PSA7_BOVIN
ID PSA7_BOVIN Reviewed; 248 AA.
AC Q3ZBG0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Proteasome subunit alpha type-7;
GN Name=PSMA7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
RX PubMed=12015144; DOI=10.1016/s0969-2126(02)00748-7;
RA Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N.,
RA Tsukihara T.;
RT "The structure of the mammalian 20S proteasome at 2.75 A resolution.";
RL Structure 10:609-618(2002).
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 (PubMed:12015144). PSMA7 interacts directly with the PSMG1-PSMG2
CC heterodimer which promotes 20S proteasome assembly (By similarity).
CC Interacts with HIF1A (By similarity). Interacts with RAB7A (By
CC similarity). Interacts with PRKN (By similarity). Interacts with ABL1
CC and ABL2 (By similarity). Interacts with EMAP2 (By similarity).
CC Interacts with MAVS (By similarity). {ECO:0000250|UniProtKB:O14818,
CC ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14818}. Nucleus
CC {ECO:0000250|UniProtKB:O14818}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:O14818}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BC103328; AAI03329.1; -; mRNA.
DR RefSeq; NP_001029405.1; NM_001034233.2.
DR PDB; 1IRU; X-ray; 2.75 A; D/R=1-248.
DR PDB; 7DR6; EM; 4.10 A; O/a=1-248.
DR PDB; 7DR7; EM; 3.30 A; A/O=1-248.
DR PDB; 7DRW; EM; 4.20 A; D/P=1-248.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3ZBG0; -.
DR SMR; Q3ZBG0; -.
DR STRING; 9913.ENSBTAP00000006760; -.
DR PaxDb; Q3ZBG0; -.
DR PeptideAtlas; Q3ZBG0; -.
DR PRIDE; Q3ZBG0; -.
DR Ensembl; ENSBTAT00000006760; ENSBTAP00000006760; ENSBTAG00000005127.
DR GeneID; 505050; -.
DR KEGG; bta:505050; -.
DR CTD; 5688; -.
DR VEuPathDB; HostDB:ENSBTAG00000005127; -.
DR VGNC; VGNC:33442; PSMA7.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000159695; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; Q3ZBG0; -.
DR OMA; KICMLDH; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106212; -.
DR EvolutionaryTrace; Q3ZBG0; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000005127; Expressed in oocyte and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
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; IPR035190; Proteasome_alpha7.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF40; PTHR11599:SF40; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Glycoprotein; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..248
FT /note="Proteasome subunit alpha type-7"
FT /id="PRO_0000274035"
FT MOD_RES 153
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT CARBOHYD 130
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 229..240
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 248 AA; 27869 MW; E38C9307D8E30D2C CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQPLKIL NPEEIEKYVA EIEKEKEENE
KKKQKKAS
