ID   PSA3_SPIOL              Reviewed;         249 AA.
AC   O24362;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Proteasome subunit alpha type-3;
DE   AltName: Full=20S proteasome alpha subunit G;
DE   AltName: Full=20S proteasome subunit alpha-7;
DE   AltName: Full=Proteasome component C8;
GN   Name=PAG1; Synonyms=PSC8;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9207846; DOI=10.1023/a:1005839501822;
RA   Ito N., Tomizawa K., Tanaka K., Matsui M., Kendrick R.E., Sato T.,
RA   Nakagawa H.;
RT   "Characterization of 26S proteasome alpha- and beta-type and ATPase
RT   subunits from spinach and their expression during early stages of seedling
RT   development.";
RL   Plant Mol. Biol. 34:307-316(1997).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D78173; BAA21651.1; -; mRNA.
DR   PIR; T09139; T09139.
DR   AlphaFoldDB; O24362; -.
DR   SMR; O24362; -.
DR   OrthoDB; 1222564at2759; -.
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:0006511; P:ubiquitin-dependent 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; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..249
FT                   /note="Proteasome subunit alpha type-3"
FT                   /id="PRO_0000124100"
SQ   SEQUENCE   249 AA;  27285 MW;  8B7DB2B4D74FB3FA CRC64;
     MSSIGTGYDL SVTTFSPDGR VFQIEYAAKA VDNSGTAVGI KCKDGIVLGV EKLIQSKMML
     PGSNRRIHSV HRHSGMAVAG LAADGRQIVA RAKSEATNYE SVYGEAVPVK ELADRVASYV
     HLCTLYWWLR PFGCGVILGG YDRDGPQLYM VEPSGISYRY FGAAIGKGKQ AAKTEIEKLK
     LSEMTCREGI IEVAKIIYKV HDEAKDKAFE LEMSWICDES KREHQKVPDN LLQEAKAAAT
     AALEEMDAD