PSMD3_CAEEL
ID PSMD3_CAEEL Reviewed; 504 AA.
AC Q04908;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit rpn-3;
GN Name=rpn-3; ORFNames=C30C11.2;
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=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).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q04908; Q95Y72: dss-1; NbExp=2; IntAct=EBI-312239, EBI-312245;
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
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DR EMBL; FO080722; CCD66158.1; -; Genomic_DNA.
DR PIR; S44783; S44783.
DR RefSeq; NP_498869.1; NM_066468.4.
DR AlphaFoldDB; Q04908; -.
DR SMR; Q04908; -.
DR BioGRID; 41400; 66.
DR DIP; DIP-25350N; -.
DR IntAct; Q04908; 4.
DR STRING; 6239.C30C11.2; -.
DR EPD; Q04908; -.
DR PaxDb; Q04908; -.
DR PeptideAtlas; Q04908; -.
DR EnsemblMetazoa; C30C11.2.1; C30C11.2.1; WBGene00004460.
DR GeneID; 176196; -.
DR KEGG; cel:CELE_C30C11.2; -.
DR UCSC; C30C11.2; c. elegans.
DR CTD; 176196; -.
DR WormBase; C30C11.2; CE00101; WBGene00004460; rpn-3.
DR eggNOG; KOG2581; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_019858_1_2_1; -.
DR InParanoid; Q04908; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR PhylomeDB; Q04908; -.
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:Q04908; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004460; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035267; PSMD3.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Proteasome; Reference proteome.
FT CHAIN 1..504
FT /note="26S proteasome non-ATPase regulatory subunit 3"
FT /id="PRO_0000173818"
FT DOMAIN 254..433
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 504 AA; 57507 MW; 062E476685FCD0A7 CRC64;
MAPKTGETVV EKMEVDEAKQ DVPATEPAKD LNAIAVENIK EQLAALDKGE EHLITRVLQV
LPKTRKQIND NVLYKLVSSH LSSDAQFAEG MLKYLHYTPA ADTEVQPMDT SNVKTKSPKK
GVKPVFASPE SDCYLRLLVL LHLYAQKKNT EALALGENQL TSIYNFDRRT LDGLAAKTLY
FLCVIYEREG RLFDHQGFLN SRLRTATLRN FSESQAVLIC WLLRCYLINR QYQSAAHLVS
KVAFPDNASN NDLARYMYYQ GRIKALQLDY NSAAGYFLQA QRKAPQEGAI GFKQAVQKWV
VVIGLLQGEI PDRSVFRQPI YRKCLAHYLD LSRGVRDGDV ARFNHNLEQF KTQFEADDTL
TLIVRLRQNV IKTAIKQISL AYSRIYIKDI AKKLYITNET ETEYIVAKAI ADGAIDAVIT
SDVRDGPRYM QSSETADIYR TSEPQAHFDT RIRYCLELHN QAVKALRYPP KKKIAVETIE
QAREREQQEL EFAKELADED DDDF
