PSA7_ENCCU
ID PSA7_ENCCU Reviewed; 242 AA.
AC Q8SQP9;
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=Probable proteasome subunit alpha type-7;
DE AltName: Full=26S proteasome alpha-type subunit PRE10;
DE AltName: Full=Multicatalytic endopeptidase complex subunit PRE10;
GN Name=PRE10; OrderedLocusNames=ECU09_0330;
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: The proteasome degrades poly-ubiquitinated proteins in the
CC cytoplasm and in the nucleus. It is essential for the regulated
CC turnover of proteins and for the removal of misfolded proteins. The
CC proteasome is a multicatalytic proteinase complex that is characterized
CC by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC adjacent to the leaving group at neutral or slightly basic pH. It has
CC an ATP-dependent proteolytic activity (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 T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; AL590451; CAD27004.1; -; Genomic_DNA.
DR RefSeq; XP_955585.1; XM_950492.1.
DR AlphaFoldDB; Q8SQP9; -.
DR SMR; Q8SQP9; -.
DR STRING; 284813.Q8SQP9; -.
DR GeneID; 860369; -.
DR KEGG; ecu:ECU09_0330; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_0330; -.
DR HOGENOM; CLU_035750_0_0_1; -.
DR InParanoid; Q8SQP9; -.
DR OMA; NGQHCIN; -.
DR OrthoDB; 1222564at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR037555; Proteasome_alpha_3.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..242
FT /note="Probable proteasome subunit alpha type-7"
FT /id="PRO_0000382754"
SQ SEQUENCE 242 AA; 26999 MW; E61FDC0E5AC3050E CRC64;
MSNLDFCTIY TTTGQIDQLS YAQKAADSGD TCIGMKSKHG VVLLAEKPRV SPLYILESDE
KIRKIGNTIG VVCTGMSSDT FYVGCAIKDY VFHHKENFNE DPTPGMMKVY LNDIFHYFTR
GINLRVLGAN TLTSVYKDGS FSLLHTDCSG KTLSYKAACI GKGTRRIKTE LEKLDIDTMT
IEEMVDVGVK VLYMAHDPSK DKEFDIEIGI ASMETGGDLR KLENHEIRPL VGKYKHISVD
ED