TF3C4_MOUSE
ID TF3C4_MOUSE Reviewed; 817 AA.
AC Q8BMQ2; Q148Y1; Q8BKZ4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=General transcription factor 3C polypeptide 4;
DE EC=2.3.1.48;
DE AltName: Full=TF3C-delta;
DE AltName: Full=Transcription factor IIIC 90 kDa subunit;
DE Short=TFIIIC 90 kDa subunit;
DE Short=TFIIIC90;
DE AltName: Full=Transcription factor IIIC subunit delta;
GN Name=Gtf3c4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential for RNA polymerase III to make a number of small
CC nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-
CC associated (VA) RNA of both cellular and viral origin. Has histone
CC acetyltransferase activity (HAT) with unique specificity for free and
CC nucleosomal H3. May cooperate with GTF3C5 in facilitating the
CC recruitment of TFIIIB and RNA polymerase through direct interactions
CC with BRF1, POLR3C and POLR3F. May be localized close to the A box (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and POLR3F (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BMQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMQ2-2; Sequence=VSP_010577;
CC Name=3;
CC IsoId=Q8BMQ2-3; Sequence=VSP_010578;
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 4 family. {ECO:0000305}.
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DR EMBL; AK030351; BAC26916.1; -; mRNA.
DR EMBL; AK047698; BAC33130.1; -; mRNA.
DR EMBL; AL732526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08398.1; -; Genomic_DNA.
DR EMBL; BC061476; AAH61476.1; -; mRNA.
DR EMBL; BC117919; AAI17920.1; -; mRNA.
DR EMBL; BC117920; AAI17921.1; -; mRNA.
DR CCDS; CCDS15847.1; -. [Q8BMQ2-1]
DR RefSeq; NP_001159505.1; NM_001166033.1.
DR RefSeq; NP_766565.2; NM_172977.3. [Q8BMQ2-1]
DR AlphaFoldDB; Q8BMQ2; -.
DR BioGRID; 234628; 16.
DR IntAct; Q8BMQ2; 16.
DR MINT; Q8BMQ2; -.
DR STRING; 10090.ENSMUSP00000042265; -.
DR iPTMnet; Q8BMQ2; -.
DR PhosphoSitePlus; Q8BMQ2; -.
DR EPD; Q8BMQ2; -.
DR jPOST; Q8BMQ2; -.
DR MaxQB; Q8BMQ2; -.
DR PaxDb; Q8BMQ2; -.
DR PeptideAtlas; Q8BMQ2; -.
DR PRIDE; Q8BMQ2; -.
DR ProteomicsDB; 258857; -. [Q8BMQ2-1]
DR ProteomicsDB; 258858; -. [Q8BMQ2-2]
DR ProteomicsDB; 258859; -. [Q8BMQ2-3]
DR Antibodypedia; 31705; 216 antibodies from 27 providers.
DR DNASU; 269252; -.
DR Ensembl; ENSMUST00000037117; ENSMUSP00000042265; ENSMUSG00000035666. [Q8BMQ2-1]
DR GeneID; 269252; -.
DR KEGG; mmu:269252; -.
DR UCSC; uc008ize.2; mouse. [Q8BMQ2-1]
DR CTD; 9329; -.
DR MGI; MGI:2138937; Gtf3c4.
DR VEuPathDB; HostDB:ENSMUSG00000035666; -.
DR eggNOG; ENOG502QTDJ; Eukaryota.
DR GeneTree; ENSGT00390000011873; -.
DR InParanoid; Q8BMQ2; -.
DR OMA; WKPSHED; -.
DR OrthoDB; 966939at2759; -.
DR TreeFam; TF328412; -.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR BioGRID-ORCS; 269252; 20 hits in 77 CRISPR screens.
DR ChiTaRS; Gtf3c4; mouse.
DR PRO; PR:Q8BMQ2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BMQ2; protein.
DR Bgee; ENSMUSG00000035666; Expressed in metanephric mesenchyme and 253 other tissues.
DR ExpressionAtlas; Q8BMQ2; baseline and differential.
DR Genevisible; Q8BMQ2; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045803; DUF5921.
DR InterPro; IPR044230; GTF3C4.
DR InterPro; IPR024761; TFIIIC_delta_N.
DR InterPro; IPR024764; TFIIIC_Znf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15496; PTHR15496; 1.
DR Pfam; PF19336; DUF5921; 1.
DR Pfam; PF12657; TFIIIC_delta; 1.
DR Pfam; PF12660; zf-TFIIIC; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Ubl conjugation.
FT CHAIN 1..817
FT /note="General transcription factor 3C polypeptide 4"
FT /id="PRO_0000209714"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKN8"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKN8"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKN8"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKN8"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKN8"
FT VAR_SEQ 1..323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010577"
FT VAR_SEQ 270..817
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010578"
FT CONFLICT 21
FT /note="E -> Q (in Ref. 1; BAC26916)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="P -> H (in Ref. 1; BAC26916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 91613 MW; 895ED56D1B7B1F05 CRC64;
MSEADQALVG PKADEPSPPA EEKDEGGGKE AAADAAPGPS ASFRLMVTRR EPAVKLQYAV
SGLEPLSWSE DHRVSVSTAR SVAVLELICD VHNPGQDLVI HRTSVPAPLN SCLLKVGSKT
EVAECKEKFA SSKDPTISQT FMLDRMFNPE GKALPPMRGF KYTSWSPMGC DANGRCLLAA
LTMDNRLTVQ VNLNRLQWVQ LVDLTEIYGD RLYETSYRLS KNEAPEGNLG DFAEFQRRHS
MQTPVRMEWS SICTTQQVKH NNECRDVSSV LLAVLFENGN IAVWQFQLPF VGKESISSCN
TIESGISSPS VLFWWEYEHN NRKMSGLIVG SAFGPVKILP VNLKAVKGYF TLRQPVVLWK
EMDKLPVHSI KCVPLYHPYQ KCSCSLVVAA RGSYVFWCLL LISKAGLNVH NSHVTGLHSL
PIVSITADKQ NGTVYTCSSD GKVRQLIPIF TDVALKFEHQ LIKLSDVFGS VRTHGIAVSP
CGAYLAIITT EGMMNGLHPV NKNYQVQFVT LKTFEEAAAQ LLESSVQNLF KQVDLIDLVR
WKILKDKHIP QFLHEALEKK IESSGVTYFW RFKLFLLRIL YQSMQKSPSE ALWKPTHEDS
KILLVDSPGM GDGEDEQQEE GTSKQGTKAG LQEKSKEGDT EETPEDSLTA GGDTGGREPV
EEKLLEIQGK IEAVEMHLTR EHMKRVLGEV YLHTWITENT SIPTRGLCNF LMSDEDYDDR
TAQVLIGHIS KKMNKQTFPE RCSLCKEILP FTDRKQAVCS NGHIWLRCFL TYQSCQSLIY
RRCLLHDSIA RHPVPEDPDW IKRLLQSPCP FCDSPVF
