PSA6_BOVIN
ID PSA6_BOVIN Reviewed; 246 AA.
AC Q2YDE4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Proteasome subunit alpha type-6;
GN Name=PSMA6;
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=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-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). {ECO:0000250|UniProtKB:P60900}.
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). Interacts with ALKBH4 (By similarity).
CC {ECO:0000250|UniProtKB:P60900, ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P60900,
CC ECO:0000250|UniProtKB:Q9QUM9}. Nucleus {ECO:0000250|UniProtKB:P60900}.
CC Note=Translocated from the cytoplasm into the nucleus following
CC interaction with AKIRIN2, which bridges the proteasome with the nuclear
CC import receptor IPO9 (By similarity). Colocalizes with TRIM5 in
CC cytoplasmic bodies (By similarity). {ECO:0000250|UniProtKB:P60900,
CC ECO:0000250|UniProtKB:Q9QUM9}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BC110260; AAI10261.1; -; mRNA.
DR RefSeq; NP_001039427.1; NM_001045962.1.
DR PDB; 1IRU; X-ray; 2.75 A; A/O=1-246.
DR PDB; 7DR6; EM; 4.10 A; L/e=1-246.
DR PDB; 7DR7; EM; 3.30 A; E/L=1-246.
DR PDB; 7DRW; EM; 4.20 A; A/f=1-246.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q2YDE4; -.
DR SMR; Q2YDE4; -.
DR STRING; 9913.ENSBTAP00000012773; -.
DR MEROPS; T01.971; -.
DR PaxDb; Q2YDE4; -.
DR PeptideAtlas; Q2YDE4; -.
DR PRIDE; Q2YDE4; -.
DR Ensembl; ENSBTAT00000012773; ENSBTAP00000012773; ENSBTAG00000009683.
DR GeneID; 507213; -.
DR KEGG; bta:507213; -.
DR CTD; 5687; -.
DR VEuPathDB; HostDB:ENSBTAG00000009683; -.
DR VGNC; VGNC:33441; PSMA6.
DR eggNOG; KOG0182; Eukaryota.
DR GeneTree; ENSGT00550000074807; -.
DR HOGENOM; CLU_035750_4_1_1; -.
DR InParanoid; Q2YDE4; -.
DR OMA; YGYDMPV; -.
DR OrthoDB; 1222564at2759; -.
DR EvolutionaryTrace; Q2YDE4; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000009683; Expressed in semen and 103 other tissues.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
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:0005844; C:polysome; IEA:Ensembl.
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:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
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 CDD; cd03754; proteasome_alpha_type_6; 1.
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; IPR034642; Proteasome_subunit_alpha6.
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..246
FT /note="Proteasome subunit alpha type-6"
FT /id="PRO_0000274034"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60900"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60900"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60900"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60900"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60900"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUM9"
FT CARBOHYD 5
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT TURN 8..12
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64;
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
ALAERD
