SFC1_SCHPO
ID SFC1_SCHPO Reviewed; 456 AA.
AC O14229; Q9UTT3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Transcription factor tau subunit sfc1;
DE AltName: Full=TFIIIC subunit sfc1;
DE AltName: Full=Transcription factor C subunit 1;
GN Name=sfc1; Synonyms=tfc1; ORFNames=SPAC6F12.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 286-456.
RA Kawamukai M.;
RT "S.pombe unknown protein.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, IDENTIFICATION IN TFIIIC, AND INTERACTION WITH SFC3; SFC4 AND
RP SFC6.
RX PubMed=10906331; DOI=10.1074/jbc.m004635200;
RA Huang Y., Hamada M., Maraia R.J.;
RT "Isolation and cloning of four subunits of a fission yeast TFIIIC complex
RT that includes an ortholog of the human regulatory protein TFIIICbeta.";
RL J. Biol. Chem. 275:31480-31487(2000).
RN [4]
RP FUNCTION.
RX PubMed=16751097; DOI=10.1016/j.cell.2006.04.028;
RA Noma K., Cam H.P., Maraia R.J., Grewal S.I.S.;
RT "A role for TFIIIC transcription factor complex in genome organization.";
RL Cell 125:859-872(2006).
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 sfc3 and sfc6. Serves as a scaffold critical for
CC tauA-DNA spatial configuration and tauB-DNA stability. Localizes to
CC chromatin insulator sequence without recruiting RNA polymerase III and
CC plays a role in nuclear organization. {ECO:0000269|PubMed:10906331,
CC ECO:0000269|PubMed:16751097}.
CC -!- SUBUNIT: Component of the TFIIIC complex including sfc1, sfc3, sfc4,
CC sfc6 and sfc7. The subunits are organized in two globular domains, tauA
CC and tauB, connected by a proteolysis-sensitive and flexible linker.
CC Interacts with sfc3, sfc4 and sfc6. {ECO:0000269|PubMed:10906331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; CU329670; CAB11095.2; -; Genomic_DNA.
DR EMBL; AB032716; BAA84655.1; -; mRNA.
DR PIR; T11662; T11662.
DR RefSeq; NP_593297.1; NM_001018727.2.
DR PDB; 4BJI; X-ray; 1.45 A; A=186-396.
DR PDB; 4BJJ; X-ray; 2.40 A; A=1-110.
DR PDBsum; 4BJI; -.
DR PDBsum; 4BJJ; -.
DR AlphaFoldDB; O14229; -.
DR SMR; O14229; -.
DR BioGRID; 279302; 9.
DR IntAct; O14229; 1.
DR STRING; 4896.SPAC6F12.11c.1; -.
DR iPTMnet; O14229; -.
DR MaxQB; O14229; -.
DR PaxDb; O14229; -.
DR EnsemblFungi; SPAC6F12.11c.1; SPAC6F12.11c.1:pep; SPAC6F12.11c.
DR GeneID; 2542856; -.
DR KEGG; spo:SPAC6F12.11c; -.
DR PomBase; SPAC6F12.11c; sfc1.
DR VEuPathDB; FungiDB:SPAC6F12.11c; -.
DR eggNOG; KOG2473; Eukaryota.
DR HOGENOM; CLU_016809_1_1_1; -.
DR InParanoid; O14229; -.
DR OMA; PPEYFVR; -.
DR PhylomeDB; O14229; -.
DR Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:O14229; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; NAS:PomBase.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:PomBase.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:PomBase.
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; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..456
FT /note="Transcription factor tau subunit sfc1"
FT /id="PRO_0000116669"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:4BJJ"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:4BJJ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4BJJ"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:4BJJ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4BJJ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4BJJ"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4BJJ"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:4BJJ"
FT STRAND 86..98
FT /evidence="ECO:0007829|PDB:4BJJ"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4BJJ"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4BJI"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:4BJI"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4BJI"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4BJI"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:4BJI"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:4BJI"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4BJI"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:4BJI"
SQ SEQUENCE 456 AA; 52745 MW; 00DA3FCA512EFAFC CRC64;
MNSLKISDNE YALIEHPGFA NNKDAFFQTL GGVQSIQKAC QTSFQNPKQA LLELNLRPKD
KYHHPVQARV QSRNDLLVTI KKMDNSVQNV SRIRQVFLFR DMADFQYSTQ NSPFVQKLDS
TLRVLDYNAI NKFSIDLTPV QRKHVDMPPP PVFSQTSLPM SYNFLQNPLV GRVRLPNGKT
TIVNLKGQCR VWIITTNMGV ESVPTCRHSK LGEPSKTIQE VIEALKPLFE KRPVWTRRAL
LNHLDPSYTH YLKFALPYLS YLWTSGPFRD TYTRFGYDPR KDSNAAAYQA LFFKLKLNGK
HKGTKTHVFD GKTLFPTNRV YQVCDIVDPT IAPLLKDTQL RSECHRDTGW YRSGRYYKVR
DLMREKLFAL IEGEMPSEVA VNMILNAEEV EESDRYSNFD EQDNTDLNDT VRGLNTSATD
DRINDLMRNL MKRSQEHEGF EDLEEIDDDY DDIFGD
