RPC6_MOUSE
ID RPC6_MOUSE Reviewed; 316 AA.
AC Q921X6; Q544K6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC6;
DE Short=RNA polymerase III subunit C6;
DE AltName: Full=DNA-directed RNA polymerase III subunit F;
GN Name=Polr3f;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Lung;
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].
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=Spleen, and 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).
RN [4]
RP STRUCTURE BY NMR OF 11-79.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RPC34 subunit in RNA polymerase III from mouse.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. May direct RNA Pol III binding
CC to the TFIIIB-DNA complex. Plays a key role in sensing and limiting
CC infection by intracellular bacteria and DNA viruses. Acts as nuclear
CC and cytosolic DNA sensor involved in innate immune response. Can sense
CC non-self dsDNA that serves as template for transcription into dsRNA.
CC The non-self RNA polymerase III transcripts induce type I interferon
CC and NF- Kappa-B through the RIG-I pathway (By similarity).
CC Preferentially binds double-stranded DNA (dsDNA) (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9H1D9}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G
CC form a Pol III subcomplex (By similarity). Directly interacts with
CC POLR3C (By similarity). Interacts with TBP and TFIIIB90 and GTF3C4 (By
CC similarity). Interacts with MAF1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9H1D9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AK036166; BAC29327.1; -; mRNA.
DR EMBL; AK076538; BAC36385.1; -; mRNA.
DR EMBL; AK144679; BAE26008.1; -; mRNA.
DR EMBL; BC009159; AAH09159.1; -; mRNA.
DR CCDS; CCDS16820.1; -.
DR RefSeq; NP_084039.2; NM_029763.3.
DR PDB; 2DK8; NMR; -; A=11-78.
DR PDBsum; 2DK8; -.
DR AlphaFoldDB; Q921X6; -.
DR SMR; Q921X6; -.
DR BioGRID; 214030; 17.
DR IntAct; Q921X6; 3.
DR STRING; 10090.ENSMUSP00000028914; -.
DR iPTMnet; Q921X6; -.
DR PhosphoSitePlus; Q921X6; -.
DR EPD; Q921X6; -.
DR MaxQB; Q921X6; -.
DR PaxDb; Q921X6; -.
DR PRIDE; Q921X6; -.
DR ProteomicsDB; 300477; -.
DR Antibodypedia; 24572; 197 antibodies from 29 providers.
DR DNASU; 70408; -.
DR Ensembl; ENSMUST00000028914; ENSMUSP00000028914; ENSMUSG00000027427.
DR GeneID; 70408; -.
DR KEGG; mmu:70408; -.
DR UCSC; uc008mrg.1; mouse.
DR CTD; 10621; -.
DR MGI; MGI:1924086; Polr3f.
DR VEuPathDB; HostDB:ENSMUSG00000027427; -.
DR eggNOG; KOG3233; Eukaryota.
DR GeneTree; ENSGT00390000009679; -.
DR HOGENOM; CLU_033661_1_0_1; -.
DR InParanoid; Q921X6; -.
DR OMA; CEYMRDW; -.
DR OrthoDB; 1287786at2759; -.
DR PhylomeDB; Q921X6; -.
DR TreeFam; TF103051; -.
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; 70408; 16 hits in 73 CRISPR screens.
DR EvolutionaryTrace; Q921X6; -.
DR PRO; PR:Q921X6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q921X6; protein.
DR Bgee; ENSMUSG00000027427; Expressed in saccule of membranous labyrinth and 248 other tissues.
DR ExpressionAtlas; Q921X6; baseline and differential.
DR Genevisible; Q921X6; MM.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
DR GO; GO:0003690; F:double-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:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR007832; RNA_pol_Rpc34.
DR InterPro; IPR016049; RNA_pol_Rpc34-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12780; PTHR12780; 1.
DR Pfam; PF05158; RNA_pol_Rpc34; 1.
DR PIRSF; PIRSF028763; RNA_pol_Rpc34; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; DNA-directed RNA polymerase;
KW Immunity; Innate immunity; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H1D9"
FT CHAIN 2..316
FT /note="DNA-directed RNA polymerase III subunit RPC6"
FT /id="PRO_0000073973"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1D9"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H1D9"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H1D9"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2DK8"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:2DK8"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:2DK8"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:2DK8"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2DK8"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2DK8"
SQ SEQUENCE 316 AA; 35652 MW; 0CEB63A5B3536421 CRC64;
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR AVAINRLLSM
GQLDLLRSNT GLLYRIKDSQ NAGKMKGSDN QEKLVYQIIE DAGNKGIWSR DIRYKSNLPL
TEINKILKNL ESKKLIKAVK SVAASKKKVY MLYNLQPDRS VTGGAWYSDQ DFESEFVEVL
NQQCFKFLQS KAETARESKQ NPVIQRNSSF ASSHEVWKYI CELGISKVEL SMEDIETILN
TLIYDGKVEM TIIAAKEGTV GSVDGHMKLY RAVNPILPPT GVVRAPCGLC PVFEDCHEGG
EISPSNCIYM TEWLEF
