PRS6A_CAEEL
ID PRS6A_CAEEL Reviewed; 430 AA.
AC O76371;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=26S protease regulatory subunit 6A {ECO:0000250|UniProtKB:P17980};
DE AltName: Full=Proteasome regulatory particle ATPase-like protein 5 {ECO:0000312|WormBase:F56H1.4};
GN Name=rpt-5 {ECO:0000312|WormBase:F56H1.4};
GN ORFNames=F56H1.4 {ECO:0000312|WormBase:F56H1.4};
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 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins
CC (PubMed:27528192). This complex plays a key role in the maintenance of
CC protein homeostasis by removing misfolded or damaged proteins, which
CC could impair cellular functions, and by removing proteins whose
CC functions are no longer required (By similarity). Therefore, the
CC proteasome participates in numerous cellular processes, including cell
CC cycle progression, apoptosis, or DNA damage repair (By similarity).
CC Belongs to the heterohexameric ring of AAA (ATPases associated with
CC diverse cellular activities) proteins that unfolds ubiquitinated target
CC proteins that are concurrently translocated into a proteolytic chamber
CC and degraded into peptides (By similarity).
CC {ECO:0000250|UniProtKB:P17980, ECO:0000269|PubMed:27528192}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases including the PSMC3
CC homolog rpt-5 and few additional components.
CC {ECO:0000250|UniProtKB:P17980}.
CC -!- INTERACTION:
CC O76371; Q10920: psmd-9; NbExp=3; IntAct=EBI-317201, EBI-317193;
CC O76371; O17071: rpt-4; NbExp=10; IntAct=EBI-317201, EBI-320304;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in larval arrest
CC and up-regulation of the aspartic protease ddi-1, indicative of
CC proteasomal dysfunction. RNAi-mediated knockdown in a ddi-1, png-1,
CC sel-11 or sel-1 mutant background results in reduced or failed
CC expression of the proteasomal subunit rpt-3.
CC {ECO:0000269|PubMed:27528192}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284601; CCD62966.1; -; Genomic_DNA.
DR PIR; T33155; T33155.
DR RefSeq; NP_491672.1; NM_059271.3.
DR AlphaFoldDB; O76371; -.
DR SMR; O76371; -.
DR IntAct; O76371; 4.
DR STRING; 6239.F56H1.4; -.
DR EPD; O76371; -.
DR PaxDb; O76371; -.
DR PeptideAtlas; O76371; -.
DR EnsemblMetazoa; F56H1.4.1; F56H1.4.1; WBGene00004505.
DR GeneID; 172238; -.
DR KEGG; cel:CELE_F56H1.4; -.
DR UCSC; F56H1.4.2; c. elegans.
DR CTD; 172238; -.
DR WormBase; F56H1.4; CE17915; WBGene00004505; rpt-5.
DR eggNOG; KOG0652; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_4_1; -.
DR InParanoid; O76371; -.
DR OMA; HEKAAMG; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; O76371; -.
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:O76371; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004505; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035254; PSMC3.
DR PANTHER; PTHR23073:SF90; PTHR23073:SF90; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..430
FT /note="26S protease regulatory subunit 6A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442335"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 430 AA; 48126 MW; 1B6DAA1E8E40E3EC CRC64;
MSQTPPPKDG KNPEAMEVED AIDEEILKMS TEDLKSRTHL LDNEIRIMRS EVQRINHSAT
TLKERIKENT ERIKVNKTLP YLVSNVVELL DLEDNTEEEG ANVDLDAQKT KCAVIKTSTR
ATYFLPVVGL VDPDELKPGD LVGVNKDSYL ILEKLPAEYD SRVKAMEVDE RPTEQYSDIG
GCDKQIQELI EAVVLPMTHK DRFVNLGIHP PKGVLMYGPP GTGKTMMARA VAAQTKSTFL
KLAGPQLVQM FIGDGAKLVR DAFALAKEKA PAIIFIDELD AIGTKRFDSE KAGDREVQRT
MLELLNQLDG FQPNDDIKVI AATNRIDVLD PALLRSGRLD RKIELPHPNE DARARIMQIH
SRKMNVNKDV NFEELARCTD DFNGAQCKAV CVEAGMIALR RDATEILHED FMDAILEVQA
KKKASLNYYA
