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 15-JUN-2002 (Rel. 41, 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 PRE3 OR YJL001W OR 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; 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; RA de Haan M., Smits P.H.M., Grivell L.A.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. 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 at peptide bonds with very broad CC specificity. CC -!- PATHWAY: Involved in an ATP/ubiquitin-dependent non-lysosomal CC proteolytic pathway. CC -!- SUBUNIT: 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 PEPTIDASE FAMILY T1B. 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; S43669; S43669. DR PDB; 1RYP; 15-APR-98. DR MEROPS; T01.010; -. DR SGD; S0003538; PRE3. DR InterPro; IPR000243; Proteasome_B. DR InterPro; IPR001353; Protsme_protease. DR Pfam; PF00227; proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR PROSITE; PS00854; PROTEASOME_B; 1. KW Proteasome; Hydrolase; Protease; 3D-structure; Zymogen. FT PROPEP 1 19 BY SIMILARITY. FT CHAIN 20 215 PROTEASOME COMPONENT PRE3. 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 //