RPC2_HUMAN
ID RPC2_HUMAN Reviewed; 1133 AA.
AC Q9NW08; A8K6H0; B3KV73; F5H1E6; Q9NW59;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE RNA POL III
RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, Teratocarcinoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [6]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [7]
RP FUNCTION.
RX PubMed=19609254; DOI=10.1038/ni.1779;
RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA Hornung V.;
RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA
RT polymerase III-transcribed RNA intermediate.";
RL Nat. Immunol. 10:1065-1072(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [10]
RP VARIANTS HLD8 620-ASN--LYS-652 DEL; HIS-768 AND GLU-926, AND INVOLVEMENT IN
RP HLD8.
RX PubMed=22036171; DOI=10.1016/j.ajhg.2011.10.003;
RA Saitsu H., Osaka H., Sasaki M., Takanashi J., Hamada K., Yamashita A.,
RA Shibayama H., Shiina M., Kondo Y., Nishiyama K., Tsurusaki Y., Miyake N.,
RA Doi H., Ogata K., Inoue K., Matsumoto N.;
RT "Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits cause
RT an autosomal-recessive hypomyelinating leukoencephalopathy.";
RL Am. J. Hum. Genet. 89:644-651(2011).
RN [11]
RP VARIANTS HLD8 LYS-503 AND GLU-523.
RX PubMed=22036172; DOI=10.1016/j.ajhg.2011.10.006;
RA Tetreault M., Choquet K., Orcesi S., Tonduti D., Balottin U., Teichmann M.,
RA Fribourg S., Schiffmann R., Brais B., Vanderver A., Bernard G.;
RT "Recessive mutations in POLR3B, encoding the second largest subunit of Pol
RT III, cause a rare hypomyelinating leukodystrophy.";
RL Am. J. Hum. Genet. 89:652-655(2011).
RN [12]
RP VARIANTS HLD8 PHE-104; GLY-268; CYS-442; GLU-523 AND ARG-527.
RX PubMed=23355746; DOI=10.1136/jmedgenet-2012-101357;
RA Daoud H., Tetreault M., Gibson W., Guerrero K., Cohen A.,
RA Gburek-Augustat J., Synofzik M., Brais B., Stevens C.A.,
RA Sanchez-Carpintero R., Goizet C., Naidu S., Vanderver A., Bernard G.;
RT "Mutations in POLR3A and POLR3B are a major cause of hypomyelinating
RT leukodystrophies with or without dental abnormalities and/or
RT hypogonadotropic hypogonadism.";
RL J. Med. Genet. 50:194-197(2013).
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 (By similarity). 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, such as Epstein-Barr
CC virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B
CC through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254,
CC ECO:0000269|PubMed:19631370}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NW08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NW08-2; Sequence=VSP_045286;
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 8, with or without
CC oligodontia and/or hypogonadotropic hypogonadism (HLD8) [MIM:614381]:
CC An autosomal recessive neurodegenerative disorder characterized by
CC early childhood onset of cerebellar ataxia and mild intellectual
CC disabilities associated with diffuse hypomyelination apparent on brain
CC MRI. Variable features include oligodontia and/or hypogonadotropic
CC hypogonadism. {ECO:0000269|PubMed:22036171,
CC ECO:0000269|PubMed:22036172, ECO:0000269|PubMed:23355746}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY092084; AAM18214.1; -; mRNA.
DR EMBL; AK001161; BAA91527.1; ALT_INIT; mRNA.
DR EMBL; AK001250; BAA91581.1; ALT_INIT; mRNA.
DR EMBL; AK122713; BAG53685.1; -; mRNA.
DR EMBL; AK291635; BAF84324.1; -; mRNA.
DR EMBL; AC009721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97780.1; -; Genomic_DNA.
DR EMBL; BC046238; AAH46238.1; -; mRNA.
DR CCDS; CCDS53824.1; -. [Q9NW08-2]
DR CCDS; CCDS9105.1; -. [Q9NW08-1]
DR RefSeq; NP_001154180.1; NM_001160708.1. [Q9NW08-2]
DR RefSeq; NP_060552.4; NM_018082.5. [Q9NW08-1]
DR PDB; 7A6H; EM; 3.30 A; B=1-1133.
DR PDB; 7AE1; EM; 2.80 A; B=1-1133.
DR PDB; 7AE3; EM; 3.10 A; B=1-1133.
DR PDB; 7AEA; EM; 3.40 A; B=1-1133.
DR PDB; 7AST; EM; 4.00 A; M=1-1133.
DR PDB; 7D58; EM; 2.90 A; B=1-1133.
DR PDB; 7D59; EM; 3.10 A; B=1-1133.
DR PDB; 7DN3; EM; 3.50 A; B=1-1133.
DR PDB; 7DU2; EM; 3.35 A; B=1-1133.
DR PDB; 7FJI; EM; 3.60 A; B=1-1133.
DR PDB; 7FJJ; EM; 3.60 A; B=1-1133.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; Q9NW08; -.
DR SMR; Q9NW08; -.
DR BioGRID; 120828; 103.
DR IntAct; Q9NW08; 24.
DR MINT; Q9NW08; -.
DR STRING; 9606.ENSP00000228347; -.
DR iPTMnet; Q9NW08; -.
DR MetOSite; Q9NW08; -.
DR PhosphoSitePlus; Q9NW08; -.
DR BioMuta; POLR3B; -.
DR DMDM; 29428029; -.
DR EPD; Q9NW08; -.
DR jPOST; Q9NW08; -.
DR MassIVE; Q9NW08; -.
DR MaxQB; Q9NW08; -.
DR PaxDb; Q9NW08; -.
DR PeptideAtlas; Q9NW08; -.
DR PRIDE; Q9NW08; -.
DR ProteomicsDB; 25631; -.
DR ProteomicsDB; 82885; -. [Q9NW08-1]
DR Antibodypedia; 30662; 177 antibodies from 28 providers.
DR DNASU; 55703; -.
DR Ensembl; ENST00000228347.9; ENSP00000228347.4; ENSG00000013503.10. [Q9NW08-1]
DR Ensembl; ENST00000539066.5; ENSP00000445721.1; ENSG00000013503.10. [Q9NW08-2]
DR GeneID; 55703; -.
DR KEGG; hsa:55703; -.
DR MANE-Select; ENST00000228347.9; ENSP00000228347.4; NM_018082.6; NP_060552.4.
DR UCSC; uc001tlp.3; human. [Q9NW08-1]
DR CTD; 55703; -.
DR DisGeNET; 55703; -.
DR GeneCards; POLR3B; -.
DR GeneReviews; POLR3B; -.
DR HGNC; HGNC:30348; POLR3B.
DR HPA; ENSG00000013503; Low tissue specificity.
DR MalaCards; POLR3B; -.
DR MIM; 614366; gene.
DR MIM; 614381; phenotype.
DR neXtProt; NX_Q9NW08; -.
DR OpenTargets; ENSG00000013503; -.
DR Orphanet; 85186; Endosteal sclerosis-cerebellar hypoplasia syndrome.
DR Orphanet; 88637; Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome.
DR PharmGKB; PA134867680; -.
DR VEuPathDB; HostDB:ENSG00000013503; -.
DR eggNOG; KOG0215; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; Q9NW08; -.
DR OMA; LAYCSWC; -.
DR PhylomeDB; Q9NW08; -.
DR TreeFam; TF103047; -.
DR PathwayCommons; Q9NW08; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; Q9NW08; -.
DR SIGNOR; Q9NW08; -.
DR BioGRID-ORCS; 55703; 798 hits in 1095 CRISPR screens.
DR ChiTaRS; POLR3B; human.
DR GenomeRNAi; 55703; -.
DR Pharos; Q9NW08; Tbio.
DR PRO; PR:Q9NW08; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NW08; protein.
DR Bgee; ENSG00000013503; Expressed in secondary oocyte and 163 other tissues.
DR ExpressionAtlas; Q9NW08; baseline and differential.
DR Genevisible; Q9NW08; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA: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; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP: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 3D-structure; Alternative splicing; Antiviral defense; Disease variant;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Leukodystrophy;
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_0000048092"
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 VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045286"
FT VARIANT 104
FT /note="L -> F (in HLD8)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072344"
FT VARIANT 268
FT /note="S -> G (in HLD8)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072345"
FT VARIANT 442
FT /note="R -> C (in HLD8; dbSNP:rs1442212683)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072346"
FT VARIANT 503
FT /note="T -> K (in HLD8; dbSNP:rs267608683)"
FT /evidence="ECO:0000269|PubMed:22036172"
FT /id="VAR_067005"
FT VARIANT 523
FT /note="V -> E (in HLD8; dbSNP:rs138249161)"
FT /evidence="ECO:0000269|PubMed:22036172,
FT ECO:0000269|PubMed:23355746"
FT /id="VAR_067006"
FT VARIANT 527
FT /note="C -> R (in HLD8)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072347"
FT VARIANT 620..652
FT /note="Missing (in HLD8)"
FT /evidence="ECO:0000269|PubMed:22036171"
FT /id="VAR_067007"
FT VARIANT 740
FT /note="T -> A (in dbSNP:rs17038460)"
FT /id="VAR_057255"
FT VARIANT 768
FT /note="R -> H (in HLD8; dbSNP:rs267608687)"
FT /evidence="ECO:0000269|PubMed:22036171"
FT /id="VAR_067008"
FT VARIANT 926
FT /note="D -> E (in HLD8; dbSNP:rs267608689)"
FT /evidence="ECO:0000269|PubMed:22036171"
FT /id="VAR_067009"
FT CONFLICT 258
FT /note="E -> A (in Ref. 1; AAM18214)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="T -> I (in Ref. 2; BAG53685)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="R -> C (in Ref. 2; BAA91527)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7AE3"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:7DU2"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 365..391
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 488..492
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:7D59"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 552..564
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 592..600
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 621..626
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 635..640
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 661..664
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 680..692
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 699..702
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 707..714
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 737..744
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 755..758
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 759..764
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 769..779
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 797..799
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:7D59"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 864..873
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 879..889
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 896..898
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 900..902
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 905..911
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 913..915
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 933..937
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 940..953
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 969..978
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 983..987
FT /evidence="ECO:0007829|PDB:7D58"
FT TURN 992..994
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 995..997
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1002..1013
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1021..1025
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1039..1042
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1045..1047
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1049..1057
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1061..1068
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1069..1072
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1074..1080
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1081..1083
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1093..1096
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1097..1107
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1108..1119
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1123..1130
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 1133 AA; 127785 MW; F0B3AFF892DDED7D CRC64;
MDVLAEEFGN LTPEQLAAPI 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 IVKLASNLGV EDVNLLCGEE LSYPNVFLVF
LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK
KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE
PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV
KTKTIELIEF 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 NIIPRLKLSK YNE
