ID PSB6_YEAST STANDARD; PRT; 215 AA. AC P38624; DT 01-OCT-1994 (Rel. 30, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) 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; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=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 REVISIONS 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 SEQUENCE FROM N.A. RC STRAIN=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., Tovan D., Tzermia M., Van Broekhoven A., RA Vandenbol M., Wedler D.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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215. RX MEDLINE=97242404; PubMed=9087403; 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 -!- PATHWAY: Involved in an ATP/ubiquitin-dependent non-lysosomal CC proteolytic pathway. 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: Cytoplasmic and nuclear. 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. DR EMBL; Z49276; CAA89290.1; -. DR EMBL; Z49277; CAA89292.1; -. DR EMBL; X87611; CAA60921.1; ALT_INIT. DR EMBL; X86020; CAA60015.1; -. DR EMBL; S78566; AAB34629.1; -. DR PIR; S61337; S61337. 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 IntAct; P38624; -. DR GermOnline; 141617; -. DR MEROPS; T01.010; -. DR SGD; S000003538; PRE3. 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. KW 3D-structure; Hydrolase; Protease; Proteasome; Threonine protease; KW Zymogen. FT PROPEP 1 19 By similarity. FT CHAIN 20 215 Proteasome component PRE3. FT TURN 13 14 FT STRAND 17 17 FT STRAND 22 27 FT TURN 28 29 FT STRAND 30 35 FT STRAND 39 41 FT TURN 42 43 FT STRAND 44 47 FT STRAND 53 57 FT TURN 58 59 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 134 135 FT STRAND 139 141 FT STRAND 143 146 FT HELIX 148 153 FT HELIX 154 160 FT TURN 163 164 FT HELIX 167 184 FT STRAND 185 185 FT TURN 186 187 FT STRAND 192 198 FT TURN 199 200 FT STRAND 201 207 FT HELIX 209 212 FT TURN 213 213 SQ SEQUENCE 215 AA; 23547 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 //