ID   TF3C5_MOUSE             Reviewed;         520 AA.
AC   Q8R2T8; Q8BLE3; Q8R0D0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=General transcription factor 3C polypeptide 5;
DE   AltName: Full=TF3C-epsilon;
DE   AltName: Full=Transcription factor IIIC 63 kDa subunit;
DE            Short=TFIIIC 63 kDa subunit;
DE            Short=TFIIIC63;
DE   AltName: Full=Transcription factor IIIC subunit epsilon;
GN   Name=Gtf3c5;
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   TISSUE=Eye;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-520 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC   -!- FUNCTION: Involved in RNA polymerase III-mediated transcription.
CC       Integral, tightly associated component of the DNA-binding TFIIIC2
CC       subcomplex that directly binds tRNA and virus-associated RNA promoters
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC       with BRF1, GTF3C6 and TBP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R2T8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R2T8-2; Sequence=VSP_010356;
CC   -!- SIMILARITY: Belongs to the TFIIIC subunit 5 family. {ECO:0000305}.
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DR   EMBL; BC027055; AAH27055.1; -; mRNA.
DR   EMBL; BC027247; AAH27247.1; -; mRNA.
DR   EMBL; BC039171; AAH39171.1; -; mRNA.
DR   EMBL; AK045419; BAC32354.1; -; mRNA.
DR   CCDS; CCDS15842.1; -. [Q8R2T8-2]
DR   CCDS; CCDS71012.1; -. [Q8R2T8-1]
DR   RefSeq; NP_001277413.1; NM_001290484.1. [Q8R2T8-1]
DR   RefSeq; NP_683730.1; NM_148928.3. [Q8R2T8-2]
DR   AlphaFoldDB; Q8R2T8; -.
DR   SMR; Q8R2T8; -.
DR   BioGRID; 213934; 2.
DR   IntAct; Q8R2T8; 2.
DR   MINT; Q8R2T8; -.
DR   STRING; 10090.ENSMUSP00000109521; -.
DR   iPTMnet; Q8R2T8; -.
DR   PhosphoSitePlus; Q8R2T8; -.
DR   SwissPalm; Q8R2T8; -.
DR   EPD; Q8R2T8; -.
DR   MaxQB; Q8R2T8; -.
DR   PaxDb; 10090-ENSMUSP00000028157; -.
DR   ProteomicsDB; 263294; -. [Q8R2T8-1]
DR   ProteomicsDB; 263295; -. [Q8R2T8-2]
DR   Pumba; Q8R2T8; -.
DR   Antibodypedia; 18242; 216 antibodies from 25 providers.
DR   DNASU; 70239; -.
DR   Ensembl; ENSMUST00000028157.9; ENSMUSP00000028157.9; ENSMUSG00000026816.15. [Q8R2T8-2]
DR   Ensembl; ENSMUST00000113889.9; ENSMUSP00000109521.3; ENSMUSG00000026816.15. [Q8R2T8-1]
DR   GeneID; 70239; -.
DR   KEGG; mmu:70239; -.
DR   UCSC; uc012bsz.2; mouse. [Q8R2T8-1]
DR   AGR; MGI:1917489; -.
DR   CTD; 9328; -.
DR   MGI; MGI:1917489; Gtf3c5.
DR   VEuPathDB; HostDB:ENSMUSG00000026816; -.
DR   eggNOG; KOG2473; Eukaryota.
DR   GeneTree; ENSGT00390000004458; -.
DR   HOGENOM; CLU_026463_0_0_1; -.
DR   InParanoid; Q8R2T8; -.
DR   OMA; PPEYFVR; -.
DR   OrthoDB; 5479651at2759; -.
DR   PhylomeDB; Q8R2T8; -.
DR   TreeFam; TF313581; -.
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; 70239; 25 hits in 80 CRISPR screens.
DR   ChiTaRS; Gtf3c5; mouse.
DR   PRO; PR:Q8R2T8; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8R2T8; Protein.
DR   Bgee; ENSMUSG00000026816; Expressed in forelimb bud and 243 other cell types or tissues.
DR   ExpressionAtlas; Q8R2T8; baseline and differential.
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:0000995; F:RNA polymerase III general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IEA:InterPro.
DR   Gene3D; 3.30.200.160; TFIIIC, subcomplex tauA, subunit Sfc1, barrel domain; 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:SF5; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 5; 1.
DR   PANTHER; PTHR13230; GENERAL TRANSCRIPTION FACTOR IIIC, POLYPEPTIDE 5; 1.
DR   Pfam; PF09734; Tau95; 1.
DR   Pfam; PF17682; Tau95_N; 1.
DR   Genevisible; Q8R2T8; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Transcription.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5Q8"
FT   CHAIN           2..520
FT                   /note="General transcription factor 3C polypeptide 5"
FT                   /id="PRO_0000209716"
FT   REGION          466..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..520
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5Q8"
FT   VAR_SEQ         465..470
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010356"
FT   CONFLICT        145
FT                   /note="M -> T (in Ref. 1; AAH27247)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   520 AA;  60502 MW;  02687D323638FD0B CRC64;
     MAAAEPDADP KAAIPVDLRR ERRLVCVEYP GVVRNEAKML QTLGGEESVS RIYTDPTKRL
     ELYFRPKDPY CHPVCANRFS TSSLLLRIRK RTRRRRGVLG DEAHPQVTFN LEIIGIISTI
     YKFQGMSDFQ YLAVHTEAGG KHVSMYDRVL MRKPEKEEFF HQELPLYIPP PIFSRLDTPV
     DYFYRPETQH REGYHNPTIS GENLIGLSRA RRPHNAIFVN FEDTEVPEQP LEAAVQTWKK
     ACTNPIDQKV EEELRKLFDI RPVWSRNAVK SNVSVHPDKL KILLPYMAYY MITGPWRSLW
     IRFGYDPRKH PDAKIYQVLD FRIRCGMKYG YGSRDMPVKA KRSTYNYSLP ITVKKTSNQP
     GTMHDLKQGL GPSGTDGPRK LTYNKYKLKD SVYIFREGAL PPYRQMFYQL CDLNVEELQK
     IVHRNDGTET VCTERDGWCL PKTTDHLRDT MSLMILQTIR SERPALFSNT GKADRGKEQL
     MFESGEEEEE EEEEEEEEEE DFKPSDGSEN EMETEILDYV
//