PSMD9_DROME
ID PSMD9_DROME Reviewed; 220 AA.
AC Q9VFS8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 9 {ECO:0000250|UniProtKB:O00233};
DE AltName: Full=26S proteasome regulatory subunit p27 {ECO:0000250|UniProtKB:O00233};
DE Short=dp27 {ECO:0000303|PubMed:23622245};
GN ORFNames=CG9588;
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:AAF54971.1}
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:AAF54971.1}
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:0000312|EMBL:AAL48686.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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:0000305}
RP INTERACTION WITH PI31 AND RPT5, AND MUTAGENESIS OF GLU-9; ARG-10; LEU-11;
RP PRO-114; ASP-121; VAL-185 AND ARG-187.
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, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). {ECO:0000250|UniProtKB:O00233}.
CC -!- SUBUNIT: Interacts with PI31; this interaction is increased by PI31
CC ADP-ribosylation. Interacts with Rpt5. {ECO:0000269|PubMed:23622245}.
CC -!- INTERACTION:
CC Q9VFS8; Q9V637: PI31; NbExp=3; IntAct=EBI-166054, EBI-144377;
CC -!- SIMILARITY: Belongs to the proteasome subunit p27 family.
CC {ECO:0000250|UniProtKB:O00233}.
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DR EMBL; AE014297; AAF54971.1; -; Genomic_DNA.
DR EMBL; AY071064; AAL48686.1; -; mRNA.
DR RefSeq; NP_650301.1; NM_142044.4.
DR AlphaFoldDB; Q9VFS8; -.
DR SMR; Q9VFS8; -.
DR BioGRID; 66752; 14.
DR IntAct; Q9VFS8; 19.
DR STRING; 7227.FBpp0082314; -.
DR PaxDb; Q9VFS8; -.
DR DNASU; 41672; -.
DR EnsemblMetazoa; FBtr0082849; FBpp0082314; FBgn0038166.
DR GeneID; 41672; -.
DR KEGG; dme:Dmel_CG9588; -.
DR UCSC; CG9588-RA; d. melanogaster.
DR FlyBase; FBgn0038166; CG9588.
DR VEuPathDB; VectorBase:FBgn0038166; -.
DR eggNOG; KOG3129; Eukaryota.
DR GeneTree; ENSGT00390000004147; -.
DR HOGENOM; CLU_073146_2_1_1; -.
DR InParanoid; Q9VFS8; -.
DR OMA; GCNIVPL; -.
DR OrthoDB; 1405146at2759; -.
DR PhylomeDB; Q9VFS8; -.
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; 41672; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41672; -.
DR PRO; PR:Q9VFS8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038166; Expressed in seminal fluid secreting gland and 31 other tissues.
DR Genevisible; Q9VFS8; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR040815; Nas2_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035269; PSMD9.
DR PANTHER; PTHR12651; PTHR12651; 1.
DR Pfam; PF18265; Nas2_N; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Reference proteome.
FT CHAIN 1..220
FT /note="26S proteasome non-ATPase regulatory subunit 9"
FT /id="PRO_0000424893"
FT DOMAIN 102..200
FT /note="PDZ"
FT /evidence="ECO:0000255"
FT COILED 4..32
FT /evidence="ECO:0000255"
FT COILED 61..91
FT /evidence="ECO:0000255"
FT MUTAGEN 9
FT /note="E->A: Abolishes interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 10
FT /note="R->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 11
FT /note="L->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 114
FT /note="P->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 121
FT /note="D->A: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 185
FT /note="V->T: Does not affect interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
FT MUTAGEN 187
FT /note="R->A: Abolishes interaction with PI31."
FT /evidence="ECO:0000269|PubMed:23622245"
SQ SEQUENCE 220 AA; 23898 MW; C618E8D04262293A CRC64;
MAAGTTTKER LERLINAKKQ LEAQINRNGQ ILAANDNVGM SGPLVDAEGF PRNDIDVYQV
RLARQTIICL QNDHKELMNQ IQTLLNQYHS EIATTDPELV NRASALDLDS DRSPGGANIT
DLAPARAIVV VNLVSPDSPA ERAGLCAGDA ILRFGSINSG NFKGDLAQIG ELVRNMQSQN
VQLKVKRGEQ QLDLILVPKT WSGRGLLGCN IVLPPEAMDH
