ID PSB6_YEAST Reviewed; 215 AA. AC P38624; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JUL-2007, entry version 73. DE Proteasome component PRE3 precursor (EC 3.4.25.1) (Macropain subunit DE PRE3) (Proteinase YSCE subunit PRE3) (Multicatalytic endopeptidase DE complex subunit PRE3). GN Name=PRE3; OrderedLocusNames=YJL001W; ORFNames=J1407; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; 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 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 [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215. RX MEDLINE=97242404; PubMed=9087403; DOI=10.1038/386463a0; RA Groll M., Ditzel L., Lowe 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). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex CC which 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. The proteasome has an ATP-dependent proteolytic CC activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl- CC peptide-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 yeast proteasome seems to be composed of 14 different CC subunits which form a highly ordered ring-shaped structure. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- MISCELLANEOUS: Present with 7250 molecules/cell. CC -!- SIMILARITY: Belongs to the peptidase T1B family. 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 PIR; S61337; S61337. DR PDB; 1FNT; X-ray; H/V=20-215. DR PDB; 1G0U; X-ray; 2/N=20-215. DR PDB; 1G65; X-ray; 2/N=20-215. DR PDB; 1JD2; X-ray; N/U=20-215. DR PDB; 1RYP; X-ray; H/V=11-215. DR PDB; 1Z7Q; X-ray; H/V=20-215. DR PDB; 2FNY; X-ray; 2/N=-. DR DIP; DIP:1527N; -. DR IntAct; P38624; -. DR MEROPS; T01.010; -. DR PeptideAtlas; P38624; -. DR Ensembl; YJL001W; Saccharomyces cerevisiae. DR GenomeReviews; Y13136_GR; YJL001W. DR KEGG; sce:YJL001W; -. DR CYGD; YJL001w; -. DR SGD; S000003538; PRE3. DR BioCyc; SCER-S28-01:SCER-S28-01-003082-MONOMER; -. DR LinkHub; P38624; -. DR GermOnline; YJL001W; Saccharomyces cerevisiae. DR GO; GO:0019774; C:proteasome core complex, beta-subunit compl...; IPI:SGD. DR GO; GO:0004175; F:endopeptidase activity; TAS:SGD. DR GO; GO:0006950; P:response to stress; TAS:SGD. DR GO; GO:0030437; P:sporulation (sensu Fungi); TAS:SGD. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:SGD. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR001353; Proteasome_A_B. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR PROSITE; PS00854; PROTEASOME_B; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus; KW Protease; Proteasome; Threonine protease; Zymogen. FT PROPEP 1 19 By similarity. FT /FTId=PRO_0000026643. FT CHAIN 20 215 Proteasome component PRE3. FT /FTId=PRO_0000026644. FT STRAND 22 26 FT STRAND 28 35 FT STRAND 39 41 FT STRAND 44 49 FT STRAND 53 57 FT STRAND 60 66 FT HELIX 68 89 FT HELIX 94 107 FT HELIX 109 111 FT STRAND 114 122 FT TURN 123 125 FT STRAND 126 132 FT STRAND 139 147 FT HELIX 150 160 FT HELIX 167 184 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 //