PSA2_BOVIN
ID PSA2_BOVIN Reviewed; 234 AA.
AC Q3T0Y5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Proteasome subunit alpha type-2;
GN Name=PSMA2;
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). {ECO:0000250|UniProtKB:P25787}.
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:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25787}. Nucleus
CC {ECO:0000250|UniProtKB:P25787}. 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 cytoplasmic bodies (By similarity).
CC {ECO:0000250|UniProtKB:P25787, ECO:0000250|UniProtKB:P49722}.
CC -!- PTM: Phosphorylated on tyrosine residues; which may be important for
CC nuclear import. {ECO:0000250|UniProtKB:P17220}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BC102206; AAI02207.1; -; mRNA.
DR RefSeq; NP_001029834.1; NM_001034662.2.
DR PDB; 1IRU; X-ray; 2.75 A; B/P=2-234.
DR PDB; 7DR6; EM; 4.10 A; M/f=1-234.
DR PDB; 7DR7; EM; 3.30 A; F/M=1-234.
DR PDB; 7DRW; EM; 4.20 A; B/h=1-234.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3T0Y5; -.
DR SMR; Q3T0Y5; -.
DR BioGRID; 195708; 3.
DR STRING; 9913.ENSBTAP00000001309; -.
DR MEROPS; T01.972; -.
DR PaxDb; Q3T0Y5; -.
DR PeptideAtlas; Q3T0Y5; -.
DR PRIDE; Q3T0Y5; -.
DR Ensembl; ENSBTAT00000001309; ENSBTAP00000001309; ENSBTAG00000000990.
DR GeneID; 539141; -.
DR KEGG; bta:539141; -.
DR CTD; 5683; -.
DR VEuPathDB; HostDB:ENSBTAG00000000990; -.
DR VGNC; VGNC:55751; PSMA2.
DR eggNOG; KOG0181; Eukaryota.
DR GeneTree; ENSGT00550000074870; -.
DR HOGENOM; CLU_035750_4_1_1; -.
DR InParanoid; Q3T0Y5; -.
DR OMA; YQEQIPT; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106207; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; Q3T0Y5; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000000990; Expressed in tongue muscle and 104 other tissues.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
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; IPR001353; Proteasome_sua/b.
DR InterPro; IPR034644; Proteasome_subunit_alpha2.
DR PANTHER; PTHR11599:SF16; PTHR11599:SF16; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT CHAIN 2..234
FT /note="Proteasome subunit alpha type-2"
FT /id="PRO_0000239865"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49722"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 121
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17220"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 64..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 131..139
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 234 AA; 25899 MW; 63CB56A233583836 CRC64;
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA
