RPC7_HUMAN
ID RPC7_HUMAN Reviewed; 223 AA.
AC O15318; A8MTH0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC7;
DE Short=RNA polymerase III subunit C7;
DE AltName: Full=DNA-directed RNA polymerase III subunit G;
DE AltName: Full=RNA polymerase III 32 kDa apha subunit;
DE Short=RPC32-alpha {ECO:0000303|PubMed:20154270};
DE AltName: Full=RNA polymerase III 32 kDa subunit;
DE Short=RPC32;
GN Name=POLR3G;
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], AND INTERACTION WITH POLR3C AND POLR3F.
RC TISSUE=Cervix carcinoma;
RX PubMed=9171375; DOI=10.1101/gad.11.10.1315;
RA Wang Z., Roeder R.G.;
RT "Three human RNA polymerase III-specific subunits form a subcomplex with a
RT selective function in specific transcription initiation.";
RL Genes Dev. 11:1315-1326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Corpus callosum;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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 IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20154270; DOI=10.1073/pnas.0914980107;
RA Haurie V., Durrieu-Gaillard S., Dumay-Odelot H., Da Silva D., Rey C.,
RA Prochazkova M., Roeder R.G., Besser D., Teichmann M.;
RT "Two isoforms of human RNA polymerase III with specific functions in cell
RT growth and transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4176-4181(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP INTERACTION WITH POLR3C.
RX PubMed=21358628; DOI=10.1038/nsmb.1996;
RA Lefevre S., Dumay-Odelot H., El-Ayoubi L., Budd A., Legrand P., Pinaud N.,
RA Teichmann M., Fribourg S.;
RT "Structure-function analysis of hRPC62 provides insights into RNA
RT polymerase III transcription initiation.";
RL Nat. Struct. Mol. Biol. 18:352-358(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP SUBCELLULAR LOCATION, INDUCTION BY NANOG AND POU5F1, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21898682; DOI=10.1002/stem.714;
RA Wong R.C., Pollan S., Fong H., Ibrahim A., Smith E.L., Ho M., Laslett A.L.,
RA Donovan P.J.;
RT "A novel role for an RNA polymerase III subunit POLR3G in regulating
RT pluripotency in human embryonic stem cells.";
RL Stem Cells 29:1517-1527(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION IN RNA POL III SUBCOMPLEXES, AND TISSUE SPECIFICITY.
RX PubMed=24107381; DOI=10.1101/gr.161570.113;
RA Renaud M., Praz V., Vieu E., Florens L., Washburn M.P., l'Hote P.,
RA Hernandez N.;
RT "Gene duplication and neofunctionalization: POLR3G and POLR3GL.";
RL Genome Res. 24:37-51(2014).
RN [16]
RP INTERACTION WITH POLR3C.
RX PubMed=26394183; DOI=10.1016/j.jsb.2015.09.004;
RA Boissier F., Dumay-Odelot H., Teichmann M., Fribourg S.;
RT "Structural analysis of human RPC32beta-RPC62 complex.";
RL J. Struct. Biol. 192:313-319(2015).
RN [17]
RP INDUCTION.
RX PubMed=27339422; DOI=10.1002/stem.2444;
RA Jin S., Collin J., Zhu L., Montaner D., Armstrong L., Neganova I., Lako M.;
RT "A novel role for miR-1305 in regulation of pluripotency-differentiation
RT balance, cell cycle, and apoptosis in human pluripotent stem cells.";
RL Stem Cells 34:2306-2317(2016).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=28494942; DOI=10.1016/j.stemcr.2017.04.016;
RA Lund R.J., Rahkonen N., Malonzo M., Kauko L., Emani M.R., Kivinen V.,
RA Naervae E., Kemppainen E., Laiho A., Skottman H., Hovatta O., Rasool O.,
RA Nykter M., Laehdesmaeki H., Lahesmaa R.;
RT "RNA polymerase III subunit POLR3G regulates specific subsets of polyA(+)
RT and smallRNA transcriptomes and splicing in human pluripotent stem cells.";
RL Stem Cell Reports 8:1442-1454(2017).
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 (PubMed:20154270). May direct
CC with other members of the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G
CC subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the
CC interactions between TFIIIB and POLR3F. May be involved either in the
CC recruitment and stabilization of the subcomplex within RNA polymerase
CC III, or in stimulating catalytic functions of other subunits during
CC initiation. 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, such as Epstein-Barr virus-encoded RNAs
CC (EBERs), induce type I interferon and NF- Kappa-B through the RIG-I
CC pathway (PubMed:19609254, PubMed:19631370).
CC {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370,
CC ECO:0000269|PubMed:20154270}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). RPC3/POLR3C, RPC6/POLR3F and
CC RPC7/POLR3G form a Pol III subcomplex. Directly interacts with
CC POLR3C/RPC62 (PubMed:21358628, PubMed:24107381, PubMed:26394183). Also
CC found a trimeric complex with POLR3C and POLR3GL (PubMed:24107381).
CC {ECO:0000250, ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:21358628,
CC ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:26394183}.
CC -!- INTERACTION:
CC O15318; Q9BUI4: POLR3C; NbExp=7; IntAct=EBI-12362221, EBI-5452779;
CC O15318; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-12362221, EBI-710067;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154270,
CC ECO:0000269|PubMed:21898682}. Cytoplasm {ECO:0000250|UniProtKB:Q6NXY9}.
CC Note=Excluded from nucleoli (PubMed:21898682). In zygotes and the 2-
CC cell stage embryos, mainly in the cytoplasm. Starts to localize to the
CC nucleus in the 8-16 cell stage embryo and early blastocysts (By
CC similarity). {ECO:0000250|UniProtKB:Q6NXY9,
CC ECO:0000269|PubMed:21898682}.
CC -!- TISSUE SPECIFICITY: Barely detectable in differentiated tissues.
CC Expressed in embryonic stem cells and in other dividing cells, such as
CC some tumor cell lines. {ECO:0000269|PubMed:20154270,
CC ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:28494942}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated in embryonic stem cells upon
CC differentiation into embroid bodies (at protein level)
CC (PubMed:20154270, PubMed:21898682, PubMed:28494942). An analogous down-
CC regulation is observed during differentiation of induced pluripotent
CC stem cells (PubMed:21898682). {ECO:0000269|PubMed:20154270,
CC ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:28494942}.
CC -!- INDUCTION: Induced by NANOG and POU5F1/OCT4 (PubMed:21898682).
CC Negatively regulated by the interaction of microRNA MIR1305 with 3
CC miRNA responsive elements (miREs) in its 3'-UTR (PubMed:27339422).
CC {ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:27339422}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63676.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U93868; AAB63676.1; ALT_FRAME; mRNA.
DR EMBL; AK295434; BAG58376.1; -; mRNA.
DR EMBL; AC027323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95980.1; -; Genomic_DNA.
DR CCDS; CCDS43337.1; -.
DR RefSeq; NP_006458.2; NM_006467.2.
DR RefSeq; XP_005248461.1; XM_005248404.3.
DR RefSeq; XP_011541402.1; XM_011543100.2.
DR RefSeq; XP_011541403.1; XM_011543101.2.
DR RefSeq; XP_011541404.1; XM_011543102.2.
DR RefSeq; XP_016864446.1; XM_017008957.1.
DR PDB; 7A6H; EM; 3.30 A; Q=1-223.
DR PDB; 7AE1; EM; 2.80 A; Q=1-223.
DR PDB; 7AE3; EM; 3.10 A; Q=1-223.
DR PDB; 7AEA; EM; 3.40 A; Q=1-223.
DR PDB; 7D58; EM; 2.90 A; Q=1-223.
DR PDB; 7D59; EM; 3.10 A; Q=1-223.
DR PDB; 7DN3; EM; 3.50 A; Q=1-223.
DR PDB; 7DU2; EM; 3.35 A; Q=1-223.
DR PDB; 7FJI; EM; 3.60 A; Q=1-223.
DR PDB; 7FJJ; EM; 3.60 A; Q=1-223.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; O15318; -.
DR SMR; O15318; -.
DR BioGRID; 115867; 42.
DR DIP; DIP-59079N; -.
DR IntAct; O15318; 8.
DR STRING; 9606.ENSP00000382058; -.
DR iPTMnet; O15318; -.
DR PhosphoSitePlus; O15318; -.
DR BioMuta; POLR3G; -.
DR EPD; O15318; -.
DR jPOST; O15318; -.
DR MassIVE; O15318; -.
DR MaxQB; O15318; -.
DR PaxDb; O15318; -.
DR PeptideAtlas; O15318; -.
DR PRIDE; O15318; -.
DR ProteomicsDB; 48580; -.
DR Antibodypedia; 4114; 115 antibodies from 25 providers.
DR DNASU; 10622; -.
DR Ensembl; ENST00000504930.5; ENSP00000421637.1; ENSG00000113356.13.
DR Ensembl; ENST00000651687.1; ENSP00000498469.1; ENSG00000113356.13.
DR GeneID; 10622; -.
DR KEGG; hsa:10622; -.
DR MANE-Select; ENST00000651687.1; ENSP00000498469.1; NM_006467.3; NP_006458.2.
DR UCSC; uc003kjq.3; human.
DR CTD; 10622; -.
DR DisGeNET; 10622; -.
DR GeneCards; POLR3G; -.
DR HGNC; HGNC:30075; POLR3G.
DR HPA; ENSG00000113356; Low tissue specificity.
DR MIM; 617456; gene.
DR neXtProt; NX_O15318; -.
DR OpenTargets; ENSG00000113356; -.
DR PharmGKB; PA134986024; -.
DR VEuPathDB; HostDB:ENSG00000113356; -.
DR eggNOG; ENOG502RY1A; Eukaryota.
DR GeneTree; ENSGT00940000164875; -.
DR HOGENOM; CLU_084309_0_0_1; -.
DR InParanoid; O15318; -.
DR OMA; HKDWREK; -.
DR OrthoDB; 1403784at2759; -.
DR PhylomeDB; O15318; -.
DR TreeFam; TF103052; -.
DR PathwayCommons; O15318; -.
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; O15318; -.
DR SIGNOR; O15318; -.
DR BioGRID-ORCS; 10622; 35 hits in 1011 CRISPR screens.
DR ChiTaRS; POLR3G; human.
DR GenomeRNAi; 10622; -.
DR Pharos; O15318; Tbio.
DR PRO; PR:O15318; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15318; protein.
DR Bgee; ENSG00000113356; Expressed in dorsal root ganglion and 139 other tissues.
DR ExpressionAtlas; O15318; baseline and differential.
DR Genevisible; O15318; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0008283; P:cell population proliferation; IEP:MGI.
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:0006359; P:regulation of transcription by RNA polymerase III; TAS:ProtInc.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:UniProtKB.
DR InterPro; IPR024661; RNA_pol_III_Rpc31.
DR PANTHER; PTHR15367; PTHR15367; 1.
DR Pfam; PF11705; RNA_pol_3_Rpc31; 1.
DR PIRSF; PIRSF000777; RNA_polIII_C31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; DNA-directed RNA polymerase;
KW Immunity; Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..223
FT /note="DNA-directed RNA polymerase III subunit RPC7"
FT /id="PRO_0000073978"
FT REGION 110..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CONFLICT 96
FT /note="K -> Q (in Ref. 1; AAB63676)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="E -> V (in Ref. 1; AAB63676)"
FT /evidence="ECO:0000305"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7DU2"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7DU2"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:7D59"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:7D59"
SQ SEQUENCE 223 AA; 25914 MW; 95E506D527962DD9 CRC64;
MAGNKGRGRA AYTFNIEAVG FSKGEKLPDV VLKPPPLFPD TDYKPVPLKT GEGEEYMLAL
KQELRETMKR MPYFIETPEE RQDIERYSKR YMKVYKEEWI PDWRRLPREM MPRNKCKKAG
PKPKKAKDAG KGTPLTNTED VLKKMEELEK RGDGEKSDEE NEEKEGSKEK SKEGDDDDDD
DAAEQEEYDE EEQEEENDYI NSYFEDGDDF GADSDDNMDE ATY
