ID   PSA7L_MACFA             Reviewed;         250 AA.
AC   Q4R7D9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Proteasome subunit alpha type-7-like;
GN   Name=PSMA7L; ORFNames=QtsA-15547;
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). Inhibits the transactivation function of HIF-1A
CC       under both normoxic and hypoxia-mimicking conditions. The interaction
CC       with EMAP2 increases the proteasome-mediated HIF-1A degradation under
CC       the hypoxic conditions. Plays a role in hepatitis C virus internal
CC       ribosome entry site-mediated translation. Mediates nuclear
CC       translocation of the androgen receptor (AR) and thereby enhances
CC       androgen-mediated transactivation. Promotes MAVS degradation and
CC       thereby negatively regulates MAVS-mediated innate immune response.
CC       {ECO:0000250|UniProtKB:O14818}.
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       PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which
CC       promotes 20S proteasome assembly. Interacts with HIF1A. Interacts with
CC       RAB7A. Interacts with PRKN. Interacts with ABL1 and ABL2. Interacts
CC       with EMAP2. Interacts with MAVS. {ECO:0000250|UniProtKB:O14818}.
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; AB168880; BAE00983.1; -; mRNA.
DR   RefSeq; NP_001270892.1; NM_001283963.1.
DR   AlphaFoldDB; Q4R7D9; -.
DR   SMR; Q4R7D9; -.
DR   STRING; 9541.ENSMFAP00000046072; -.
DR   GlyCosmos; Q4R7D9; 1 site, No reported glycans.
DR   eggNOG; KOG0183; Eukaryota.
DR   OrthoDB; 166567at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03755; proteasome_alpha_type_7; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   PANTHER; PTHR11599:SF144; PROTEASOME SUBUNIT ALPHA-TYPE 8; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycoprotein; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..250
FT                   /note="Proteasome subunit alpha type-7-like"
FT                   /id="PRO_0000276764"
FT   CARBOHYD        132
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  27880 MW;  4AD0F26D3C9EA236 CRC64;
     MASRYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGT NIVVLGVEKK SVAKLQDERT
     VRKICALDDH VCMAFAGLTA DARVVINRAR VECQSHKLTV EDPVTVEYIT RFIATLKQKY
     TQSNGRRPFG ISALIVGFDD DGIPRLYQTD PSGTYHAWKA NAIGRSAKTV REFLEKNYTE
     DAIASDNEAI KLAIKALLEV VQSGGKNIEL AIIRRNQPLK MFSAKEVELY VTEIEKEKEE
     AEKKKSKKSV
//