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 24-JAN-2024, entry version 157. 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 EMDB; EMD-10586; -. DR EMDB; EMD-3913; -. DR EMDB; EMD-3914; -. DR EMDB; EMD-3915; -. DR EMDB; EMD-3916; -. DR SMR; P34064; -. DR BioGRID; 248293; 2. DR IntAct; P34064; 1. DR STRING; 10116.ENSRNOP00000026928; -. DR MEROPS; T01.975; -. DR GlyCosmos; P34064; 1 site, No reported glycans. DR GlyGen; P34064; 1 site. DR iPTMnet; P34064; -. DR PhosphoSitePlus; P34064; -. DR SwissPalm; P34064; -. DR jPOST; P34064; -. DR PaxDb; 10116-ENSRNOP00000026928; -. DR UCSC; RGD:61848; rat. DR AGR; RGD:61848; -. 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-174113; SCF-beta-TrCP mediated degradation of Emi1. 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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 PANTHER; PTHR11599:SF14; PROTEASOME SUBUNIT ALPHA TYPE-5; 1. DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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 //