RPC3_YEAST
ID RPC3_YEAST Reviewed; 654 AA.
AC P32349; D6W4J0; Q06591;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC3;
DE Short=RNA polymerase III subunit C3;
DE AltName: Full=C82;
DE AltName: Full=DNA-directed III 74 kDa polypeptide;
DE Short=C74;
GN Name=RPC82; Synonyms=RPC3; OrderedLocusNames=YPR190C; ORFNames=P9677.11;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1406632; DOI=10.1128/mcb.12.10.4433-4440.1992;
RA Chiannilkulchai N., Stalder R., Riva M., Carles C., Werner M., Sentenac A.;
RT "RPC82 encodes the highly conserved, third-largest subunit of RNA
RT polymerase C (III) from Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:4433-4440(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP 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 core component of RNA polymerase III which synthesizes small
CC RNAs, such as 5S rRNA and tRNAs.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits.
CC -!- INTERACTION:
CC P32349; P32910: RPC34; NbExp=3; IntAct=EBI-15821, EBI-15835;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; X63500; CAA45072.1; -; Genomic_DNA.
DR EMBL; U25841; AAB64619.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11606.1; -; Genomic_DNA.
DR PIR; S58820; S58820.
DR RefSeq; NP_015516.1; NM_001184287.1.
DR PDB; 5FJ8; EM; 3.90 A; O=1-654.
DR PDB; 5FJ9; EM; 4.60 A; O=1-654.
DR PDB; 5FJA; EM; 4.65 A; O=1-654.
DR PDB; 6CNB; EM; 4.10 A; O=1-654.
DR PDB; 6CNC; EM; 4.10 A; O=1-654.
DR PDB; 6CND; EM; 4.80 A; O=1-654.
DR PDB; 6CNF; EM; 4.50 A; O=1-654.
DR PDB; 6EU0; EM; 4.00 A; O=1-654.
DR PDB; 6EU1; EM; 3.40 A; O=1-654.
DR PDB; 6EU2; EM; 3.40 A; O=1-654.
DR PDB; 6EU3; EM; 3.30 A; O=1-654.
DR PDB; 6F40; EM; 3.70 A; O=1-654.
DR PDB; 6F41; EM; 4.30 A; O=1-654.
DR PDB; 6F42; EM; 5.50 A; O=1-654.
DR PDB; 6F44; EM; 4.20 A; O=1-654.
DR PDB; 6TUT; EM; 3.25 A; O=1-654.
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; P32349; -.
DR SMR; P32349; -.
DR BioGRID; 36362; 605.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-934N; -.
DR IntAct; P32349; 22.
DR MINT; P32349; -.
DR STRING; 4932.YPR190C; -.
DR iPTMnet; P32349; -.
DR MaxQB; P32349; -.
DR PaxDb; P32349; -.
DR PRIDE; P32349; -.
DR EnsemblFungi; YPR190C_mRNA; YPR190C; YPR190C.
DR GeneID; 856320; -.
DR KEGG; sce:YPR190C; -.
DR SGD; S000006394; RPC82.
DR VEuPathDB; FungiDB:YPR190C; -.
DR eggNOG; KOG2587; Eukaryota.
DR GeneTree; ENSGT00390000002799; -.
DR HOGENOM; CLU_010734_0_0_1; -.
DR InParanoid; P32349; -.
DR OMA; QLKMVNE; -.
DR BioCyc; YEAST:G3O-34313-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:P32349; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32349; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003697; F:single-stranded 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 Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH.
DR InterPro; IPR008806; RNA_pol_III_Rpc82_C.
DR InterPro; IPR039748; RPC3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12949; PTHR12949; 1.
DR Pfam; PF08221; HTH_9; 1.
DR Pfam; PF05645; RNA_pol_Rpc82; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Zinc.
FT CHAIN 1..654
FT /note="DNA-directed RNA polymerase III subunit RPC3"
FT /id="PRO_0000073966"
FT REGION 381..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..602
FT /note="Leucine-zipper"
FT COMPBIAS 429..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 637
FT /note="V -> L (in Ref. 1; CAA45072)"
FT /evidence="ECO:0000305"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 234..257
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 469..477
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 484..499
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 519..525
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 570..598
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 600..608
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 621..648
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 649..652
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 654 AA; 74017 MW; B39FA74F4A18BADE CRC64;
MDELLGEALS AENQTGESTV ESEKLVTPED VMTISSLEQR TLNPDLFLYK ELVKAHLGER
AASVIGMLVA LGRLSVRELV EKIDGMDVDS VKTTLVSLTQ LRCVKYLQET AISGKKTTYY
YYNEEGIHIL LYSGLIIDEI ITQMRVNDEE EHKQLVAEIV QNVISLGSLT VEDYLSSVTS
DSMKYTISSL FVQLCEMGYL IQISKLHYTP IEDLWQFLYE KHYKNIPRNS PLSDLKKRSQ
AKMNAKTDFA KIINKPNELS QILTVDPKTS LRIVKPTVSL TINLDRFMKG RRSKQLINLA
KTRVGSVTAQ VYKIALRLTE QKSPKIRDPL TQTGLLQDLE EAKSFQDEAE LVEEKTPGLT
FNAIDLARHL PAELDLRGSL LSRKPSDNKK RSGSNAAASL PSKKLKTEDG FVIPALPAAV
SKSLQESGDT QEEDEEEEDL DADTEDPHSA SLINSHLKIL ASSNFPFLNE TKPGVYYVPY
SKLMPVLKSS VYEYVIASTL GPSAMRLSRC IRDNKLVSEK IINSTALMKE KDIRSTLASL
IRYNSVEIQE VPRTADRSAS RAVFLFRCKE THSYNFMRQN LEWNMANLLF KKEKLKQENS
TLLKKANRDD VKGRENELLL PSELNQLKMV NERELNVFAR LSRLLSLWEV FQMA
