RPC8_YEAST
ID RPC8_YEAST Reviewed; 212 AA.
AC P35718; D6VX52;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC8;
DE Short=RNA polymerase III subunit C8;
DE AltName: Full=DNA-directed RNA polymerase III 25 kDa polypeptide;
DE AltName: Full=RNA polymerase III subunit C25;
GN Name=RPC25; OrderedLocusNames=YKL144C; ORFNames=UNF1, YKL1;
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=8065349; DOI=10.1128/mcb.14.9.6164-6170.1994;
RA Sadhale P.P., Woychik N.A.;
RT "C25, an essential RNA polymerase III subunit related to the RNA polymerase
RT II subunit RPB7.";
RL Mol. Cell. Biol. 14:6164-6170(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1574929; DOI=10.1002/yea.320080309;
RA Abraham P.R., Mulder A., Van'T Riet J., Planta R.J., Raue H.A.;
RT "Molecular cloning and physical analysis of an 8.2 kb segment of chromosome
RT XI of Saccharomyces cerevisiae reveals five tightly linked genes.";
RL Yeast 8:227-238(1992).
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 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 RPC17.
RX PubMed=12482973; DOI=10.1128/mcb.23.1.195-205.2003;
RA Siaut M., Zaros C., Levivier E., Ferri M.L., Court M., Werner M.,
RA Callebaut I., Thuriaux P., Sentenac A., Conesa C.;
RT "An Rpb4/Rpb7-like complex in yeast RNA polymerase III contains the
RT orthologue of mammalian CGRP-RCP.";
RL Mol. Cell. Biol. 23:195-205(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH RPC17, AND
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
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 tRNA. The RPC25/RPC8-RPC17/RPC9
CC subcomplex may bind Pol III transcripts emerging from the adjacent exit
CC pore during elongation.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. RPC25/RPC8 and RPC17/RPC9 form a Pol III
CC subcomplex. {ECO:0000269|PubMed:16818233}.
CC -!- INTERACTION:
CC P35718; P04051: RPO31; NbExp=3; IntAct=EBI-15854, EBI-15810;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U11048; AAA20241.1; -; Genomic_DNA.
DR EMBL; Z25464; CAA80954.1; -; Genomic_DNA.
DR EMBL; Z28144; CAA81985.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09018.1; -; Genomic_DNA.
DR PIR; S37973; S37973.
DR RefSeq; NP_012778.1; NM_001179710.1.
DR PDB; 2CKZ; X-ray; 3.20 A; B/D=1-212.
DR PDB; 5FJ8; EM; 3.90 A; G=1-212.
DR PDB; 5FJ9; EM; 4.60 A; G=1-212.
DR PDB; 5FJA; EM; 4.65 A; G=1-212.
DR PDB; 6CNB; EM; 4.10 A; G=1-212.
DR PDB; 6CNC; EM; 4.10 A; G=1-212.
DR PDB; 6CND; EM; 4.80 A; G=1-212.
DR PDB; 6CNF; EM; 4.50 A; G=1-212.
DR PDB; 6EU0; EM; 4.00 A; G=1-212.
DR PDB; 6EU1; EM; 3.40 A; G=1-212.
DR PDB; 6EU2; EM; 3.40 A; G=1-212.
DR PDB; 6EU3; EM; 3.30 A; G=1-212.
DR PDB; 6F40; EM; 3.70 A; G=1-212.
DR PDB; 6F41; EM; 4.30 A; G=1-212.
DR PDB; 6F42; EM; 5.50 A; G=1-212.
DR PDB; 6F44; EM; 4.20 A; G=1-212.
DR PDB; 6TUT; EM; 3.25 A; G=1-212.
DR PDBsum; 2CKZ; -.
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; P35718; -.
DR SMR; P35718; -.
DR BioGRID; 33992; 472.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-1414N; -.
DR IntAct; P35718; 16.
DR MINT; P35718; -.
DR STRING; 4932.YKL144C; -.
DR iPTMnet; P35718; -.
DR MaxQB; P35718; -.
DR PaxDb; P35718; -.
DR PRIDE; P35718; -.
DR EnsemblFungi; YKL144C_mRNA; YKL144C; YKL144C.
DR GeneID; 853713; -.
DR KEGG; sce:YKL144C; -.
DR SGD; S000001627; RPC25.
DR VEuPathDB; FungiDB:YKL144C; -.
DR eggNOG; KOG3297; Eukaryota.
DR GeneTree; ENSGT00390000004383; -.
DR HOGENOM; CLU_073901_1_1_1; -.
DR InParanoid; P35718; -.
DR OMA; LGPTLWW; -.
DR BioCyc; YEAST:G3O-31919-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 EvolutionaryTrace; P35718; -.
DR PRO; PR:P35718; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35718; 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:0003899; F:DNA-directed 5'-3' RNA polymerase activity; 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; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013238; RNA_pol_III_Rbc25.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR004519; RNAP_E/RPC8.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF08292; RNA_pol_Rbc25; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
DR TIGRFAMs; TIGR00448; rpoE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..212
FT /note="DNA-directed RNA polymerase III subunit RPC8"
FT /id="PRO_0000073996"
FT REGION 166..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2CKZ"
SQ SEQUENCE 212 AA; 24326 MW; 7A2422D5B0CEEEC5 CRC64;
MFILSKIADL VRIPPDQFHR DTISAITHQL NNKFANKIIP NVGLCITIYD LLTVEEGQLK
PGDGSSYINV TFRAVVFKPF LGEIVTGWIS KCTAEGIKVS LLGIFDDIFI PQNMLFEGCY
YTPEESAWIW PMDEETKLYF DVNEKIRFRI EREVFVDVKP KSPKERELEE RAQLENEIEG
KNEETPQNEK PPAYALLGSC QTDGMGLVSW WE
