ID RPC3_MOUSE Reviewed; 533 AA. AC Q9D483; Q8R0I2; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 29-MAY-2024, entry version 149. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC3; DE Short=RNA polymerase III subunit C3; DE AltName: Full=DNA-directed RNA polymerase III subunit C; GN Name=Polr3c {ECO:0000312|MGI:MGI:1921664}; 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] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Testis; 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 MRNA] (ISOFORM 2). RC TISSUE=Salivary gland; 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates CC (By similarity). Specific peripheric component of RNA polymerase III CC (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, CC snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. Part CC of POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer, coordinates the CC dynamics of Pol III stalk and clamp modules during the transition from CC apo to elongation state (By similarity). Pol III plays a key role in CC sensing and limiting infection by intracellular bacteria and DNA CC viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate CC immune response. Can sense non-self dsDNA that serves as template for CC transcription into dsRNA. The non-self RNA polymerase III transcripts, CC such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I CC interferon and NF-kappa-B through the RIG-I pathway. Preferentially CC binds single-stranded DNA (ssDNA) in a sequence-independent manner (By CC similarity). {ECO:0000250|UniProtKB:Q9BUI4}. CC -!- SUBUNIT: Component of the RNA polymerase III complex consisting of 17 CC subunits: a ten-subunit horseshoe-shaped catalytic core composed of CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and CC CRCP/RPC9, protruding from the core and functioning primarily in CC transcription initiation; and additional subunits homologous to general CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3- CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both CC transcription initiation and termination. Directly interacts with CC POLR3G/RPC7 and POLR3GL. Directly interacts with POLR3F/RPC6. Interacts CC with GTF3C4. As part of the RNA polymerase III complex, interacts with CC PKP2. {ECO:0000250, ECO:0000250|UniProtKB:Q9BUI4}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUI4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D483-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D483-2; Sequence=VSP_010678, VSP_010679; CC -!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase CC subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK016716; BAB30395.1; -; mRNA. DR EMBL; BC026793; AAH26793.1; -; mRNA. DR CCDS; CCDS51010.1; -. [Q9D483-1] DR RefSeq; NP_083201.1; NM_028925.1. [Q9D483-1] DR RefSeq; XP_006502250.1; XM_006502187.3. [Q9D483-1] DR AlphaFoldDB; Q9D483; -. DR SMR; Q9D483; -. DR BioGRID; 216732; 2. DR STRING; 10090.ENSMUSP00000122435; -. DR iPTMnet; Q9D483; -. DR PhosphoSitePlus; Q9D483; -. DR EPD; Q9D483; -. DR MaxQB; Q9D483; -. DR PaxDb; 10090-ENSMUSP00000029741; -. DR PeptideAtlas; Q9D483; -. DR ProteomicsDB; 299940; -. [Q9D483-1] DR ProteomicsDB; 299941; -. [Q9D483-2] DR Pumba; Q9D483; -. DR Antibodypedia; 33966; 299 antibodies from 24 providers. DR DNASU; 74414; -. DR Ensembl; ENSMUST00000029741.9; ENSMUSP00000029741.3; ENSMUSG00000028099.9. [Q9D483-1] DR Ensembl; ENSMUST00000141377.8; ENSMUSP00000115300.2; ENSMUSG00000028099.9. [Q9D483-2] DR Ensembl; ENSMUST00000154679.8; ENSMUSP00000122435.2; ENSMUSG00000028099.9. [Q9D483-1] DR GeneID; 74414; -. DR KEGG; mmu:74414; -. DR UCSC; uc008qoa.2; mouse. [Q9D483-1] DR UCSC; uc008qoc.2; mouse. [Q9D483-2] DR AGR; MGI:1921664; -. DR CTD; 10623; -. DR MGI; MGI:1921664; Polr3c. DR VEuPathDB; HostDB:ENSMUSG00000028099; -. DR eggNOG; KOG2587; Eukaryota. DR GeneTree; ENSGT00390000002799; -. DR HOGENOM; CLU_023294_1_1_1; -. DR InParanoid; Q9D483; -. DR OMA; QHNLLWH; -. DR OrthoDB; 2875034at2759; -. DR PhylomeDB; Q9D483; -. DR TreeFam; TF103048; -. 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 Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR BioGRID-ORCS; 74414; 24 hits in 83 CRISPR screens. DR PRO; PR:Q9D483; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q9D483; Protein. DR Bgee; ENSMUSG00000028099; Expressed in placenta labyrinth and 254 other cell types or tissues. DR ExpressionAtlas; Q9D483; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB. DR Gene3D; 6.10.140.1450; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 4. DR InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH. DR InterPro; IPR008806; RNA_pol_III_Rpc82_C. DR InterPro; IPR039748; RPC3. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR12949:SF0; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3; 1. DR PANTHER; PTHR12949; RNA POLYMERASE III DNA DIRECTED -RELATED; 1. DR Pfam; PF08221; HTH_9; 1. DR Pfam; PF05645; RNA_pol_Rpc82; 1. DR Pfam; PF20912; RPC3_helical; 1. PE 1: Evidence at protein level; KW Alternative splicing; Antiviral defense; DNA-binding; KW DNA-directed RNA polymerase; Immunity; Innate immunity; KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transferase. FT CHAIN 1..533 FT /note="DNA-directed RNA polymerase III subunit RPC3" FT /id="PRO_0000073964" FT REGION 162..181 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9BUI4" FT VAR_SEQ 199..202 FT /note="GKRR -> DFTS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010678" FT VAR_SEQ 203..533 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010679" FT CONFLICT 171 FT /note="R -> P (in Ref. 2; AAH26793)" FT /evidence="ECO:0000305" SQ SEQUENCE 533 AA; 60706 MW; 6869DE76F7CBC2B0 CRC64; MTQAEIKLCS LLLQEHFGEI VEKIGVHLVR TGSQPLRVIA HDTKASLDQV KKALCVLIHH NLVLYHVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYG DTGELIVEEL LLNGKMTMSA VVKKVADRLT ETMEDGKTMD YAEVSNAFVR LADTHFVQRC PLVPDTDSSD RGPPPPAPTL VINEKDMYLV PKLSLIGKGK RRRSSDEDAT GEPKAKKPRY TDNKEPSPDD GIYWQVNLDR FHQHFRDQAI VSAVANRMDQ TSSEIVRTML RMSEITTPSS APYTQPLSSN EIFRSLPVGY NISKQVLDQY LTLLADDPLE FIGKSGDSGG GMFVINLHKA LASLATATLE SVIQERFGSR CARIFRLVLQ KKHLEQKQVE DFAMIPAKEA KDMLYKMLSE NFILLQEIPK TPDHAPSRTF YLYTVNVLSA ARMLLHRCYK SIANLIERRQ FETKENKRLL EKSQRVEAIM ASMQATGAEE VQLQEIEEMI TAPERQQLET LKRNVNKLDA SEIQVDETIF LLESYIESTM KRQ //