PSA3_BOVIN
ID PSA3_BOVIN Reviewed; 255 AA.
AC Q58DU5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Proteasome subunit alpha type-3;
GN Name=PSMA3;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
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 [3]
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). Binds to the C-terminus of CDKN1A and thereby
CC mediates its degradation. Negatively regulates the membrane trafficking
CC of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
CC {ECO:0000250|UniProtKB:P25788}.
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 AURKB (By similarity). Interacts with
CC CDKN1A (By similarity). Interacts with MDM2 and RB1 (By similarity).
CC Interacts with the C-terminus of TBXA2R isoform 2 (By similarity).
CC Interacts with DNAJB2 (By similarity). {ECO:0000250|UniProtKB:P25788,
CC ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus
CC {ECO:0000250|UniProtKB:P25788}. 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:P25788}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BT021502; AAX46349.1; -; mRNA.
DR EMBL; BC109554; AAI09555.1; -; mRNA.
DR RefSeq; NP_001029407.1; NM_001034235.1.
DR PDB; 1IRU; X-ray; 2.75 A; G/U=2-255.
DR PDB; 7DR6; EM; 4.10 A; R/d=1-255.
DR PDB; 7DR7; EM; 3.30 A; D/R=1-255.
DR PDB; 7DRW; EM; 4.20 A; G/d=1-255.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q58DU5; -.
DR SMR; Q58DU5; -.
DR IntAct; Q58DU5; 1.
DR STRING; 9913.ENSBTAP00000003636; -.
DR PaxDb; Q58DU5; -.
DR PRIDE; Q58DU5; -.
DR Ensembl; ENSBTAT00000003636; ENSBTAP00000003636; ENSBTAG00000002808.
DR GeneID; 505176; -.
DR KEGG; bta:505176; -.
DR CTD; 5684; -.
DR VEuPathDB; HostDB:ENSBTAG00000002808; -.
DR VGNC; VGNC:33438; PSMA3.
DR eggNOG; KOG0184; Eukaryota.
DR GeneTree; ENSGT00550000074912; -.
DR HOGENOM; CLU_035750_0_0_1; -.
DR InParanoid; Q58DU5; -.
DR OMA; SMYMHAY; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106208; -.
DR EvolutionaryTrace; Q58DU5; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000002808; Expressed in oocyte and 107 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:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0052548; P:regulation of endopeptidase activity; 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; IPR037555; Proteasome_alpha_3.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PTHR11599:SF10; 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:P25788"
FT CHAIN 2..255
FT /note="Proteasome subunit alpha type-3"
FT /id="PRO_0000240275"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 255 AA; 28405 MW; F078CC44D597EFA7 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDV VKEVAKIIYI VHDEVKDKAF ELELSWVGEI TNGRHEIVPK DVREEAEKYA
KESLKEEDES DDDNM
