ID   PSA7_SOLLC              Reviewed;         259 AA.
AC   O24030;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Proteasome subunit alpha type-7;
DE   AltName: Full=20S proteasome alpha subunit D;
DE   AltName: Full=20S proteasome subunit alpha-4;
GN   Name=PAD1; Synonyms=PSR5;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lukullus;
RA   Ziethe K., Stenzel I., Hertel S.C., Koeck M.;
RT   "Cloning and characterization of PSR5, a tomato cDNA encoding a 20S subunit
RT   from the proteasome repressed by phosphate starvation.";
RL   (er) Plant Gene Register PGR98-065(1998).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; Y14339; CAA74725.1; -; mRNA.
DR   PIR; T07744; T07744.
DR   AlphaFoldDB; O24030; -.
DR   SMR; O24030; -.
DR   STRING; 4081.O24030; -.
DR   PaxDb; 4081-Solyc01g111450-2-1; -.
DR   eggNOG; KOG0183; Eukaryota.
DR   InParanoid; O24030; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; O24030; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03755; proteasome_alpha_type_7; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   PANTHER; PTHR11599:SF249; PROTEASOME SUBUNIT ALPHA TYPE-7-A-RELATED; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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; Reference proteome.
FT   CHAIN           1..259
FT                   /note="Proteasome subunit alpha type-7"
FT                   /id="PRO_0000124162"
SQ   SEQUENCE   259 AA;  28480 MW;  700B3638C9F0FB52 CRC64;
     MARYDRAITV FSPDGHLFQV EYAMEAVRKG NAAVGVRGTD TVVLGVEKKS TPKLQDSRSV
     RKIVNLDDHI ALACAGLKAD ARVLVNKARI ECQSHRLTVE DPVTVEYITR YIAGLQQKYT
     QSGGVRPFGL STLIIGFDPH TGVPSLYQTD PSGTFSAWKA NATGRNSNST REFLEKNYKE
     TSGQETVKLA IRALLEVVES GGKNIEVAVM TKEHGLKQLE EAEIDAIVAE IEAEKAAAEA
     AKRPHRRNLV ELKFVLNYP
//