RPC2_MOUSE
ID RPC2_MOUSE Reviewed; 1133 AA.
AC P59470; Q6NVF3;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC2;
DE Short=RNA polymerase III subunit C2;
DE EC=2.7.7.6;
DE AltName: Full=C128;
DE AltName: Full=DNA-directed RNA polymerase III 127.6 kDa polypeptide;
DE AltName: Full=DNA-directed RNA polymerase III subunit B;
GN Name=Polr3b;
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=Brain, and Mammary 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, 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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest core component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the
CC polymerase catalytic activity and forms the polymerase active center
CC together with the largest subunit. Pol III is composed of mobile
CC elements and RPC2 is part of the core element with the central large
CC cleft and probably a clamp element that moves to open and close the
CC cleft. 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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC044796; AAH44796.1; ALT_INIT; mRNA.
DR EMBL; BC068143; AAH68143.1; -; mRNA.
DR EMBL; AK039366; BAC30327.1; -; mRNA.
DR CCDS; CCDS24081.1; -.
DR RefSeq; NP_081699.1; NM_027423.1.
DR AlphaFoldDB; P59470; -.
DR SMR; P59470; -.
DR BioGRID; 214044; 32.
DR STRING; 10090.ENSMUSP00000076418; -.
DR iPTMnet; P59470; -.
DR PhosphoSitePlus; P59470; -.
DR EPD; P59470; -.
DR MaxQB; P59470; -.
DR PaxDb; P59470; -.
DR PeptideAtlas; P59470; -.
DR PRIDE; P59470; -.
DR ProteomicsDB; 300436; -.
DR Antibodypedia; 30662; 177 antibodies from 28 providers.
DR DNASU; 70428; -.
DR Ensembl; ENSMUST00000077175; ENSMUSP00000076418; ENSMUSG00000034453.
DR GeneID; 70428; -.
DR KEGG; mmu:70428; -.
DR UCSC; uc007gku.1; mouse.
DR CTD; 55703; -.
DR MGI; MGI:1917678; Polr3b.
DR VEuPathDB; HostDB:ENSMUSG00000034453; -.
DR eggNOG; KOG0215; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P59470; -.
DR OMA; LAYCSWC; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P59470; -.
DR TreeFam; TF103047; -.
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; 70428; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Polr3b; mouse.
DR PRO; PR:P59470; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P59470; protein.
DR Bgee; ENSMUSG00000034453; Expressed in embryonic post-anal tail and 219 other tissues.
DR ExpressionAtlas; P59470; baseline and differential.
DR Genevisible; P59470; MM.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside 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: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 CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; DNA-directed RNA polymerase; Immunity; Innate immunity;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1133
FT /note="DNA-directed RNA polymerase III subunit RPC2"
FT /id="PRO_0000048093"
FT ZN_FING 1080..1095
FT /note="C4-type"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1083
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 465
FT /note="V -> E (in Ref. 2; BAC30327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1133 AA; 127715 MW; 7B900B187F2753AF CRC64;
MDVLAEEFGS LTPEQLTAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK
ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT
RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI
QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF
KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG
PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK
RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS
TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC
PSDTPEGEAC GLVKNLALMT HITTDMEDGP IIKLAGNLGV EDVNLLCGEE LSYPNVFLVF
LNGNILGVIR DHKKLVSTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK
KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE
PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV
KTKTIELIDF EKLPAGQNAT VAVMSYSGYD IEDALVLNKA SLDRGFGRCL VYKNAKCTLK
RYTNQTFDKV MGPMLDAATR KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL
EGSNVPQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR
HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK AGVLDGRFHY
GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA YIYFGPVYYQ KLKHMVLDKM
HARARGPRAV LTRQPTEGRS RDGGLRLGEM ERDCLIGYGA SMLLLERLMI SSDAFEVDVC
GQCGLLGYSG WCHYCKSSCH VSSLRIPYAC KLLFQELQSM NIIPRLKLAK YNE
