PSMD3_DROME
ID PSMD3_DROME Reviewed; 494 AA.
AC P25161; B5RIX5; Q8T460; Q9VJ09;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Probable 26S proteasome non-ATPase regulatory subunit 3;
DE Short=26S proteasome subunit S3;
DE AltName: Full=Diphenol oxidase A2 component;
DE Short=DOX-A2;
DE AltName: Full=Regulatory particle non-ATPase 3;
GN Name=Rpn3; Synonyms=Dox-A2; ORFNames=CG42641;
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 [GENOMIC DNA].
RX PubMed=1909680; DOI=10.1016/0378-1119(91)90279-k;
RA Pentz E.S., Wright T.R.F.;
RT "Drosophila melanogaster diphenol oxidase A2: gene structure and homology
RT with the mouse mast-cell tum- transplantation antigen, P91A.";
RL Gene 103:239-242(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=12421421; DOI=10.1046/j.1365-2583.2002.00374.x;
RA Ma J., Katz E., Belote J.M.;
RT "Expression of proteasome subunit isoforms during spermatogenesis in
RT Drosophila melanogaster.";
RL Insect Mol. Biol. 11:627-639(2002).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Blood (crystal) cells and cuticle.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the diphenol oxidase A2 component
CC involved in catecholamine metabolism, melanin formation, and
CC sclerotization of the cuticle. {ECO:0000305|PubMed:1909680}.
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; M63010; AAB00732.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53749.1; -; Genomic_DNA.
DR EMBL; AY089337; AAL90075.1; -; mRNA.
DR EMBL; BT044249; ACH92314.1; -; mRNA.
DR PIR; JH0665; JH0665.
DR RefSeq; NP_001260557.1; NM_001273628.1.
DR RefSeq; NP_477300.1; NM_057952.4.
DR AlphaFoldDB; P25161; -.
DR SMR; P25161; -.
DR BioGRID; 61163; 21.
DR DIP; DIP-18295N; -.
DR IntAct; P25161; 8.
DR STRING; 7227.FBpp0291495; -.
DR PaxDb; P25161; -.
DR PRIDE; P25161; -.
DR DNASU; 35176; -.
DR EnsemblMetazoa; FBtr0302289; FBpp0291495; FBgn0261396.
DR EnsemblMetazoa; FBtr0336843; FBpp0307804; FBgn0261396.
DR GeneID; 35176; -.
DR KEGG; dme:Dmel_CG42641; -.
DR CTD; 35176; -.
DR FlyBase; FBgn0261396; Rpn3.
DR VEuPathDB; VectorBase:FBgn0261396; -.
DR eggNOG; KOG2581; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_019858_1_2_1; -.
DR InParanoid; P25161; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR PhylomeDB; P25161; -.
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-6798695; Neutrophil degranulation.
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 BioGRID-ORCS; 35176; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Rpn3; fly.
DR GenomeRNAi; 35176; -.
DR PRO; PR:P25161; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261396; Expressed in secondary oocyte and 20 other tissues.
DR ExpressionAtlas; P25161; baseline and differential.
DR Genevisible; P25161; DM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000502; C:proteasome complex; IDA:FlyBase.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:FlyBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; ISS:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035267; PSMD3.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Proteasome; Reference proteome.
FT CHAIN 1..494
FT /note="Probable 26S proteasome non-ATPase regulatory
FT subunit 3"
FT /id="PRO_0000173821"
FT DOMAIN 247..426
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 458..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 204
FT /note="D -> H (in Ref. 4; AAL90075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56004 MW; 8659CBCAFF95B735 CRC64;
MTNATDIGAN DVEMEVDPTA ETLADEKKNQ DVAAVQEIRE QIRQIEKGVA SKESRFILRV
LRNLPNTRRK LNGVVFRNLA QSIYPAGADR EAAVALMPAV EKDATELPDV PKKQVATKAP
IAEVDAYFYL LLLVKLIDAS DLKRAGISAD ALMAKISIQN RRTLDLIGAK SYFYFSRVAE
LKNSLEGIRS FLHARLRTAT LRNDFEGQAV LINCLLRNYL HYALYDQADK LVKKSVYPES
ASNNEWARFL YYLGRIKAAK LEYSDAHKHL VQALRKSPQH AAIGFRQTVQ KLIIVVELLL
GNIPERVVFR QAGLRQSLGA YFQLTQAVRL GNLKRFGDVV SQYGPKFQLD HTFTLIIRLR
HNVIKTAIRS IGLSYSRISP QDIAKRLMLD SAEDAEFIVS KAIRDGVIEA TLDPAQNFMR
SKESTDIYST REPQLAFHER ISFCLNLHNQ SVKAMRYPPK SYGKDLESAE ERREREQQDL
ELAKEMAEDD EDGF
