ID RPN3_YEAST Reviewed; 523 AA. AC P40016; D3DLS0; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 5. DT 27-MAR-2024, entry version 188. DE RecName: Full=26S proteasome regulatory subunit RPN3; GN Name=RPN3; Synonyms=SUN2; OrderedLocusNames=YER021W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8668124; DOI=10.1007/bf02172912; RA Kawamura M., Kominami K., Takeuchi J., Toh-e A.; RT "A multicopy suppressor of nin1-1 of the yeast Saccharomyces cerevisiae is RT a counterpart of the Drosophila melanogaster diphenol oxidase A2 gene, Dox- RT A2."; RL Mol. Gen. Genet. 251:146-152(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9017604; DOI=10.1091/mbc.8.1.171; RA Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A., RA Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y., RA Tanahashi N., Tanaka K., Toh-e A.; RT "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S RT proteasome are encoded by two multicopy suppressors of nin1-1."; RL Mol. Biol. Cell 8:171-187(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT ALA-2. RX PubMed=12504901; DOI=10.1016/s0003-9861(02)00639-2; RA Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.; RT "N-terminal modifications of the 19S regulatory particle subunits of the RT yeast proteasome."; RL Arch. Biochem. Biophys. 409:341-348(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [8] RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME. RX PubMed=22927375; DOI=10.1073/pnas.1213333109; RA Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E., RA Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.; RT "Near-atomic resolution structural model of the yeast 26S proteasome."; RL Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012). CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is CC involved in the ATP-dependent degradation of ubiquitinated proteins. CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as CC the 20S proteasome, capped at one or both ends by the 19S regulatory CC complex (RC). The RC is composed of at least 18 different subunits in CC two subcomplexes, the base and the lid, which form the portions CC proximal and distal to the 20S proteolytic core, respectively (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC P40016; Q12250: RPN5; NbExp=4; IntAct=EBI-15927, EBI-15935; CC P40016; Q06103: RPN7; NbExp=7; IntAct=EBI-15927, EBI-15940; CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}. CC -!- MISCELLANEOUS: Present with 16700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}. 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; D78023; BAA11208.1; -; Genomic_DNA. DR EMBL; U18778; AAB64554.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07674.1; -; Genomic_DNA. DR PIR; S50479; S50479. DR RefSeq; NP_010938.1; NM_001178912.1. DR PDB; 3J47; EM; -; S=455-478. DR PDB; 3JCK; EM; 3.50 A; A=131-523. DR PDB; 3JCO; EM; 4.80 A; S=1-523. DR PDB; 3JCP; EM; 4.60 A; S=1-523. DR PDB; 4CR2; EM; 7.70 A; S=1-523. DR PDB; 4CR3; EM; 9.30 A; S=1-523. DR PDB; 4CR4; EM; 8.80 A; S=1-523. DR PDB; 5A5B; EM; 9.50 A; S=1-523. DR PDB; 5MPB; EM; 7.80 A; S=1-523. DR PDB; 5MPC; EM; 7.70 A; S=1-523. DR PDB; 5MPD; EM; 4.10 A; S=1-523. DR PDB; 5MPE; EM; 4.50 A; S=1-523. DR PDB; 5WVI; EM; 6.30 A; S=1-523. DR PDB; 5WVK; EM; 4.20 A; S=1-523. DR PDB; 6FVT; EM; 4.10 A; S=18-492. DR PDB; 6FVU; EM; 4.50 A; S=18-492. DR PDB; 6FVV; EM; 5.40 A; S=18-492. DR PDB; 6FVW; EM; 4.50 A; S=18-492. DR PDB; 6FVX; EM; 4.90 A; S=18-492. DR PDB; 6FVY; EM; 6.10 A; S=18-492. DR PDB; 6J2C; EM; 7.00 A; S=1-523. DR PDB; 6J2N; EM; 7.50 A; S=1-523. DR PDB; 6J2Q; EM; 3.80 A; S=1-523. DR PDB; 6J2X; EM; 3.80 A; S=1-523. DR PDB; 6J30; EM; 4.50 A; S=1-523. DR PDB; 7QO3; EM; 6.10 A; S=1-523. DR PDB; 7QO5; EM; 6.00 A; S=1-523. DR PDBsum; 3J47; -. DR PDBsum; 3JCK; -. DR PDBsum; 3JCO; -. DR PDBsum; 3JCP; -. DR PDBsum; 4CR2; -. DR PDBsum; 4CR3; -. DR PDBsum; 4CR4; -. DR PDBsum; 5A5B; -. DR PDBsum; 5MPB; -. DR PDBsum; 5MPC; -. DR PDBsum; 5MPD; -. DR PDBsum; 5MPE; -. DR PDBsum; 5WVI; -. DR PDBsum; 5WVK; -. DR PDBsum; 6FVT; -. DR PDBsum; 6FVU; -. DR PDBsum; 6FVV; -. DR PDBsum; 6FVW; -. DR PDBsum; 6FVX; -. DR PDBsum; 6FVY; -. DR PDBsum; 6J2C; -. DR PDBsum; 6J2N; -. DR PDBsum; 6J2Q; -. DR PDBsum; 6J2X; -. DR PDBsum; 6J30; -. DR PDBsum; 7QO3; -. DR PDBsum; 7QO5; -. DR AlphaFoldDB; P40016; -. DR EMDB; EMD-14082; -. DR EMDB; EMD-14084; -. DR EMDB; EMD-3136; -. DR EMDB; EMD-3536; -. DR EMDB; EMD-3537; -. DR EMDB; EMD-4321; -. DR EMDB; EMD-4322; -. DR EMDB; EMD-4323; -. DR EMDB; EMD-4324; -. DR EMDB; EMD-6693; -. DR EMDB; EMD-6694; -. DR EMDB; EMD-9769; -. DR EMDB; EMD-9770; -. DR EMDB; EMD-9771; -. DR EMDB; EMD-9772; -. DR EMDB; EMD-9773; -. DR SMR; P40016; -. DR BioGRID; 36755; 159. DR ComplexPortal; CPX-2262; 26S Proteasome complex. DR DIP; DIP-1322N; -. DR IntAct; P40016; 38. DR MINT; P40016; -. DR STRING; 4932.YER021W; -. DR MEROPS; X13.001; -. DR iPTMnet; P40016; -. DR MaxQB; P40016; -. DR PaxDb; 4932-YER021W; -. DR PeptideAtlas; P40016; -. DR EnsemblFungi; YER021W_mRNA; YER021W; YER021W. DR GeneID; 856742; -. DR KEGG; sce:YER021W; -. DR AGR; SGD:S000000823; -. DR SGD; S000000823; RPN3. DR VEuPathDB; FungiDB:YER021W; -. DR eggNOG; KOG2581; Eukaryota. DR GeneTree; ENSGT00940000153653; -. DR HOGENOM; CLU_019858_1_2_1; -. DR InParanoid; P40016; -. DR OMA; AKLWFYI; -. DR OrthoDB; 514836at2759; -. DR BioCyc; YEAST:G3O-30205-MONOMER; -. DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-SCE-5689880; Ub-specific processing proteases. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 856742; 8 hits in 10 CRISPR screens. DR PRO; PR:P40016; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P40016; Protein. DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal. DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:SGD. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal. DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR InterPro; IPR013586; 26S_Psome_reg_C. DR InterPro; IPR000717; PCI_dom. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1. DR PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1. DR Pfam; PF01399; PCI; 1. DR Pfam; PF08375; Rpn3_C; 1. DR SMART; SM00753; PAM; 1. DR SMART; SM00088; PINT; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein; KW Proteasome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12504901" FT CHAIN 2..523 FT /note="26S proteasome regulatory subunit RPN3" FT /id="PRO_0000173827" FT DOMAIN 270..450 FT /note="PCI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185" FT REGION 480..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 480..496 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..516 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:12504901" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT CONFLICT 355 FT /note="G -> S (in Ref. 1; no nucleotide entry and 2; FT BAA11208)" FT /evidence="ECO:0000305" FT HELIX 132..149 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 153..161 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 163..172 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 175..195 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 201..224 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 227..243 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 248..255 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 266..282 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 289..298 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 307..323 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 330..333 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 337..340 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 343..354 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 357..372 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 376..380 FT /evidence="ECO:0007829|PDB:3JCK" FT TURN 381..383 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 384..397 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 400..403 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 404..410 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 416..428 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:3JCK" FT TURN 438..441 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 442..445 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 456..477 FT /evidence="ECO:0007829|PDB:3JCK" SQ SEQUENCE 523 AA; 60393 MW; B08B58663DDA85DC CRC64; MASTAVMMDV DSSGVNDLHH SEKKYAEEDQ VQELLKVLNE ISKTTLTLDP RYIWRSLKDL SSLRNQELLN AETLCFTVNV LYPDSSSFKK NLLKFITSNH KSSVPGSAEL RNSYPASFYS VNTEKKTIEV TAEINCFMHL LVQLFLWDSK ELEQLVEFNR KVVIPNLLCY YNLRSLNLIN AKLWFYIYLS HETLARSSEE INSDNQNIIL RSTMMKFLKI ASLKHDNETK AMLINLILRD FLNNGEVDSA SDFISKLEYP HTDVSSSLEA RYFFYLSKIN AIQLDYSTAN EYIIAAIRKA PHNSKSLGFL QQSNKLHCCI QLLMGDIPEL SFFHQSNMQK SLLPYYHLTK AVKLGDLKKF TSTITKYKQL LLKDDTYQLC VRLRSNVIKT GIRIISLTYK KISLRDICLK LNLDSEQTVE YMVSRAIRDG VIEAKINHED GFIETTELLN IYDSEDPQQV FDERIKFANQ LHDEYLVSMR YPEDKKTQQN EKSENGENDD DTLDGDLMDD MSDISDLDDL GFL //