PRS6B_YEAST
ID PRS6B_YEAST Reviewed; 428 AA.
AC P33298; D6VT28;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=26S proteasome regulatory subunit 6B homolog;
DE AltName: Full=Protein YNT1;
DE AltName: Full=Tat-binding homolog 2;
GN Name=RPT3; Synonyms=YNT1, YTA2; OrderedLocusNames=YDR394W;
GN ORFNames=D9509.14;
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].
RX PubMed=7803857; DOI=10.1091/mbc.5.8.899;
RA Campbell C.L., Tanaka N., White K.H., Thorsness P.E.;
RT "Mitochondrial morphological and functional defects in yeast caused by yme1
RT are suppressed by mutation of a 26S protease subunit homologue.";
RL Mol. Biol. Cell 5:899-905(1994).
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 1-6, AND ACETYLATION AT MET-1.
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY
RP 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 [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: 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 P33298; P50086: NAS6; NbExp=10; IntAct=EBI-13905, EBI-14028;
CC P33298; P32628: RAD23; NbExp=2; IntAct=EBI-13905, EBI-14668;
CC P33298; P43588: RPN11; NbExp=3; IntAct=EBI-13905, EBI-11219;
CC P33298; P32496: RPN12; NbExp=3; IntAct=EBI-13905, EBI-15953;
CC P33298; Q04062: RPN9; NbExp=3; IntAct=EBI-13905, EBI-15944;
CC P33298; P33299: RPT1; NbExp=6; IntAct=EBI-13905, EBI-13910;
CC P33298; P33298: RPT3; NbExp=3; IntAct=EBI-13905, EBI-13905;
CC P33298; P53549: RPT4; NbExp=6; IntAct=EBI-13905, EBI-18520;
CC P33298; P33297: RPT5; NbExp=7; IntAct=EBI-13905, EBI-13920;
CC P33298; Q01939: RPT6; NbExp=7; IntAct=EBI-13905, EBI-13914;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- PTM: N-acetylated by NAT3. {ECO:0000269|PubMed:12504901}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X73570; CAA51972.1; -; Genomic_DNA.
DR EMBL; U06229; AAA81916.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64836.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12238.1; -; Genomic_DNA.
DR PIR; S69678; S69678.
DR RefSeq; NP_010682.3; NM_001180702.3.
DR PDB; 2DZN; X-ray; 2.20 A; B/D/F=348-428.
DR PDB; 2DZO; X-ray; 3.00 A; B/D=348-428.
DR PDB; 3JCO; EM; 4.80 A; K=1-428.
DR PDB; 3JCP; EM; 4.60 A; K=1-428.
DR PDB; 4CR2; EM; 7.70 A; K=1-428.
DR PDB; 4CR3; EM; 9.30 A; K=1-428.
DR PDB; 4CR4; EM; 8.80 A; K=1-428.
DR PDB; 5A5B; EM; 9.50 A; K=1-428.
DR PDB; 5MP9; EM; 4.10 A; K=1-428.
DR PDB; 5MPA; EM; 4.50 A; K=1-428.
DR PDB; 5MPB; EM; 7.80 A; K=1-428.
DR PDB; 5MPC; EM; 7.70 A; K=1-428.
DR PDB; 5WVI; EM; 6.30 A; K=1-428.
DR PDB; 5WVK; EM; 4.20 A; K=1-428.
DR PDB; 6EF0; EM; 4.43 A; K=157-428.
DR PDB; 6EF1; EM; 4.73 A; K=153-428.
DR PDB; 6EF2; EM; 4.27 A; K=170-428.
DR PDB; 6EF3; EM; 4.17 A; K=1-428.
DR PDB; 6FVT; EM; 4.10 A; K=35-428.
DR PDB; 6FVU; EM; 4.50 A; K=35-428.
DR PDB; 6FVV; EM; 5.40 A; K=35-428.
DR PDB; 6FVW; EM; 4.50 A; K=45-428.
DR PDB; 6FVX; EM; 4.90 A; K=35-428.
DR PDB; 6FVY; EM; 6.10 A; K=35-428.
DR PDB; 6J2C; EM; 7.00 A; K=1-428.
DR PDB; 6J2N; EM; 7.50 A; K=1-428.
DR PDB; 6J2Q; EM; 3.80 A; K=1-428.
DR PDB; 6J2X; EM; 3.80 A; K=1-428.
DR PDB; 6J30; EM; 4.50 A; K=1-428.
DR PDB; 7QO5; EM; 6.00 A; K=1-428.
DR PDBsum; 2DZN; -.
DR PDBsum; 2DZO; -.
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; P33298; -.
DR SMR; P33298; -.
DR BioGRID; 32456; 452.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1587N; -.
DR IntAct; P33298; 99.
DR MINT; P33298; -.
DR STRING; 4932.YDR394W; -.
DR iPTMnet; P33298; -.
DR MaxQB; P33298; -.
DR PaxDb; P33298; -.
DR PRIDE; P33298; -.
DR EnsemblFungi; YDR394W_mRNA; YDR394W; YDR394W.
DR GeneID; 852003; -.
DR KEGG; sce:YDR394W; -.
DR SGD; S000002802; RPT3.
DR VEuPathDB; FungiDB:YDR394W; -.
DR eggNOG; KOG0727; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P33298; -.
DR OMA; AYAAQVK; -.
DR BioCyc; YEAST:G3O-29942-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 EvolutionaryTrace; P33298; -.
DR PRO; PR:P33298; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33298; 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:0042802; F:identical protein binding; IPI:IntAct.
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; 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; 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; IPR035256; PSMC4.
DR PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR Pfam; PF00004; AAA; 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; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..428
FT /note="26S proteasome regulatory subunit 6B homolog"
FT /id="PRO_0000084697"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 342
FT /note="S -> Y (in Ref. 1; CAA51972 and 2; AAA81916)"
FT /evidence="ECO:0000305"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:2DZO"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:2DZN"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:2DZN"
SQ SEQUENCE 428 AA; 47894 MW; E12F0995A60732BD CRC64;
MEELGIVTPV EKAVEEKPAV KSYASLLAQL NGTVNNNSAL SNVNSDIYFK LKKLEKEYEL
LTLQEDYIKD EQRHLKRELK RAQEEVKRIQ SVPLVIGQFL EPIDQNTGIV SSTTGMSYVV
RILSTLDREL LKPSMSVALH RHSNALVDIL PPDSDSSISV MGENEKPDVT YADVGGLDMQ
KQEIREAVEL PLVQADLYEQ IGIDPPRGVL LYGPPGTGKT MLVKAVANST KAAFIRVNGS
EFVHKYLGEG PRMVRDVFRL ARENAPSIIF IDEVDSIATK RFDAQTGSDR EVQRILIELL
TQMDGFDQST NVKVIMATNR ADTLDPALLR PGRLDRKIEF PSLRDRRERR LIFGTIASKM
SLAPEADLDS LIIRNDSLSG AVIAAIMQEA GLRAVRKNRY VILQSDLEEA YATQVKTDNT
VDKFDFYK
