ID PRS6A_YEAST Reviewed; 434 AA.
AC P33297; D6W2H6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 209.
DE RecName: Full=26S proteasome regulatory subunit 6A;
DE AltName: Full=Tat-binding protein homolog 1;
DE Short=TBP-1;
GN Name=RPT5; Synonyms=YTA1; OrderedLocusNames=YOR117W;
GN ORFNames=O3258, YOR3258W;
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=C836;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-9, AND ACETYLATION AT ALA-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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND IDENTIFICATION BY
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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: 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). {ECO:0000250}.
CC -!- INTERACTION:
CC P33297; P38348: HSM3; NbExp=6; IntAct=EBI-13920, EBI-21152;
CC P33297; P40555: NAS2; NbExp=8; IntAct=EBI-13920, EBI-14024;
CC P33297; P38764: RPN1; NbExp=4; IntAct=EBI-13920, EBI-15913;
CC P33297; P38886: RPN10; NbExp=2; IntAct=EBI-13920, EBI-15949;
CC P33297; P53196: RPN14; NbExp=5; IntAct=EBI-13920, EBI-23691;
CC P33297; P33299: RPT1; NbExp=5; IntAct=EBI-13920, EBI-13910;
CC P33297; P33298: RPT3; NbExp=6; IntAct=EBI-13920, EBI-13905;
CC P33297; P53549: RPT4; NbExp=10; IntAct=EBI-13920, EBI-18520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
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; X73569; CAA51971.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62114.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64037.1; -; Genomic_DNA.
DR EMBL; Z75025; CAA99315.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10892.1; -; Genomic_DNA.
DR PIR; S46605; S46605.
DR RefSeq; NP_014760.3; NM_001183536.3.
DR PDB; 3JCO; EM; 4.80 A; M=1-434.
DR PDB; 3JCP; EM; 4.60 A; M=1-434.
DR PDB; 3WHK; X-ray; 2.60 A; A/B/C/D/E/F/G/H=356-434.
DR PDB; 3WHL; X-ray; 4.00 A; A/C/E/G=356-434.
DR PDB; 4CR2; EM; 7.70 A; M=1-434.
DR PDB; 4CR3; EM; 9.30 A; M=1-434.
DR PDB; 4CR4; EM; 8.80 A; M=1-434.
DR PDB; 5A5B; EM; 9.50 A; M=1-434.
DR PDB; 5MP9; EM; 4.10 A; M=1-434.
DR PDB; 5MPA; EM; 4.50 A; M=1-434.
DR PDB; 5MPB; EM; 7.80 A; M=1-434.
DR PDB; 5MPC; EM; 7.70 A; M=1-434.
DR PDB; 5WVI; EM; 6.30 A; M=1-434.
DR PDB; 5WVK; EM; 4.20 A; M=1-434.
DR PDB; 6EF0; EM; 4.43 A; M=176-433.
DR PDB; 6EF1; EM; 4.73 A; M=173-434.
DR PDB; 6EF2; EM; 4.27 A; M=165-434.
DR PDB; 6EF3; EM; 4.17 A; M=1-434.
DR PDB; 6FVT; EM; 4.10 A; M=14-434.
DR PDB; 6FVU; EM; 4.50 A; M=14-434.
DR PDB; 6FVV; EM; 5.40 A; M=14-434.
DR PDB; 6FVW; EM; 4.50 A; M=14-434.
DR PDB; 6FVX; EM; 4.90 A; M=14-434.
DR PDB; 6FVY; EM; 6.10 A; M=14-434.
DR PDB; 6J2C; EM; 7.00 A; M=1-434.
DR PDB; 6J2N; EM; 7.50 A; M=1-434.
DR PDB; 6J2Q; EM; 3.80 A; M=1-434.
DR PDB; 6J2X; EM; 3.80 A; M=1-434.
DR PDB; 6J30; EM; 4.50 A; M=1-434.
DR PDB; 7QO4; EM; 7.00 A; M=1-434.
DR PDB; 7QO5; EM; 6.00 A; M=1-434.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 3WHK; -.
DR PDBsum; 3WHL; -.
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; 7QO4; -.
DR PDBsum; 7QO5; -.
DR AlphaFoldDB; P33297; -.
DR EMDB; EMD-14084; -.
DR EMDB; EMD-3534; -.
DR EMDB; EMD-3535; -.
DR EMDB; EMD-4321; -.
DR EMDB; EMD-4322; -.
DR EMDB; EMD-4323; -.
DR EMDB; EMD-4324; -.
DR EMDB; EMD-9042; -.
DR EMDB; EMD-9043; -.
DR EMDB; EMD-9044; -.
DR EMDB; EMD-9045; -.
DR EMDB; EMD-9772; -.
DR EMDB; EMD-9773; -.
DR SMR; P33297; -.
DR BioGRID; 34513; 755.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1590N; -.
DR IntAct; P33297; 42.
DR MINT; P33297; -.
DR STRING; 4932.YOR117W; -.
DR iPTMnet; P33297; -.
DR MaxQB; P33297; -.
DR PaxDb; 4932-YOR117W; -.
DR PeptideAtlas; P33297; -.
DR EnsemblFungi; YOR117W_mRNA; YOR117W; YOR117W.
DR GeneID; 854284; -.
DR KEGG; sce:YOR117W; -.
DR AGR; SGD:S000005643; -.
DR SGD; S000005643; RPT5.
DR VEuPathDB; FungiDB:YOR117W; -.
DR eggNOG; KOG0652; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_4_1; -.
DR InParanoid; P33297; -.
DR OMA; NKISHEH; -.
DR OrthoDB; 1707207at2759; -.
DR BioCyc; YEAST:G3O-33646-MONOMER; -.
DR BRENDA; 5.6.1.5; 984.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 854284; 7 hits in 10 CRISPR screens.
DR PRO; PR:P33297; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33297; Protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; ISS:SGD.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IMP: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:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Proteasome; 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 6A"
FT /id="PRO_0000084708"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12504901,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 180
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:3WHK"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 388..404
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:3WHK"
SQ SEQUENCE 434 AA; 48256 MW; C215422033FCE830 CRC64;
MATLEELDAQ TLPGDDELDQ EILNLSTQEL QTRAKLLDNE IRIFRSELQR LSHENNVMLE
KIKDNKEKIK NNRQLPYLVA NVVEVMDMNE IEDKENSEST TQGGNVNLDN TAVGKAAVVK
TSSRQTVFLP MVGLVDPDKL KPNDLVGVNK DSYLILDTLP SEFDSRVKAM EVDEKPTETY
SDVGGLDKQI EELVEAIVLP MKRADKFKDM GIRAPKGALM YGPPGTGKTL LARACAAQTN
ATFLKLAAPQ LVQMYIGEGA KLVRDAFALA KEKAPTIIFI DELDAIGTKR FDSEKSGDRE
VQRTMLELLN QLDGFSSDDR VKVLAATNRV DVLDPALLRS GRLDRKIEFP LPSEDSRAQI
LQIHSRKMTT DDDINWQELA RSTDEFNGAQ LKAVTVEAGM IALRNGQSSV KHEDFVEGIS
EVQARKSKSV SFYA
//
