PSDE_DICDI
ID PSDE_DICDI Reviewed; 306 AA.
AC Q86IJ1; O00850; Q559F3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory subunit RPN11;
DE AltName: Full=Sks1 multidrug resistance protein homolog;
GN Name=psmD14; Synonyms=sks1; ORFNames=DDB_G0272566;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA De Maria A.C., Gomes S.L.;
RT "Characterization of the sks1 multidrug resistance gene homolog in
RT Dictyostelium discoideum.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14 subfamily.
CC {ECO:0000305}.
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DR EMBL; U96916; AAB57823.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL70920.1; -; Genomic_DNA.
DR RefSeq; XP_644863.1; XM_639771.1.
DR AlphaFoldDB; Q86IJ1; -.
DR SMR; Q86IJ1; -.
DR STRING; 44689.DDB0191298; -.
DR MEROPS; M67.001; -.
DR PaxDb; Q86IJ1; -.
DR EnsemblProtists; EAL70920; EAL70920; DDB_G0272566.
DR GeneID; 8618542; -.
DR KEGG; ddi:DDB_G0272566; -.
DR dictyBase; DDB_G0272566; psmD14.
DR eggNOG; KOG1555; Eukaryota.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; Q86IJ1; -.
DR OMA; VFQTRMM; -.
DR PhylomeDB; Q86IJ1; -.
DR Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-5689901; Metalloprotease DUBs.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q86IJ1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0000502; C:proteasome complex; ISS:dictyBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
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; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Proteasome;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..306
FT /note="26S proteasome non-ATPase regulatory subunit 14"
FT /id="PRO_0000315595"
FT DOMAIN 31..166
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 113..126
FT /note="JAMM motif"
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 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT CONFLICT 193..194
FT /note="LN -> SI (in Ref. 1; AAB57823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 34451 MW; 53FA4B37CECD86EE CRC64;
MNRSLMSLLG REGLGEKITD ATPLPDTAET IHISSLALLK MLQHARAGVP LEVMGLMLGE
LIDEYTIRVI DVFAMPQSGT SVSVEAIDPV FQTKMLDMLK QTGRDEIVIG WYHSHPGFGC
WLSSVDVNTQ QSFEQLQSRA VAVVVDPLQS VRGKVVIDAF RTIKTSPTAE PRQITSNLGH
LQDPSIQALI HGLNRNYYSI AINYRKNELE QKMLLNLHKK KWTEGLIVDK FDTHEQSNEK
QINNLLELTK QYQKSIQDED KIEPEKKEVS AVGKLDPKRH LISDVHTLMA NNVVRVLTVM
LDTVTF
