PSMD4_DROME
ID PSMD4_DROME Reviewed; 396 AA.
AC P55035; Q86R87; Q9V473;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 4;
DE AltName: Full=26S proteasome regulatory subunit RPN10;
DE AltName: Full=26S proteasome regulatory subunit S5A;
DE AltName: Full=54 kDa subunit of mu particle;
DE AltName: Full=Multiubiquitin chain-binding protein;
DE AltName: Full=p54;
GN Name=Rpn10; Synonyms=PROS-54, Pros54; ORFNames=CG7619;
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 [GENOMIC DNA].
RX PubMed=7649173; DOI=10.1111/j.1432-1033.1995.tb20753.x;
RA Haracska L., Udvardy A.;
RT "Cloning and sequencing a non-ATPase subunit of the regulatory complex of
RT the Drosophila 26S protease.";
RL Eur. J. Biochem. 231:720-725(1995).
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 INTERACTION WITH UBCD4.
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=11862484; DOI=10.1007/s00438-001-0623-8;
RA Canning M., Kirby R., Finnegan D.;
RT "UbcD4, a ubiquitin-conjugating enzyme in Drosophila melanogaster expressed
RT in pole cells.";
RL Mol. Genet. Genomics 266:907-913(2002).
CC -!- FUNCTION: Binds and presumably selects ubiquitin-conjugates for
CC destruction.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively (By
CC similarity). Interacts with Ubc4. {ECO:0000250,
CC ECO:0000269|PubMed:11862484}.
CC -!- INTERACTION:
CC P55035; P52486: Ubc4; NbExp=2; IntAct=EBI-146479, EBI-224571;
CC P55035; Q9VWD9: Ubqn; NbExp=4; IntAct=EBI-146479, EBI-100499;
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90071.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S79502; AAB35145.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51741.1; -; Genomic_DNA.
DR EMBL; AY089333; AAL90071.2; ALT_INIT; mRNA.
DR PIR; S66528; S66528.
DR RefSeq; NP_001262168.1; NM_001275239.1.
DR RefSeq; NP_524204.1; NM_079480.3.
DR AlphaFoldDB; P55035; -.
DR SMR; P55035; -.
DR BioGRID; 65632; 29.
DR DIP; DIP-22777N; -.
DR IntAct; P55035; 15.
DR MINT; P55035; -.
DR STRING; 7227.FBpp0078024; -.
DR PaxDb; P55035; -.
DR PRIDE; P55035; -.
DR EnsemblMetazoa; FBtr0078368; FBpp0078024; FBgn0015283.
DR EnsemblMetazoa; FBtr0333453; FBpp0305644; FBgn0015283.
DR GeneID; 40388; -.
DR KEGG; dme:Dmel_CG7619; -.
DR CTD; 40388; -.
DR FlyBase; FBgn0015283; Rpn10.
DR VEuPathDB; VectorBase:FBgn0015283; -.
DR eggNOG; KOG2884; Eukaryota.
DR GeneTree; ENSGT00530000064050; -.
DR HOGENOM; CLU_033293_0_0_1; -.
DR InParanoid; P55035; -.
DR OMA; IQGEDGM; -.
DR OrthoDB; 1244685at2759; -.
DR PhylomeDB; P55035; -.
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-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; P55035; -.
DR BioGRID-ORCS; 40388; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40388; -.
DR PRO; PR:P55035; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0015283; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; P55035; baseline and differential.
DR Genevisible; P55035; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
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:0031593; F:polyubiquitin modification-dependent protein binding; ISS:FlyBase.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02809; UIM; 3.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00726; UIM; 3.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 3.
PE 1: Evidence at protein level;
KW Proteasome; Reference proteome; Repeat.
FT CHAIN 1..396
FT /note="26S proteasome non-ATPase regulatory subunit 4"
FT /id="PRO_0000173830"
FT DOMAIN 1..188
FT /note="VWFA"
FT DOMAIN 212..231
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 276..295
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 303..322
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 225..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 9
FT /note="C -> S (in Ref. 1; AAB35145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42618 MW; 061418F6F7FE819F CRC64;
MVLESTMICF DNSDFQRNGD YFPTRLIVQR DGINLVCLTK LRSNPENNVG LMTLSNTVEV
LATLTSDAGR IFSKMHLVQP KGEINLLTGI RIAHLVLKHR QGKNHKMRIV VFVGSPINHE
EGDLVKQAKR LKKEKVNVDI VSFGDHGNNN EILTAFINAL NGKDGTGSHL VSVPRGSVLS
DALLSSPIIQ GEDGMGGAGL GGNVFEFGVD PNEDPELALA LRVSMEEQRQ RQESEQRRAN
PDGAPPTGGD AGGGGGVSGS GPGNEESAGA ENEANTEEAM LQRALALSTE TPEDNLPDFA
NMTEEEQIAF AMQMSMQDAP DDSVTQQAKR PKTDEANAPM DVDEDYSEVI GDPAFLQSVL
ENLPGVDPQS EAVRDAVGSL NKDKDKKSDG KDSQKK
