PRS8_CAEEL
ID PRS8_CAEEL Reviewed; 416 AA.
AC Q9XTT9;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=26S proteasome regulatory subunit 8 {ECO:0000250|UniProtKB:P62195};
DE AltName: Full=26S proteasome AAA-ATPase subunit rpt-6 {ECO:0000250|UniProtKB:P62195};
DE AltName: Full=Proteasome regulatory particle ATPase-like protein 6 {ECO:0000312|WormBase:Y49E10.1};
GN Name=rpt-6 {ECO:0000312|WormBase:Y49E10.1};
GN ORFNames=Y49E10.1 {ECO:0000312|WormBase:Y49E10.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ELT-2,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-206.
RX PubMed=30265660; DOI=10.1371/journal.pgen.1007693;
RA Olaitan A.O., Aballay A.;
RT "Non-proteolytic activity of 19S proteasome subunit RPT-6 regulates GATA
RT transcription during response to infection.";
RL PLoS Genet. 14:E1007693-E1007693(2018).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins
CC (PubMed:30265660). 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 (PubMed:30265660). 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). In addition, regulates gene
CC expression in response to bacterial infection (PubMed:30265660). Binds
CC to the GATA transcription factor elt-2 to control its transcriptional
CC activity and thus the expression of elt-2-dependent genes in response
CC to infection by Gram-negative bacteria such as P.aeruginosa
CC (PubMed:30265660). {ECO:0000250|UniProtKB:P62195,
CC ECO:0000269|PubMed:30265660}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC (Probable). The 26S proteasome consists of a 20S core particle (CP) and
CC two 19S regulatory subunits (RP) (By similarity). Interacts with elt-2
CC (PubMed:30265660). {ECO:0000250|UniProtKB:P62195,
CC ECO:0000269|PubMed:30265660, ECO:0000305|PubMed:30265660}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
CC {ECO:0000305|PubMed:30265660}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L4 stage of larval
CC development inhibits activity of the proteasome (PubMed:30265660).
CC RNAi-mediated knockdown at the L4 larval stage also results in
CC increased mortality and transcription of immune genes containing the
CC elt-2 binding motif when exposed to Gram-negative bacteria such as
CC P.aeruginosa (PubMed:30265660). RNAi-mediated knockdown at this stage,
CC furthermore, prevents the recovery of P.aeruginosa infected animals
CC treated with the antibiotic streptomycin (PubMed:30265660).
CC {ECO:0000269|PubMed:30265660}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000255|RuleBase:RU003651}.
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DR EMBL; BX284603; CAB11558.1; -; Genomic_DNA.
DR PIR; T27048; T27048.
DR RefSeq; NP_499609.1; NM_067208.4.
DR AlphaFoldDB; Q9XTT9; -.
DR SMR; Q9XTT9; -.
DR DIP; DIP-27139N; -.
DR IntAct; Q9XTT9; 4.
DR STRING; 6239.Y49E10.1; -.
DR EPD; Q9XTT9; -.
DR PaxDb; Q9XTT9; -.
DR PeptideAtlas; Q9XTT9; -.
DR EnsemblMetazoa; Y49E10.1.1; Y49E10.1.1; WBGene00004506.
DR GeneID; 176661; -.
DR KEGG; cel:CELE_Y49E10.1; -.
DR UCSC; Y49E10.1; c. elegans.
DR CTD; 176661; -.
DR WormBase; Y49E10.1; CE22219; WBGene00004506; rpt-6.
DR eggNOG; KOG0728; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_1_1; -.
DR InParanoid; Q9XTT9; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9XTT9; -.
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:Q9XTT9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004506; 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 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; Transcription; Transcription regulation.
FT CHAIN 1..416
FT /note="26S proteasome regulatory subunit 8"
FT /id="PRO_0000447609"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT SITE 206
FT /note="Mediates interaction with elt-2"
FT /evidence="ECO:0000305|PubMed:30265660"
FT MUTAGEN 206
FT /note="K->R: Impaired interaction with elt-2."
FT /evidence="ECO:0000269|PubMed:30265660"
SQ SEQUENCE 416 AA; 46250 MW; 8F6E840EF99B1298 CRC64;
MAPPASTASS ADPSKPTAQK LTEESDEKTL RKYFSTKVDD AQQKVADKSQ NVRRLQAQRN
ELNTKVRMLK EELQQLHEQG SYVGEVSKAM DKKKVLVKVH PEGKYVVDVD KSIDINSLNT
GARVALRADS YALHKLLPNK VDPLVSLMMV EKVPDSTYEM VGGLDKQIKE IKEVIELPVK
HPELFDALGI AQPKGVLLFG PPGTGKTLLA RAVAHHTECT FIRVSGSELV QKFIGEGARM
VRELFVMARE HAPSIIFMDE IDSIGSSRVE GSSGGDSEVQ RTMLELLNQL DGFEATKNIK
VIMATNRIDI LDPALLRPGR IDRKIEFPAP DEKARADILK IHSRKMNLMR GINMAKIAEQ
IPGASGAEVK SVCTEAGMFA LRERRIHVTQ EDFEMAVGKV MQKDSEKNMS IKKLWK
