RPN1_ENCCU
ID RPN1_ENCCU Reviewed; 795 AA.
AC Q8SS65;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=26S proteasome regulatory subunit RPN1;
GN Name=RPN1; OrderedLocusNames=ECU04_0310;
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 S2 family. {ECO:0000305}.
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DR EMBL; AL590444; CAD25218.1; -; Genomic_DNA.
DR RefSeq; NP_584714.1; NM_001041064.1.
DR AlphaFoldDB; Q8SS65; -.
DR STRING; 284813.Q8SS65; -.
DR GeneID; 858862; -.
DR KEGG; ecu:ECU04_0310; -.
DR VEuPathDB; MicrosporidiaDB:ECU04_0310; -.
DR HOGENOM; CLU_019273_0_0_1; -.
DR InParanoid; Q8SS65; -.
DR OMA; MAPPENP; -.
DR OrthoDB; 229956at2759; -.
DR Proteomes; UP000000819; Chromosome IV.
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; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..795
FT /note="26S proteasome regulatory subunit RPN1"
FT /id="PRO_0000382763"
FT REPEAT 374..410
FT /note="PC 1"
FT REPEAT 411..445
FT /note="PC 2"
FT REPEAT 447..480
FT /note="PC 3"
FT REPEAT 624..658
FT /note="PC 4"
SQ SEQUENCE 795 AA; 89127 MW; 6654367B915F8516 CRC64;
MEEGELKIIV ERIQDPDIDI QNNALNMLFD VTKSSHSKSI DTINFQYLAD NLDVLEDVCK
RLEGNKKRWL CDIISAICVV DDERKLLAYR VEGNIIDLKE WGHLYVKKLI GCIADVKNNK
MDFPFAKTRD VGRECIDFLF KHNAEFEAID FLVEVGGIET VLDYVDTHNY NRIVLYLEDM
NSFVDLEEVI LKIYLKMGDH SRYVVGLIRR QKSKEAIEYV RSIEDRDYKK QCLYILARCN
LYYEASDPEE KYILSNGYIK DVYREIGAEL EIDKPSKMDA ILKGFKYDKD TRQLASIGIA
NGFVHMGYGR DPIFLPQEGD SRVPLDYEAI LGCDVPDLIS VFGSIGVIES WNSEKVMETL
QEHIFADFSY RKTGSLLGLA LSGLRNFEER PAILALLSNN LQSSSSIHVI ATLLGIEAMF
SGTQAEEVRE LLQPLMFSDS SEVVFFTSFT LGSVFCGSAD EDLTSLMLQT FVEKGKESET
QFFRFLMLGL ASLFYRRKDV ECGIMEIGGA LSKHESILIK GFQYVGTGDS NVIESILTDS
FTGDTDALLE SLGLLSCALV SMGDETSSQM VGRIVSSSLL LDSSHLRSVL PLCYSILYPS
NPQVNVLDML EKSLNIGETN CIISTIVSLG LIGAGTLNSR ITKILDQQYS YYYKDSKVLP
VLKIAQGLVS LGKGLLSISP LYFDKTTFMP KNTIGLFSTV FMLLDSSISP LVSSHAYMFF
LLCQACTQKY VTCSEKINIR VGHPINTVGM VGEPKKLSSV QTHTSPVVLS EKIRAETDEN
VCSSYIEDVL ILKKN