ID   PSB1_CAEEL              Reviewed;         258 AA.
AC   P34286; Q9BMU3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Proteasome subunit beta type-1;
DE   AltName: Full=Proteasome subunit beta 6;
GN   Name=pbs-6; ORFNames=C02F5.9;
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=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin'i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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       P34286; O17200: fbxa-166; NbExp=3; IntAct=EBI-313778, EBI-313801;
CC       P34286; Q9XVK6: wve-1; NbExp=3; IntAct=EBI-313778, EBI-312105;
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; FO080288; CCD62635.1; -; Genomic_DNA.
DR   EMBL; AF303265; AAG50223.1; -; mRNA.
DR   PIR; S44611; S44611.
DR   RefSeq; NP_498806.1; NM_066405.4.
DR   AlphaFoldDB; P34286; -.
DR   SMR; P34286; -.
DR   BioGRID; 41365; 46.
DR   DIP; DIP-24619N; -.
DR   IntAct; P34286; 14.
DR   STRING; 6239.C02F5.9; -.
DR   EPD; P34286; -.
DR   PaxDb; P34286; -.
DR   PeptideAtlas; P34286; -.
DR   EnsemblMetazoa; C02F5.9.1; C02F5.9.1; WBGene00003952.
DR   GeneID; 176161; -.
DR   KEGG; cel:CELE_C02F5.9; -.
DR   UCSC; C02F5.9.1; c. elegans.
DR   CTD; 176161; -.
DR   WormBase; C02F5.9; CE26745; WBGene00003952; pbs-6.
DR   eggNOG; KOG0179; Eukaryota.
DR   GeneTree; ENSGT00550000075035; -.
DR   HOGENOM; CLU_035750_1_1_1; -.
DR   InParanoid; P34286; -.
DR   OMA; IDQDGQG; -.
DR   OrthoDB; 1092660at2759; -.
DR   PhylomeDB; P34286; -.
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-6798695; Neutrophil degranulation.
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:P34286; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003952; 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; ISS:UniProtKB.
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; IPR035202; Proteasome_beta1.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
DR   Pfam; PF00227; Proteasome; 1.
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   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Proteasome subunit beta type-1"
FT                   /id="PRO_0000148035"
SQ   SEQUENCE   258 AA;  28930 MW;  0ADDB88824AFD87D CRC64;
     MTSFTGITAV ANATNEMAMF KQAMKEVAAH PEWMSSRQIE RQRWNPYSME GGSTCAISGE
     NFAIVASDTR MTQNDINILT RDAEKIQILN DNIILTTSGF YGDVLQLKKV LQSRLHKYRF
     DYRSDMSVDL CAELLSRNLY YRRFFPYYTG AILAGIDEHG KGAVFSYDPI GCIERLGYSA
     SGAAEPMIIP FLDCQIGHVT LSEGYERPEL TLDRAISLMK DSFRGAAERE ISTGDKIHLV
     IAEAGKPVVV KFLPLRED