PRS10_YEAST
ID PRS10_YEAST Reviewed; 437 AA.
AC P53549; D6W2W0; Q08718;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=26S proteasome subunit RPT4;
DE AltName: Full=26S protease subunit SUG2;
DE AltName: Full=Proteasomal cap subunit;
GN Name=RPT4; Synonyms=CRL13, PCS1, SUG2; OrderedLocusNames=YOR259C;
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=8955118; DOI=10.1074/jbc.271.51.32810;
RA Russell S.J., Sathyanarayana U.G., Johnston S.A.;
RT "Isolation and characterization of SUG2. A novel ATPase family component of
RT the yeast 26 S proteasome.";
RL J. Biol. Chem. 271:32810-32817(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9151663; DOI=10.1083/jcb.137.3.539;
RA McDonald H.B., Byers B.;
RT "A proteasome cap subunit required for spindle pole body duplication in
RT yeast.";
RL J. Cell Biol. 137:539-553(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(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 2-10, AND ACETYLATION AT SER-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 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 P53549; P43588: RPN11; NbExp=3; IntAct=EBI-18520, EBI-11219;
CC P53549; P33299: RPT1; NbExp=5; IntAct=EBI-18520, EBI-13910;
CC P53549; P33298: RPT3; NbExp=6; IntAct=EBI-18520, EBI-13905;
CC P53549; P33297: RPT5; NbExp=10; IntAct=EBI-18520, EBI-13920;
CC P53549; Q01939: RPT6; NbExp=3; IntAct=EBI-18520, EBI-13914;
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; U43720; AAA85134.1; -; Genomic_DNA.
DR EMBL; U93262; AAB51594.1; -; Genomic_DNA.
DR EMBL; Z75167; CAA99481.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11026.1; -; Genomic_DNA.
DR PIR; S67156; S67156.
DR RefSeq; NP_014902.3; NM_001183678.3.
DR PDB; 3JCO; EM; 4.80 A; L=1-437.
DR PDB; 3JCP; EM; 4.60 A; L=1-437.
DR PDB; 4CR2; EM; 7.70 A; L=1-437.
DR PDB; 4CR3; EM; 9.30 A; L=1-437.
DR PDB; 4CR4; EM; 8.80 A; L=1-437.
DR PDB; 5A5B; EM; 9.50 A; L=1-437.
DR PDB; 5MP9; EM; 4.10 A; L=1-437.
DR PDB; 5MPA; EM; 4.50 A; L=1-437.
DR PDB; 5MPB; EM; 7.80 A; L=1-437.
DR PDB; 5MPC; EM; 7.70 A; L=1-437.
DR PDB; 5WVI; EM; 6.30 A; L=1-437.
DR PDB; 5WVK; EM; 4.20 A; L=1-437.
DR PDB; 6EF0; EM; 4.43 A; L=164-436.
DR PDB; 6EF1; EM; 4.73 A; L=166-436.
DR PDB; 6EF2; EM; 4.27 A; L=166-429.
DR PDB; 6EF3; EM; 4.17 A; L=1-437.
DR PDB; 6FVT; EM; 4.10 A; L=49-436.
DR PDB; 6FVU; EM; 4.50 A; L=49-436.
DR PDB; 6FVV; EM; 5.40 A; L=49-436.
DR PDB; 6FVW; EM; 4.50 A; L=49-436.
DR PDB; 6FVX; EM; 4.90 A; L=49-436.
DR PDB; 6FVY; EM; 6.10 A; L=49-436.
DR PDB; 6J2C; EM; 7.00 A; L=1-437.
DR PDB; 6J2N; EM; 7.50 A; L=1-437.
DR PDB; 6J2Q; EM; 3.80 A; L=1-437.
DR PDB; 6J2X; EM; 3.80 A; L=1-437.
DR PDB; 6J30; EM; 4.50 A; L=1-437.
DR PDB; 7QO5; EM; 6.00 A; L=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; P53549; -.
DR SMR; P53549; -.
DR BioGRID; 34649; 842.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1589N; -.
DR IntAct; P53549; 52.
DR MINT; P53549; -.
DR STRING; 4932.YOR259C; -.
DR iPTMnet; P53549; -.
DR MaxQB; P53549; -.
DR PaxDb; P53549; -.
DR PRIDE; P53549; -.
DR EnsemblFungi; YOR259C_mRNA; YOR259C; YOR259C.
DR GeneID; 854433; -.
DR KEGG; sce:YOR259C; -.
DR SGD; S000005785; RPT4.
DR VEuPathDB; FungiDB:YOR259C; -.
DR eggNOG; KOG0651; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_2_1; -.
DR InParanoid; P53549; -.
DR OMA; YNMTTFE; -.
DR BioCyc; YEAST:G3O-33750-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:P53549; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P53549; protein.
DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
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; ISS:SGD.
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:0006289; P:nucleotide-excision repair; IGI: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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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; Acetylation; ATP-binding; Direct protein sequencing;
KW Nucleotide-binding; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..437
FT /note="26S proteasome subunit RPT4"
FT /id="PRO_0000084737"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CONFLICT 121
FT /note="A -> P (in Ref. 1; AAA85134)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="V -> A (in Ref. 1; AAA85134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49408 MW; 0EA42A599E2B2E2A CRC64;
MSEEQDPLLA GLGETSGDNH TQQSHEQQPE QPQETEEHHE EEPSRVDPEQ EAHNKALNQF
KRKLLEHRRY DDQLKQRRQN IRDLEKLYDK TENDIKALQS IGQLIGEVMK ELSEEKYIVK
ASSGPRYIVG VRNSVDRSKL KKGVRVTLDI TTLTIMRILP RETDPLVYNM TSFEQGEITF
DGIGGLTEQI RELREVIELP LKNPEIFQRV GIKPPKGVLL YGPPGTGKTL LAKAVAATIG
ANFIFSPASG IVDKYIGESA RIIREMFAYA KEHEPCIIFM DEVDAIGGRR FSEGTSADRE
IQRTLMELLT QMDGFDNLGQ TKIIMATNRP DTLDPALLRP GRLDRKVEIP LPNEAGRLEI
FKIHTAKVKK TGEFDFEAAV KMSDGFNGAD IRNCATEAGF FAIRDDRDHI NPDDLMKAVR
KVAEVKKLEG TIEYQKL
