PRS4_YEAST
ID PRS4_YEAST Reviewed; 437 AA.
AC P40327; D6VRY1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=26S proteasome regulatory subunit 4 homolog;
DE AltName: Full=Tat-binding homolog 5;
GN Name=RPT2; Synonyms=YHS4, YTA5; OrderedLocusNames=YDL007W; ORFNames=D2920;
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 204508 / S288c;
RX PubMed=7754704; DOI=10.1002/yea.320100903;
RA Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C.,
RA Vetter I., Feldmann H.;
RT "Identification of a set of yeast genes coding for a novel family of
RT putative ATPases with high similarity to constituents of the 26S protease
RT complex.";
RL Yeast 10:1141-1155(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-229.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=7721833; DOI=10.1074/jbc.270.16.9178;
RA Lucero H.A., Chojnicki E.W.T., Mandiyan S., Nelson H., Nelson N.;
RT "Cloning and expression of a yeast gene encoding a protein with ATPase
RT activity and high identity to the subunit 4 of the human 26 S protease.";
RL J. Biol. Chem. 270:9178-9184(1995).
RN [3]
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 [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 2-11, AND MYRISTOYLATION AT GLY-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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-234; LYS-255 AND LYS-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(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: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). Has ATPase activity. {ECO:0000250}.
CC -!- INTERACTION:
CC P40327; P38764: RPN1; NbExp=6; IntAct=EBI-13901, EBI-15913;
CC P40327; P43588: RPN11; NbExp=2; IntAct=EBI-13901, EBI-11219;
CC P40327; P33299: RPT1; NbExp=8; IntAct=EBI-13901, EBI-13910;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X81070; CAA56957.1; -; Genomic_DNA.
DR EMBL; L17040; AAA97498.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88352.1; -; Genomic_DNA.
DR EMBL; Z74055; CAA98563.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11841.1; -; Genomic_DNA.
DR PIR; S46613; S46613.
DR RefSeq; NP_010277.1; NM_001180066.1.
DR PDB; 3JCO; EM; 4.80 A; I=1-437.
DR PDB; 3JCP; EM; 4.60 A; I=1-437.
DR PDB; 4CR2; EM; 7.70 A; I=1-437.
DR PDB; 4CR3; EM; 9.30 A; I=1-437.
DR PDB; 4CR4; EM; 8.80 A; I=1-437.
DR PDB; 5A5B; EM; 9.50 A; I=1-437.
DR PDB; 5MP9; EM; 4.10 A; I=1-437.
DR PDB; 5MPA; EM; 4.50 A; I=1-437.
DR PDB; 5MPB; EM; 7.80 A; I=1-437.
DR PDB; 5MPC; EM; 7.70 A; I=1-437.
DR PDB; 5WVI; EM; 6.30 A; I=1-437.
DR PDB; 5WVK; EM; 4.20 A; I=1-437.
DR PDB; 6EF0; EM; 4.43 A; I=166-436.
DR PDB; 6EF1; EM; 4.73 A; I=167-437.
DR PDB; 6EF2; EM; 4.27 A; I=178-437.
DR PDB; 6EF3; EM; 4.17 A; I=1-437.
DR PDB; 6FVT; EM; 4.10 A; I=53-437.
DR PDB; 6FVU; EM; 4.50 A; I=54-437.
DR PDB; 6FVV; EM; 5.40 A; I=53-437.
DR PDB; 6FVW; EM; 4.50 A; I=53-437.
DR PDB; 6FVX; EM; 4.90 A; I=53-437.
DR PDB; 6FVY; EM; 6.10 A; I=53-437.
DR PDB; 6J2C; EM; 7.00 A; I=1-437.
DR PDB; 6J2N; EM; 7.50 A; I=1-437.
DR PDB; 6J2Q; EM; 3.80 A; I=1-437.
DR PDB; 6J2X; EM; 3.80 A; I=1-437.
DR PDB; 6J30; EM; 4.50 A; I=1-437.
DR PDB; 7QO5; EM; 6.00 A; I=1-437.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5MP9; -.
DR PDBsum; 5MPA; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6EF0; -.
DR PDBsum; 6EF1; -.
DR PDBsum; 6EF2; -.
DR PDBsum; 6EF3; -.
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; 7QO5; -.
DR AlphaFoldDB; P40327; -.
DR SMR; P40327; -.
DR BioGRID; 32047; 377.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-6282N; -.
DR IntAct; P40327; 38.
DR MINT; P40327; -.
DR STRING; 4932.YDL007W; -.
DR iPTMnet; P40327; -.
DR MaxQB; P40327; -.
DR PaxDb; P40327; -.
DR PRIDE; P40327; -.
DR EnsemblFungi; YDL007W_mRNA; YDL007W; YDL007W.
DR GeneID; 851557; -.
DR KEGG; sce:YDL007W; -.
DR SGD; S000002165; RPT2.
DR VEuPathDB; FungiDB:YDL007W; -.
DR eggNOG; KOG0726; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; P40327; -.
DR OMA; ARCKLRY; -.
DR BioCyc; YEAST:G3O-29438-MON; -.
DR BRENDA; 5.6.1.5; 984.
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-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:P40327; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40327; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0036402; F:proteasome-activating activity; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0043171; P:peptide catabolic process; IMP:SGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:SGD.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Lipoprotein; Myristate; Nucleotide-binding; Nucleus;
KW Proteasome; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..437
FT /note="26S proteasome regulatory subunit 4 homolog"
FT /id="PRO_0000084685"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 229
FT /note="K->Q: 73% loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:7721833"
FT CONFLICT 347
FT /note="K -> N (in Ref. 2; AAA97498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48828 MW; EB735354C3A0EBD4 CRC64;
MGQGVSSGQD KKKKKGSNQK PKYEPPVQSK FGRKKRKGGP ATAEKLPNIY PSTRCKLKLL
RMERIKDHLL LEEEFVSNSE ILKPFEKKQE EEKKQLEEIR GNPLSIGTLE EIIDDDHAIV
TSPTMPDYYV SILSFVDKEL LEPGCSVLLH HKTMSIVGVL QDDADPMVSV MKMDKSPTES
YSDIGGLESQ IQEIKESVEL PLTHPELYEE MGIKPPKGVI LYGAPGTGKT LLAKAVANQT
SATFLRIVGS ELIQKYLGDG PRLCRQIFKV AGENAPSIVF IDEIDAIGTK RYDSNSGGER
EIQRTMLELL NQLDGFDDRG DVKVIMATNK IETLDPALIR PGRIDRKILF ENPDLSTKKK
ILGIHTSKMN LSEDVNLETL VTTKDDLSGA DIQAMCTEAG LLALRERRMQ VTAEDFKQAK
ERVMKNKVEE NLEGLYL
