RPC3_MOUSE
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 03-AUG-2022, entry version 140.
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. {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}.
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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 PRIDE; Q9D483; -.
DR ProteomicsDB; 299940; -. [Q9D483-1]
DR ProteomicsDB; 299941; -. [Q9D483-2]
DR Antibodypedia; 33966; 256 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 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; FETNECD; -.
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 78 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: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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; IPR039748; RPC3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12949; PTHR12949; 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
