RPC6_HUMAN
ID RPC6_HUMAN Reviewed; 316 AA.
AC Q9H1D9; A8K4C7; O15319;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC6;
DE Short=RNA polymerase III subunit C6;
DE AltName: Full=DNA-directed RNA polymerase III subunit F;
DE AltName: Full=RNA polymerase III 39 kDa subunit;
DE Short=RPC39;
GN Name=POLR3F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9171375; DOI=10.1101/gad.11.10.1315;
RA Wang Z., Roeder R.G.;
RT "Three human RNA polymerase III-specific subunits form a subcomplex with a
RT selective function in specific transcription initiation.";
RL Genes Dev. 11:1315-1326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH GTF3C4.
RX PubMed=10523658; DOI=10.1128/mcb.19.11.7697;
RA Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.;
RT "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the
RT RNA polymerase III machinery and contains a histone-specific
RT acetyltransferase activity.";
RL Mol. Cell. Biol. 19:7697-7704(1999).
RN [7]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [8]
RP INTERACTION WITH MAF1.
RX PubMed=18377933; DOI=10.1016/j.jmb.2008.02.060;
RA Goodfellow S.J., Graham E.L., Kantidakis T., Marshall L., Coppins B.A.,
RA Oficjalska-Pham D., Gerard M., Lefebvre O., White R.J.;
RT "Regulation of RNA polymerase III transcription by Maf1 in mammalian
RT cells.";
RL J. Mol. Biol. 378:481-491(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, INTERACTION WITH POLR3C, AND MUTAGENESIS OF 137-LYS--LYS-140 AND
RP 173-GLU--GLU-175.
RX PubMed=21358628; DOI=10.1038/nsmb.1996;
RA Lefevre S., Dumay-Odelot H., El-Ayoubi L., Budd A., Legrand P., Pinaud N.,
RA Teichmann M., Fribourg S.;
RT "Structure-function analysis of hRPC62 provides insights into RNA
RT polymerase III transcription initiation.";
RL Nat. Struct. Mol. Biol. 18:352-358(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-7, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP STRUCTURE BY NMR OF 60-155.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of winged-helix domain in RNA polymerase III 39kDa
RT polypeptide.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [16]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [17]
RP FUNCTION.
RX PubMed=19609254; DOI=10.1038/ni.1779;
RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA Hornung V.;
RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA
RT polymerase III-transcribed RNA intermediate.";
RL Nat. Immunol. 10:1065-1072(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. May direct RNA Pol III binding
CC to the TFIIIB-DNA complex. Plays a key role in sensing and limiting
CC infection by intracellular bacteria and DNA viruses. Acts as nuclear
CC and cytosolic DNA sensor involved in innate immune response. Can sense
CC non-self dsDNA that serves as template for transcription into dsRNA.
CC The non-self RNA polymerase III transcripts, such as Epstein-Barr
CC virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B
CC through the RIG-I pathway. Preferentially binds double-stranded DNA
CC (dsDNA) (PubMed:21358628). {ECO:0000269|PubMed:19609254,
CC ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21358628}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G
CC form a Pol III subcomplex (By similarity). Directly interacts with
CC POLR3C (PubMed:21358628). Interacts with TBP and TFIIIB90 and GTF3C4
CC (By similarity) (PubMed:10523658). Interacts with MAF1
CC (PubMed:18377933). {ECO:0000250, ECO:0000269|PubMed:10523658,
CC ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:18377933,
CC ECO:0000269|PubMed:21358628}.
CC -!- INTERACTION:
CC Q9H1D9; Q92870-2: APBB2; NbExp=3; IntAct=EBI-710067, EBI-21535880;
CC Q9H1D9; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-710067, EBI-1166928;
CC Q9H1D9; P41091: EIF2S3; NbExp=3; IntAct=EBI-710067, EBI-1054228;
CC Q9H1D9; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-710067, EBI-10226858;
CC Q9H1D9; P28799: GRN; NbExp=3; IntAct=EBI-710067, EBI-747754;
CC Q9H1D9; P54652: HSPA2; NbExp=3; IntAct=EBI-710067, EBI-356991;
CC Q9H1D9; P04792: HSPB1; NbExp=3; IntAct=EBI-710067, EBI-352682;
CC Q9H1D9; O60333-2: KIF1B; NbExp=3; IntAct=EBI-710067, EBI-10975473;
CC Q9H1D9; D3DTS7: PMP22; NbExp=3; IntAct=EBI-710067, EBI-25882629;
CC Q9H1D9; Q12796: PNRC1; NbExp=3; IntAct=EBI-710067, EBI-2827376;
CC Q9H1D9; Q9BUI4: POLR3C; NbExp=2; IntAct=EBI-710067, EBI-5452779;
CC Q9H1D9; O15318: POLR3G; NbExp=3; IntAct=EBI-710067, EBI-12362221;
CC Q9H1D9; Q9BT43: POLR3GL; NbExp=4; IntAct=EBI-710067, EBI-2855862;
CC Q9H1D9; Q13523: PRPF4B; NbExp=2; IntAct=EBI-710067, EBI-395940;
CC Q9H1D9; P60891: PRPS1; NbExp=3; IntAct=EBI-710067, EBI-749195;
CC Q9H1D9; O76024: WFS1; NbExp=3; IntAct=EBI-710067, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; U93869; AAB63677.1; -; mRNA.
DR EMBL; AK290892; BAF83581.1; -; mRNA.
DR EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10240.1; -; Genomic_DNA.
DR EMBL; BC012588; AAH12588.1; -; mRNA.
DR CCDS; CCDS13135.1; -.
DR RefSeq; NP_001269455.1; NM_001282526.1.
DR RefSeq; NP_006457.2; NM_006466.3.
DR PDB; 2DK5; NMR; -; A=78-155.
DR PDB; 2YU3; NMR; -; A=61-142.
DR PDB; 7A6H; EM; 3.30 A; P=1-316.
DR PDB; 7AE1; EM; 2.80 A; P=1-316.
DR PDB; 7AE3; EM; 3.10 A; P=1-316.
DR PDB; 7AEA; EM; 3.40 A; P=1-316.
DR PDB; 7AST; EM; 4.00 A; Z=1-316.
DR PDB; 7D58; EM; 2.90 A; P=1-316.
DR PDB; 7D59; EM; 3.10 A; P=1-316.
DR PDB; 7DN3; EM; 3.50 A; P=1-316.
DR PDB; 7DU2; EM; 3.35 A; P=1-316.
DR PDB; 7FJI; EM; 3.60 A; P=1-316.
DR PDB; 7FJJ; EM; 3.60 A; P=1-316.
DR PDBsum; 2DK5; -.
DR PDBsum; 2YU3; -.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; Q9H1D9; -.
DR SMR; Q9H1D9; -.
DR BioGRID; 115866; 47.
DR DIP; DIP-34646N; -.
DR IntAct; Q9H1D9; 50.
DR MINT; Q9H1D9; -.
DR STRING; 9606.ENSP00000366828; -.
DR iPTMnet; Q9H1D9; -.
DR MetOSite; Q9H1D9; -.
DR PhosphoSitePlus; Q9H1D9; -.
DR BioMuta; POLR3F; -.
DR DMDM; 20139728; -.
DR EPD; Q9H1D9; -.
DR jPOST; Q9H1D9; -.
DR MassIVE; Q9H1D9; -.
DR MaxQB; Q9H1D9; -.
DR PaxDb; Q9H1D9; -.
DR PeptideAtlas; Q9H1D9; -.
DR PRIDE; Q9H1D9; -.
DR ProteomicsDB; 80402; -.
DR Antibodypedia; 24572; 197 antibodies from 29 providers.
DR DNASU; 10621; -.
DR Ensembl; ENST00000377603.5; ENSP00000366828.4; ENSG00000132664.12.
DR GeneID; 10621; -.
DR KEGG; hsa:10621; -.
DR MANE-Select; ENST00000377603.5; ENSP00000366828.4; NM_006466.4; NP_006457.2.
DR UCSC; uc002wqv.5; human.
DR CTD; 10621; -.
DR GeneCards; POLR3F; -.
DR HGNC; HGNC:15763; POLR3F.
DR HPA; ENSG00000132664; Low tissue specificity.
DR MIM; 617455; gene.
DR neXtProt; NX_Q9H1D9; -.
DR OpenTargets; ENSG00000132664; -.
DR PharmGKB; PA33520; -.
DR VEuPathDB; HostDB:ENSG00000132664; -.
DR eggNOG; KOG3233; Eukaryota.
DR GeneTree; ENSGT00390000009679; -.
DR HOGENOM; CLU_033661_1_0_1; -.
DR InParanoid; Q9H1D9; -.
DR OMA; CEYMRDW; -.
DR OrthoDB; 1287786at2759; -.
DR PhylomeDB; Q9H1D9; -.
DR TreeFam; TF103051; -.
DR PathwayCommons; Q9H1D9; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; Q9H1D9; -.
DR SIGNOR; Q9H1D9; -.
DR BioGRID-ORCS; 10621; 699 hits in 1095 CRISPR screens.
DR ChiTaRS; POLR3F; human.
DR EvolutionaryTrace; Q9H1D9; -.
DR GeneWiki; POLR3F; -.
DR GenomeRNAi; 10621; -.
DR Pharos; Q9H1D9; Tbio.
DR PRO; PR:Q9H1D9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H1D9; protein.
DR Bgee; ENSG00000132664; Expressed in cerebellar hemisphere and 146 other tissues.
DR Genevisible; Q9H1D9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; NAS:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR007832; RNA_pol_Rpc34.
DR InterPro; IPR016049; RNA_pol_Rpc34-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12780; PTHR12780; 1.
DR Pfam; PF05158; RNA_pol_Rpc34; 1.
DR PIRSF; PIRSF028763; RNA_pol_Rpc34; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; DNA-binding;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..316
FT /note="DNA-directed RNA polymerase III subunit RPC6"
FT /id="PRO_0000073972"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT MUTAGEN 137..140
FT /note="KAVK->EAVE: Strongly impaired dsDNA-binding. No
FT effect on interaction with POLR3C."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 173..175
FT /note="ESE->KSK: Strongly impaired dsDNA-binding. No effect
FT on interaction with POLR3C."
FT /evidence="ECO:0000269|PubMed:21358628"
FT CONFLICT 2
FT /note="A -> G (in Ref. 1; AAB63677)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..53
FT /note="HIEAQQRAVA -> QYRSPAAGSS (in Ref. 1; AAB63677)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..290
FT /note="AKEGTVGSVDGHMKLYRAVNPIIPPTGLVRAPCGLC -> CKRRHSWQCRWT
FT HETVQGSQSNHPSHRFGPGHPVDSA (in Ref. 1; AAB63677)"
FT /evidence="ECO:0000305"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2YU3"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2YU3"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:2DK5"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2DK5"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:2DK5"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:2DK5"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2DK5"
FT HELIX 174..198
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 316 AA; 35684 MW; 49B1360AF8B365ED CRC64;
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR AVAINRLLSM
GQLDLLRSNT GLLYRIKDSQ NAGKMKGSDN QEKLVYQIIE DAGNKGIWSR DIRYKSNLPL
TEINKILKNL ESKKLIKAVK SVAASKKKVY MLYNLQPDRS VTGGAWYSDQ DFESEFVEVL
NQQCFKFLQS KAETARESKQ NPMIQRNSSF ASSHEVWKYI CELGISKVEL SMEDIETILN
TLIYDGKVEM TIIAAKEGTV GSVDGHMKLY RAVNPIIPPT GLVRAPCGLC PVFDDCHEGG
EISPSNCIYM TEWLEF
