PSA1_BOVIN
ID PSA1_BOVIN Reviewed; 263 AA.
AC Q3T0X5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Proteasome subunit alpha type-1;
GN Name=PSMA1;
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:P25786}.
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 NOTCH3 (By similarity). Interacts
CC with ZFAND1 (By similarity). {ECO:0000250|UniProtKB:P25786,
CC ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus
CC {ECO:0000250|UniProtKB:P25786}. 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:P25786}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BC102216; AAI02217.1; -; mRNA.
DR RefSeq; NP_001030387.1; NM_001035310.2.
DR PDB; 1IRU; X-ray; 2.75 A; F/T=1-263.
DR PDB; 7DR6; EM; 4.10 A; Q/c=1-263.
DR PDB; 7DR7; EM; 3.30 A; C/Q=1-263.
DR PDB; 7DRW; EM; 4.20 A; F/b=1-263.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3T0X5; -.
DR SMR; Q3T0X5; -.
DR STRING; 9913.ENSBTAP00000008621; -.
DR MEROPS; T01.976; -.
DR PaxDb; Q3T0X5; -.
DR PeptideAtlas; Q3T0X5; -.
DR PRIDE; Q3T0X5; -.
DR Ensembl; ENSBTAT00000008621; ENSBTAP00000008621; ENSBTAG00000006564.
DR GeneID; 515503; -.
DR KEGG; bta:515503; -.
DR CTD; 5682; -.
DR VEuPathDB; HostDB:ENSBTAG00000006564; -.
DR VGNC; VGNC:97304; PSMA1.
DR eggNOG; KOG0863; Eukaryota.
DR GeneTree; ENSGT00550000074855; -.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; Q3T0X5; -.
DR OMA; NTQVYGK; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106206; -.
DR EvolutionaryTrace; Q3T0X5; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000006564; Expressed in semen and 105 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; 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; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PTHR11599:SF12; 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; Immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..263
FT /note="Proteasome subunit alpha type-1"
FT /id="PRO_0000274031"
FT REGION 232..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18420"
FT MOD_RES 110
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 78..99
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 263 AA; 29586 MW; 24142C5BCEFE8DED CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP
QRKAQPTQPA DEPAEKADEP MEH
