PSD11_DROME
ID PSD11_DROME Reviewed; 422 AA.
AC Q7KLV9; A1Z9U3;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE AltName: Full=26S proteasome regulatory complex subunit p42B;
DE AltName: Full=26S proteasome regulatory subunit Rpn6;
GN Name=Rpn6; ORFNames=CG10149;
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 B).
RC 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 [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] (ISOFORM B).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND INTERACTION WITH ALIEN.
RX PubMed=12426099; DOI=10.1016/s0378-1119(02)00930-7;
RA Lier S., Paululat A.;
RT "The proteasome regulatory particle subunit Rpn6 is required for Drosophila
RT development and interacts physically with signalosome subunit Alien/CSN2.";
RL Gene 298:109-119(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 30-422, FUNCTION, AND INTERACTION
RP WITH PROSALPHA2 AND RPT6.
RX PubMed=22187461; DOI=10.1073/pnas.1117648108;
RA Pathare G.R., Nagy I., Bohn S., Unverdorben P., Hubert A., Korner R.,
RA Nickell S., Lasker K., Sali A., Tamura T., Nishioka T., Forster F.,
RA Baumeister W., Bracher A.;
RT "The proteasomal subunit Rpn6 is a molecular clamp holding the core and
RT regulatory subcomplexes together.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:149-154(2012).
CC -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, RPN6 is required for proteasome
CC assembly (By similarity). May act as linker between 19S regulatory
CC subunit and the 20S proteasome core. {ECO:0000250,
CC ECO:0000269|PubMed:22187461}.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S regulatory
CC subunits. Interacts with alien/CSN2. Interacts with Prosalpha2 and
CC Rpt6. {ECO:0000269|PubMed:12426099, ECO:0000269|PubMed:22187461}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q7KLV9-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q7KLV9-2; Sequence=VSP_044401;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the female germline, more
CC precisely in the nurse cells of maturing egg chambers. Also detected in
CC the somatic follicle cells. Highly expressed during oogenesis and early
CC blastoderm embryos. After the beginning of zygotic transcription,
CC present in the elongating germband and later in the mesodermal region
CC and the developing hindgut and posterior midgut. In late embryos,
CC shortly before hatching, becomes restricted to the brain hemispheres,
CC the central nervous system, the embryonic gonads and the gut. In third
CC instar larval tissues, expressed in the larval brain and in all
CC imaginal disks. {ECO:0000269|PubMed:12426099}.
CC -!- DISRUPTION PHENOTYPE: Embryos develop and hatch normally but fail to
CC outlive early larval stages. During the first and second instar larval
CC stages larvae become immobile and sluggish and die without any
CC observable defects. Lethality is probably the result of additive
CC defects in overall cell proliferation rather than of distinct
CC developmental disorders. {ECO:0000269|PubMed:12426099}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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DR EMBL; AF145309; AAF08390.1; -; mRNA.
DR EMBL; AE013599; AAF58212.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58213.2; -; Genomic_DNA.
DR EMBL; AF160939; AAD46879.1; -; mRNA.
DR EMBL; BT089015; ACT98662.1; -; mRNA.
DR RefSeq; NP_001246325.1; NM_001259396.2. [Q7KLV9-1]
DR RefSeq; NP_477474.1; NM_058126.5. [Q7KLV9-1]
DR RefSeq; NP_725412.2; NM_166065.3. [Q7KLV9-2]
DR PDB; 3TXM; X-ray; 3.00 A; A=30-422.
DR PDB; 3TXN; X-ray; 2.50 A; A=30-422.
DR PDBsum; 3TXM; -.
DR PDBsum; 3TXN; -.
DR AlphaFoldDB; Q7KLV9; -.
DR SMR; Q7KLV9; -.
DR BioGRID; 62384; 37.
DR DIP; DIP-60004N; -.
DR IntAct; Q7KLV9; 4.
DR STRING; 7227.FBpp0086603; -.
DR iPTMnet; Q7KLV9; -.
DR PaxDb; Q7KLV9; -.
DR PRIDE; Q7KLV9; -.
DR DNASU; 36638; -.
DR EnsemblMetazoa; FBtr0087474; FBpp0086603; FBgn0028689. [Q7KLV9-2]
DR EnsemblMetazoa; FBtr0087475; FBpp0086604; FBgn0028689. [Q7KLV9-1]
DR EnsemblMetazoa; FBtr0306558; FBpp0297513; FBgn0028689. [Q7KLV9-1]
DR GeneID; 36638; -.
DR KEGG; dme:Dmel_CG10149; -.
DR UCSC; CG10149-RA; d. melanogaster.
DR UCSC; CG10149-RB; d. melanogaster. [Q7KLV9-1]
DR CTD; 36638; -.
DR FlyBase; FBgn0028689; Rpn6.
DR VEuPathDB; VectorBase:FBgn0028689; -.
DR eggNOG; KOG1463; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR HOGENOM; CLU_029573_2_1_1; -.
DR InParanoid; Q7KLV9; -.
DR PhylomeDB; Q7KLV9; -.
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; 36638; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36638; -.
DR PRO; PR:Q7KLV9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028689; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q7KLV9; baseline and differential.
DR Genevisible; Q7KLV9; 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:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035295; PSMD11.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF6; PTHR10678:SF6; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Proteasome;
KW Reference proteome.
FT CHAIN 1..422
FT /note="26S proteasome non-ATPase regulatory subunit 11"
FT /id="PRO_0000419982"
FT DOMAIN 224..392
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1
FT /note="M -> MTELLKENRSNEARRRKM (in isoform A)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044401"
FT HELIX 39..60
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:3TXN"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 123..139
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:3TXN"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:3TXN"
FT TURN 310..315
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 317..339
FT /evidence="ECO:0007829|PDB:3TXN"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:3TXN"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:3TXN"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3TXN"
FT TURN 380..383
FT /evidence="ECO:0007829|PDB:3TXN"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3TXN"
SQ SEQUENCE 422 AA; 47263 MW; 57F1D24C4303F8C5 CRC64;
MAGATLFERA QALSSVNREE QDSSLLNKLV RDQEGAENDE ERIRIKEQGI LQQGELYKQE
GKAKELADLI KVTRPFLSSI SKAKAAKLVR SLVDMFLDMD AGTGIEVQLC KDCIEWAKQE
KRTFLRQSLE ARLIALYFDT ALYTEALALG AQLLRELKKL DDKNLLVEVQ LLESKTYHAL
SNLPKARAAL TSARTTANAI YCPPKVQGAL DLQSGILHAA DERDFKTAFS YFYEAFEGFD
SVDSVKALTS LKYMLLCKIM LGQSDDVNQL VSGKLAITYS GRDIDAMKSV AEASHKRSLA
DFQAALKEYK KELAEDVIVQ AHLGTLYDTM LEQNLCRIIE PYSRVQVAHV AESIQLPMPQ
VEKKLSQMIL DKKFSGILDQ GEGVLIVFEE TPVDKTYERV LETIQSMGKV VDTLYQKAKK
LS
