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PSMD6_DROME
ID   PSMD6_DROME             Reviewed;         389 AA.
AC   Q9V3G7;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 6;
DE   AltName: Full=26S proteasome regulatory subunit S10;
DE   AltName: Full=Protein Rpn7;
GN   Name=Rpn7; ORFNames=CG5378;
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].
RC   TISSUE=Head;
RA   Hoelzl H., Kapelari B., Kellermann J., Nitsch M., Seemueller E., Voges D.,
RA   Udvardy A., Mueller S.A., Engel A., Baumeister W.;
RT   "The regulatory complex of the Drosophila 26S proteasomes.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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=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).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S10 family.
CC       {ECO:0000305}.
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DR   EMBL; AF145308; AAF08389.1; -; mRNA.
DR   EMBL; AE014297; AAF56000.1; -; Genomic_DNA.
DR   EMBL; AY052008; AAK93432.1; -; mRNA.
DR   RefSeq; NP_651048.1; NM_142791.3.
DR   AlphaFoldDB; Q9V3G7; -.
DR   SMR; Q9V3G7; -.
DR   BioGRID; 67596; 37.
DR   DIP; DIP-23841N; -.
DR   IntAct; Q9V3G7; 7.
DR   STRING; 7227.FBpp0083687; -.
DR   PaxDb; Q9V3G7; -.
DR   PRIDE; Q9V3G7; -.
DR   DNASU; 42641; -.
DR   EnsemblMetazoa; FBtr0084294; FBpp0083687; FBgn0028688.
DR   GeneID; 42641; -.
DR   KEGG; dme:Dmel_CG5378; -.
DR   UCSC; CG5378-RA; d. melanogaster.
DR   CTD; 42641; -.
DR   FlyBase; FBgn0028688; Rpn7.
DR   VEuPathDB; VectorBase:FBgn0028688; -.
DR   eggNOG; KOG0687; Eukaryota.
DR   GeneTree; ENSGT00510000046608; -.
DR   HOGENOM; CLU_031814_0_0_1; -.
DR   InParanoid; Q9V3G7; -.
DR   OMA; SLYNCHY; -.
DR   OrthoDB; 1194691at2759; -.
DR   PhylomeDB; Q9V3G7; -.
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; 42641; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 42641; -.
DR   PRO; PR:Q9V3G7; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0028688; Expressed in secondary oocyte and 22 other tissues.
DR   Genevisible; Q9V3G7; 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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035268; PSMD6.
DR   InterPro; IPR019585; Rpn7/CSN1.
DR   InterPro; IPR045135; Rpn7_N.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR14145; PTHR14145; 1.
DR   PANTHER; PTHR14145:SF1; PTHR14145:SF1; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF10602; RPN7; 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..389
FT                   /note="26S proteasome non-ATPase regulatory subunit 6"
FT                   /id="PRO_0000173841"
FT   DOMAIN          193..361
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ   SEQUENCE   389 AA;  45381 MW;  CCC1DE0C7393B6FA CRC64;
     MPAENLEEQG LEKNPNLELA QTKFLLTLAE YKQDAALKAK LLEAIRTENM APWYEHICSE
     LGWTVDKDLL ARMKENNRVE VEQLDAAIED AEKNLGEMEV REANLKKSEY LCRIGDKAAA
     ETAFRKTYEK TVSLGHRLDI VFHLIRLGLF YLDHDLITRN IDKAKYLIEE GGDWDRRNRL
     KVYQGVYSVA VRDFKAAATF FLDTVSTFTS YELMDYPTFV RYTVYVAMIA LPRNELRDKV
     IKGSEIQEVL HGLPDVKQFL FSLYNCQYEN FYVHLAGVEK QLRLDYLIHP HYRYYVREMR
     ILGYTQLLES YRSLTLQYMA ESFGVTVEYI DQELARFIAA GRLHAKVDRV GGIVETNRPD
     NKNWQYQATI KQGDLLLNRI QKLSRVINI
 
 
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