RPA14_YEAST
ID RPA14_YEAST Reviewed; 137 AA.
AC P50106; D6VSD7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA14;
DE Short=A14;
DE AltName: Full=DNA-directed RNA polymerase I 14 kDa polypeptide;
GN Name=RPA14; OrderedLocusNames=YDR156W; ORFNames=YD8358.11;
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 PROTEIN SEQUENCE OF 17-22; 44-51 AND
RP 95-112.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7768955; DOI=10.1074/jbc.270.22.13534;
RA Smid A., Riva M., Bouet F., Sentenac A., Carles C.;
RT "The association of three subunits with yeast RNA polymerase is stabilized
RT by A14.";
RL J. Biol. Chem. 270:13534-13540(1995).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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).
RN [8]
RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [9]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x;
RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
RT "Rpa12p, a conserved RNA polymerase I subunit with two functional
RT domains.";
RL Mol. Microbiol. 43:1105-1113(2002).
RN [10]
RP INTERACTION WITH RPA43.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [11]
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 [12]
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 [13]
RP FUNCTION.
RX PubMed=12888498; DOI=10.1093/nar/gkg652;
RA Meka H., Daoust G., Arnvig K.B., Werner F., Brick P., Onesti S.;
RT "Structural and functional homology between the RNAP(I) subunits A14/A43
RT and the archaeal RNAP subunits E/F.";
RL Nucleic Acids Res. 31:4391-4400(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-112, STRUCTURE BY ELECTRON
RP MICROSCOPY (12.00 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. RPA14 seems to play a role in the stability of subunits
CC RPO26 and RPA43. In vitro, the RPA14-RPA43 subcomplex binds single-
CC stranded RNA. {ECO:0000269|PubMed:12888498,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. {ECO:0000269|PubMed:11918799,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- INTERACTION:
CC P50106; P46669: RPA43; NbExp=2; IntAct=EBI-15750, EBI-15745;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U23208; AAA70171.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90377.1; -; Genomic_DNA.
DR EMBL; AY557664; AAS55990.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11997.1; -; Genomic_DNA.
DR PIR; S57981; S57981.
DR RefSeq; NP_010440.1; NM_001180463.1.
DR PDB; 2RF4; X-ray; 3.10 A; B/D/F=1-112.
DR PDB; 4C2M; X-ray; 2.80 A; D/S=1-137.
DR PDB; 4C3H; X-ray; 3.27 A; D=1-137.
DR PDB; 4C3I; X-ray; 3.00 A; D=1-137.
DR PDB; 4C3J; X-ray; 3.35 A; D=1-137.
DR PDB; 4YM7; X-ray; 5.50 A; AD/BD/CD/DD/ED/FD=1-137.
DR PDB; 5G5L; EM; 4.80 A; D=1-137.
DR PDB; 5LMX; EM; 4.90 A; D=1-137.
DR PDB; 5M3F; EM; 3.80 A; D=1-137.
DR PDB; 5M3M; EM; 4.00 A; D=1-137.
DR PDB; 5M5W; EM; 3.80 A; D=1-137.
DR PDB; 5M5X; EM; 4.00 A; D=1-137.
DR PDB; 5M5Y; EM; 4.00 A; D=1-137.
DR PDB; 5M64; EM; 4.60 A; D=1-137.
DR PDB; 5N5Y; EM; 7.70 A; D=1-137.
DR PDB; 5N5Z; EM; 7.70 A; D=1-137.
DR PDB; 5N60; EM; 7.70 A; D=1-137.
DR PDB; 5N61; EM; 3.40 A; D=1-137.
DR PDB; 5OA1; EM; 4.40 A; D=1-137.
DR PDB; 5W5Y; EM; 3.80 A; D=1-137.
DR PDB; 5W64; EM; 4.20 A; D=1-137.
DR PDB; 5W65; EM; 4.30 A; D=1-137.
DR PDB; 5W66; EM; 3.90 A; D=1-137.
DR PDB; 6H67; EM; 3.60 A; D=1-137.
DR PDB; 6H68; EM; 4.60 A; D=1-137.
DR PDB; 6HKO; EM; 3.42 A; D=1-137.
DR PDB; 6HLQ; EM; 3.18 A; D=1-137.
DR PDB; 6HLR; EM; 3.18 A; D=1-137.
DR PDB; 6HLS; EM; 3.21 A; D=1-137.
DR PDB; 6RQH; EM; 3.70 A; D=1-137.
DR PDB; 6RQL; EM; 2.90 A; D=1-137.
DR PDB; 6RQT; EM; 4.00 A; D=1-137.
DR PDB; 6RRD; EM; 3.10 A; D=1-137.
DR PDB; 6RUI; EM; 2.70 A; D=1-137.
DR PDB; 6RUO; EM; 3.50 A; D=1-137.
DR PDB; 6RWE; EM; 3.00 A; D=1-137.
DR PDB; 6TPS; EM; 3.54 A; D=1-137.
DR PDBsum; 2RF4; -.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P50106; -.
DR SMR; P50106; -.
DR BioGRID; 32208; 436.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-2053N; -.
DR IntAct; P50106; 2.
DR MINT; P50106; -.
DR STRING; 4932.YDR156W; -.
DR iPTMnet; P50106; -.
DR MaxQB; P50106; -.
DR PaxDb; P50106; -.
DR PRIDE; P50106; -.
DR EnsemblFungi; YDR156W_mRNA; YDR156W; YDR156W.
DR GeneID; 851734; -.
DR KEGG; sce:YDR156W; -.
DR SGD; S000002563; RPA14.
DR VEuPathDB; FungiDB:YDR156W; -.
DR eggNOG; ENOG502S8XT; Eukaryota.
DR HOGENOM; CLU_132185_0_0_1; -.
DR InParanoid; P50106; -.
DR OMA; MISIDTT; -.
DR BioCyc; YEAST:G3O-29748-MON; -.
DR EvolutionaryTrace; P50106; -.
DR PRO; PR:P50106; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P50106; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR DisProt; DP00884; -.
DR InterPro; IPR013239; RNA_polI_Rpa14.
DR Pfam; PF08203; RNA_polI_A14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Transcription.
FT CHAIN 1..137
FT /note="DNA-directed RNA polymerase I subunit RPA14"
FT /id="PRO_0000073962"
FT REGION 100..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 7..11
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2RF4"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6HKO"
SQ SEQUENCE 137 AA; 14585 MW; D2318636ABDE68B9 CRC64;
MMKGSRRTGN NTATTLNTPV VIHATQLPQH VSTDEVLQFL ESFIDEKENI IDSTTMNTIS
GNAADADAAA VANTSLNIDT NLSSSISQLK RIQRDFKGLP PAQDFSAAPI QVSTTEKKET
SIGVSATGGK KTTFADE
