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 13-SEP-2023, entry version 146. 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; 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 Specific core component of RNA polymerase III which synthesizes small CC RNAs, such as 5S rRNA and tRNAs. May direct with other members of the CC subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the CC interactions between TFIIIB and POLR3F. May be involved either in the CC recruitment and stabilization of the subcomplex within RNA polymerase CC III, or in stimulating catalytic functions of other subunits during CC initiation. Plays a key role in sensing and limiting infection by CC intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic CC DNA sensor involved in innate immune response. Can sense non-self dsDNA CC that serves as template for transcription into dsRNA. The non-self RNA CC polymerase III transcripts induce type I interferon and NF-Kappa-B CC through the RIG-I pathway. Preferentially binds single-stranded DNA CC (ssDNA) in a sequence-independent manner. CC {ECO:0000250|UniProtKB:Q9BUI4}. CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex CC consisting of 17 subunits (By similarity). RPC3/POLR3C, RPC6/POLR3F and CC RPC7/POLR3G form a Pol III subcomplex (By similarity). Directly CC interacts with POLR3G and POLR3GL. Directly interacts with CC POLR3F/RPC39. Interacts with GTF3C4. As part of the RNA polymerase III CC (Pol III) complex, interacts with PKP2 (By similarity). CC {ECO:0000250|UniProtKB:Q9BUI4}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. 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.ENSMUSP00000029741; -. DR iPTMnet; Q9D483; -. DR PhosphoSitePlus; Q9D483; -. DR EPD; Q9D483; -. DR MaxQB; Q9D483; -. DR PaxDb; Q9D483; -. DR PeptideAtlas; Q9D483; -. DR ProteomicsDB; 299940; -. [Q9D483-1] DR ProteomicsDB; 299941; -. [Q9D483-2] DR Antibodypedia; 33966; 279 antibodies from 24 providers. DR DNASU; 74414; -. DR Ensembl; ENSMUST00000029741; ENSMUSP00000029741; ENSMUSG00000028099. [Q9D483-1] DR Ensembl; ENSMUST00000141377; ENSMUSP00000115300; ENSMUSG00000028099. [Q9D483-2] DR Ensembl; ENSMUST00000154679; ENSMUSP00000122435; ENSMUSG00000028099. [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 251 other tissues. DR ExpressionAtlas; Q9D483; baseline and differential. DR Genevisible; Q9D483; MM. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. 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. 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 //