ID   PSA2_XENLA              Reviewed;         234 AA.
AC   P24495; Q6INM4;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Proteasome subunit alpha type-2;
DE   AltName: Full=Macropain subunit C3;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE            Short=xC3;
DE   AltName: Full=Proteasome component C3;
GN   Name=psma2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1872843; DOI=10.1016/0006-291x(91)91025-8;
RA   Fujii G., Tashiro K., Emori Y., Saigo K., Tanaka K., Shiokawa K.;
RT   "Deduced primary structure of a Xenopus proteasome subunit XC3 and
RT   expression of its mRNA during early development.";
RL   Biochem. Biophys. Res. Commun. 178:1233-1239(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC       proteolytic degradation of most intracellular proteins. This complex
CC       plays numerous essential roles within the cell by associating with
CC       different regulatory particles. Associated with two 19S regulatory
CC       particles, forms the 26S proteasome and thus participates in the ATP-
CC       dependent degradation of ubiquitinated proteins. The 26S proteasome
CC       plays a key role in the maintenance of protein homeostasis by removing
CC       misfolded or damaged proteins that could impair cellular functions, and
CC       by removing proteins whose functions are no longer required. Associated
CC       with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC       independent protein degradation. This type of proteolysis is required
CC       in several pathways including spermatogenesis (20S-PA200 complex) or
CC       generation of a subset of MHC class I-presented antigenic peptides
CC       (20S-PA28 complex). {ECO:0000250|UniProtKB:P25787}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       {ECO:0000250|UniProtKB:P25787}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25787}. Nucleus
CC       {ECO:0000250|UniProtKB:P25787}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; S51111; AAB19485.1; -; mRNA.
DR   EMBL; BC072254; AAH72254.1; -; mRNA.
DR   PIR; JH0421; JH0421.
DR   RefSeq; NP_001084053.1; NM_001090584.1.
DR   RefSeq; XP_018124841.1; XM_018269352.1.
DR   AlphaFoldDB; P24495; -.
DR   SMR; P24495; -.
DR   BioGRID; 100604; 1.
DR   MEROPS; T01.972; -.
DR   MaxQB; P24495; -.
DR   DNASU; 399279; -.
DR   GeneID; 108720001; -.
DR   GeneID; 399279; -.
DR   KEGG; xla:108720001; -.
DR   KEGG; xla:399279; -.
DR   CTD; 108720001; -.
DR   CTD; 399279; -.
DR   Xenbase; XB-GENE-964716; psma2.L.
DR   Xenbase; XB-GENE-17337233; psma2.S.
DR   OrthoDB; 1222564at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 108720001; Expressed in muscle tissue and 19 other tissues.
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_0000124080"
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;  25834 MW;  DAD6E27698410FA2 CRC64;
     MAERGYSFSL TTFSPSGKLV QIEYALAAVA AGAPSVGIKA TNGVVLATEK KQKSILYDEQ
     SAHKVEPITK HIGMVYSGMG PDYRVLVRRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
     YTQSGGVRPF GVSLLIAGWD EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
     DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFKR LTPAEVKDYL AAIA