PSMD1_DROME
ID PSMD1_DROME Reviewed; 1020 AA.
AC Q9V3P6; B5RIH8; Q8IGU4; Q8T075; Q9GSE5; Q9GU70;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE AltName: Full=26S proteasome regulatory complex subunit p110;
DE AltName: Full=26S proteasome regulatory subunit RPN2;
GN Name=Rpn2; ORFNames=CG11888;
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] (ISOFORM A), PROTEIN SEQUENCE OF 844-856, AND
RP FUNCTION.
RC STRAIN=Berkeley; TISSUE=Embryo;
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., Baumeister W.;
RT "The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit
RT composition and localization of a deubiquitylating enzyme.";
RL J. Cell Biol. 150:119-130(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-531 (ISOFORM A).
RC STRAIN=Berkeley, and Oregon-R; TISSUE=Embryo;
RX PubMed=11157774; DOI=10.1101/gad.862801;
RA Sullivan E.O., Santiago C., Parker E.D., Dominski Z., Yang X.,
RA Lanzotti D.J., Ingledue T.C., Marzluff W.F., Duronio R.J.;
RT "Drosophila stem loop binding protein coordinates accumulation of mature
RT histone mRNA with cell cycle progression.";
RL Genes Dev. 15:173-187(2001).
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] (ISOFORM A).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291; SER-298; SER-303;
RP SER-305 AND THR-310, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000269|PubMed:10893261}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9V3P6-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V3P6-2; Sequence=VSP_011611;
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39648.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF145303; AAF08384.1; -; mRNA.
DR EMBL; AF186594; AAG16726.2; -; Genomic_DNA.
DR EMBL; AF312231; AAG33625.1; -; mRNA.
DR EMBL; AE014297; AAF56868.1; -; Genomic_DNA.
DR EMBL; AY069503; AAL39648.1; ALT_INIT; mRNA.
DR EMBL; BT001598; AAN71353.1; -; mRNA.
DR EMBL; BT044102; ACH92167.1; -; mRNA.
DR RefSeq; NP_001263058.1; NM_001276129.1. [Q9V3P6-1]
DR RefSeq; NP_651677.2; NM_143420.3. [Q9V3P6-1]
DR AlphaFoldDB; Q9V3P6; -.
DR SMR; Q9V3P6; -.
DR BioGRID; 68320; 39.
DR IntAct; Q9V3P6; 6.
DR STRING; 7227.FBpp0084754; -.
DR iPTMnet; Q9V3P6; -.
DR PaxDb; Q9V3P6; -.
DR PRIDE; Q9V3P6; -.
DR DNASU; 43449; -.
DR EnsemblMetazoa; FBtr0085385; FBpp0084754; FBgn0028692. [Q9V3P6-1]
DR EnsemblMetazoa; FBtr0334532; FBpp0306599; FBgn0028692. [Q9V3P6-1]
DR GeneID; 43449; -.
DR KEGG; dme:Dmel_CG11888; -.
DR UCSC; CG11888-RA; d. melanogaster. [Q9V3P6-1]
DR CTD; 6185; -.
DR FlyBase; FBgn0028692; Rpn2.
DR VEuPathDB; VectorBase:FBgn0028692; -.
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; Q9V3P6; -.
DR OMA; MIMVQQN; -.
DR PhylomeDB; Q9V3P6; -.
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; 43449; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43449; -.
DR PRO; PR:Q9V3P6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0028692; Expressed in eye disc (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9V3P6; baseline and differential.
DR Genevisible; Q9V3P6; DM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; 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:0034515; C:proteasome storage granule; IBA:GO_Central.
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; IMP:FlyBase.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat.
FT CHAIN 1..1020
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000173804"
FT REPEAT 418..452
FT /note="PC 1"
FT REPEAT 456..489
FT /note="PC 2"
FT REPEAT 491..525
FT /note="PC 3"
FT REPEAT 526..560
FT /note="PC 4"
FT REPEAT 562..595
FT /note="PC 5"
FT REPEAT 596..631
FT /note="PC 6"
FT REPEAT 632..664
FT /note="PC 7"
FT REPEAT 666..701
FT /note="PC 8"
FT REPEAT 702..742
FT /note="PC 9"
FT REPEAT 745..777
FT /note="PC 10"
FT REGION 279..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 41..114
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11157774"
FT /id="VSP_011611"
FT CONFLICT 646
FT /note="E -> G (in Ref. 5; AAN71353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 113199 MW; 8DE7AA5264742EB1 CRC64;
MSLTSAAGII SLLDEPMPDL KVFALKKLDN IVDEFWPEIS ESIEKIEMLH EDRSFPENKL
AGMVASKVFY HLGSFEDALT YALGAGDLFD VNARNEYTET IIAKCIDFYI AQRVEFIENP
KEASVVDERL EGIVNRMIQR CLDDNQFRQA LGIALETRRM DTFKDAIMKS DDVRGMLAYA
YNVTMSLIQN RGFRNEVLRC LVSLYRDLGV PDYVNMCQCL IFLEDPFAVA EMLDNLTRSS
VETNNLMAYQ IAFDLYESAT QEFLGNVLQH LKNTAPIPTA LPSTFKPQGT TSEDGAKSEG
DKSKSDEDIT EETPADDKVE RTIDSLNEVE KLHQKNIEKL ISILSGEVSI DLQLQFLIRS
NHADLQVLRG TKEAVRVSIC HTATVIANAF MHSGTTSDQF LRDNLDWLAR ATNWAKLTAT
ASLGVIHRGH EKDSLALMQS YLPKEAGPSS GYSEGGALYA LGLIHANHGA NIIDYLLQQL
KDAQNENVRH GGCLGLGLAG MGTHRQDLYE QLKFNLYQDD AVTGEAAGIA MGMVMLGSKN
AQAIEDMVSY AQETQHEKIL RGLAVGISLT MFSRLEEADP LVTSLSSDKD PVLRRSGMYT
IAMAYNGTGS NKAIRKLLHV AVSDVNDDVR RAAVTAIGFI LFRSPEQCPS VVSLLAESYN
PHVRYGAAMA LGIACAGTGL REAIALLEPM VKFDPVNFVR QGALIASAMI LIQHTDQSCP
KSTFFRQLYA EVISNKHEDV MAKYGAILAQ GIIDAGGRNA TLSLQSRTGH TNLQAVVGML
AFTQYWYWFP LAHTLSLAFT PTCVIGLNSD LKMPKMEYKS AAKPSLYAYP APLEEKKSEE
REKVATAVLS IAARQKRREN ADKKEDEKMD VDEDSKEGAA VKKDEEAKAD EKMVTDEKPK
KKDEKEKKKE EDKEKEAAGT SSEKDKDKEK DKKEKKEPEP TSEILQNPAR VLRQQLKVLS
VIDGQSYEPL KDVTIGGIIV FQHTGKAEDQ ELVEPVAAFG PMNDEEKEPE PPEPFEYIED
