PRS7_YEAST
ID PRS7_YEAST Reviewed; 467 AA.
AC P33299; D6VX51;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=26S proteasome regulatory subunit 7 homolog;
DE AltName: Full=Protein CIM5;
DE AltName: Full=Tat-binding homolog 3;
GN Name=RPT1; Synonyms=CIM5, YTA3; OrderedLocusNames=YKL145W;
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 28383 / FL100 / VTT C-80102;
RX PubMed=8247132; DOI=10.1038/366358a0;
RA Ghislain M., Udvardy A., Mann C.;
RT "S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase.";
RL Nature 366:358-362(1993).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [6]
RP INTERACTION WITH CIC1.
RX PubMed=11500370; DOI=10.1093/emboj/20.16.4423;
RA Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
RT "Cic1, an adaptor protein specifically linking the 26S proteasome to its
RT substrate, the SCF component Cdc4.";
RL EMBO J. 20:4423-4431(2001).
RN [7]
RP BLOCKAGE OF N-TERMINUS.
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-231, AND
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 [11]
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 -!- SUBUNIT: Interacts with UBR1 and CIC1. {ECO:0000269|PubMed:10688918,
CC ECO:0000269|PubMed:11500370}.
CC -!- INTERACTION:
CC P33299; P48510: DSK2; NbExp=3; IntAct=EBI-13910, EBI-6174;
CC P33299; P38348: HSM3; NbExp=9; IntAct=EBI-13910, EBI-21152;
CC P33299; P22141: PRE1; NbExp=2; IntAct=EBI-13910, EBI-13988;
CC P33299; P32628: RAD23; NbExp=7; IntAct=EBI-13910, EBI-14668;
CC P33299; P38764: RPN1; NbExp=13; IntAct=EBI-13910, EBI-15913;
CC P33299; P43588: RPN11; NbExp=3; IntAct=EBI-13910, EBI-11219;
CC P33299; P53196: RPN14; NbExp=7; IntAct=EBI-13910, EBI-23691;
CC P33299; P40327: RPT2; NbExp=8; IntAct=EBI-13910, EBI-13901;
CC P33299; P33298: RPT3; NbExp=6; IntAct=EBI-13910, EBI-13905;
CC P33299; P53549: RPT4; NbExp=5; IntAct=EBI-13910, EBI-18520;
CC P33299; P33297: RPT5; NbExp=4; IntAct=EBI-13910, EBI-13920;
CC P33299; Q01939: RPT6; NbExp=6; IntAct=EBI-13910, EBI-13914;
CC P33299; P19812: UBR1; NbExp=2; IntAct=EBI-13910, EBI-19909;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 105 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; Z22817; CAA80470.1; -; Genomic_DNA.
DR EMBL; X73571; CAA51973.1; -; Genomic_DNA.
DR EMBL; Z28145; CAA81986.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09017.1; -; Genomic_DNA.
DR PIR; S34354; S34354.
DR RefSeq; NP_012777.1; NM_001179711.1.
DR PDB; 3JCO; EM; 4.80 A; H=1-467.
DR PDB; 3JCP; EM; 4.60 A; H=1-467.
DR PDB; 3VLF; X-ray; 3.80 A; B/D=381-467.
DR PDB; 4A3V; X-ray; 3.80 A; B/D=378-467.
DR PDB; 4CR2; EM; 7.70 A; H=1-467.
DR PDB; 4CR3; EM; 9.30 A; H=1-467.
DR PDB; 4CR4; EM; 8.80 A; H=1-467.
DR PDB; 4JPO; X-ray; 5.00 A; C/D=379-467.
DR PDB; 5A5B; EM; 9.50 A; H=1-467.
DR PDB; 5MP9; EM; 4.10 A; H=1-467.
DR PDB; 5MPA; EM; 4.50 A; H=1-467.
DR PDB; 5MPB; EM; 7.80 A; H=1-467.
DR PDB; 5MPC; EM; 7.70 A; H=1-467.
DR PDB; 5WVI; EM; 6.30 A; H=1-467.
DR PDB; 5WVK; EM; 4.20 A; H=1-467.
DR PDB; 6EF0; EM; 4.43 A; H=201-457.
DR PDB; 6EF1; EM; 4.73 A; H=194-455.
DR PDB; 6EF2; EM; 4.27 A; H=194-466.
DR PDB; 6EF3; EM; 4.17 A; H=1-467.
DR PDB; 6FVT; EM; 4.10 A; H=42-467.
DR PDB; 6FVU; EM; 4.50 A; H=42-467.
DR PDB; 6FVV; EM; 5.40 A; H=42-458.
DR PDB; 6FVW; EM; 4.50 A; H=42-467.
DR PDB; 6FVX; EM; 4.90 A; H=42-467.
DR PDB; 6FVY; EM; 6.10 A; H=42-467.
DR PDB; 6J2C; EM; 7.00 A; H=1-467.
DR PDB; 6J2N; EM; 7.50 A; H=1-467.
DR PDB; 6J2Q; EM; 3.80 A; H=1-467.
DR PDB; 6J2X; EM; 3.80 A; H=1-467.
DR PDB; 6J30; EM; 4.50 A; H=1-467.
DR PDB; 7QO5; EM; 6.00 A; H=1-467.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 3VLF; -.
DR PDBsum; 4A3V; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 4JPO; -.
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; P33299; -.
DR SMR; P33299; -.
DR BioGRID; 33991; 662.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-2883N; -.
DR IntAct; P33299; 86.
DR MINT; P33299; -.
DR STRING; 4932.YKL145W; -.
DR iPTMnet; P33299; -.
DR SWISS-2DPAGE; P33299; -.
DR MaxQB; P33299; -.
DR PaxDb; P33299; -.
DR PRIDE; P33299; -.
DR EnsemblFungi; YKL145W_mRNA; YKL145W; YKL145W.
DR GeneID; 853712; -.
DR KEGG; sce:YKL145W; -.
DR SGD; S000001628; RPT1.
DR VEuPathDB; FungiDB:YKL145W; -.
DR eggNOG; KOG0729; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_6_0_1; -.
DR InParanoid; P33299; -.
DR OMA; INGYKKF; -.
DR BioCyc; YEAST:G3O-31920-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-6798695; Neutrophil degranulation.
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:P33299; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P33299; 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:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:SGD.
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; IPI: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; IPR035245; PSMC2.
DR PANTHER; PTHR23073:SF13; PTHR23073:SF13; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..467
FT /note="26S proteasome regulatory subunit 7 homolog"
FT /id="PRO_0000084719"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 467 AA; 51983 MW; 8454BBC9D549EC5C CRC64;
MPPKEDWEKY KAPLEDDDKK PDDDKIVPLT EGDIQVLKSY GAAPYAAKLK QTENDLKDIE
ARIKEKAGVK ESDTGLAPSH LWDIMGDRQR LGEEHPLQVA RCTKIIKGNG ESDETTTDNN
NSGNSNSNSN QQSTDADEDD EDAKYVINLK QIAKFVVGLG ERVSPTDIEE GMRVGVDRSK
YNIELPLPPR IDPSVTMMTV EEKPDVTYSD VGGCKDQIEK LREVVELPLL SPERFATLGI
DPPKGILLYG PPGTGKTLCA RAVANRTDAT FIRVIGSELV QKYVGEGARM VRELFEMART
KKACIIFFDE IDAVGGARFD DGAGGDNEVQ RTMLELITQL DGFDPRGNIK VMFATNRPNT
LDPALLRPGR IDRKVEFSLP DLEGRANIFR IHSKSMSVER GIRWELISRL CPNSTGAELR
SVCTEAGMFA IRARRKVATE KDFLKAVDKV ISGYKKFSST SRYMQYN
