ID   PSA3_ACACA              Reviewed;         252 AA.
AC   P90513;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Proteasome subunit alpha type-3;
DE   Flags: Fragment;
OS   Acanthamoeba castellanii (Amoeba).
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=5755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xu P., Zot H.G.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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; U85398; AAB41645.1; -; mRNA.
DR   AlphaFoldDB; P90513; -.
DR   SMR; P90513; -.
DR   PRIDE; P90513; -.
DR   VEuPathDB; AmoebaDB:ACA1_072980; -.
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:0008233; F:peptidase activity; IEA:UniProt.
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; IPR037555; Proteasome_alpha_3.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
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..252
FT                   /note="Proteasome subunit alpha type-3"
FT                   /id="PRO_0000124094"
FT   NON_TER         1
SQ   SEQUENCE   252 AA;  27728 MW;  71898276B50C2E79 CRC64;
     SIGTGYDLSS TTFSPDGRVF QVEYAAKAVD NSGTALGLRV KDGVVLAVEK LLVSKMLVPN
     TNRRIHTVDR HCGLAMSGLV ADGRQLVSRG RAEATSYREF YGTDISGKVL NERLSNFVQL
     YSLYGSVRPF GTSVILGCVD KNGPQLYMIE PSGISWGYFG VAIGKGARAA KTEIEKLKLS
     EMTAREAIKE AAKIIYSVHD DAKDKAFELE LSWVCEETGN LHKFVPKDLL EEAEKYAKQA
     LEEEEDMSEE ED