ID   PSA2_CARAU              Reviewed;         234 AA.
AC   O73672;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Proteasome subunit alpha type-2;
GN   Name=psma2;
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].
RC   TISSUE=Ovary;
RA   Horiguchi R., Tokumoto M., Tokumoto T.;
RT   "Goldfish proteasome subunit alpha 2.";
RL   Submitted (APR-1998) 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. PSMA2 may
CC       have a potential regulatory effect on another component(s) of the
CC       proteasome complex through tyrosine phosphorylation (By similarity).
CC       {ECO:0000250}.
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; AB013342; BAA25915.1; -; mRNA.
DR   AlphaFoldDB; O73672; -.
DR   SMR; O73672; -.
DR   MEROPS; T01.972; -.
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   InterPro; IPR034644; Proteasome_subunit_alpha2.
DR   PANTHER; PTHR11599:SF16; PTHR11599:SF16; 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   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..234
FT                   /note="Proteasome subunit alpha type-2"
FT                   /id="PRO_0000124081"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         121
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  25878 MW;  3B690B11D7DD98F9 CRC64;
     MADRGYSFSL TTFSPSGKLV QIEYALAAVA AGAPSVGIKA SNGVVLATEK KQKSILYDEQ
     SVHKIEPITK HIGMVYSGMG PDYRVLVRRA RKLAQQYFLV YQEPIPTGQL VQRVASVMQE
     YTQSGGVRPF GVSLLIAGWD EDRPYLFQSD PSGAYFAWKA TAMGKSYVNG KTFLEKRYNE
     DLELEDAIHT AILTLKESFE GQMTEENIEV GICNEAGFRR LSPAEVKDYL AAIA