TFC3_YEAST
ID TFC3_YEAST Reviewed; 1160 AA.
AC P34111; D6VPL5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Transcription factor tau 138 kDa subunit;
DE AltName: Full=TFIIIC 138 kDa subunit;
DE AltName: Full=Transcription factor C subunit 3;
GN Name=TFC3; Synonyms=TSV115; OrderedLocusNames=YAL001C; ORFNames=FUN24;
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], PROTEIN SEQUENCE OF 124-143; 331-347;
RP 440-453; 508-520 AND 539-547, FUNCTION, AND IDENTIFICATION IN TFIIIC.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1279682; DOI=10.1073/pnas.89.21.10512;
RA Lefebvre O., Carles C., Conesa C., Swanson R.N., Bouet F., Riva M.,
RA Sentenac A.;
RT "TFC3: gene encoding the B-block binding subunit of the yeast transcription
RT factor IIIC.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10512-10516(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-349.
RX PubMed=8083243; DOI=10.1016/s0021-9258(17)31663-0;
RA Lefebvre O., Rueth J., Sentenac A.;
RT "A mutation in the largest subunit of yeast TFIIIC affects tRNA and 5 S RNA
RT synthesis. Identification of two classes of suppressors.";
RL J. Biol. Chem. 269:23374-23381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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 FUNCTION.
RX PubMed=2651441; DOI=10.1016/s0021-9258(18)83263-x;
RA Gabrielsen O.S., Marzouki N., Ruet A., Sentenac A., Fromageot P.;
RT "Two polypeptide chains in yeast transcription factor tau interact with
RT DNA.";
RL J. Biol. Chem. 264:7505-7511(1989).
RN [7]
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 [8]
RP INTERACTION WITH TFC1; 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 [9]
RP FUNCTION.
RX PubMed=9418847; DOI=10.1128/mcb.18.1.1;
RA Arrebola R., Manaud N., Rozenfeld S., Marsolier M.C., Lefebvre O.,
RA Carles C., Thuriaux P., Conesa C., Sentenac A.;
RT "Tau91, an essential subunit of yeast transcription factor IIIC, cooperates
RT with tau138 in DNA binding.";
RL Mol. Cell. Biol. 18:1-9(1998).
RN [10]
RP INTERACTION WITH TFC1 AND TFC6.
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, 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 tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and
CC similar genes. TFC3 is essential for cell viability. Cooperates with
CC TFC6 in DNA binding. {ECO:0000269|PubMed:1279682,
CC ECO:0000269|PubMed:2651441, ECO:0000269|PubMed:9418847}.
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 TFC1, TFC4 and TFC6.
CC {ECO:0000269|PubMed:12533520, ECO:0000269|PubMed:1279682,
CC ECO:0000269|PubMed:2180956, ECO:0000269|PubMed:7688737}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M98261; AAA34378.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04956.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06985.1; -; Genomic_DNA.
DR PIR; A46423; A46423.
DR RefSeq; NP_009400.1; NM_001178148.1.
DR PDB; 5AIM; X-ray; 1.40 A; A/B=546-641.
DR PDBsum; 5AIM; -.
DR AlphaFoldDB; P34111; -.
DR SMR; P34111; -.
DR BioGRID; 31789; 174.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-6739N; -.
DR IntAct; P34111; 3.
DR MINT; P34111; -.
DR STRING; 4932.YAL001C; -.
DR iPTMnet; P34111; -.
DR MaxQB; P34111; -.
DR PaxDb; P34111; -.
DR PRIDE; P34111; -.
DR EnsemblFungi; YAL001C_mRNA; YAL001C; YAL001C.
DR GeneID; 851262; -.
DR KEGG; sce:YAL001C; -.
DR SGD; S000000001; TFC3.
DR VEuPathDB; FungiDB:YAL001C; -.
DR eggNOG; ENOG502QVPM; Eukaryota.
DR HOGENOM; CLU_005481_0_0_1; -.
DR InParanoid; P34111; -.
DR OMA; YKGHVVK; -.
DR BioCyc; YEAST:G3O-28816-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:P34111; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P34111; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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:0071168; P:protein localization to chromatin; IMP: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; IBA:GO_Central.
DR CDD; cd16169; Tau138_eWH; 1.
DR InterPro; IPR044210; Tfc3-like.
DR InterPro; IPR035625; Tfc3_eWH.
DR InterPro; IPR007309; TFIIIC_Bblock-bd.
DR PANTHER; PTHR15180; PTHR15180; 2.
DR Pfam; PF04182; B-block_TFIIIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1160
FT /note="Transcription factor tau 138 kDa subunit"
FT /id="PRO_0000072497"
FT REGION 475..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 349
FT /note="G->E: In TSV115; thermosensitive. Level of TFIIIC
FT and its affinity for tDNA reduced. tDNA binding activity
FT very sensitive to mild heat treatments, and TFIIIC-DNA
FT interaction inhibited at moderate salt concentrations."
FT /evidence="ECO:0000269|PubMed:8083243"
FT HELIX 546..565
FT /evidence="ECO:0007829|PDB:5AIM"
FT STRAND 568..573
FT /evidence="ECO:0007829|PDB:5AIM"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:5AIM"
FT HELIX 593..604
FT /evidence="ECO:0007829|PDB:5AIM"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:5AIM"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:5AIM"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:5AIM"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:5AIM"
SQ SEQUENCE 1160 AA; 132108 MW; 3ACB7893ED536581 CRC64;
MVLTIYPDEL VQIVSDKIAS NKGKITLNQL WDISGKYFDL SDKKVKQFVL SCVILKKDIE
VYCDGAITTK NVTDIIGDAN HSYSVGITED SLWTLLTGYT KKESTIGNSA FELLLEVAKS
GEKGINTMDL AQVTGQDPRS VTGRIKKINH LLTSSQLIYK GHVVKQLKLK KFSHDGVDSN
PYINIRDHLA TIVEVVKRSK NGIRQIIDLK RELKFDKEKR LSKAFIAAIA WLDEKEYLKK
VLVVSPKNPA IKIRCVKYVK DIPDSKGSPS FEYDSNSADE DSVSDSKAAF EDEDLVEGLD
NFNATDLLQN QGLVMEEKED AVKNEVLLNR FYPLQNQTYD IADKSGLKGI STMDVVNRIT
GKEFQRAFTK SSEYYLESVD KQKENTGGYR LFRIYDFEGK KKFFRLFTAQ NFQKLTNAED
EISVPKGFDE LGKSRTDLKT LNEDNFVALN NTVRFTTDSD GQDIFFWHGE LKIPPNSKKT
PNKNKRKRQV KNSTNASVAG NISNPKRIKL EQHVSTAQEP KSAEDSPSSN GGTVVKGKVV
NFGGFSARSL RSLQRQRAIL KVMNTIGGVA YLREQFYESV SKYMGSTTTL DKKTVRGDVD
LMVESEKLGA RTEPVSGRKI IFLPTVGEDA IQRYILKEKD SKKATFTDVI HDTEIYFFDQ
TEKNRFHRGK KSVERIRKFQ NRQKNAKIKA SDDAISKKST SVNVSDGKIK RRDKKVSAGR
TTVVVENTKE DKTVYHAGTK DGVQALIRAV VVTKSIKNEI MWDKITKLFP NNSLDNLKKK
WTARRVRMGH SGWRAYVDKW KKMLVLAIKS EKISLRDVEE LDLIKLLDIW TSFDEKEIKR
PLFLYKNYEE NRKKFTLVRD DTLTHSGNDL AMSSMIQREI SSLKKTYTRK ISASTKDLSK
SQSDDYIRTV IRSILIESPS TTRNEIEALK NVGNESIDNV IMDMAKEKQI YLHGSKLECT
DTLPDILENR GNYKDFGVAF QYRCKVNELL EAGNAIVINQ EPSDISSWVL IDLISGELLN
MDVIPMVRNV RPLTYTSRRF EIRTLTPPLI IYANSQTKLN TARKSAVKVP LGKPFSRLWV
NGSGSIRPNI WKQVVTMVVN EIIFHPGITL SRLQSRCREV LSLHEISEIC KWLLERQVLI
TTDFDGYWVN HNWYSIYEST
