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 24-JAN-2024, entry version 148.
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}.
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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.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 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.
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
//
