ID   PSA7_CARAU              Reviewed;         251 AA.
AC   Q9PTW9;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Proteasome subunit alpha type-7;
DE   AltName: Full=Proteasome subunit alpha 4;
GN   Name=psma7;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10601855; DOI=10.1046/j.1432-1327.2000.00962.x;
RA   Tokumoto M., Horiguchi R., Nagahama Y., Ishikawa K., Tokumoto T.;
RT   "Two proteins, a goldfish 20S proteasome subunit and the protein
RT   interacting with 26S proteasome, change in the meiotic cell cycle.";
RL   Eur. J. Biochem. 267:97-103(2000).
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; AB027707; BAA89276.1; -; mRNA.
DR   AlphaFoldDB; Q9PTW9; -.
DR   SMR; Q9PTW9; -.
DR   MEROPS; T01.974; -.
DR   Ensembl; ENSCART00000014844; ENSCARP00000014062; ENSCARG00000006496.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
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; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Proteasome subunit alpha type-7"
FT                   /id="PRO_0000124146"
SQ   SEQUENCE   251 AA;  28084 MW;  2272608595D32B58 CRC64;
     MAARYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGK DIVVLGVEKK SVAKLQEERT
     VRKICALDEH VCMAFAGLTA DARIVINRAR VECQSHRLTV EDPVTVEYIT RYIATLKQRY
     TQSNGRRPFG ISALIVGFDF DGTPRLYQTD PSGTYHAWKA NAIGRSAKTV REFLEKNYTD
     EAIASDNDAI KLAIKALLEV VQSGGKNIEL AVIRRNQPLK ILESKEIETL VAEIEKEKEE
     EAEKKKQKKS S