PRS8_YEAST
ID PRS8_YEAST Reviewed; 405 AA.
AC Q01939; D6VU92;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=26S proteasome regulatory subunit 8 homolog;
DE AltName: Full=Protein CIM3;
DE AltName: Full=Protein SUG1;
DE AltName: Full=Tat-binding protein TBY1;
GN Name=RPT6; Synonyms=CIM3, CRL3, SUG1, TBPY, TBY1;
GN OrderedLocusNames=YGL048C;
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].
RX PubMed=1614516; DOI=10.1038/357698a0;
RA Swaffield J.C., Bromberg J.F., Johnston S.A.;
RT "Alterations in a yeast protein resembling HIV Tat-binding protein relieve
RT requirement for an acidic activation domain in GAL4.";
RL Nature 357:698-700(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1388730; DOI=10.1089/dna.1992.11.579;
RA Goyer C., Lee H.S., Malo D., Sonenberg N.;
RT "Isolation of a yeast gene encoding a protein homologous to the human Tat-
RT binding protein TBP-1.";
RL DNA Cell Biol. 11:579-585(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [7]
RP PROTEIN SEQUENCE OF 2-9, AND ACETYLATION AT THR-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 [8]
RP CHARACTERIZATION.
RA Gerlinger U.-M., Wolf D.H., Hilt W.;
RT "The proteasome is linked to cycloheximide resistance in yeast: CRL3 is a
RT subunit of the 26S proteasome.";
RL Enzyme Protein 48:317-317(1995).
RN [9]
RP CHARACTERIZATION.
RX PubMed=8628401; DOI=10.1038/379655a0;
RA Rubin D.M., Coux O., Wefes I., Hengartner C., Young R.A., Goldberg A.L.,
RA Finley D.;
RT "Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S
RT proteasome.";
RL Nature 379:655-657(1996).
RN [10]
RP INTERACTION WITH UBR1.
RX PubMed=10688918; DOI=10.1073/pnas.060025497;
RA Xie Y., Varshavsky A.;
RT "Physical association of ubiquitin ligases and the 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000).
RN [11]
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 [12]
RP INTERACTION WITH OLA1.
RX PubMed=16284124; DOI=10.1074/mcp.m500303-mcp200;
RA Guerrero C., Tagwerker C., Kaiser P., Huang L.;
RT "An integrated mass spectrometry-based proteomic approach: quantitative
RT analysis of tandem affinity-purified in vivo cross-linked protein complexes
RT (QTAX) to decipher the 26 S proteasome-interacting network.";
RL Mol. Cell. Proteomics 5:366-378(2006).
RN [13]
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).
RN [14]
RP FUNCTION, AND INTERACTION WITH TMA17.
RX PubMed=25042801; DOI=10.1016/j.molcel.2014.06.017;
RA Hanssum A., Zhong Z., Rousseau A., Krzyzosiak A., Sigurdardottir A.,
RA Bertolotti A.;
RT "An inducible chaperone adapts proteasome assembly to stress.";
RL Mol. Cell 55:566-577(2014).
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, ECO:0000269|PubMed:25042801}.
CC -!- SUBUNIT: May form a homodimer or a heterodimer with a related family
CC member. Interacts with OLA1, TMA17, and UBR1.
CC {ECO:0000269|PubMed:10688918, ECO:0000269|PubMed:16284124,
CC ECO:0000269|PubMed:25042801}.
CC -!- INTERACTION:
CC Q01939; P31384: CCR4; NbExp=3; IntAct=EBI-13914, EBI-4396;
CC Q01939; P34909: MOT2; NbExp=2; IntAct=EBI-13914, EBI-12174;
CC Q01939; P32628: RAD23; NbExp=6; IntAct=EBI-13914, EBI-14668;
CC Q01939; P38764: RPN1; NbExp=3; IntAct=EBI-13914, EBI-15913;
CC Q01939; P43588: RPN11; NbExp=2; IntAct=EBI-13914, EBI-11219;
CC Q01939; P53196: RPN14; NbExp=9; IntAct=EBI-13914, EBI-23691;
CC Q01939; P33299: RPT1; NbExp=6; IntAct=EBI-13914, EBI-13910;
CC Q01939; P33298: RPT3; NbExp=7; IntAct=EBI-13914, EBI-13905;
CC Q01939; P53549: RPT4; NbExp=3; IntAct=EBI-13914, EBI-18520;
CC Q01939; P13393: SPT15; NbExp=2; IntAct=EBI-13914, EBI-19129;
CC Q01939; P10591: SSA1; NbExp=2; IntAct=EBI-13914, EBI-8591;
CC Q01939; P19812: UBR1; NbExp=4; IntAct=EBI-13914, EBI-19909;
CC Q01939; P33202: UFD4; NbExp=3; IntAct=EBI-13914, EBI-20010;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- MISCELLANEOUS: Present with 4700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X66400; CAA47023.1; -; Genomic_DNA.
DR EMBL; L01626; AAA35138.1; -; Genomic_DNA.
DR EMBL; Z72570; CAA96750.1; -; Genomic_DNA.
DR EMBL; AY693135; AAT93154.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08053.1; -; Genomic_DNA.
DR PIR; S64052; S64052.
DR RefSeq; NP_011467.1; NM_001180913.1.
DR PDB; 3JCO; EM; 4.80 A; J=1-405.
DR PDB; 3JCP; EM; 4.60 A; J=1-405.
DR PDB; 4CR2; EM; 7.70 A; J=1-405.
DR PDB; 4CR3; EM; 9.30 A; J=1-405.
DR PDB; 4CR4; EM; 8.80 A; J=1-405.
DR PDB; 5A5B; EM; 9.50 A; J=1-405.
DR PDB; 5MP9; EM; 4.10 A; J=1-405.
DR PDB; 5MPA; EM; 4.50 A; J=1-405.
DR PDB; 5MPB; EM; 7.80 A; J=1-405.
DR PDB; 5MPC; EM; 7.70 A; J=1-405.
DR PDB; 5WVI; EM; 6.30 A; J=1-405.
DR PDB; 5WVK; EM; 4.20 A; J=1-405.
DR PDB; 6EF0; EM; 4.43 A; J=130-405.
DR PDB; 6EF1; EM; 4.73 A; J=133-405.
DR PDB; 6EF2; EM; 4.27 A; J=144-405.
DR PDB; 6EF3; EM; 4.17 A; J=1-405.
DR PDB; 6FVT; EM; 4.10 A; J=1-405.
DR PDB; 6FVU; EM; 4.50 A; J=1-405.
DR PDB; 6FVV; EM; 5.40 A; J=1-405.
DR PDB; 6FVW; EM; 4.50 A; J=3-405.
DR PDB; 6FVX; EM; 4.90 A; J=1-405.
DR PDB; 6FVY; EM; 6.10 A; J=1-405.
DR PDB; 6J2C; EM; 7.00 A; J=1-405.
DR PDB; 6J2N; EM; 7.50 A; J=1-405.
DR PDB; 6J2Q; EM; 3.80 A; J=1-405.
DR PDB; 6J2X; EM; 3.80 A; J=1-405.
DR PDB; 6J30; EM; 4.50 A; J=1-405.
DR PDB; 7QO5; EM; 6.00 A; J=1-405.
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; Q01939; -.
DR BMRB; Q01939; -.
DR SMR; Q01939; -.
DR BioGRID; 33200; 751.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-979N; -.
DR IntAct; Q01939; 84.
DR MINT; Q01939; -.
DR STRING; 4932.YGL048C; -.
DR CarbonylDB; Q01939; -.
DR iPTMnet; Q01939; -.
DR MaxQB; Q01939; -.
DR PaxDb; Q01939; -.
DR PRIDE; Q01939; -.
DR EnsemblFungi; YGL048C_mRNA; YGL048C; YGL048C.
DR GeneID; 852834; -.
DR KEGG; sce:YGL048C; -.
DR SGD; S000003016; RPT6.
DR VEuPathDB; FungiDB:YGL048C; -.
DR eggNOG; KOG0728; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; Q01939; -.
DR OMA; TANCRVA; -.
DR BioCyc; YEAST:G3O-30558-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:Q01939; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q01939; protein.
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:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IDA:SGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IGI:SGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; 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 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 InterPro; IPR035261; PSMC5.
DR PANTHER; PTHR23073:SF102; PTHR23073:SF102; 1.
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; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..405
FT /note="26S proteasome regulatory subunit 8 homolog"
FT /id="PRO_0000084730"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CONFLICT 41
FT /note="V -> G (in Ref. 1; CAA47023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45272 MW; 9C59E92A0794F60F CRC64;
MTAAVTSSNI VLETHESGIK PYFEQKIQET ELKIRSKTEN VRRLEAQRNA LNDKVRFIKD
ELRLLQEPGS YVGEVIKIVS DKKVLVKVQP EGKYIVDVAK DINVKDLKAS QRVCLRSDSY
MLHKVLENKA DPLVSLMMVE KVPDSTYDMV GGLTKQIKEI KEVIELPVKH PELFESLGIA
QPKGVILYGP PGTGKTLLAR AVAHHTDCKF IRVSGAELVQ KYIGEGSRMV RELFVMAREH
APSIIFMDEI DSIGSTRVEG SGGGDSEVQR TMLELLNQLD GFETSKNIKI IMATNRLDIL
DPALLRPGRI DRKIEFPPPS VAARAEILRI HSRKMNLTRG INLRKVAEKM NGCSGADVKG
VCTEAGMYAL RERRIHVTQE DFELAVGKVM NKNQETAISV AKLFK
