PBS5_CAEEL
ID PBS5_CAEEL Reviewed; 284 AA.
AC Q9XUV0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Proteasome subunit pbs-5 {ECO:0000312|WormBase:K05C4.1};
DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
DE Flags: Precursor;
GN Name=pbs-5 {ECO:0000312|WormBase:K05C4.1};
GN ORFNames=K05C4.1 {ECO:0000312|WormBase:K05C4.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27528192; DOI=10.7554/elife.17721;
RA Lehrbach N.J., Ruvkun G.;
RT "Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic
RT protease DDI-1.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins
CC (PubMed:27528192). This complex plays numerous essential roles within
CC the cell by associating with different regulatory particles (By
CC similarity). Associated with two 19S regulatory particles, forms the
CC 26S proteasome and thus participates in the ATP-dependent degradation
CC of ubiquitinated proteins (By similarity). The 26S proteasome plays a
CC key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required (By
CC similarity). {ECO:0000250|UniProtKB:P28074,
CC ECO:0000269|PubMed:27528192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28074};
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. {ECO:0000250|UniProtKB:P28074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250|UniProtKB:P28074}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Constitutive skn-1-
CC dependent expression of the proteasomal subunit rpt-3. Double knockout
CC with ddi-1, sel-1, sel-9, png-1 or skn-1a results in failed expression
CC of the proteasomal subunit rpt-3. {ECO:0000269|PubMed:27528192}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BX284601; CAB04567.1; -; Genomic_DNA.
DR PIR; T23336; T23336.
DR RefSeq; NP_493558.1; NM_061157.4.
DR AlphaFoldDB; Q9XUV0; -.
DR SMR; Q9XUV0; -.
DR DIP; DIP-25961N; -.
DR IntAct; Q9XUV0; 4.
DR STRING; 6239.K05C4.1; -.
DR MEROPS; T01.A09; -.
DR EPD; Q9XUV0; -.
DR PaxDb; Q9XUV0; -.
DR PeptideAtlas; Q9XUV0; -.
DR EnsemblMetazoa; K05C4.1.1; K05C4.1.1; WBGene00003951.
DR GeneID; 173334; -.
DR KEGG; cel:CELE_K05C4.1; -.
DR UCSC; K05C4.1.1; c. elegans.
DR CTD; 173334; -.
DR WormBase; K05C4.1; CE19969; WBGene00003951; pbs-5.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000166784; -.
DR HOGENOM; CLU_035750_7_1_1; -.
DR InParanoid; Q9XUV0; -.
DR OMA; NLGMAMQ; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; Q9XUV0; -.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q9XUV0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003951; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT CHAIN 1..284
FT /note="Proteasome subunit pbs-5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442337"
FT PROPEP 1..64
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P28074"
FT /id="PRO_0000442336"
FT ACT_SITE 65
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28074"
SQ SEQUENCE 284 AA; 31230 MW; A382E295F2C50604 CRC64;
MWGETFDDFE NDEGEMAMAK QNLIAEPARA DFTFAKLPLG IQPVDFMKTH FAETAGKSMQ
FRKGTTTLAF VYEPATPADK GGIIVAVDSR ASSGEYISSK SVMKILDIGD RMVATMAGGA
ADCQFWTRIV AKYCTLYELR EKTSITVSAA SKYFANTLYG YRGQGLSVGS MVAGYDKKGP
QIFKVDSEGD RCQLKVCSVG SGSLNAYGIL DNHYKPKMTD DEARKLGLRA IMHATYRDSG
SGGVCNLCHI TPTEKIRLPP MDVSKLWYEF ADELGRDITY NPVE
