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   24-JAN-2024, entry version 151.
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   SMR; Q8BMQ2; -.
DR   BioGRID; 234628; 17.
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; 10090-ENSMUSP00000042265; -.
DR   PeptideAtlas; Q8BMQ2; -.
DR   ProteomicsDB; 258857; -. [Q8BMQ2-1]
DR   ProteomicsDB; 258858; -. [Q8BMQ2-2]
DR   ProteomicsDB; 258859; -. [Q8BMQ2-3]
DR   Pumba; Q8BMQ2; -.
DR   Antibodypedia; 31705; 263 antibodies from 27 providers.
DR   DNASU; 269252; -.
DR   Ensembl; ENSMUST00000037117.6; ENSMUSP00000042265.6; ENSMUSG00000035666.15. [Q8BMQ2-1]
DR   GeneID; 269252; -.
DR   KEGG; mmu:269252; -.
DR   UCSC; uc008ize.2; mouse. [Q8BMQ2-1]
DR   AGR; MGI:2138937; -.
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; 5395638at2759; -.
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; 21 hits in 83 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 257 other cell types or tissues.
DR   ExpressionAtlas; Q8BMQ2; baseline and differential.
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 at RNA polymerase III promoter; IEA:InterPro.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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:SF2; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 4; 1.
DR   PANTHER; PTHR15496; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 4 FAMILY; 1.
DR   Pfam; PF19336; DUF5921; 1.
DR   Pfam; PF12657; TFIIIC_delta; 1.
DR   Pfam; PF12660; zf-TFIIIC; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   Genevisible; Q8BMQ2; MM.
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
//