RPN6_YEAST
ID RPN6_YEAST Reviewed; 434 AA.
AC Q12377; D6VRQ3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=26S proteasome regulatory subunit RPN6;
DE AltName: Full=Proteasome non-ATPase subunit 4;
GN Name=RPN6; Synonyms=NAS4; OrderedLocusNames=YDL097C; ORFNames=D2381;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-9, AND ACETYLATION AT SER-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 [5]
RP FUNCTION.
RX PubMed=9426256; DOI=10.1016/s0378-1119(97)00524-6;
RA Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A.,
RA DeMartino G.N., Tanahashi N., Tanaka K.;
RT "cDNA cloning and functional analysis of p44.5 and p55, two regulatory
RT subunits of the 26S proteasome.";
RL Gene 203:241-250(1997).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
RX PubMed=12486135; DOI=10.1074/jbc.m209420200;
RA Santamaria P.G., Finley D., Ballesta J.P., Remacha M.;
RT "Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential
RT for the assembly and activity of the 26 S proteasome.";
RL J. Biol. Chem. 278:6687-6695(2003).
RN [7]
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 [8]
RP FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, AND
RP MUTAGENESIS OF PHE-132 AND LEU-377.
RX PubMed=15611133; DOI=10.1074/jbc.m409364200;
RA Isono E., Saito N., Kamata N., Saeki Y., Toh-E A.;
RT "Functional analysis of Rpn6p, a lid component of the 26 S proteasome,
RT using temperature-sensitive rpn6 mutants of the yeast Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 280:6537-6547(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, RPN6 is required for proteasome
CC assembly. {ECO:0000269|PubMed:12486135, ECO:0000269|PubMed:15611133,
CC ECO:0000269|PubMed:9426256}.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S regulatory
CC subunits. {ECO:0000269|PubMed:12486135, ECO:0000269|PubMed:15611133}.
CC -!- INTERACTION:
CC Q12377; Q12250: RPN5; NbExp=8; IntAct=EBI-308, EBI-15935;
CC Q12377; Q08723: RPN8; NbExp=3; IntAct=EBI-308, EBI-36176;
CC Q12377; Q04062: RPN9; NbExp=3; IntAct=EBI-308, EBI-15944;
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- MISCELLANEOUS: Present with 16800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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DR EMBL; X95644; CAA64916.1; -; Genomic_DNA.
DR EMBL; Z74145; CAA98664.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11763.1; -; Genomic_DNA.
DR PIR; S67639; S67639.
DR RefSeq; NP_010186.1; NM_001180156.1.
DR PDB; 3J47; EM; -; Q=407-431.
DR PDB; 3JCK; EM; 3.50 A; C=1-434.
DR PDB; 3JCO; EM; 4.80 A; Q=1-434.
DR PDB; 3JCP; EM; 4.60 A; Q=1-434.
DR PDB; 4CR2; EM; 7.70 A; Q=1-434.
DR PDB; 4CR3; EM; 9.30 A; Q=1-434.
DR PDB; 4CR4; EM; 8.80 A; Q=1-434.
DR PDB; 5A5B; EM; 9.50 A; Q=1-434.
DR PDB; 5MPB; EM; 7.80 A; Q=1-434.
DR PDB; 5MPC; EM; 7.70 A; Q=1-434.
DR PDB; 5MPD; EM; 4.10 A; Q=1-434.
DR PDB; 5MPE; EM; 4.50 A; Q=1-434.
DR PDB; 5WVI; EM; 6.30 A; Q=1-434.
DR PDB; 5WVK; EM; 4.20 A; Q=1-434.
DR PDB; 6FVT; EM; 4.10 A; Q=1-434.
DR PDB; 6FVU; EM; 4.50 A; Q=1-434.
DR PDB; 6FVV; EM; 5.40 A; Q=1-434.
DR PDB; 6FVW; EM; 4.50 A; Q=1-434.
DR PDB; 6FVX; EM; 4.90 A; Q=1-434.
DR PDB; 6FVY; EM; 6.10 A; Q=1-434.
DR PDB; 6J2C; EM; 7.00 A; Q=1-434.
DR PDB; 6J2N; EM; 7.50 A; Q=1-434.
DR PDB; 6J2Q; EM; 3.80 A; Q=1-434.
DR PDB; 6J2X; EM; 3.80 A; Q=1-434.
DR PDB; 6J30; EM; 4.50 A; Q=1-434.
DR PDB; 7QO3; EM; 6.10 A; Q=1-434.
DR PDB; 7QO5; EM; 6.00 A; Q=1-434.
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; Q12377; -.
DR SMR; Q12377; -.
DR BioGRID; 31965; 738.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1581N; -.
DR IntAct; Q12377; 39.
DR MINT; Q12377; -.
DR STRING; 4932.YDL097C; -.
DR iPTMnet; Q12377; -.
DR MaxQB; Q12377; -.
DR PaxDb; Q12377; -.
DR PRIDE; Q12377; -.
DR EnsemblFungi; YDL097C_mRNA; YDL097C; YDL097C.
DR GeneID; 851461; -.
DR KEGG; sce:YDL097C; -.
DR SGD; S000002255; RPN6.
DR VEuPathDB; FungiDB:YDL097C; -.
DR eggNOG; KOG1463; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR HOGENOM; CLU_029573_2_1_1; -.
DR InParanoid; Q12377; -.
DR OMA; LYFDTGM; -.
DR BioCyc; YEAST:G3O-29500-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:Q12377; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12377; protein.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:UniProtKB.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR GO; GO:0043248; P:proteasome assembly; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Proteasome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..434
FT /note="26S proteasome regulatory subunit RPN6"
FT /id="PRO_0000173860"
FT DOMAIN 235..404
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12504901,
FT ECO:0007744|PubMed:22814378"
FT MUTAGEN 132
FT /note="F->L: In rpn6-2; temperature-sensitive mutant that
FT shows defects in proteasome assembly when incubated at 37
FT degrees Celsius; when associated with P-377."
FT /evidence="ECO:0000269|PubMed:15611133"
FT MUTAGEN 377
FT /note="L->P: In rpn6-2; temperature-sensitive mutant that
FT shows defects in proteasome assembly when incubated at 37
FT degrees Celsius; when associated with L-132."
FT /evidence="ECO:0000269|PubMed:15611133"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 254..272
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 317..321
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 329..351
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:3JCK"
SQ SEQUENCE 434 AA; 49774 MW; A8B1F7E6F73A4024 CRC64;
MSLPGSKLEE ARRLVNEKQY NEAEQVYLSL LDKDSSQSSA AAGASVDDKR RNEQETSILE
LGQLYVTMGA KDKLREFIPH STEYMMQFAK SKTVKVLKTL IEKFEQVPDS LDDQIFVCEK
SIEFAKREKR VFLKHSLSIK LATLHYQKKQ YKDSLALIND LLREFKKLDD KPSLVDVHLL
ESKVYHKLRN LAKSKASLTA ARTAANSIYC PTQTVAELDL MSGILHCEDK DYKTAFSYFF
ESFESYHNLT THNSYEKACQ VLKYMLLSKI MLNLIDDVKN ILNAKYTKET YQSRGIDAMK
AVAEAYNNRS LLDFNTALKQ YEKELMGDEL TRSHFNALYD TLLESNLCKI IEPFECVEIS
HISKIIGLDT QQVEGKLSQM ILDKIFYGVL DQGNGWLYVY ETPNQDATYD SALELVGQLN
KVVDQLFEKA SVLY
