ID PSB6_YEAST Reviewed; 215 AA. AC P38624; D6VWH4; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 05-SEP-2012, entry version 126. DE RecName: Full=Proteasome component PRE3; DE EC=3.4.25.1; DE AltName: Full=Macropain subunit PRE3; DE AltName: Full=Multicatalytic endopeptidase complex subunit PRE3; DE AltName: Full=Proteinase YSCE subunit PRE3; DE Flags: Precursor; GN Name=PRE3; OrderedLocusNames=YJL001W; ORFNames=J1407; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=94185793; PubMed=7907993; DOI=10.1016/0014-5793(94)80455-9; RA Enenkel C., Lehmann H., Kipper J., Gueckel R., Hilt W., Wolf D.H.; RT "PRE3, highly homologous to the human major histocompatibility RT complex-linked LMP2 (RING12) gene, codes for a yeast proteasome RT subunit necessary for the peptidylglutamyl-peptide hydrolyzing RT activity."; RL FEBS Lett. 341:193-196(1994). RN [2] RP SEQUENCE REVISION TO N-TERMINUS. RX MEDLINE=95300795; PubMed=7781614; RA Chen P., Hochstrasser M.; RT "Biogenesis, structure and function of the yeast 20S proteasome."; RL EMBO J. 14:2620-2630(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=96208490; PubMed=8641269; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., RA Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT X."; RL EMBO J. 15:2031-2049(1996). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, AND MASS RP SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215 OF COMPLEX WITH THE RP 20S PROTEASOME, PROTEOLYTIC PROCESSING, AND ACTIVE SITE. RX MEDLINE=97242404; PubMed=9087403; DOI=10.1038/386463a0; RA Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., RA Huber R.; RT "Structure of 20S proteasome from yeast at 2.4-A resolution."; RL Nature 386:463-471(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE RP 20S PROTEASOME AND A 11S REGULATORY COMPLEX. RX PubMed=11081519; DOI=10.1038/35040607; RA Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., RA Wang C.C., Hill C.P.; RT "Structural basis for the activation of 20S proteasomes by 11S RT regulators."; RL Nature 408:115-120(2000). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE RP 20S PROTEASOME. RX PubMed=11062564; DOI=10.1038/80992; RA Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., RA Glickman M.H., Finley D.; RT "A gated channel into the proteasome core particle."; RL Nat. Struct. Biol. 7:1062-1067(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE RP 20S PROTEASOME AND A TMC-95-BASED INHIBITOR. RX PubMed=16793518; DOI=10.1016/j.chembiol.2006.04.005; RA Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.; RT "TMC-95-based inhibitor design provides evidence for the catalytic RT versatility of the proteasome."; RL Chem. Biol. 13:607-614(2006). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE RP 20S PROTEASOME AND SALINOSPORAMIDE. RX PubMed=16608349; DOI=10.1021/ja058320b; RA Groll M., Huber R., Potts B.C.M.; RT "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) RT in complex with the 20S proteasome reveal important consequences of RT beta-lactone ring opening and a mechanism for irreversible binding."; RL J. Am. Chem. Soc. 128:5136-5141(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE RP 20S PROTEASOME AND BORTEZOMIB. RX PubMed=16531229; DOI=10.1016/j.str.2005.11.019; RA Groll M., Berkers C.R., Ploegh H.L., Ovaa H.; RT "Crystal structure of the boronic acid-based proteasome inhibitor RT bortezomib in complex with the yeast 20S proteasome."; RL Structure 14:451-456(2006). CC -!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in CC the cytoplasm and in the nucleus. It is essential for the CC regulated turnover of proteins and for the removal of misfolded CC proteins. The proteasome is a multicatalytic proteinase complex CC that is characterized by its ability to cleave peptides with Arg, CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. It has an ATP-dependent proteolytic activity. CC PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide- CC hydrolyzing activity. CC -!- FUNCTION: This subunit is necessary for the peptidylglutamyl- CC peptide hydrolyzing activity. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and CC two 19S regulatory subunits. The 20S proteasome core is composed CC of 28 subunits that are arranged in four stacked rings, resulting CC in a barrel-shaped structure. The two end rings are each formed by CC seven alpha subunits, and the two central rings are each formed by CC seven beta subunits. The catalytic chamber with the active sites CC is on the inside of the barrel. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- MISCELLANEOUS: The side chain of Thr-20 acts as nucleophile, and CC the N-terminal amino group acts as proton acceptor. CC -!- MISCELLANEOUS: Present with 7250 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA55591.1; Type=Erroneous initiation; CC Sequence=CAA60921.1; Type=Erroneous initiation; 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; X78991; CAA55591.1; ALT_INIT; Genomic_DNA. DR EMBL; Z49276; CAA89290.1; -; Genomic_DNA. DR EMBL; Z49277; CAA89292.1; -; Genomic_DNA. DR EMBL; X87611; CAA60921.1; ALT_INIT; Genomic_DNA. DR EMBL; X86020; CAA60015.1; -; mRNA. DR EMBL; S78566; AAB34629.1; -; mRNA. DR EMBL; BK006943; DAA08790.1; -; Genomic_DNA. DR PIR; S61337; S61337. DR RefSeq; NP_012533.1; NM_001181435.1. DR PDB; 1FNT; X-ray; 3.20 A; H/V=20-215. DR PDB; 1G0U; X-ray; 2.40 A; 2/N=20-215. DR PDB; 1G65; X-ray; 2.25 A; 2/N=20-215. DR PDB; 1JD2; X-ray; 3.00 A; N/U=20-215. DR PDB; 1RYP; X-ray; 1.90 A; H/V=11-215. DR PDB; 1VSY; X-ray; 3.00 A; H/V=21-215. DR PDB; 1Z7Q; X-ray; 3.22 A; H/V=20-215. DR PDB; 2F16; X-ray; 2.80 A; 2/N=20-215. DR PDB; 2FAK; X-ray; 2.80 A; 2/N=20-215. DR PDB; 2GPL; X-ray; 2.81 A; 2/N=20-215. DR PDB; 2ZCY; X-ray; 2.90 A; 1/N=20-215. DR PDB; 3BDM; X-ray; 2.70 A; 1/N=20-215. DR PDB; 3D29; X-ray; 2.60 A; 2/N=20-215. DR PDB; 3DY3; X-ray; 2.81 A; 2/N=20-215. DR PDB; 3DY4; X-ray; 2.80 A; 2/N=20-215. DR PDB; 3E47; X-ray; 3.00 A; 2/N=20-215. DR PDB; 3GPJ; X-ray; 2.70 A; 2/N=20-215. DR PDB; 3GPT; X-ray; 2.41 A; 2/N=20-215. DR PDB; 3GPW; X-ray; 2.50 A; 2/N=20-215. DR PDB; 3HYE; X-ray; 2.50 A; 2/N=20-215. DR PDB; 3L5Q; X-ray; 3.00 A; B/D=21-215. DR PDB; 3MG0; X-ray; 2.68 A; 2/N=20-215. DR PDB; 3MG4; X-ray; 3.11 A; 2/N=20-215. DR PDB; 3MG6; X-ray; 2.60 A; 2/N=20-215. DR PDB; 3MG7; X-ray; 2.78 A; 2/N=20-215. DR PDB; 3MG8; X-ray; 2.59 A; 2/N=20-215. DR PDB; 3NZJ; X-ray; 2.40 A; 2/N=1-215. DR PDB; 3NZW; X-ray; 2.50 A; 2/N=1-215. DR PDB; 3NZX; X-ray; 2.70 A; 2/N=1-215. DR PDB; 3OEU; X-ray; 2.60 A; 2/N=20-215. DR PDB; 3OEV; X-ray; 2.85 A; 2/N=20-215. DR PDB; 3OKJ; X-ray; 2.70 A; 2/N=20-215. DR PDB; 3SDI; X-ray; 2.65 A; 2/N=20-215. DR PDB; 3SDK; X-ray; 2.70 A; 2/N=20-215. DR PDB; 3SHJ; X-ray; 2.80 A; 2/N=20-215. DR PDB; 3TDD; X-ray; 2.70 A; 2/N=20-215. DR PDB; 3UN4; X-ray; 3.40 A; N/b=20-215. DR PDB; 3UN8; X-ray; 2.70 A; N/b=20-215. DR PDBsum; 1FNT; -. DR PDBsum; 1G0U; -. DR PDBsum; 1G65; -. DR PDBsum; 1JD2; -. DR PDBsum; 1RYP; -. DR PDBsum; 1VSY; -. DR PDBsum; 1Z7Q; -. DR PDBsum; 2F16; -. DR PDBsum; 2FAK; -. DR PDBsum; 2GPL; -. DR PDBsum; 2ZCY; -. DR PDBsum; 3BDM; -. DR PDBsum; 3D29; -. DR PDBsum; 3DY3; -. DR PDBsum; 3DY4; -. DR PDBsum; 3E47; -. DR PDBsum; 3GPJ; -. DR PDBsum; 3GPT; -. DR PDBsum; 3GPW; -. DR PDBsum; 3HYE; -. DR PDBsum; 3L5Q; -. DR PDBsum; 3MG0; -. DR PDBsum; 3MG4; -. DR PDBsum; 3MG6; -. DR PDBsum; 3MG7; -. DR PDBsum; 3MG8; -. DR PDBsum; 3NZJ; -. DR PDBsum; 3NZW; -. DR PDBsum; 3NZX; -. DR PDBsum; 3OEU; -. DR PDBsum; 3OEV; -. DR PDBsum; 3OKJ; -. DR PDBsum; 3SDI; -. DR PDBsum; 3SDK; -. DR PDBsum; 3SHJ; -. DR PDBsum; 3TDD; -. DR PDBsum; 3UN4; -. DR PDBsum; 3UN8; -. DR ProteinModelPortal; P38624; -. DR SMR; P38624; 20-215. DR DIP; DIP-1527N; -. DR IntAct; P38624; 21. DR MINT; MINT-401012; -. DR STRING; P38624; -. DR MEROPS; T01.010; -. DR UCD-2DPAGE; P38624; -. DR PeptideAtlas; P38624; -. DR EnsemblFungi; YJL001W; YJL001W; YJL001W. DR GeneID; 853456; -. DR KEGG; sce:YJL001W; -. DR CYGD; YJL001w; -. DR SGD; S000003538; PRE3. DR eggNOG; COG0638; -. DR GeneTree; ENSGT00510000046484; -. DR HOGENOM; HOG000091079; -. DR KO; K02738; -. DR OMA; GTSIMAV; -. DR OrthoDB; EOG454D82; -. DR EvolutionaryTrace; P38624; -. DR NextBio; 974026; -. DR ArrayExpress; P38624; -. DR Genevestigator; P38624; -. DR GermOnline; YJL001W; Saccharomyces cerevisiae. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:SGD. DR GO; GO:0005634; C:nucleus; IC:SGD. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:SGD. DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD. DR GO; GO:0004175; F:endopeptidase activity; IMP:SGD. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR PROSITE; PS00854; PROTEASOME_B_1; 1. DR PROSITE; PS51476; PROTEASOME_B_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus; KW Phosphoprotein; Protease; Proteasome; Reference proteome; KW Threonine protease; Zymogen. FT PROPEP 1 19 Removed in mature form. FT /FTId=PRO_0000026643. FT CHAIN 20 215 Proteasome component PRE3. FT /FTId=PRO_0000026644. FT ACT_SITE 20 20 Nucleophile. FT MOD_RES 91 91 Phosphothreonine. FT STRAND 22 27 FT STRAND 30 35 FT STRAND 39 41 FT STRAND 44 49 FT STRAND 53 57 FT STRAND 60 67 FT HELIX 68 89 FT HELIX 94 107 FT TURN 108 111 FT STRAND 114 122 FT TURN 123 125 FT STRAND 126 132 FT TURN 134 136 FT STRAND 139 147 FT HELIX 148 153 FT HELIX 154 160 FT HELIX 167 184 FT STRAND 185 187 FT STRAND 192 198 FT STRAND 201 207 FT HELIX 209 212 SQ SEQUENCE 215 AA; 23548 MW; BD1FCE649678D86B CRC64; MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT DKLTRVHDKI WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV FKELCYENKD NLTAGIIVAG YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS TFIYGYCDKN FRENMSKEET VDFIKHSLSQ AIKWDGSSGG VIRMVVLTAA GVERLIFYPD EYEQL //