ID   RPN11_ENCCU             Reviewed;         294 AA.
AC   Q8SQY3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=26S proteasome regulatory subunit RPN11;
GN   Name=RPN11; OrderedLocusNames=ECU11_0570;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC       degrades poly-ubiquitinated proteins in the cytoplasm and in the
CC       nucleus. It is essential for the regulated turnover of proteins and for
CC       the removal of misfolded proteins. The proteasome is a multicatalytic
CC       proteinase complex that is characterized by its ability to cleave
CC       peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC       at neutral or slightly basic pH (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is composed of 28
CC       subunits that are arranged in four stacked rings, resulting in a
CC       barrel-shaped structure. The two end rings are each formed by seven
CC       alpha subunits, and the two central rings are each formed by seven beta
CC       subunits. The catalytic chamber with the active sites is on the inside
CC       of the barrel (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; AL590450; CAD25967.1; -; Genomic_DNA.
DR   RefSeq; NP_586363.1; NM_001042196.1.
DR   AlphaFoldDB; Q8SQY3; -.
DR   SMR; Q8SQY3; -.
DR   STRING; 284813.Q8SQY3; -.
DR   MEROPS; M67.A11; -.
DR   GeneID; 860016; -.
DR   KEGG; ecu:ECU11_0570; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0570; -.
DR   HOGENOM; CLU_052991_0_1_1; -.
DR   InParanoid; Q8SQY3; -.
DR   OMA; PCEILAD; -.
DR   OrthoDB; 1031881at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR035299; PSMD14.
DR   PANTHER; PTHR10410:SF22; PTHR10410:SF22; 1.
DR   Pfam; PF01398; JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW   Proteasome; Reference proteome; Zinc.
FT   CHAIN           1..294
FT                   /note="26S proteasome regulatory subunit RPN11"
FT                   /id="PRO_0000382902"
FT   DOMAIN          21..156
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           103..116
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   294 AA;  33173 MW;  FC72AF9B745566DC CRC64;
     MFSGFVGPDD GEPTSDASET VQISSLALLK MLKHGRAGIP LEVMGLMLGE FVDEYTVKVV
     DVFAMPQSGT NVTVESVDPI FQMEMMSILK ATGRHETVVG WYHSHPGFGC WLSTVDISTQ
     QSFEKLCKRA VAVVVDPIQS VKGKVVIDAF RLIDNQLGVL GGEPRQVTSN IGYLKTPTLI
     SIIHGLNKHY YSFNITCRKN DFEQKMLLNL HRKTWADNLK LGDVRSKREE ALKLIESYGK
     AFEEEKNLAG KNPDMAKVGR IDYRRRLLEK CEESIMENTI YSLLYSIHRY IFTQ