TFC1_YEAST
ID TFC1_YEAST Reviewed; 649 AA.
AC P32367; D6VQC1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Transcription factor tau 95 kDa subunit;
DE AltName: Full=TFIIIC 95 kDa subunit;
DE AltName: Full=Transcription factor C subunit 1;
GN Name=TFC1; OrderedLocusNames=YBR123C; ORFNames=YBR0919;
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 36-48; 108-118;
RP 194-201; 246-251; 372-376; 405-422 AND 616-631.
RX PubMed=2052571; DOI=10.1073/pnas.88.11.4887;
RA Swanson R.N., Conesa C., Lefebvre O., Carles C., Ruet A., Quemeneur E.,
RA Gagnon J., Sentenac A.;
RT "Isolation of TFC1, a gene encoding one of two DNA-binding subunits of
RT yeast transcription factor tau (TFIIIC).";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4887-4891(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1737746; DOI=10.1016/s0021-9258(19)50670-6;
RA Parsons M.C., Weil P.A.;
RT "Cloning of TFC1, the Saccharomyces cerevisiae gene encoding the 95-kDa
RT subunit of transcription factor TFIIIC.";
RL J. Biol. Chem. 267:2894-2901(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
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 [6]
RP IDENTIFICATION IN TFIIIC.
RX PubMed=2180956; DOI=10.1016/s0021-9258(19)34089-x;
RA Parsons M.C., Weil P.A.;
RT "Purification and characterization of Saccharomyces cerevisiae
RT transcription factor TFIIIC. Polypeptide composition defined with
RT polyclonal antibodies.";
RL J. Biol. Chem. 265:5095-5103(1990).
RN [7]
RP FUNCTION, INTERACTION WITH TFC3; TFC4 AND TFC6, AND PHOSPHORYLATION.
RX PubMed=7688737; DOI=10.1016/s0021-9258(17)46809-8;
RA Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.;
RT "On the subunit composition, stoichiometry, and phosphorylation of the
RT yeast transcription factor TFIIIC/tau.";
RL J. Biol. Chem. 268:18047-18052(1993).
RN [8]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [9]
RP FUNCTION, INTERACTION WITH TFC3 AND TFC6, AND MUTAGENESIS OF GLU-447.
RX PubMed=12533520; DOI=10.1074/jbc.m213310200;
RA Jourdain S., Acker J., Ducrot C., Sentenac A., Lefebvre O.;
RT "The tau95 subunit of yeast TFIIIC influences upstream and downstream
RT functions of TFIIIC.DNA complexes.";
RL J. Biol. Chem. 278:10450-10457(2003).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, 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).
CC -!- FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to
CC intragenic promoter elements. Upstream of the transcription start site,
CC TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is
CC sufficient for RNA polymerase III recruitment and function. Part of the
CC tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and
CC similar genes. Participates in the interconnection of tauA with tauB
CC via its contacts with TFC3 and TFC6. Serves as a scaffold critical for
CC tauA-DNA spatial configuration and tauB-DNA stability.
CC {ECO:0000269|PubMed:12533520, ECO:0000269|PubMed:7688737}.
CC -!- SUBUNIT: Component of the TFIIIC complex composed of TFC1, TFC3, TFC4,
CC TFC6, TFC7 and TFC8. The subunits are organized in two globular
CC domains, tauA and tauB, connected by a proteolysis-sensitive and
CC flexible linker. Interacts with TFC3, TFC4 and TFC6.
CC {ECO:0000269|PubMed:12533520, ECO:0000269|PubMed:2180956,
CC ECO:0000269|PubMed:7688737}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 15800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 5 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; M63385; AAA35144.1; -; Genomic_DNA.
DR EMBL; M80922; AAA35142.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55625.1; -; Genomic_DNA.
DR EMBL; Z35992; CAA85080.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07241.1; -; Genomic_DNA.
DR PIR; A39711; A39711.
DR RefSeq; NP_009681.3; NM_001178471.3.
DR PDB; 6YJ6; EM; 3.10 A; B=1-649.
DR PDBsum; 6YJ6; -.
DR AlphaFoldDB; P32367; -.
DR SMR; P32367; -.
DR BioGRID; 32825; 205.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-2235N; -.
DR IntAct; P32367; 13.
DR MINT; P32367; -.
DR STRING; 4932.YBR123C; -.
DR iPTMnet; P32367; -.
DR MaxQB; P32367; -.
DR PaxDb; P32367; -.
DR PRIDE; P32367; -.
DR EnsemblFungi; YBR123C_mRNA; YBR123C; YBR123C.
DR GeneID; 852421; -.
DR KEGG; sce:YBR123C; -.
DR SGD; S000000327; TFC1.
DR VEuPathDB; FungiDB:YBR123C; -.
DR eggNOG; KOG2473; Eukaryota.
DR GeneTree; ENSGT00390000004458; -.
DR HOGENOM; CLU_020038_0_0_1; -.
DR InParanoid; P32367; -.
DR OMA; KYELGCM; -.
DR BioCyc; YEAST:G3O-29080-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:P32367; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32367; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IC:ComplexPortal.
DR Gene3D; 3.30.200.160; -; 1.
DR InterPro; IPR019136; TF_IIIC_su-5_HTH.
DR InterPro; IPR040454; TF_IIIC_Tfc1/Sfc1.
DR InterPro; IPR041499; Tfc1/Sfc1_N.
DR InterPro; IPR042536; TFIIIC_tauA_Sfc1.
DR PANTHER; PTHR13230; PTHR13230; 1.
DR Pfam; PF09734; Tau95; 1.
DR Pfam; PF17682; Tau95_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..649
FT /note="Transcription factor tau 95 kDa subunit"
FT /id="PRO_0000209717"
FT REPEAT 221..239
FT /note="1"
FT REPEAT 400..419
FT /note="2"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..419
FT /note="2 X repeats, Pro-rich"
FT REGION 556..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..300
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 564..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 447
FT /note="E->K: Temperature-sensitive. TFCIII-DNA complexes
FT present a shift in their 5' border, generate slow-migrating
FT TFIIIB-DNA complexes upon stripping TFIIIC by heparin or
FT heat treatment, and allow initiation at downstream sites.
FT TFIIIC-DNA complexes highly unstable at high temperatures."
FT /evidence="ECO:0000269|PubMed:12533520"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 147..159
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 181..185
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 472..490
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:6YJ6"
SQ SEQUENCE 649 AA; 73554 MW; FD39EB5E2ED4D8C6 CRC64;
MPVEEPLATL SSIPDSSADQ APPLIADEFT LDLPRIPSLE LPLNVSTKHS SIQKAIKMCG
GIEKVKEAFK EHGPIESQHG LQLYLNDDTD SDGSKSYFNE HPVIGKRVPF RDESVILKVT
MPKGTLSKNN NSVKDSIKSL KDSNKLRVTP VSIVDNTIKF REMSDFQIKL DNVPSAREFK
SSFGSLEWNN FKSFVNSVPD NDSQPQENIG NLILDRSVKI PSTDFQLPPP PKLSMVGFPL
LYKYKANPFA KKKKNGVTEV KGTYIKNYQL FVHDLSDKTV IPSQAHEQVL YDFEVAKKTK
VYPGTKSDSK FYESLEECLK ILRELFARRP IWVKRHLDGI VPKKIHHTMK IALALISYRF
TMGPWRNTYI KFGIDPRSSV EYAQYQTEYF KIERKLLSSP IVKKNVPKPP PLVFESDTPG
GIDSRFKFDG KRIPWYLMLQ IDLLIGEPNI AEVFHNVEYL DKANELTGWF KELDLVKIRR
IVKYELGCMV QGNYEYNKYK LKYFKTMLFV KESMVPENKN SEEGMGVNTN KDADGDINMD
AGSQMSSNAI EEDKGIAAGD DFDDNGAITE EPDDAALENE EMDTDQNLKV PASIDDDVDD
VDADEEEQES FDVKTASFQD IINKIAKLDP KTAETMKSEL KGFVDEVDL
