PSA4_BOVIN
ID PSA4_BOVIN Reviewed; 261 AA.
AC Q3ZCK9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Proteasome subunit alpha type-4;
GN Name=PSMA4;
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 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). {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 (PubMed:12015144). {ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25789}. Nucleus
CC {ECO:0000250|UniProtKB:P25789}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9 (By similarity).
CC Colocalizes with TRIM5 in the cytoplasmic bodies (By similarity).
CC {ECO:0000250|UniProtKB:P25789, ECO:0000250|UniProtKB:Q9R1P0}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BC102102; AAI02103.1; -; mRNA.
DR RefSeq; NP_001029553.1; NM_001034381.2.
DR PDB; 1IRU; X-ray; 2.75 A; C/Q=1-261.
DR PDB; 7DR6; EM; 4.10 A; N/g=1-261.
DR PDB; 7DR7; EM; 3.30 A; G/N=1-261.
DR PDB; 7DRW; EM; 4.20 A; C/j=1-261.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3ZCK9; -.
DR SMR; Q3ZCK9; -.
DR STRING; 9913.ENSBTAP00000019203; -.
DR MEROPS; T01.973; -.
DR PaxDb; Q3ZCK9; -.
DR PRIDE; Q3ZCK9; -.
DR Ensembl; ENSBTAT00000019203; ENSBTAP00000019203; ENSBTAG00000014440.
DR GeneID; 510423; -.
DR KEGG; bta:510423; -.
DR CTD; 5685; -.
DR VEuPathDB; HostDB:ENSBTAG00000014440; -.
DR VGNC; VGNC:33439; PSMA4.
DR eggNOG; KOG0178; Eukaryota.
DR GeneTree; ENSGT00550000074827; -.
DR HOGENOM; CLU_035750_4_3_1; -.
DR InParanoid; Q3ZCK9; -.
DR OMA; YVLNDNM; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106209; -.
DR EvolutionaryTrace; Q3ZCK9; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000014440; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT CHAIN 1..261
FT /note="Proteasome subunit alpha type-4"
FT /id="PRO_0000274032"
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"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 80..101
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 261 AA; 29484 MW; 7867422B1B31F3B9 CRC64;
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK
EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
EEEEAKAERE KKEKEQKEKD K
