RPC10_MOUSE
ID RPC10_MOUSE Reviewed; 108 AA.
AC Q9CQZ7; Q9D1U1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC10;
DE Short=RNA polymerase III subunit C10;
DE AltName: Full=DNA-directed RNA polymerase III subunit K;
DE AltName: Full=RNA polymerase III subunit C11;
DE Short=RPC11;
GN Name=Polr3k;
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;
RC TISSUE=Cerebellum, Embryonic liver, Forelimb, and Mammary gland;
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase III which synthesizes small RNAs, such as
CC 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection
CC by intracellular bacteria and DNA viruses. Acts as nuclear and
CC cytosolic DNA sensor involved in innate immune response. Can sense non-
CC self dsDNA that serves as template for transcription into dsRNA. The
CC non-self RNA polymerase III transcripts induce type I interferon and
CC NF-kappa-B through the RIG-I pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2Y1}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250|UniProtKB:Q9Y2Y1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AK005152; BAB23846.1; -; mRNA.
DR EMBL; AK010875; BAB27239.1; -; mRNA.
DR EMBL; AK021353; BAB32384.1; -; mRNA.
DR EMBL; AK031110; BAC27257.1; -; mRNA.
DR CCDS; CCDS17225.1; -.
DR RefSeq; NP_080177.1; NM_025901.3.
DR AlphaFoldDB; Q9CQZ7; -.
DR SMR; Q9CQZ7; -.
DR BioGRID; 211869; 12.
DR STRING; 10090.ENSMUSP00000044582; -.
DR PhosphoSitePlus; Q9CQZ7; -.
DR EPD; Q9CQZ7; -.
DR MaxQB; Q9CQZ7; -.
DR PaxDb; Q9CQZ7; -.
DR PRIDE; Q9CQZ7; -.
DR ProteomicsDB; 260923; -.
DR Antibodypedia; 1811; 153 antibodies from 24 providers.
DR DNASU; 67005; -.
DR Ensembl; ENSMUST00000039551; ENSMUSP00000044582; ENSMUSG00000038628.
DR GeneID; 67005; -.
DR KEGG; mmu:67005; -.
DR UCSC; uc008onw.1; mouse.
DR CTD; 51728; -.
DR MGI; MGI:1914255; Polr3k.
DR VEuPathDB; HostDB:ENSMUSG00000038628; -.
DR eggNOG; KOG2906; Eukaryota.
DR GeneTree; ENSGT00550000075071; -.
DR HOGENOM; CLU_093932_3_0_1; -.
DR InParanoid; Q9CQZ7; -.
DR OMA; MVKFCPK; -.
DR OrthoDB; 1508693at2759; -.
DR PhylomeDB; Q9CQZ7; -.
DR TreeFam; TF103031; -.
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; 67005; 32 hits in 75 CRISPR screens.
DR ChiTaRS; Polr3k; mouse.
DR PRO; PR:Q9CQZ7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQZ7; protein.
DR Bgee; ENSMUSG00000038628; Expressed in ciliary body and 263 other tissues.
DR Genevisible; Q9CQZ7; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0006386; P:termination of RNA polymerase III transcription; IBA:GO_Central.
DR GO; GO:0042779; P:tRNA 3'-trailer cleavage; IEA:InterPro.
DR CDD; cd10509; Zn-ribbon_RPC11; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034014; Zn_ribbon_RPC11_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW Antiviral defense; DNA-directed RNA polymerase; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Reference proteome; Transcription; Zinc;
KW Zinc-finger.
FT CHAIN 1..108
FT /note="DNA-directed RNA polymerase III subunit RPC10"
FT /id="PRO_0000121476"
FT ZN_FING 5..28
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 65..107
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT CONFLICT 15
FT /note="E -> V (in Ref. 1; BAB32384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 108 AA; 12330 MW; 3D650FCDB48F9D1B CRC64;
MLLFCPGCGN GLIVEEGQRC HRFACNTCPY VHNITRKVTN RKYPKLKEVD DVLGGAAAWE
NVDSTAEPCP KCEHPRAYFM QLQTRSADEP MTTFYKCCNA QCGHRWRD
