RPN3_YEAST
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 03-AUG-2022, entry version 180.
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}.
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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 SMR; P40016; -.
DR BioGRID; 36755; 153.
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; P40016; -.
DR PRIDE; P40016; -.
DR EnsemblFungi; YER021W_mRNA; YER021W; YER021W.
DR GeneID; 856742; -.
DR KEGG; sce:YER021W; -.
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 BioCyc; YEAST:G3O-30205-MON; -.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
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; IPR035267; PSMD3.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 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
