PSA5_BOVIN
ID PSA5_BOVIN Reviewed; 241 AA.
AC Q5E987;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Proteasome subunit alpha type-5;
GN Name=PSMA5;
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=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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). {ECO:0000250|UniProtKB:P28066}.
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). PSMA5 interacts directly with the PSMG1-PSMG2
CC heterodimer which promotes 20S proteasome assembly (By similarity).
CC {ECO:0000250|UniProtKB:P28066, ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28066}. Nucleus
CC {ECO:0000250|UniProtKB:P28066}. 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:P28066}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; BT021033; AAX09050.1; -; mRNA.
DR EMBL; BC102343; AAI02344.1; -; mRNA.
DR RefSeq; NP_001015566.1; NM_001015566.1.
DR PDB; 1IRU; X-ray; 2.75 A; E/S=1-241.
DR PDB; 7DR6; EM; 4.10 A; P/b=1-241.
DR PDB; 7DR7; EM; 3.30 A; B/P=1-241.
DR PDB; 7DRW; EM; 4.20 A; E/R=1-241.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q5E987; -.
DR SMR; Q5E987; -.
DR STRING; 9913.ENSBTAP00000027507; -.
DR MEROPS; T01.975; -.
DR PaxDb; Q5E987; -.
DR PeptideAtlas; Q5E987; -.
DR PRIDE; Q5E987; -.
DR Ensembl; ENSBTAT00000027507; ENSBTAP00000027507; ENSBTAG00000020641.
DR GeneID; 510155; -.
DR KEGG; bta:510155; -.
DR CTD; 5686; -.
DR VEuPathDB; HostDB:ENSBTAG00000020641; -.
DR VGNC; VGNC:33440; PSMA5.
DR eggNOG; KOG0176; Eukaryota.
DR GeneTree; ENSGT00550000074958; -.
DR HOGENOM; CLU_035750_4_2_1; -.
DR InParanoid; Q5E987; -.
DR OMA; FQVEYAR; -.
DR OrthoDB; 1222564at2759; -.
DR TreeFam; TF106211; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; Q5E987; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000020641; Expressed in oocyte and 107 other tissues.
DR GO; GO:0005829; C:cytosol; 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03753; proteasome_alpha_type_5; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
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..241
FT /note="Proteasome subunit alpha type-5"
FT /id="PRO_0000274033"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2U1"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28066"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28066"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28066"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28066"
FT CARBOHYD 198
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 66..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..117
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 241 AA; 26411 MW; 5610CDA00469120A CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I
