ID   RPN2_ENCCU              Reviewed;         786 AA.
AC   Q8SSH5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=26S proteasome regulatory subunit RPN2;
GN   Name=RPN2; OrderedLocusNames=ECU02_0480;
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 proteasome subunit S1 family. {ECO:0000305}.
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DR   EMBL; AL590442; CAD25079.1; -; Genomic_DNA.
DR   RefSeq; NP_584575.1; NM_001040764.1.
DR   AlphaFoldDB; Q8SSH5; -.
DR   SMR; Q8SSH5; -.
DR   STRING; 284813.Q8SSH5; -.
DR   PRIDE; Q8SSH5; -.
DR   GeneID; 858565; -.
DR   KEGG; ecu:ECU02_0480; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_0480; -.
DR   HOGENOM; CLU_019837_0_0_1; -.
DR   InParanoid; Q8SSH5; -.
DR   OMA; INYYNIC; -.
DR   OrthoDB; 235012at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
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:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035266; PSMD1.
DR   PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome; Repeat.
FT   CHAIN           1..786
FT                   /note="26S proteasome regulatory subunit RPN2"
FT                   /id="PRO_0000382762"
FT   REPEAT          311..343
FT                   /note="PC 1"
FT   REPEAT          344..377
FT                   /note="PC 2"
FT   REPEAT          382..416
FT                   /note="PC 3"
FT   REPEAT          417..451
FT                   /note="PC 4"
FT   REPEAT          498..532
FT                   /note="PC 5"
FT   REPEAT          533..566
FT                   /note="PC 6"
FT   REPEAT          567..601
FT                   /note="PC 7"
SQ   SEQUENCE   786 AA;  87765 MW;  1124A7B0EECF9242 CRC64;
     MQTIRILPNI RALLRDGRES EAIDVINAHV DVVAPHIKDD LRYIKSSDPK TSLCLSKIYF
     VLEDYQQAIE YALRAGDLLV DDGSFYYTSI VYHMMDSADI GGDDRIRDFV LKVIGAEDVD
     DSLIGYLFSI KAYGLLKEAL VKYISDGNDC RRLLDLLISL GEEEGCLKEI YGMLAEIGPG
     KKPFIFYVID AYFYLEDVEK VKALIERLVK EDILLCYDVA FYTEDNYSPE IEVADQRVMS
     ILSGEFKKKI LGAFLLEKNL TSFKFLESIA RTRTHYLGLA NSLMNLGTSN DTLYRNNADI
     FGQSSEWAKF SEVASIGMIH LFNSNPYEIL KNYLPSEVSQ KEGGALMALG LIKAGTFSEE
     DTEYLLYFLD TEDTLTPELA YGVCLGLGLI NMGSANREIL NKLKELSKVD RTLLVEASVY
     GMGMLGLNSW SVELLEDLRT IAGETEFERV KRAVGISFSL VLMFSEEMFY DECNASNGDF
     KNYINELLYD KDSIMRANGV LSLGSAFVGT GRLGVISTLL PYINDGDDDV KRAAVIAIGL
     VCCDDRDLLV GTLEPLSENH NFFVRAAVAV VLGLFLSGTG DKVCTNILEA LMYDTNSLVR
     QSACIGVGFI TMQCNPELVP NYKRIIEKLN RLIVDKKESG AVELGAVLGR GLSEGGGRNI
     VFSVRNMSGI TSADRIAGAV LFLHYWYWHP LISMVSLCAL PTTVFCFNED LEEEEIEIPT
     SSRYNNLLIC LPDIKKARRF KQKPKEDKEI VIESPSVLTF GSRCTIKQRE ECGIDAPAIL
     FVKKKK