PSDE_DROME
ID PSDE_DROME Reviewed; 308 AA.
AC Q9V3H2; Q9NIU3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory complex subunit p37B;
DE AltName: Full=26S proteasome regulatory subunit rpn11;
DE AltName: Full=Yippee-interacting protein 5;
GN Name=Rpn11; Synonyms=yip5; ORFNames=CG18174;
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, PROTEIN SEQUENCE OF 263-271, 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).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-308.
RC TISSUE=Imaginal disk;
RA Roxstrom-Lindquist K., Faye I.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metalloprotease component of the 26S proteasome that
CC specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S
CC proteasome is involved in the ATP-dependent degradation of
CC ubiquitinated proteins. The function of the 'Lys-63'-specific
CC deubiquitination of the proteasome is unclear (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10893261}.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF145313; AAF08394.1; -; mRNA.
DR EMBL; AE014134; AAF52215.1; -; Genomic_DNA.
DR EMBL; AY070977; AAL48599.1; -; mRNA.
DR EMBL; AF195189; AAF27818.1; -; mRNA.
DR RefSeq; NP_608905.1; NM_135061.4.
DR AlphaFoldDB; Q9V3H2; -.
DR SMR; Q9V3H2; -.
DR BioGRID; 59913; 33.
DR IntAct; Q9V3H2; 8.
DR STRING; 7227.FBpp0078664; -.
DR MEROPS; M67.A11; -.
DR PaxDb; Q9V3H2; -.
DR PRIDE; Q9V3H2; -.
DR EnsemblMetazoa; FBtr0079027; FBpp0078664; FBgn0028694.
DR GeneID; 33738; -.
DR KEGG; dme:Dmel_CG18174; -.
DR CTD; 33738; -.
DR FlyBase; FBgn0028694; Rpn11.
DR VEuPathDB; VectorBase:FBgn0028694; -.
DR eggNOG; KOG1555; Eukaryota.
DR GeneTree; ENSGT00730000111116; -.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; Q9V3H2; -.
DR OMA; VFQTRMM; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; Q9V3H2; -.
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-5689901; Metalloprotease DUBs.
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; 33738; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 33738; -.
DR PRO; PR:Q9V3H2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028694; Expressed in secondary oocyte and 28 other tissues.
DR Genevisible; Q9V3H2; 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:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISS:FlyBase.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; ISS:FlyBase.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR035299; PSMD14.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR PANTHER; PTHR10410:SF22; PTHR10410:SF22; 1.
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; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Proteasome; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..308
FT /note="26S proteasome non-ATPase regulatory subunit 14"
FT /id="PRO_0000213955"
FT DOMAIN 29..164
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 111..124
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT CONFLICT 144..145
FT /note="DP -> YS (in Ref. 5; AAF27818)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> F (in Ref. 5; AAF27818)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="L -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34401 MW; CA43EEBD13B42A61 CRC64;
MDRLLRLGGA MPQAAPPTDA PVVDTAEQVY ISSLALLKML KHGRAGVPME VMGLMLGEFV
DDYTVQVIDV FAMPQTGTGV SVEAVDPVFQ AKMLDMLKQT GRPEMVVGWY HSHPGFGCWL
SGVDINTQQS FEALSERAVA VVVDPIQSVK GKVVIDAFRL INPNMLVLGQ EPRQTTSNLG
HLQKPSVQAL IHGLNRHYYS ISINYRKNEL EQKMLLNLHK KSWKDGLTLS DYNEHCSINE
DTVAEMLDLA KNYNKSLEDE EKMTPEQLAI KNVGKQDPKR HLEEKVDKVM QNNIVQCLGA
MLDTIVFK
