SFC3_SCHPO
ID SFC3_SCHPO Reviewed; 1339 AA.
AC Q9UST7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcription factor tau subunit sfc3;
DE AltName: Full=TFIIIC subunit sfc3;
DE AltName: Full=Transcription factor C subunit 3;
GN Name=sfc3 {ECO:0000312|EMBL:CAB58159.1};
GN Synonyms=tfc3 {ECO:0000250|UniProtKB:P34111}; ORFNames=SPBC336.07;
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] {ECO:0000312|EMBL:CAB58159.1}
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] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN TFIIIC, AND INTERACTION WITH SFC1; 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 [3] {ECO:0000305}
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).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595 AND SER-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(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. Cooperates with sfc6 in DNA binding. Localizes to
CC chromatin insulator sequence without recruiting RNA polymerase III and
CC plays a role in nuclear organization. {ECO:0000250|UniProtKB:P34111,
CC ECO:0000269|PubMed:10906331, 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 sfc1, sfc4 and sfc6. {ECO:0000250|UniProtKB:P34111,
CC ECO:0000269|PubMed:10906331}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB58159.1; -; Genomic_DNA.
DR PIR; T40245; T40245.
DR RefSeq; NP_596127.1; NM_001022045.2.
DR AlphaFoldDB; Q9UST7; -.
DR BioGRID; 276778; 8.
DR IntAct; Q9UST7; 3.
DR STRING; 4896.SPBC336.07.1; -.
DR iPTMnet; Q9UST7; -.
DR MaxQB; Q9UST7; -.
DR PaxDb; Q9UST7; -.
DR PRIDE; Q9UST7; -.
DR EnsemblFungi; SPBC336.07.1; SPBC336.07.1:pep; SPBC336.07.
DR GeneID; 2540246; -.
DR KEGG; spo:SPBC336.07; -.
DR PomBase; SPBC336.07; sfc3.
DR VEuPathDB; FungiDB:SPBC336.07; -.
DR eggNOG; ENOG502S2X2; Eukaryota.
DR HOGENOM; CLU_260174_0_0_1; -.
DR InParanoid; Q9UST7; -.
DR OMA; YKGHVVK; -.
DR PhylomeDB; Q9UST7; -.
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:Q9UST7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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:0042791; P:5S class rRNA transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:PomBase.
DR InterPro; IPR044210; Tfc3-like.
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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1339
FT /note="Transcription factor tau subunit sfc3"
FT /id="PRO_0000307794"
FT DNA_BIND 485..497
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 470..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1339 AA; 153642 MW; A05CA9F94180C562 CRC64;
MDSLIRHCSE EIALDGSSGC SIDRLWEFAA NFFFRQGIVQ NLDDNYKTFV WPLILKEDGI
EVWIEDEDAT GLRSKMQEIP WNYQDITIEL RARIRLFASE DRQWLTLTYK TKTDSKIQPL
AFELLSCISR YRQEGVDRIQ LCKETKQEPR SVYGRIQALE DASLISKVAI NRSRAQTALL
VLKRFESENS TINETVAQVS GKQIYNTEKI RSNICDAVQS SRNGICRHVD ARAMVNLNHS
RWERRYYARQ VTYLHNNGYL RKCLTFVPNS PERCIRCLQF IKPYISSLDA TEDDVDFTEV
DDIPEDDELE EEEPLLPSKE EFDASFLQPL ADVGPTLPQW SRFRPLEFQC FVLIRNAGFH
GVITLQILSG LTGIRFNKPL FKLLGSLVEH RSSVPNHLSH MSITRFEDKT KKSRQYRYFT
LQSQLNRLIR DGIPAETISK LLPHVHSLAG EFSPIDSSLF LNSLHHKGNM ESNAEVSPDG
MTLLPRKRGR PRKSANISVT SSPIRPSKNE NNLPSLAISP VSEGFIQNAT ISTPSTSSNL
SIAGSLTPSK TSRIYRGLAP LKNPEFNEDH VKKAEHLEPL LNVSSSVPSK NFTVSSPDHL
KYGNTSSLQV SDSQSSIDLD SSFHYPVSVD SQLSHSTGSL MANFSSPTKK RRLESVDFIF
LQRKGLILSY LVEQNGAFEI SRKMFEDLAD LKVRRNPETS RTVMDRRTFQ QTLEKLMQEK
KVRKLVIATN NGLGKLVRKD IVVQYDMKPD SPRFQQLRAQ ITTPEIEKQS TPEILKDVDV
DFLKRNTSLS RRKSMPAEIK RHKESSETKP VDKEEVKKNE KEKDDPMRLA QQLLESLAPD
FALHENTQQK SPVEKPKKLR KDRYASVEEF DYFSSTEHAS KRSVKRFKND FTSDEDETLI
RAVVITQIYY GGTNRLIKWE AVQKCFPNRD IYALTRRYLS IRQHTKFKGL QQFLSENWQQ
MYKDAVSRKD LMPYPDSVDD FDPTPYVKAS CRPYMISSSN LATTRLPRDL VDVYETYNIE
VVKQETNFRE MIFDPSLSVA SKMNAYCDMP FTMPLSLNDK QNNEGDENCE KGQLFDAKST
IKSIVAIPDA TYDARFSQER LMQYPEDILI AAHQELLDKR IITRVNSENS RLQPGRNFQF
TEKFASSLKS PLPPFLLSQA KRFNKFLLEG FQNHKNHLFE ETSNSGTLAC ILDLLSQGKL
QISIVGSKFN EYGLSEGYRT RLLEHDNINV TLVLSGKESE SKKNYGVTEK LATPPSHEPR
LWLNGKCELI EMIWMNIEQS IVYQLLRKPG ILRSQLTNLL FPGLEPREFN EVLDYFIAAG
AAIEKDGLYL NHNYLFKLT
