PSA5_RAT
ID PSA5_RAT Reviewed; 241 AA.
AC P34064;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Proteasome subunit alpha type-5;
DE AltName: Full=Macropain zeta chain;
DE AltName: Full=Multicatalytic endopeptidase complex zeta chain;
DE AltName: Full=Proteasome zeta chain;
GN Name=Psma5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1491007; DOI=10.1093/oxfordjournals.jbchem.a123933;
RA Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K.,
RA Ichihara A.;
RT "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures
RT of four other subunits.";
RL J. Biochem. 112:530-534(1992).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which
CC promotes 20S proteasome assembly. {ECO:0000250|UniProtKB:P28066}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D10756; BAA01588.1; -; mRNA.
DR PIR; JX0229; JX0229.
DR PDB; 6EPC; EM; 12.30 A; E=1-241.
DR PDB; 6EPD; EM; 15.40 A; E=1-241.
DR PDB; 6EPE; EM; 12.80 A; E=1-241.
DR PDB; 6EPF; EM; 11.80 A; E=1-241.
DR PDB; 6TU3; EM; 2.70 A; E/S=1-241.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P34064; -.
DR SMR; P34064; -.
DR BioGRID; 248293; 2.
DR IntAct; P34064; 1.
DR STRING; 10116.ENSRNOP00000026928; -.
DR MEROPS; T01.975; -.
DR GlyGen; P34064; 1 site.
DR iPTMnet; P34064; -.
DR PhosphoSitePlus; P34064; -.
DR jPOST; P34064; -.
DR PaxDb; P34064; -.
DR PRIDE; P34064; -.
DR UCSC; RGD:61848; rat.
DR RGD; 61848; Psma5.
DR eggNOG; KOG0176; Eukaryota.
DR InParanoid; P34064; -.
DR PhylomeDB; P34064; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641257; Degradation of AXIN.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P34064; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
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_0000124119"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2U1"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28066"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 HELIX 22..29
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 241 AA; 26391 MW; 97491D1974D1483D CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEG HKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSTT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I
