ID   PRS8_DROME              Reviewed;         405 AA.
AC   O18413; O45023;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=26S proteasome regulatory subunit 8;
GN   Name=Rpt6; Synonyms=DUG, Pros45, Ug; ORFNames=CG1489;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9469929; DOI=10.1016/s0378-1119(97)00564-7;
RA   Mounkes L.C., Fuller M.T.;
RT   "The DUG gene of Drosophila melanogaster encodes a structural and
RT   functional homolog of the S. cerevisiae SUG1 predicted ATPase associated
RT   with the 26S proteasome.";
RL   Gene 206:165-174(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9738875; DOI=10.1007/s004380050783;
RA   Cheng L., Roemer N., Smyth K.-A., Belote J., Nambu J.R., Schwartz L.M.;
RT   "Cloning and characterization of Pros45, the Drosophila SUG1 proteasome
RT   subunit homolog.";
RL   Mol. Gen. Genet. 259:13-20(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   INTERACTION WITH RPN6.
RX   PubMed=22187461; DOI=10.1073/pnas.1117648108;
RA   Pathare G.R., Nagy I., Bohn S., Unverdorben P., Hubert A., Korner R.,
RA   Nickell S., Lasker K., Sali A., Tamura T., Nishioka T., Forster F.,
RA   Baumeister W., Bracher A.;
RT   "The proteasomal subunit Rpn6 is a molecular clamp holding the core and
RT   regulatory subcomplexes together.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:149-154(2012).
RN   [7]
RP   INTERACTION WITH IMD AND USP2.
RX   PubMed=25027767; DOI=10.1186/s12964-014-0041-2;
RA   Engel E., Viargues P., Mortier M., Taillebourg E., Coute Y., Thevenon D.,
RA   Fauvarque M.O.;
RT   "Identifying USPs regulating immune signals in Drosophila: USP2
RT   deubiquitinates Imd and promotes its degradation by interacting with the
RT   proteasome.";
RL   Cell Commun. Signal. 12:41-41(2014).
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   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S proteasome core and two 19S
CC       regulatory subunits. Interacts with Rpn6 (PubMed:22187461). Interacts
CC       with imd and Usp2 isoform A (PubMed:25027767).
CC       {ECO:0000269|PubMed:22187461, ECO:0000269|PubMed:25027767}.
CC   -!- INTERACTION:
CC       O18413; Q9VCE1: Atg6; NbExp=3; IntAct=EBI-174806, EBI-134130;
CC       O18413; Q9VSE9: ERR; NbExp=3; IntAct=EBI-174806, EBI-166804;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
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; U97538; AAC48284.1; -; mRNA.
DR   EMBL; AF043734; AAC63219.1; -; mRNA.
DR   EMBL; AE014298; AAF50835.1; -; Genomic_DNA.
DR   EMBL; AY051732; AAK93156.1; -; mRNA.
DR   RefSeq; NP_608447.1; NM_134603.2.
DR   AlphaFoldDB; O18413; -.
DR   BMRB; O18413; -.
DR   SMR; O18413; -.
DR   BioGRID; 59383; 72.
DR   DIP; DIP-20087N; -.
DR   IntAct; O18413; 20.
DR   STRING; 7227.FBpp0076890; -.
DR   PaxDb; O18413; -.
DR   PRIDE; O18413; -.
DR   DNASU; 33105; -.
DR   EnsemblMetazoa; FBtr0077189; FBpp0076890; FBgn0020369.
DR   GeneID; 33105; -.
DR   KEGG; dme:Dmel_CG1489; -.
DR   CTD; 33105; -.
DR   FlyBase; FBgn0020369; Rpt6.
DR   VEuPathDB; VectorBase:FBgn0020369; -.
DR   eggNOG; KOG0728; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; O18413; -.
DR   OMA; TANCRVA; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; O18413; -.
DR   BRENDA; 3.4.25.1; 1994.
DR   Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DME-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DME-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-DME-202424; Downstream TCR signaling.
DR   Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR   Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT.
DR   Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR   Reactome; R-DME-216167; Nuclear CI is degraded.
DR   Reactome; R-DME-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DME-432395; Degradation of TIM.
DR   Reactome; R-DME-432524; Degradation of PER.
DR   Reactome; R-DME-432626; Circadian Clock pathway.
DR   Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-DME-4641257; Degradation of AXIN.
DR   Reactome; R-DME-4641258; Degradation of DVL.
DR   Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DME-538864; Degradation of CRY.
DR   Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-DME-5632684; Hedgehog 'on' state.
DR   Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-DME-5689603; UCH proteinases.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-DME-68949; Orc1 removal from chromatin.
DR   Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DME-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-9020702; Interleukin-1 signaling.
DR   Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DME-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; O18413; -.
DR   BioGRID-ORCS; 33105; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33105; -.
DR   PRO; PR:O18413; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0020369; Expressed in secondary oocyte and 33 other tissues.
DR   Genevisible; O18413; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005838; C:proteasome regulatory particle; IDA:FlyBase.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:FlyBase.
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; ISM:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
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; IPR035261; PSMC5.
DR   PANTHER; PTHR23073:SF102; PTHR23073:SF102; 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..405
FT                   /note="26S proteasome regulatory subunit 8"
FT                   /id="PRO_0000084727"
FT   BINDING         189..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        94
FT                   /note="F -> S (in Ref. 1; AAC48284)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   405 AA;  45857 MW;  C098EEE56B348211 CRC64;
     MTVTNRMEIE SAYHKGEGFR SYYIQKIEEL QLVVAEKHQN LRRLQAQRNE LNAKVRMLRE
     ELQLLQEQGS YVGEVVKPMD KKKVLVKVHP EGKFVVDLDK NIDINDVTPN CRVALRNESY
     TLHKILPNKV DPLVSLMMVE KVPDSTYEMV GGLDKQIKEI KEVIELPVKH PELFDALGIA
     QPKGVLLYGP PGTGKTLLAR AVAHHTECTF IRVSGSELVQ KFIGEGSRMV RELFVMAREH
     APSIIFMDEI DSIGSSRIES GSGGDSEVQR TMLELLNQLD GFEATKNIKV IMATNRIDIL
     DPALLRPGRI DRKIEFPPPN EEARLDILKI HSRKMNLTRG INLRKIAELM PGASGAEVKG
     VCTEAGMYAL RERRVHVTQE DFEMAVAKVM QKDSEKNMSI KKLWK