ID   PSA4_MACFA              Reviewed;         261 AA.
AC   Q4R932;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Proteasome subunit alpha type-4;
GN   Name=PSMA4; ORFNames=QtsA-10816;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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:P25789}.
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:P25789}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25789}. Nucleus
CC       {ECO:0000250|UniProtKB:P25789}. Note=Colocalizes with TRIM5 in the
CC       cytoplasmic bodies. {ECO:0000250|UniProtKB:Q9R1P0}.
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; AB168265; BAE00389.1; -; mRNA.
DR   RefSeq; NP_001270171.1; NM_001283242.1.
DR   AlphaFoldDB; Q4R932; -.
DR   SMR; Q4R932; -.
DR   STRING; 9541.XP_005560269.1; -.
DR   MEROPS; T01.973; -.
DR   GeneID; 101926424; -.
DR   CTD; 5685; -.
DR   eggNOG; KOG0178; Eukaryota.
DR   OrthoDB; 1222564at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
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; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034647; Proteasome_subunit_alpha4.
DR   PANTHER; PTHR11599:SF13; PTHR11599:SF13; 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   CHAIN           1..261
FT                   /note="Proteasome subunit alpha type-4"
FT                   /id="PRO_0000124104"
FT   REGION          240..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P25789"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P25789"
FT   MOD_RES         127
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P25789"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P25789"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P25789"
SQ   SEQUENCE   261 AA;  29511 MW;  430AE06230A05133 CRC64;
     MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
     FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
     YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPNGNYGGWK ATCIGNNSAA AVSMLKQDYK
     EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
     EEEEAKAERE KKEKEQKEKD K