ID   PRS7_CAEEL              Reviewed;         435 AA.
AC   Q18787;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=26S proteasome regulatory subunit 7;
DE   AltName: Full=26S proteasome AAA-ATPase subunit rpt-1;
DE   AltName: Full=Proteasome 26S subunit ATPase 2;
GN   Name=rpt-1; ORFNames=C52E4.4;
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=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: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the 26S
CC       complex (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q18787; Q20058: CELE_F35G12.12; NbExp=6; IntAct=EBI-318033, EBI-318041;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; Z78012; CAB01414.1; -; Genomic_DNA.
DR   PIR; T20152; T20152.
DR   RefSeq; NP_506005.1; NM_073604.5.
DR   AlphaFoldDB; Q18787; -.
DR   SMR; Q18787; -.
DR   BioGRID; 44665; 42.
DR   IntAct; Q18787; 2.
DR   STRING; 6239.C52E4.4.1; -.
DR   EPD; Q18787; -.
DR   PaxDb; Q18787; -.
DR   PeptideAtlas; Q18787; -.
DR   EnsemblMetazoa; C52E4.4.1; C52E4.4.1; WBGene00004501.
DR   GeneID; 179641; -.
DR   KEGG; cel:CELE_C52E4.4; -.
DR   UCSC; C52E4.4.1; c. elegans.
DR   CTD; 179641; -.
DR   WormBase; C52E4.4; CE08946; WBGene00004501; rpt-1.
DR   eggNOG; KOG0729; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_6_1_1; -.
DR   InParanoid; Q18787; -.
DR   OMA; INGYKKF; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; Q18787; -.
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:Q18787; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00004501; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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; IPR035245; PSMC2.
DR   PANTHER; PTHR23073:SF13; PTHR23073:SF13; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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..435
FT                   /note="26S proteasome regulatory subunit 7"
FT                   /id="PRO_0000084713"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   435 AA;  48611 MW;  51D54DD6DEF923B1 CRC64;
     MPDHLGDDMR KTKKDDTKEE EKNFQALDEG DIAVLKRYGQ GPYAEQLKTL DADIENCLKK
     VNELSGVKES DTGLAPPALW DIAADKQAMQ QEQPLQVARC TKIITSDKHD PRYLINVKQF
     AKFVVDLADS VAPTDIEEGM RVGVDRNKYQ IHLPLPAKID PTVTMMQVEE KPDVTYSDVG
     GCKDQIEKLR EVVETPLLHP ERYVNLGIEP PKGVLLYGPP GTGKTLCARA VANRTDACFI
     RVIGSELVQK YVGEGARMVR ELFEMARTKK ACLIFFDEID AVGGARFDDG QGGDNEVQRT
     MLELINQLDG FDPRGNIKVL MATNRPDTLD PALMRPGRLD RKVEFALPDL AGRAHILKIH
     AKQMSVERDI RYDLLARLCP NSTGAEIRSV CTEAGMFAIR ARRKVATEKD FLEAINKVVK
     GYAKFSATPR YLTHN