PSA7_SOLLC
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 25-MAY-2022, entry version 114.
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}.
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; Y14339; CAA74725.1; -; mRNA.
DR PIR; T07744; T07744.
DR AlphaFoldDB; O24030; -.
DR SMR; O24030; -.
DR STRING; 4081.Solyc01g111450.2.1; -.
DR PaxDb; O24030; -.
DR PRIDE; O24030; -.
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:0005839; C:proteasome core complex; 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 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; 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