 30066 MW; 44D848D9C2DA03AB CRC64;
MATVTVRSAP VAGFDFGNCR RNTLLTNEFT QKGHKLPSSR KTGTTIAGIV FKDGVILGAD
TRATEGMIVA DKNCSKIHYI APNVYCCGAG TAADTEMTTQ MISSNMELHS LSTGRLPRVA
TANRMLKQML FRYQGYIGAA LVLGGVDCSG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDRYKPDME EEEAKQLVRN AIAAGIFNDL GSGSNIDLCV ITKNKVDYIR PHDVANKKGV
RTGNYKYKKG TTGILSEKIT HFNLDVMEES VQTMDIS
//
