RPN9_YEAST
ID RPN9_YEAST Reviewed; 393 AA.
AC Q04062; D6VT56;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=26S proteasome regulatory subunit RPN9;
DE AltName: Full=Proteasome non-ATPase subunit 7;
GN Name=RPN9; Synonyms=NAS7; OrderedLocusNames=YDR427W; ORFNames=D9461.14;
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 [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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-6.
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 [4]
RP FUNCTION.
RX PubMed=9714768; DOI=10.1016/s0378-1119(98)00309-6;
RA Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J.,
RA Toh-e A., Tanaka K.;
RT "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two
RT novel regulatory subunits of the 26S proteasome.";
RL Gene 216:113-122(1998).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7]
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 {ECO:0000269|PubMed:9714768}.
CC -!- INTERACTION:
CC Q04062; P43588: RPN11; NbExp=5; IntAct=EBI-15944, EBI-11219;
CC Q04062; Q12250: RPN5; NbExp=8; IntAct=EBI-15944, EBI-15935;
CC Q04062; Q12377: RPN6; NbExp=3; IntAct=EBI-15944, EBI-308;
CC Q04062; Q08723: RPN8; NbExp=5; IntAct=EBI-15944, EBI-36176;
CC Q04062; P33298: RPT3; NbExp=3; IntAct=EBI-15944, EBI-13905;
CC -!- MISCELLANEOUS: Present with 12400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC {ECO:0000305}.
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DR EMBL; U33007; AAB64853.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12266.1; -; Genomic_DNA.
DR PIR; S69708; S69708.
DR RefSeq; NP_010715.3; NM_001180735.3.
DR PDB; 2MQW; NMR; -; A=1-160.
DR PDB; 2MR3; NMR; -; A=1-393.
DR PDB; 2MRI; NMR; -; A=181-356.
DR PDB; 3J47; EM; -; O=360-387.
DR PDB; 3JCK; EM; 3.50 A; F=1-393.
DR PDB; 3JCO; EM; 4.80 A; O=1-393.
DR PDB; 3JCP; EM; 4.60 A; O=1-393.
DR PDB; 4CR2; EM; 7.70 A; O=1-393.
DR PDB; 4CR3; EM; 9.30 A; O=1-393.
DR PDB; 4CR4; EM; 8.80 A; O=1-393.
DR PDB; 5A5B; EM; 9.50 A; O=1-393.
DR PDB; 5MPB; EM; 7.80 A; O=1-393.
DR PDB; 5MPC; EM; 7.70 A; O=1-393.
DR PDB; 5MPD; EM; 4.10 A; O=1-393.
DR PDB; 5MPE; EM; 4.50 A; O=1-393.
DR PDB; 5WVI; EM; 6.30 A; O=1-393.
DR PDB; 5WVK; EM; 4.20 A; O=1-393.
DR PDB; 6FVT; EM; 4.10 A; O=6-393.
DR PDB; 6FVU; EM; 4.50 A; O=6-393.
DR PDB; 6FVV; EM; 5.40 A; O=6-393.
DR PDB; 6FVW; EM; 4.50 A; O=6-393.
DR PDB; 6FVX; EM; 4.90 A; O=6-393.
DR PDB; 6FVY; EM; 6.10 A; O=6-393.
DR PDB; 6J2C; EM; 7.00 A; O=1-393.
DR PDB; 6J2N; EM; 7.50 A; O=1-393.
DR PDB; 6J2Q; EM; 3.80 A; O=1-393.
DR PDB; 6J2X; EM; 3.80 A; O=1-393.
DR PDB; 6J30; EM; 4.50 A; O=1-393.
DR PDB; 7QO3; EM; 6.10 A; O=1-393.
DR PDB; 7QO5; EM; 6.00 A; O=1-393.
DR PDB; 7QO6; EM; 6.30 A; O=1-393.
DR PDBsum; 2MQW; -.
DR PDBsum; 2MR3; -.
DR PDBsum; 2MRI; -.
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 PDBsum; 7QO6; -.
DR AlphaFoldDB; Q04062; -.
DR BMRB; Q04062; -.
DR SMR; Q04062; -.
DR BioGRID; 32485; 90.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-5261N; -.
DR IntAct; Q04062; 52.
DR MINT; Q04062; -.
DR STRING; 4932.YDR427W; -.
DR iPTMnet; Q04062; -.
DR MaxQB; Q04062; -.
DR PaxDb; Q04062; -.
DR PRIDE; Q04062; -.
DR EnsemblFungi; YDR427W_mRNA; YDR427W; YDR427W.
DR GeneID; 852037; -.
DR KEGG; sce:YDR427W; -.
DR SGD; S000002835; RPN9.
DR VEuPathDB; FungiDB:YDR427W; -.
DR eggNOG; KOG2908; Eukaryota.
DR GeneTree; ENSGT00390000001802; -.
DR HOGENOM; CLU_042989_0_0_1; -.
DR InParanoid; Q04062; -.
DR OMA; TWVQPRI; -.
DR BioCyc; YEAST:G3O-29967-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:Q04062; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04062; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:SGD.
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:SGD.
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:SGD.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035298; PSMD13.
DR InterPro; IPR040798; Rpn9_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10539; PTHR10539; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18261; Rpn9_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; Direct protein sequencing; Proteasome; Reference proteome.
FT CHAIN 1..393
FT /note="26S proteasome regulatory subunit RPN9"
FT /id="PRO_0000173870"
FT DOMAIN 187..355
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2MR3"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2MR3"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2MR3"
FT HELIX 360..384
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 385..390
FT /evidence="ECO:0007829|PDB:3JCK"
SQ SEQUENCE 393 AA; 45782 MW; 540F7DF8C23469A1 CRC64;
MFNNHEIDTI LSTLRMEADP SLHPLFEQFE KFYEEKLWFQ LSESLTKFFD DAKSTPLRLR
LYDNFVSKFY DKINQLSVVK YLLASLKDSK DFDESLKYLD DLKAQFQELD SKKQRNNGSK
DHGDGILLID SEIARTYLLK NDLVKARDLL DDLEKTLDKK DSIPLRITNS FYSTNSQYFK
FKNDFNSFYY TSLLYLSTLE PSTSITLAER QQLAYDLSIS ALLGDKIYNF GELLHHPIME
TIVNDSNYDW LFQLLNALTV GDFDKFDSLI KVQISKIPIL AQHESFLRQK ICLMTLIETV
FVKNIRMLSF EDISKATHLP KDNVEHLVMR AISLGLLKGS IDQVNELVTI SWVQPRIISG
DQITKMKDRL VEWNDQVEKL GKKMEARGQS IWV
