RPN7_YEAST
ID RPN7_YEAST Reviewed; 429 AA.
AC Q06103; D6W4A6; E9P8W9;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=26S proteasome regulatory subunit RPN7;
GN Name=RPN7; OrderedLocusNames=YPR108W; ORFNames=P8283.8;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 2-9.
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-77, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
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 [9]
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:0000250}.
CC -!- INTERACTION:
CC Q06103; P40016: RPN3; NbExp=7; IntAct=EBI-15940, EBI-15927;
CC Q06103; O94742: SEM1; NbExp=3; IntAct=EBI-15940, EBI-31337;
CC -!- MISCELLANEOUS: Present with 51900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U32445; AAB68078.1; -; Genomic_DNA.
DR EMBL; AY692769; AAT92788.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11522.1; -; Genomic_DNA.
DR PIR; S59773; S59773.
DR RefSeq; NP_015433.1; NM_001184205.1.
DR PDB; 3J47; EM; -; R=397-422.
DR PDB; 3JCK; EM; 3.50 A; D=1-429.
DR PDB; 3JCO; EM; 4.80 A; R=1-429.
DR PDB; 3JCP; EM; 4.60 A; R=1-429.
DR PDB; 4CR2; EM; 7.70 A; R=1-429.
DR PDB; 4CR3; EM; 9.30 A; R=1-429.
DR PDB; 4CR4; EM; 8.80 A; R=1-429.
DR PDB; 5A5B; EM; 9.50 A; R=1-429.
DR PDB; 5MPB; EM; 7.80 A; R=1-429.
DR PDB; 5MPC; EM; 7.70 A; R=1-429.
DR PDB; 5MPD; EM; 4.10 A; R=1-429.
DR PDB; 5MPE; EM; 4.50 A; R=1-429.
DR PDB; 5WVI; EM; 6.30 A; R=1-429.
DR PDB; 5WVK; EM; 4.20 A; R=1-429.
DR PDB; 6FVT; EM; 4.10 A; R=20-424.
DR PDB; 6FVU; EM; 4.50 A; R=20-424.
DR PDB; 6FVV; EM; 5.40 A; R=20-424.
DR PDB; 6FVW; EM; 4.50 A; R=20-424.
DR PDB; 6FVX; EM; 4.90 A; R=20-424.
DR PDB; 6FVY; EM; 6.10 A; R=20-424.
DR PDB; 6J2C; EM; 7.00 A; R=1-429.
DR PDB; 6J2N; EM; 7.50 A; R=1-429.
DR PDB; 6J2Q; EM; 3.80 A; R=1-429.
DR PDB; 6J2X; EM; 3.80 A; R=1-429.
DR PDB; 6J30; EM; 4.50 A; R=1-429.
DR PDB; 7QO3; EM; 6.10 A; R=1-429.
DR PDB; 7QO5; EM; 6.00 A; R=1-429.
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; Q06103; -.
DR SMR; Q06103; -.
DR BioGRID; 36274; 505.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-2880N; -.
DR IntAct; Q06103; 33.
DR MINT; Q06103; -.
DR STRING; 4932.YPR108W; -.
DR iPTMnet; Q06103; -.
DR MaxQB; Q06103; -.
DR PaxDb; Q06103; -.
DR PRIDE; Q06103; -.
DR EnsemblFungi; YPR108W_mRNA; YPR108W; YPR108W.
DR GeneID; 856223; -.
DR KEGG; sce:YPR108W; -.
DR SGD; S000006312; RPN7.
DR VEuPathDB; FungiDB:YPR108W; -.
DR eggNOG; KOG0687; Eukaryota.
DR GeneTree; ENSGT00510000046608; -.
DR HOGENOM; CLU_031814_1_1_1; -.
DR InParanoid; Q06103; -.
DR OMA; SLYNCHY; -.
DR BioCyc; YEAST:G3O-34248-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:Q06103; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06103; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0005838; C:proteasome regulatory particle; IBA:GO_Central.
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:0005198; F:structural molecule activity; 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; TAS:SGD.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035268; PSMD6.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR PANTHER; PTHR14145:SF1; PTHR14145:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Phosphoprotein; Proteasome;
KW Reference proteome; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..429
FT /note="26S proteasome regulatory subunit RPN7"
FT /id="PRO_0000173845"
FT REPEAT 131..164
FT /note="TPR"
FT DOMAIN 223..395
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 8
FT /note="S -> G (in Ref. 3; AAT92788)"
FT /evidence="ECO:0000305"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 96..122
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 326..342
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:3JCK"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 396..423
FT /evidence="ECO:0007829|PDB:3JCK"
SQ SEQUENCE 429 AA; 48959 MW; B21B66CD818E636D CRC64;
MVDVEEKSQE VEYVDPTVNR VPNYEVSEKA FLLTQSKVSI EQRKEAAEFV LAKIKEEEMA
PYYKYLCEEY LVNNGQSDLE HDEKSDSLNE WIKFDQELYN ELCKKNESKI KELNEKIQKL
EEDDEGELEQ AQAWINLGEY YAQIGDKDNA EKTLGKSLSK AISTGAKIDV MLTIARLGFF
YNDQLYVKEK LEAVNSMIEK GGDWERRNRY KTYYGIHCLA VRNFKEAAKL LVDSLATFTS
IELTSYESIA TYASVTGLFT LERTDLKSKV IDSPELLSLI STTAALQSIS SLTISLYASD
YASYFPYLLE TYANVLIPCK YLNRHADFFV REMRRKVYAQ LLESYKTLSL KSMASAFGVS
VAFLDNDLGK FIPNKQLNCV IDRVNGIVET NRPDNKNAQY HLLVKQGDGL LTKLQKYGAA
VRLTGSDRV
