ID   PRS4_CAEEL              Reviewed;         443 AA.
AC   O16368;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable 26S proteasome regulatory subunit 4;
GN   Name=rpt-2; ORFNames=F29G9.5;
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).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22621901; DOI=10.1091/mbc.e12-01-0055;
RA   Wilson K.J., Qadota H., Mains P.E., Benian G.M.;
RT   "UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the
RT   function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.";
RL   Mol. Biol. Cell 23:2623-2634(2012).
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). May play a role in the degradation of
CC       microtubule severing protein mei-1 (PubMed:22621901).
CC       {ECO:0000250|UniProtKB:P35998, ECO:0000269|PubMed:22621901}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 larval stage,
CC       causes 20 percent increase in mei-1 protein levels.
CC       {ECO:0000269|PubMed:22621901}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; FO080494; CCD64135.1; -; Genomic_DNA.
DR   PIR; T31800; T31800.
DR   RefSeq; NP_504558.1; NM_072157.6.
DR   AlphaFoldDB; O16368; -.
DR   SMR; O16368; -.
DR   BioGRID; 44036; 49.
DR   IntAct; O16368; 3.
DR   STRING; 6239.F29G9.5; -.
DR   EPD; O16368; -.
DR   PaxDb; O16368; -.
DR   PeptideAtlas; O16368; -.
DR   EnsemblMetazoa; F29G9.5.1; F29G9.5.1; WBGene00004502.
DR   GeneID; 178988; -.
DR   KEGG; cel:CELE_F29G9.5; -.
DR   UCSC; F29G9.5; c. elegans.
DR   CTD; 178988; -.
DR   WormBase; F29G9.5; CE09799; WBGene00004502; rpt-2.
DR   eggNOG; KOG0726; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_3_1; -.
DR   InParanoid; O16368; -.
DR   OMA; ARCKLRY; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; O16368; -.
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-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
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:O16368; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00004502; 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: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:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
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; IPR035244; 26S_subunit_4.
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   PANTHER; PTHR23073:SF77; PTHR23073:SF77; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..443
FT                   /note="Probable 26S proteasome regulatory subunit 4"
FT                   /id="PRO_0000084681"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         229..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  49723 MW;  6908E4AB5C15C642 CRC64;
     MGQQQSGFGG RGNDRGAGDG EKKEKKKYEA PIPSRIGKKK KGSKGPDAAS KLPAVTPHAR
     CRLKLLKSER IKDYLLMEQE FIQNQERLKP QEERQEEERA KVDELRGTPM AVGSLEEIID
     DQHAIVSTNV GSEHYVNIMS FVDKEQLEPG CSVLLNHKNH AVIGVLSDDT DPMVSVMKLE
     KAPQETYADV GGLDQQIQEI KEAVELPLTH PEYYEEMGIR PPKGVILYGC PGTGKTLLAK
     AVANQTSATF LRIVGSELIQ KYLGDGPKMV RELFRVAEEN APSIVFIDEI DAVGTKRYDS
     NSGGEREIQR TMLELLNQLD GFDSRGDVKV LMATNRIESL DPALIRPGRI DRKIEFPLPD
     EKTKRRIFQI HTSRMTLGKE VNLEEFITAK DELSGADIKA MCTEAGLLAL RERRMRVTME
     DFQKSKENVL YRKKEGAPEE LYL