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 10-OCT-2018, entry version 123. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. Specific core component of RNA polymerase III which CC synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with CC other members of the subcomplex RNA Pol III binding to the TFIIIB- CC DNA complex via the interactions between TFIIIB and POLR3F. May be CC involved either in the recruitment and stabilization of the CC subcomplex within RNA polymerase III, or in stimulating catalytic CC functions of other subunits during initiation. Plays a key role in CC sensing and limiting infection by intracellular bacteria and DNA CC viruses. Acts as nuclear and cytosolic DNA sensor involved in CC innate immune response. Can sense non-self dsDNA that serves as CC template for transcription into dsRNA. The non-self RNA polymerase CC III transcripts induce type I interferon and NF-Kappa-B through CC 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, CC RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex (By CC similarity). Directly interacts with POLR3G and POLR3GL. Directly CC interacts with POLR3F/RPC39. Interacts with GTF3C4. 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 Note=No experimental confirmation available.; 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 UniGene; Mm.276043; -. DR ProteinModelPortal; Q9D483; -. DR SMR; Q9D483; -. DR STRING; 10090.ENSMUSP00000029741; -. DR iPTMnet; Q9D483; -. DR PhosphoSitePlus; Q9D483; -. DR EPD; Q9D483; -. DR PaxDb; Q9D483; -. DR PeptideAtlas; Q9D483; -. DR PRIDE; Q9D483; -. 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 CTD; 10623; -. DR MGI; MGI:1921664; Polr3c. DR eggNOG; KOG2587; Eukaryota. DR eggNOG; ENOG410XPVH; LUCA. DR GeneTree; ENSGT00390000002799; -. DR HOGENOM; HOG000046475; -. DR HOVERGEN; HBG059543; -. DR InParanoid; Q9D483; -. DR KO; K03023; -. DR OMA; EQCFGKV; -. DR OrthoDB; EOG091G186Z; -. 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 PRO; PR:Q9D483; -. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000028099; Expressed in 269 organ(s), highest expression level in ileum. DR CleanEx; MM_POLR3C; -. 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:0003899; F:DNA-directed 5'-3' RNA polymerase 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: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 GO; GO:0006383; P:transcription by RNA polymerase III; IEA:GOC. DR Gene3D; 1.10.10.10; -; 4. DR InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH. DR InterPro; IPR008806; RNA_pol_III_Rpc82_C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR Pfam; PF08221; HTH_9; 1. DR Pfam; PF05645; RNA_pol_Rpc82; 1. PE 1: Evidence at protein level; KW Alternative splicing; Antiviral defense; Complete proteome; KW DNA-binding; DNA-directed RNA polymerase; Immunity; Innate immunity; KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transferase. FT CHAIN 1 533 DNA-directed RNA polymerase III subunit FT RPC3. FT /FTId=PRO_0000073964. FT MOD_RES 194 194 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BUI4}. FT VAR_SEQ 199 202 GKRR -> DFTS (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_010678. FT VAR_SEQ 203 533 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_010679. FT CONFLICT 171 171 R -> P (in Ref. 2; AAH26793). FT {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 //