ID Q9V405_DROME Unreviewed; 413 AA. AC Q9V405; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 04-MAR-2015, entry version 136. DE SubName: Full=26S proteasome regulatory complex subunit p48A {ECO:0000313|EMBL:AAF08387.1}; DE SubName: Full=CG16916 protein {ECO:0000313|EMBL:CBA35179.1}; DE SubName: Full=GH06151p {ECO:0000313|EMBL:ACI46532.1}; DE SubName: Full=Regulatory particle triple-A ATPase 3, isoform A {ECO:0000313|EMBL:AAF48001.1}; DE EC=3.6.1.15 {ECO:0000313|EMBL:AAF48001.1}; DE SubName: Full=Regulatory particle triple-A ATPase 3, isoform B {ECO:0000313|EMBL:AHN59578.1}; DE EC=3.6.1.15 {ECO:0000313|EMBL:AHN59578.1}; GN Name=Rpt3 {ECO:0000313|EMBL:AAF48001.1, GN ECO:0000313|FlyBase:FBgn0028686}; GN Synonyms=Rpt3-RA {ECO:0000313|EMBL:ACI46532.1}; GN ORFNames=CG16916 {ECO:0000313|EMBL:CBA35179.1, GN ECO:0000313|FlyBase:FBgn0028686}, Dmel_CG16916 GN {ECO:0000313|EMBL:AAF48001.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF08387.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:AAF08387.1}; RA Hoelzl H.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAF08387.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:AAF08387.1}; RX PubMed=10893261; DOI=10.1083/jcb.150.1.119; RA Hoelzl H., Kapelari B., Kellermann J., Seemueller E., Suemegi M., RA Udvardy A., Medalia O., Sperling J., Mueller S.A., Engel A., RA Baumeister W.; RT "The regulatory complex of Drosophila melanogaster 26S proteasomes. RT Subunit composition and localization of a deubiquitylating enzyme."; RL J. Cell Biol. 150:119-130(2000). RN [3] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [5] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [7] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [8] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [9] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [12] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [13] {ECO:0000313|EMBL:ACI46532.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:ACI46532.1}; RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:CBA35179.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL131 {ECO:0000313|EMBL:CBA35181.1}, ZBMEL145 RC {ECO:0000313|EMBL:CBA35182.1}, ZBMEL157 {ECO:0000313|EMBL:CBA35183.1}, RC ZBMEL186 {ECO:0000313|EMBL:CBA35184.1}, ZBMEL191 RC {ECO:0000313|EMBL:CBA35185.1}, ZBMEL229 {ECO:0000313|EMBL:CBA35186.1}, RC ZBMEL377 {ECO:0000313|EMBL:CBA35187.1}, ZBMEL398 RC {ECO:0000313|EMBL:CBA35189.1}, ZBMEL82 {ECO:0000313|EMBL:CBA35179.1}, RC and ZBMEL84 {ECO:0000313|EMBL:CBA35180.1}; RX PubMed=20150340; DOI=10.1093/molbev/msq046; RA Parsch J., Novozhilov S., Saminadin-Peter S.S., Wong K.M., RA Andolfatto P.; RT "On the utility of short intron sequences as a reference for the RT detection of positive and negative selection in Drosophila."; RL Mol. Biol. Evol. 27:1226-1234(2010). RN [15] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {ECO:0000256|RuleBase:RU003651}. 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; AF145306; AAF08387.1; -; mRNA. DR EMBL; AE014298; AAF48001.1; -; Genomic_DNA. DR EMBL; BT046144; ACI46532.1; -; mRNA. DR EMBL; AE014298; AHN59578.1; -; Genomic_DNA. DR EMBL; FN544098; CBA35179.1; -; Genomic_DNA. DR EMBL; FN544099; CBA35180.1; -; Genomic_DNA. DR EMBL; FN544100; CBA35181.1; -; Genomic_DNA. DR EMBL; FN544101; CBA35182.1; -; Genomic_DNA. DR EMBL; FN544102; CBA35183.1; -; Genomic_DNA. DR EMBL; FN544103; CBA35184.1; -; Genomic_DNA. DR EMBL; FN544104; CBA35185.1; -; Genomic_DNA. DR EMBL; FN544105; CBA35186.1; -; Genomic_DNA. DR EMBL; FN544106; CBA35187.1; -; Genomic_DNA. DR EMBL; FN544108; CBA35189.1; -; Genomic_DNA. DR RefSeq; NP_001285108.1; NM_001298179.1. DR RefSeq; NP_572686.1; NM_132458.3. DR UniGene; Dm.8238; -. DR ProteinModelPortal; Q9V405; -. DR SMR; Q9V405; 36-413. DR IntAct; Q9V405; 17. DR STRING; 7227.FBpp0073292; -. DR EnsemblMetazoa; FBtr0073436; FBpp0073292; FBgn0028686. DR EnsemblMetazoa; FBtr0346274; FBpp0312031; FBgn0028686. DR GeneID; 32047; -. DR KEGG; dme:Dmel_CG16916; -. DR UCSC; CG16916-RA; d. melanogaster. DR CTD; 32047; -. DR FlyBase; FBgn0028686; Rpt3. DR eggNOG; COG1222; -. DR GeneTree; ENSGT00550000074962; -. DR KO; K03063; -. DR OMA; NIQEEYI; -. DR OrthoDB; EOG7F24ST; -. DR PhylomeDB; Q9V405; -. DR BRENDA; 3.4.25.1; 48. DR Reactome; REACT_180649; Activation of NF-kappaB in B cells. DR Reactome; REACT_180655; ER-Phagosome pathway. DR Reactome; REACT_180671; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; REACT_180708; Antigen processing: Ubiquitination & Proteasome degradation. DR Reactome; REACT_181662; Separation of Sister Chromatids. DR Reactome; REACT_184330; Asymmetric localization of PCP proteins. DR Reactome; REACT_211248; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; REACT_215026; degradation of AXIN. DR Reactome; REACT_218589; Orc1 removal from chromatin. DR Reactome; REACT_225883; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; REACT_230692; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; REACT_232776; Regulation of ornithine decarboxylase (ODC). DR Reactome; REACT_233284; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; REACT_234235; Hh ligand biogenesis disease. DR Reactome; REACT_234707; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; REACT_238120; degradation of DVL. DR Reactome; REACT_239151; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; REACT_242866; Degradation of beta-catenin by the destruction complex. DR Reactome; REACT_247767; AUF1 (hnRNP D0) destabilizes mRNA. DR Reactome; REACT_250603; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; REACT_258701; Hedgehog ligand biogenesis. DR Reactome; REACT_260216; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; REACT_269395; GLI3 is processed to GLI3R by the proteasome. DR Reactome; REACT_271013; Degradation of GLI1 by the proteasome. DR Reactome; REACT_271479; Degradation of GLI2 by the proteasome. DR Reactome; REACT_92044; APC/C:Cdc20 mediated degradation of Securin. DR GenomeRNAi; 32047; -. DR NextBio; 776548; -. DR PRO; PR:Q9V405; -. DR Proteomes; UP000000803; Chromosome X. DR ExpressionAtlas; Q9V405; differential. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0001673; C:male germ cell nucleus; IDA:FlyBase. DR GO; GO:0005838; C:proteasome regulatory particle; IDA:FlyBase. DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; ISS:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase. DR GO; GO:0006508; P:proteolysis; IDA:FlyBase. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR005937; 26S_Psome_P45. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|RuleBase:RU003299}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Hydrolase {ECO:0000313|EMBL:AAF48001.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003299}; KW Proteasome {ECO:0000313|EMBL:AAF08387.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. SQ SEQUENCE 413 AA; 46999 MW; 34E7518BE593A0E3 CRC64; MPYNMDVLIP EKDELSDLKL KDAHSSLDEL DMEDLYVRYK KLQKTLEFIE VQEEYIKDEQ RNLKKEYLHA QEEVKRIQSV PLVIGQFLEA VDQNTGIVGS TTGSNYYVRI LSTIDRELLK PSASVALHKH SNALVDVLPP EADSSISMLQ PDEKPDVSYA DIGGMDMQKQ EIREAVELPL THFELYKQIG IDPPRGVLMY GPPGCGKTML AKAVAHHTTA SFIRVVGSEF VQKYLGEGPR MVRDVFRLAK ENAPAIIFID EIDAIATKRF DAQTGADREV QRILLELLNQ MDGFDQTTNV KVIMATNRAD TLDPALLRPG RLDRKIEFPL PDRRQKRLVF STITSKMNLS EDVDLEEFVA RPDKISGADI NAICQEAGMH AVRENRYIVL AKDFEKGYKN NIKKDEQEHE FYK //