PSMD5_DROME
ID PSMD5_DROME Reviewed; 506 AA.
AC Q9VYG1; A9UNC9; Q7K0M3; Q8SZZ0;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 5 {ECO:0000250|UniProtKB:Q16401};
DE AltName: Full=26S proteasome subunit S5B {ECO:0000250|UniProtKB:Q16401};
DE Short=dS5b {ECO:0000303|PubMed:23622245};
GN ORFNames=CG12096;
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] {ECO:0000312|EMBL:AAF48236.3}
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 [2] {ECO:0000312|EMBL:AAF48236.3}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAL39843.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-506.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000312|EMBL:AFA28457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J., Booth B., Frise E., Kapadia B., Park S., Wan K.,
RA Yu C., Celniker S.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP INTERACTION WITH PI31 AND RPT2, AND MUTAGENESIS OF GLU-44; ARG-45; LEU-46;
RP PRO-165; ASP-172; VAL-261 AND ARG-263.
RX PubMed=23622245; DOI=10.1016/j.cell.2013.03.040;
RA Cho-Park P.F., Steller H.;
RT "Proteasome regulation by ADP-ribosylation.";
RL Cell 153:614-627(2013).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome. {ECO:0000250|UniProtKB:Q16401}.
CC -!- SUBUNIT: Interacts with PI31; this interaction is increased by PI31
CC ADP-ribosylation. Interacts with Rpt2. {ECO:0000269|PubMed:23622245}.
CC -!- INTERACTION:
CC Q9VYG1; Q9V637: PI31; NbExp=2; IntAct=EBI-129453, EBI-144377;
CC Q9VYG1; Q9XZC3: Rpt5; NbExp=2; IntAct=EBI-129453, EBI-6924616;
CC -!- SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48236.3; -; Genomic_DNA.
DR EMBL; AY069698; AAL39843.1; ALT_INIT; mRNA.
DR EMBL; BT031293; ABY20534.1; -; mRNA.
DR EMBL; BT133216; AFA28457.1; -; mRNA.
DR RefSeq; NP_001285190.1; NM_001298261.1.
DR RefSeq; NP_001285191.1; NM_001298262.1.
DR RefSeq; NP_572862.2; NM_132634.4.
DR AlphaFoldDB; Q9VYG1; -.
DR BioGRID; 58654; 5.
DR IntAct; Q9VYG1; 4.
DR STRING; 7227.FBpp0073558; -.
DR PaxDb; Q9VYG1; -.
DR PRIDE; Q9VYG1; -.
DR DNASU; 32269; -.
DR EnsemblMetazoa; FBtr0073727; FBpp0073558; FBgn0030457.
DR EnsemblMetazoa; FBtr0340298; FBpp0309259; FBgn0030457.
DR EnsemblMetazoa; FBtr0340299; FBpp0309260; FBgn0030457.
DR GeneID; 32269; -.
DR KEGG; dme:Dmel_CG12096; -.
DR UCSC; CG12096-RA; d. melanogaster.
DR FlyBase; FBgn0030457; CG12096.
DR VEuPathDB; VectorBase:FBgn0030457; -.
DR eggNOG; KOG4413; Eukaryota.
DR HOGENOM; CLU_043710_0_0_1; -.
DR InParanoid; Q9VYG1; -.
DR OMA; LVAREWC; -.
DR OrthoDB; 602046at2759; -.
DR PhylomeDB; Q9VYG1; -.
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-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-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-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 BioGRID-ORCS; 32269; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32269; -.
DR PRO; PR:Q9VYG1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030457; Expressed in thoracico-abdominal ganglion (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q9VYG1; baseline and differential.
DR Genevisible; Q9VYG1; DM.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019538; PSMD5.
DR PANTHER; PTHR13554; PTHR13554; 1.
DR Pfam; PF10508; Proteasom_PSMB; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..506
FT /note="26S proteasome non-ATPase regulatory subunit 5"
FT /id="PRO_0000424894"
FT MUTAGEN 44
FT /note="E->A: Abolishes interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 45
FT /note="R->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 46
FT /note="L->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 165
FT /note="P->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 172
FT /note="D->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 261
FT /note="V->T: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 263
FT /note="R->A: Abolishes interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT CONFLICT 326
FT /note="A -> T (in Ref. 4; ABY20534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56668 MW; FDD4CA3103FDAD33 CRC64;
MEMEDNWWVT KLKALESKPQ RLDALTAMNS AIAKEAALPR QIIERLLTTD QLYDCANPAA
DSHVPKDQAV DVTLELLCHC LDQLAMDTAD EQLSSLLRRG LTHSNPALRA QVLASLFKKL
LRQLTVGQVL TLPNNELIFL ILDELKQPDT QSTSLAINIL SIVLPQRISN ADVQAKLVQL
LKQNEIVRCR AYELAVVLAK KSATLLSDVT FILDAALSEL DNDDVLLQAS VMELLVPLAE
QNHGLSYMER RRVLDIISYR VQRVEEHPLD ALLVPSIMKF FGKISVYQPL KIIGGYPHML
ACLFMQLQSE DESILPTAMD TLANLATTPQ GKILLNMHFS GAMEKSFKKY GSHTKKLSAH
IKKRLLNSLD VIYDFKTPPA TEIINIGKNW YECFAGGAHA NIIMDLINTP FPDLQMAALS
FLKTICKYNW GIVALKNTGG AVEFLLSRQK DLHRDIKYMK WQIMEILSAS AEFSPTETIR
FTAYVNEGPY HVQADLDVAT EPQGNA
