PSMD7_DROME
ID PSMD7_DROME Reviewed; 338 AA.
AC P26270; Q9W178;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 6.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 7;
DE AltName: Full=26S proteasome regulatory subunit RPN8;
DE AltName: Full=26S proteasome regulatory subunit S12;
DE AltName: Full=Proteasome subunit p39B;
DE AltName: Full=Proteasome subunit p40;
DE AltName: Full=Protein Mov34;
GN Name=Rpn8; Synonyms=Mov34; ORFNames=CG3416;
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;
RX PubMed=2209467; DOI=10.1242/dev.109.1.235;
RA Gridley T., Gray D.A., Orr-Weaver T., Soriano P., Barton D.E., Francke U.,
RA Jaenisch R.;
RT "Molecular analysis of the Mov 34 mutation: transcript disrupted by
RT proviral integration in mice is conserved in Drosophila.";
RL Development 109:235-242(1990).
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=Testis;
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 PROTEIN SEQUENCE OF 2-10, AND FUNCTION.
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).
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 -!- INTERACTION:
CC P26270; Q7KMP8: Rpn9; NbExp=3; IntAct=EBI-253612, EBI-151692;
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR EMBL; M64643; AAA28695.1; -; mRNA.
DR EMBL; AE013599; AAF47199.1; -; Genomic_DNA.
DR EMBL; AY089283; AAL90021.1; -; mRNA.
DR RefSeq; NP_001261168.1; NM_001274239.1.
DR RefSeq; NP_523845.2; NM_079121.3.
DR AlphaFoldDB; P26270; -.
DR SMR; P26270; -.
DR BioGRID; 63468; 28.
DR DIP; DIP-22847N; -.
DR IntAct; P26270; 17.
DR STRING; 7227.FBpp0305141; -.
DR MEROPS; M67.973; -.
DR PaxDb; P26270; -.
DR PRIDE; P26270; -.
DR EnsemblMetazoa; FBtr0072290; FBpp0072197; FBgn0002787.
DR EnsemblMetazoa; FBtr0332921; FBpp0305141; FBgn0002787.
DR GeneID; 37894; -.
DR KEGG; dme:Dmel_CG3416; -.
DR UCSC; CG3416-RA; d. melanogaster.
DR CTD; 37894; -.
DR FlyBase; FBgn0002787; Rpn8.
DR VEuPathDB; VectorBase:FBgn0002787; -.
DR eggNOG; KOG1556; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_3_0_1; -.
DR InParanoid; P26270; -.
DR OMA; HAMSIKT; -.
DR OrthoDB; 1275837at2759; -.
DR PhylomeDB; P26270; -.
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 SignaLink; P26270; -.
DR BioGRID-ORCS; 37894; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 37894; -.
DR PRO; PR:P26270; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002787; Expressed in eye disc (Drosophila) and 47 other tissues.
DR ExpressionAtlas; P26270; baseline and differential.
DR Genevisible; P26270; DM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IMP:FlyBase.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR CDD; cd08062; MPN_RPN7_8; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033858; MPN_RPN7_8.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10893261"
FT CHAIN 2..338
FT /note="26S proteasome non-ATPase regulatory subunit 7"
FT /id="PRO_0000213945"
FT DOMAIN 11..147
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 286..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 56
FT /note="S -> T (in Ref. 1; AAA28695)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="E -> V (in Ref. 1; AAA28695)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..146
FT /note="NSVLVIIDAKPKDLGLPTEAYISVEE -> TPCWSSSTPSPRIWACPQRRTY
FT RWRK (in Ref. 1; AAA28695)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="A -> P (in Ref. 1; AAA28695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38089 MW; 1074BBB94268B2D6 CRC64;
MPSQEVSVNK VIVHPLVLLS VVDHFNRMGK IGNQKRVVGV LLGCWRSKGV LDVSNSFAVP
FDEDDKDKSV WFLDHDYLEN MYGMFKKVNA RERVVGWYHT GPKLHQNDIA INELVRRYCP
NSVLVIIDAK PKDLGLPTEA YISVEEVHDD GSPTSKTFEH VPSEIGAEEA EEVGVEHLLR
DIKDTTVGSL SQKITNQLMG LKGLNAQLRD IKQYLQRVGD SKMPINHQIV YQLQDIFNLL
PDITNDQFTG TMYVKTNDQM LVVYLASMVR SIIALHNLIN NKLANRDAEE GKSDSKEAKE
KNKDSKDKDN KETKDKDGKK AEEKADKGKD EGGKGSRK
