PS11A_CAEEL
ID PS11A_CAEEL Reviewed; 438 AA.
AC Q20938; Q5DX45;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable 26S proteasome regulatory subunit rpn-6.1 {ECO:0000250|UniProtKB:P34481};
GN Name=rpn-6.1 {ECO:0000312|WormBase:F57B9.10a}; ORFNames=F57B9.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [2] {ECO:0000305}
RP PROBABLE FUNCTION.
RX PubMed=11559592; DOI=10.1093/embo-reports/kve184;
RA Davy A., Bello P., Thierry-Mieg N., Vaglio P., Hitti J., Doucette-Stamm L.,
RA Thierry-Mieg D., Reboul J., Boulton S., Walhout A.J., Coux O., Vidal M.;
RT "A protein-protein interaction map of the Caenorhabditis elegans 26S
RT proteasome.";
RL EMBO Rep. 2:821-828(2001).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=18824511; DOI=10.1261/rna.1139508;
RA Andachi Y.;
RT "A novel biochemical method to identify target genes of individual
RT microRNAs: identification of a new Caenorhabditis elegans let-7 target.";
RL RNA 14:2440-2451(2008).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=22922647; DOI=10.1038/nature11315;
RA Vilchez D., Morantte I., Liu Z., Douglas P.M., Merkwirth C.,
RA Rodrigues A.P., Manning G., Dillin A.;
RT "RPN-6 determines C. elegans longevity under proteotoxic stress
RT conditions.";
RL Nature 489:263-268(2012).
CC -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, rpn-6.1 is required for
CC proteasome assembly. Plays a key role in increased proteasome activity
CC in response to proteotoxic stress: induced by daf-16, promoting
CC enhanced assembly of the 26S proteasome and higher proteasome activity,
CC leading to extended lifespan. {ECO:0000269|PubMed:22922647}.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S regulatory
CC subunits (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q20938-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q20938-2; Sequence=VSP_039825;
CC -!- INDUCTION: By daf-16. {ECO:0000269|PubMed:22922647}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal, larval arrest.
CC {ECO:0000269|PubMed:18824511}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000255}.
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DR EMBL; FO081266; CCD70319.1; -; Genomic_DNA.
DR EMBL; FO081266; CCD70320.1; -; Genomic_DNA.
DR PIR; H88493; H88493.
DR RefSeq; NP_001022621.1; NM_001027450.2. [Q20938-1]
DR RefSeq; NP_001022622.1; NM_001027451.2. [Q20938-2]
DR AlphaFoldDB; Q20938; -.
DR SMR; Q20938; -.
DR BioGRID; 41186; 54.
DR STRING; 6239.F57B9.10a; -.
DR EPD; Q20938; -.
DR PaxDb; Q20938; -.
DR PeptideAtlas; Q20938; -.
DR EnsemblMetazoa; F57B9.10a.1; F57B9.10a.1; WBGene00004462. [Q20938-1]
DR EnsemblMetazoa; F57B9.10b.1; F57B9.10b.1; WBGene00004462. [Q20938-2]
DR GeneID; 175972; -.
DR KEGG; cel:CELE_F57B9.10; -.
DR UCSC; F57B9.10a; c. elegans.
DR CTD; 175972; -.
DR WormBase; F57B9.10a; CE25011; WBGene00004462; rpn-6.1. [Q20938-1]
DR WormBase; F57B9.10b; CE38077; WBGene00004462; rpn-6.1. [Q20938-2]
DR eggNOG; KOG1463; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR InParanoid; Q20938; -.
DR OMA; LYFDTGM; -.
DR OrthoDB; 1052430at2759; -.
DR PhylomeDB; Q20938; -.
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:Q20938; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004462; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0022624; C:proteasome accessory complex; TAS:UniProtKB.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IDA:UniProtKB.
DR GO; GO:0043248; P:proteasome assembly; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Proteasome; Reference proteome.
FT CHAIN 1..438
FT /note="Probable 26S proteasome regulatory subunit rpn-6.1"
FT /id="PRO_0000399034"
FT DOMAIN 239..408
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_039825"
SQ SEQUENCE 438 AA; 49091 MW; 4F6B245626C4098F CRC64;
MRETSSREDT NNIGKAPEMS GGTIMDTMTS LPHQNDQNVI RHLTNLVKSP ASGDDDIKKK
EDSIMELGNI LAQNKQTEEL RNMIEQTRPF LVSLGKAKAA KLVRDLVDLC LKIDDQDGDI
KVGLVKECIQ WATEQNRTFL RQTLTARLVR LYNDLQRYTQ ALPLAADLIR ELKKVDDKDV
LVEVELEESK AYYNLSNIGR ARASLTGART TANAIYVNPR MQAALDLQSG ILHAADEKDF
KTAFSYFYEA FEGYDSVDEK VSALTALKYM LLCKVMLDLP DEVNSLLSAK LALKYNGSDL
DAMKAIAAAA QKRSLKDFQV AFGSFPQELQ MDPVVRKHFH SLSERMLEKD LCRIIEPYSF
VQIEHVAQQI GIDRSKVEKK LSQMILDQKL SGSLDQGEGM LIVFEIAVPD EAYQTALDTI
HAMGEVVDAL YSNASKIN
