ID   PSB3_CAEEL              Reviewed;         204 AA.
AC   Q23237;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Proteasome subunit beta type-3;
DE            Short=Proteasome subunit beta 3;
GN   Name=pbs-3; ORFNames=Y38A8.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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).
CC   -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic
CC       proteinase complex which is characterized by its ability to cleave
CC       peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC       at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC       proteolytic activity (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q23237; O62102: pbs-2; NbExp=5; IntAct=EBI-314040, EBI-317386;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; FO081756; CCD73694.1; -; Genomic_DNA.
DR   PIR; T26649; T26649.
DR   RefSeq; NP_494913.1; NM_062512.3.
DR   AlphaFoldDB; Q23237; -.
DR   SMR; Q23237; -.
DR   BioGRID; 39211; 46.
DR   DIP; DIP-25063N; -.
DR   IntAct; Q23237; 7.
DR   MINT; Q23237; -.
DR   STRING; 6239.Y38A8.2.1; -.
DR   EPD; Q23237; -.
DR   PaxDb; 6239-Y38A8-2; -.
DR   PeptideAtlas; Q23237; -.
DR   EnsemblMetazoa; Y38A8.2.1; Y38A8.2.1; WBGene00003949.
DR   GeneID; 173858; -.
DR   KEGG; cel:CELE_Y38A8.2; -.
DR   UCSC; Y38A8.2.1; c. elegans.
DR   AGR; WB:WBGene00003949; -.
DR   WormBase; Y38A8.2; CE07571; WBGene00003949; pbs-3.
DR   eggNOG; KOG0180; Eukaryota.
DR   GeneTree; ENSGT00550000074820; -.
DR   HOGENOM; CLU_035750_10_0_1; -.
DR   InParanoid; Q23237; -.
DR   OMA; CSEQLYG; -.
DR   OrthoDB; 1104143at2759; -.
DR   PhylomeDB; Q23237; -.
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-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-CEL-75815; Ubiquitin-dependent degradation of Cyclin D.
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-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:Q23237; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003949; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03759; proteasome_beta_type_3; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR033811; Proteasome_beta_3.
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:SF11; PROTEASOME CORE PARTICLE SUBUNIT BETA 3; 1.
DR   Pfam; PF00227; Proteasome; 1.
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   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Proteasome subunit beta type-3"
FT                   /id="PRO_0000148061"
SQ   SEQUENCE   204 AA;  22697 MW;  323D6122149D36B2 CRC64;
     MSIMSYTGGT VVAMAGDECV CIASDLRIGE QMTTIATDQK KVHKVTDKVY VGLAGFQSDA
     RTVLEKIMFR KNLYELRENR NIKPQVLSEM ISNLAYQHRF GSYFTEPLVA GLDDTNKPYI
     CCMDTIGCVS APRDFVAVGT GQEYLLGVCE NFWRENMKPD ELFEATAQSI LSCLERDAAS
     GWGAVVYTIT KDKVNVSTIK ARMD
//