RPC4_YEAST
ID RPC4_YEAST Reviewed; 422 AA.
AC P25441; D6VRJ8; Q12073;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC4;
DE Short=RNA polymerase III subunit C4;
DE AltName: Full=C53;
DE AltName: Full=DNA-directed RNA polymerase III 47 kDa polypeptide;
GN Name=RPC53; Synonyms=RPC4; OrderedLocusNames=YDL150W; ORFNames=D1557;
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=1406624; DOI=10.1128/mcb.12.10.4314-4326.1992;
RA Mann C., Micouin J.-Y., Chiannilkulchai N., Treich I., Buhler J.-M.,
RA Sentenac A.;
RT "RPC53 encodes a subunit of Saccharomyces cerevisiae RNA polymerase C (III)
RT whose inactivation leads to a predominantly G1 arrest.";
RL Mol. Cell. Biol. 12:4314-4326(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(1996).
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 REVIEW ON THE RNA POL III COMPLEX.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN [6]
RP INTERACTION WITH RPC4.
RX PubMed=10393904; DOI=10.1073/pnas.96.14.7815;
RA Flores A., Briand J.-F., Gadal O., Andrau J.-C., Rubbi L., Van Mullem V.,
RA Boschiero C., Goussot M., Marck C., Carles C., Thuriaux P., Sentenac A.,
RA Werner M.;
RT "A protein-protein interaction map of yeast RNA polymerase III.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7815-7820(1999).
RN [7]
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 [8]
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 [9]
RP FUNCTION OF THE RPC53-RPC37 SUBCOMPLEX.
RX PubMed=16362040; DOI=10.1038/sj.emboj.7600915;
RA Landrieux E., Alic N., Ducrot C., Acker J., Riva M., Carles C.;
RT "A subcomplex of RNA polymerase III subunits involved in transcription
RT termination and reinitiation.";
RL EMBO J. 25:118-128(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-182; SER-224;
RP THR-228 AND THR-232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-228 AND THR-232, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-138 AND SER-224, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-138; SER-178 AND
RP SER-182, AND IDENTIFICATION BY 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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis.
CC The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator
CC recognition and reinitiation. {ECO:0000269|PubMed:16362040}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. Interacts with RPC37/RPC5. RPC53/RPC4,
CC RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex.
CC {ECO:0000269|PubMed:10393904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 998 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC4/POLR3D RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; X63501; CAA45073.1; -; Genomic_DNA.
DR EMBL; X97751; CAA66340.1; -; Genomic_DNA.
DR EMBL; Z74199; CAA98725.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11708.1; -; Genomic_DNA.
DR PIR; S67698; S67698.
DR RefSeq; NP_010131.1; NM_001180210.1.
DR PDB; 5FJ8; EM; 3.90 A; N=1-422.
DR PDB; 5FJ9; EM; 4.60 A; N=1-422.
DR PDB; 5FJA; EM; 4.65 A; N=1-422.
DR PDB; 6CNB; EM; 4.10 A; N=1-422.
DR PDB; 6CNC; EM; 4.10 A; N=1-422.
DR PDB; 6CND; EM; 4.80 A; N=1-422.
DR PDB; 6CNF; EM; 4.50 A; N=1-422.
DR PDB; 6EU0; EM; 4.00 A; N=1-422.
DR PDB; 6EU1; EM; 3.40 A; N=1-422.
DR PDB; 6EU2; EM; 3.40 A; N=1-422.
DR PDB; 6EU3; EM; 3.30 A; N=1-422.
DR PDB; 6F40; EM; 3.70 A; N=1-422.
DR PDB; 6F41; EM; 4.30 A; N=1-422.
DR PDB; 6F42; EM; 5.50 A; N=1-422.
DR PDB; 6F44; EM; 4.20 A; N=1-422.
DR PDB; 6TUT; EM; 3.25 A; N=1-422.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P25441; -.
DR SMR; P25441; -.
DR BioGRID; 31911; 171.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-1003N; -.
DR IntAct; P25441; 22.
DR MINT; P25441; -.
DR STRING; 4932.YDL150W; -.
DR iPTMnet; P25441; -.
DR MaxQB; P25441; -.
DR PaxDb; P25441; -.
DR PRIDE; P25441; -.
DR EnsemblFungi; YDL150W_mRNA; YDL150W; YDL150W.
DR GeneID; 851404; -.
DR KEGG; sce:YDL150W; -.
DR SGD; S000002309; RPC53.
DR VEuPathDB; FungiDB:YDL150W; -.
DR eggNOG; KOG3122; Eukaryota.
DR GeneTree; ENSGT00390000013948; -.
DR HOGENOM; CLU_056234_0_0_1; -.
DR InParanoid; P25441; -.
DR OMA; NADHQHI; -.
DR BioCyc; YEAST:G3O-29547-MON; -.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:P25441; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P25441; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR InterPro; IPR007811; RPC4.
DR PANTHER; PTHR13408; PTHR13408; 1.
DR Pfam; PF05132; RNA_pol_Rpc4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..422
FT /note="DNA-directed RNA polymerase III subunit RPC4"
FT /id="PRO_0000073969"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 25..29
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT CONFLICT 42
FT /note="E -> K (in Ref. 1; CAA45073)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> LGL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..285
FT /note="NA -> KR (in Ref. 1; CAA45073)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="Q -> H (in Ref. 1; CAA45073)"
FT /evidence="ECO:0000305"
FT HELIX 275..295
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6EU3"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 422 AA; 46667 MW; 206FBAC274BC72D5 CRC64;
MSSNKGNGRL PSLKDSSSNG GGSAKPSLKF KPKAVARKSK EEREAAASKV KLEEESKRGN
DKKHFNNKNK RVTGAGGQQR RMAKYLNNTH VISSGPLAAG NFVSEKGDLR RGFIKSEGSG
SSLVQKGLET IDNGAESSEN EAEDDDNEGV ASKSKKKFNM GKEFEARNLI EDEDDGESEK
SSDVDMDDEE WRSKRIEQLF PVRPVRVRHE DVETVKREIQ EALSEKPTRE PTPSVKTEPV
GTGLQSYLEE RERQVNEKLA DLGLEKEFQS VDGKEAAAEL ELLNADHQHI LRKLKKMNNK
PERFMVFQLP TRLPAFERPA VKEEKEDMET QASDPSKKKK NIKKKDTKDA LSTRELAGKV
GSIRVHKSGK LSVKIGNVVM DIGKGAETTF LQDVIALSIA DDASSAELLG RVDGKIVVTP
QI
