RPN5_YEAST
ID RPN5_YEAST Reviewed; 445 AA.
AC Q12250; D6VRK1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=26S proteasome regulatory subunit RPN5;
DE AltName: Full=Proteasome non-ATPase subunit 5;
GN Name=RPN5; Synonyms=NAS5; OrderedLocusNames=YDL147W; ORFNames=D1572;
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=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(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 2-8, 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 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 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:9426256}.
CC -!- INTERACTION:
CC Q12250; Q03981: CSN9; NbExp=5; IntAct=EBI-15935, EBI-33535;
CC Q12250; P43588: RPN11; NbExp=7; IntAct=EBI-15935, EBI-11219;
CC Q12250; P40016: RPN3; NbExp=4; IntAct=EBI-15935, EBI-15927;
CC Q12250; Q12377: RPN6; NbExp=8; IntAct=EBI-15935, EBI-308;
CC Q12250; Q08723: RPN8; NbExp=8; IntAct=EBI-15935, EBI-36176;
CC Q12250; Q04062: RPN9; NbExp=8; IntAct=EBI-15935, EBI-15944;
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- MISCELLANEOUS: Present with 5710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC {ECO:0000305}.
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DR EMBL; X97751; CAA66344.1; -; Genomic_DNA.
DR EMBL; Z74195; CAA98721.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11711.1; -; Genomic_DNA.
DR PIR; S67695; S67695.
DR RefSeq; NP_010134.1; NM_001180207.1.
DR PDB; 3J47; EM; -; P=409-442.
DR PDB; 3JCK; EM; 3.50 A; B=1-445.
DR PDB; 3JCO; EM; 4.80 A; P=1-445.
DR PDB; 3JCP; EM; 4.60 A; P=1-445.
DR PDB; 4CR2; EM; 7.70 A; P=1-445.
DR PDB; 4CR3; EM; 9.30 A; P=1-445.
DR PDB; 4CR4; EM; 8.80 A; P=1-445.
DR PDB; 5A5B; EM; 9.50 A; P=1-445.
DR PDB; 5MPB; EM; 7.80 A; P=1-445.
DR PDB; 5MPC; EM; 7.70 A; P=1-445.
DR PDB; 5MPD; EM; 4.10 A; P=1-445.
DR PDB; 5MPE; EM; 4.50 A; P=1-445.
DR PDB; 5WVI; EM; 6.30 A; P=1-445.
DR PDB; 5WVK; EM; 4.20 A; P=1-445.
DR PDB; 5ZMR; NMR; -; A=1-136.
DR PDB; 6FVT; EM; 4.10 A; P=1-440.
DR PDB; 6FVU; EM; 4.50 A; P=1-440.
DR PDB; 6FVV; EM; 5.40 A; P=1-440.
DR PDB; 6FVW; EM; 4.50 A; P=1-440.
DR PDB; 6FVX; EM; 4.90 A; P=1-440.
DR PDB; 6FVY; EM; 6.10 A; P=1-440.
DR PDB; 6J2C; EM; 7.00 A; P=1-445.
DR PDB; 6J2N; EM; 7.50 A; P=1-445.
DR PDB; 6J2Q; EM; 3.80 A; P=1-445.
DR PDB; 6J2X; EM; 3.80 A; P=1-445.
DR PDB; 6J30; EM; 4.50 A; P=1-445.
DR PDB; 7QO3; EM; 6.10 A; P=1-445.
DR PDB; 7QO5; EM; 6.00 A; P=1-445.
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; 5ZMR; -.
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; Q12250; -.
DR SMR; Q12250; -.
DR BioGRID; 31914; 625.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1578N; -.
DR IntAct; Q12250; 58.
DR MINT; Q12250; -.
DR STRING; 4932.YDL147W; -.
DR iPTMnet; Q12250; -.
DR MaxQB; Q12250; -.
DR PaxDb; Q12250; -.
DR PRIDE; Q12250; -.
DR EnsemblFungi; YDL147W_mRNA; YDL147W; YDL147W.
DR GeneID; 851408; -.
DR KEGG; sce:YDL147W; -.
DR SGD; S000002306; RPN5.
DR VEuPathDB; FungiDB:YDL147W; -.
DR eggNOG; KOG1498; Eukaryota.
DR GeneTree; ENSGT00940000153510; -.
DR HOGENOM; CLU_033860_2_0_1; -.
DR InParanoid; Q12250; -.
DR OMA; AENEMFK; -.
DR BioCyc; YEAST:G3O-29544-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:Q12250; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12250; protein.
DR GO; GO:0008180; C:COP9 signalosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IDA:SGD.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0000338; P:protein deneddylation; IMP:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035297; PSMD12.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR040896; RPN5_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR PANTHER; PTHR10855:SF1; PTHR10855:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18098; RPN5_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; Proteasome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..445
FT /note="26S proteasome regulatory subunit RPN5"
FT /id="PRO_0000173865"
FT DOMAIN 233..407
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 STRAND 3..5
FT /evidence="ECO:0007829|PDB:5ZMR"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5ZMR"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5ZMR"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 49..68
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5ZMR"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5ZMR"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 211..231
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 337..356
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 408..439
FT /evidence="ECO:0007829|PDB:3JCK"
SQ SEQUENCE 445 AA; 51768 MW; E5DC7F8E6AE27736 CRC64;
MSRDAPIKAD KDYSQILKEE FPKIDSLAQN DCNSALDQLL VLEKKTRQAS DLASSKEVLA
KIVDLLASRN KWDDLNEQLT LLSKKHGQLK LSIQYMIQKV MEYLKSSKSL DLNTRISVIE
TIRVVTENKI FVEVERARVT KDLVEIKKEE GKIDEAADIL CELQVETYGS MEMSEKIQFI
LEQMELSILK GDYSQATVLS RKILKKTFKN PKYESLKLEY YNLLVKISLH KREYLEVAQY
LQEIYQTDAI KSDEAKWKPV LSHIVYFLVL SPYGNLQNDL IHKIQNDNNL KKLESQESLV
KLFTTNELMR WPIVQKTYEP VLNEDDLAFG GEANKHHWED LQKRVIEHNL RVISEYYSRI
TLLRLNELLD LTESQTETYI SDLVNQGIIY AKVNRPAKIV NFEKPKNSSQ LLNEWSHNVD
ELLEHIETIG HLITKEEIMH GLQAK
