ID RPC3_HUMAN Reviewed; 534 AA. AC Q9BUI4; O15317; Q9Y3R6; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 08-NOV-2023, entry version 170. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC3; DE Short=RNA polymerase III subunit C3; DE AltName: Full=DNA-directed RNA polymerase III subunit C; DE AltName: Full=RNA polymerase III 62 kDa subunit; DE Short=RPC62; GN Name=POLR3C; 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], INTERACTION WITH POLR3G AND POLR3F, AND VARIANT RP ARG-243. 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 [MRNA], AND IDENTIFICATION AS ANTIGEN IN SYSTEMIC RP SCLEROSIS. RX PubMed=12384934; DOI=10.1002/art.10521; RA Kuwana M., Kimura K., Kawakami Y.; RT "Identification of an immunodominant epitope on RNA polymerase III RT recognized by systemic sclerosis sera: application to enzyme-linked RT immunosorbent assay."; RL Arthritis Rheum. 46:2742-2747(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Totaro A.; RT "Genomic structure of human RNA polymerase III subunit (RPC62)."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [5] RP INTERACTION WITH GTF3C4. RX PubMed=10523658; DOI=10.1128/mcb.19.11.7697; RA Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.; RT "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RT RNA polymerase III machinery and contains a histone-specific RT acetyltransferase activity."; RL Mol. Cell. Biol. 19:7697-7704(1999). RN [6] RP INTERACTION WITH PKP2. RX PubMed=11416169; DOI=10.1073/pnas.141219498; RA Mertens C., Hofmann I., Wang Z., Teichmann M., Sepehri Chong S., RA Schnoelzer M., Franke W.W.; RT "Nuclear particles containing RNA polymerase III complexes associated with RT the junctional plaque protein plakophilin 2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7795-7800(2001). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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 [9] 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 [10] 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 [11] 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 [12] RP IDENTIFICATION BY 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 INTERACTION WITH POLR3G AND POLR3GL. 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 [14] {ECO:0007744|PDB:2XUB, ECO:0007744|PDB:2XV4} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, INTERACTION WITH POLR3F; RP POLR3G AND POLR3GL, AND MUTAGENESIS OF 51-LYS-LYS-52; LEU-312; ARG-357; RP 364-ARG--ARG-367; LYS-389; 445-ASN--ARG-449 AND 466-ARG--ILE-470. 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 [15] {ECO:0007744|PDB:5AFQ} RP X-RAY CRYSTALLOGRAPHY (7.00 ANGSTROMS) IN COMPLEX WITH POLR3GL. 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). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Specific core component of RNA polymerase III which synthesizes small CC RNAs, such as 5S rRNA and tRNAs. May direct with other members of the 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. Preferentially binds single-stranded DNA (ssDNA) in a CC sequence-independent manner (PubMed:21358628). CC {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, CC ECO:0000269|PubMed:21358628}. 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 (PubMed:9171375, CC PubMed:12391170). Directly interacts with POLR3G and POLR3GL CC (PubMed:24107381, PubMed:21358628, PubMed:26394183). Directly interacts CC with POLR3F/RPC39 (PubMed:26394183). Interacts with GTF3C4 CC (PubMed:10523658). As part of the RNA polymerase III (Pol III) complex, CC interacts with PKP2 (PubMed:11416169). {ECO:0000250, CC ECO:0000269|PubMed:10523658, ECO:0000269|PubMed:11416169, CC ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:21358628, CC ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:26394183, CC ECO:0000269|PubMed:9171375}. CC -!- INTERACTION: CC Q9BUI4; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-5452779, EBI-5661893; CC Q9BUI4; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-5452779, EBI-11523526; CC Q9BUI4; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-5452779, EBI-744115; CC Q9BUI4; Q96MT8-3: CEP63; NbExp=5; IntAct=EBI-5452779, EBI-11522539; CC Q9BUI4; P38432: COIL; NbExp=3; IntAct=EBI-5452779, EBI-945751; CC Q9BUI4; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-5452779, EBI-11988027; CC Q9BUI4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-5452779, EBI-744099; CC Q9BUI4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-5452779, EBI-618309; CC Q9BUI4; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-5452779, EBI-2514791; CC Q9BUI4; Q0VD86: INCA1; NbExp=3; IntAct=EBI-5452779, EBI-6509505; CC Q9BUI4; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-5452779, EBI-715394; CC Q9BUI4; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-5452779, EBI-739493; CC Q9BUI4; O95198: KLHL2; NbExp=3; IntAct=EBI-5452779, EBI-746999; CC Q9BUI4; P52294: KPNA1; NbExp=3; IntAct=EBI-5452779, EBI-358383; CC Q9BUI4; O00505: KPNA3; NbExp=3; IntAct=EBI-5452779, EBI-358297; CC Q9BUI4; O15131: KPNA5; NbExp=5; IntAct=EBI-5452779, EBI-540602; CC Q9BUI4; O60684: KPNA6; NbExp=5; IntAct=EBI-5452779, EBI-359923; CC Q9BUI4; O95678: KRT75; NbExp=3; IntAct=EBI-5452779, EBI-2949715; CC Q9BUI4; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-5452779, EBI-1216080; CC Q9BUI4; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-5452779, EBI-10963850; CC Q9BUI4; P26367: PAX6; NbExp=3; IntAct=EBI-5452779, EBI-747278; CC Q9BUI4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5452779, EBI-79165; CC Q9BUI4; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-5452779, EBI-10171633; CC Q9BUI4; Q9H1D9: POLR3F; NbExp=2; IntAct=EBI-5452779, EBI-710067; CC Q9BUI4; O15318: POLR3G; NbExp=7; IntAct=EBI-5452779, EBI-12362221; CC Q9BUI4; Q9BT43: POLR3GL; NbExp=7; IntAct=EBI-5452779, EBI-2855862; CC Q9BUI4; P78424: POU6F2; NbExp=3; IntAct=EBI-5452779, EBI-12029004; CC Q9BUI4; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-5452779, EBI-11322432; CC Q9BUI4; Q13464: ROCK1; NbExp=3; IntAct=EBI-5452779, EBI-876651; CC Q9BUI4; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-5452779, EBI-1378139; CC Q9BUI4; P23497-2: SP100; NbExp=3; IntAct=EBI-5452779, EBI-6589365; CC Q9BUI4; A1L306: TNR; NbExp=3; IntAct=EBI-5452779, EBI-10182881; CC Q9BUI4; Q12933: TRAF2; NbExp=3; IntAct=EBI-5452779, EBI-355744; CC Q9BUI4; P14373: TRIM27; NbExp=6; IntAct=EBI-5452779, EBI-719493; CC Q9BUI4; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-5452779, EBI-11530712; CC Q9BUI4; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-5452779, EBI-12227803; CC Q9BUI4; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-5452779, EBI-12894399; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- MISCELLANEOUS: Antibodies against POLR3C have been found in the sera of CC patients with systemic sclerosis (SSc). CC -!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase CC subunit family. {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; U93867; AAB63675.1; -; mRNA. DR EMBL; AY091463; AAM12033.1; -; mRNA. DR EMBL; AJ238221; CAB41919.1; -; Genomic_DNA. DR EMBL; AJ238222; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238223; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238224; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238225; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238226; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238227; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238228; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238229; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238230; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238231; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238232; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238233; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; AJ238234; CAB41919.1; JOINED; Genomic_DNA. DR EMBL; BC002586; AAH02586.1; -; mRNA. DR CCDS; CCDS72864.1; -. DR RefSeq; NP_001290385.1; NM_001303456.1. DR RefSeq; NP_006459.3; NM_006468.7. DR PDB; 2XUB; X-ray; 2.80 A; A=1-534. DR PDB; 2XV4; X-ray; 2.95 A; S=1-534. DR PDB; 5AFQ; X-ray; 7.00 A; A/B=1-534. DR PDB; 7A6H; EM; 3.30 A; O=1-534. DR PDB; 7AE1; EM; 2.80 A; O=1-534. DR PDB; 7AE3; EM; 3.10 A; O=1-534. DR PDB; 7AEA; EM; 3.40 A; O=1-534. DR PDB; 7AST; EM; 4.00 A; X=1-534. DR PDB; 7D58; EM; 2.90 A; O=1-534. DR PDB; 7D59; EM; 3.10 A; O=1-534. DR PDB; 7DN3; EM; 3.50 A; O=1-534. DR PDB; 7DU2; EM; 3.35 A; O=1-534. DR PDB; 7FJI; EM; 3.60 A; O=1-534. DR PDB; 7FJJ; EM; 3.60 A; O=1-534. DR PDB; 8ITY; EM; 3.90 A; O=1-534. DR PDB; 8IUE; EM; 4.10 A; O=1-534. DR PDB; 8IUH; EM; 3.40 A; O=1-534. DR PDBsum; 2XUB; -. DR PDBsum; 2XV4; -. DR PDBsum; 5AFQ; -. 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 PDBsum; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR AlphaFoldDB; Q9BUI4; -. DR SMR; Q9BUI4; -. DR BioGRID; 115868; 106. DR ComplexPortal; CPX-2393; DNA-directed RNA polymerase III complex, POLR3G variant. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR DIP; DIP-59078N; -. DR IntAct; Q9BUI4; 50. DR STRING; 9606.ENSP00000334564; -. DR GlyGen; Q9BUI4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BUI4; -. DR MetOSite; Q9BUI4; -. DR PhosphoSitePlus; Q9BUI4; -. DR SwissPalm; Q9BUI4; -. DR BioMuta; POLR3C; -. DR DMDM; 60393871; -. DR EPD; Q9BUI4; -. DR jPOST; Q9BUI4; -. DR MassIVE; Q9BUI4; -. DR MaxQB; Q9BUI4; -. DR PaxDb; 9606-ENSP00000334564; -. DR PeptideAtlas; Q9BUI4; -. DR ProteomicsDB; 79088; -. DR Pumba; Q9BUI4; -. DR Antibodypedia; 33966; 267 antibodies from 24 providers. DR DNASU; 10623; -. DR Ensembl; ENST00000334163.4; ENSP00000334564.3; ENSG00000186141.10. DR Ensembl; ENST00000698751.1; ENSP00000513913.1; ENSG00000186141.10. DR GeneID; 10623; -. DR KEGG; hsa:10623; -. DR MANE-Select; ENST00000334163.4; ENSP00000334564.3; NM_006468.8; NP_006459.3. DR UCSC; uc001eoh.3; human. DR AGR; HGNC:30076; -. DR CTD; 10623; -. DR DisGeNET; 10623; -. DR GeneCards; POLR3C; -. DR HGNC; HGNC:30076; POLR3C. DR HPA; ENSG00000186141; Low tissue specificity. DR MIM; 617454; gene. DR neXtProt; NX_Q9BUI4; -. DR OpenTargets; ENSG00000186141; -. DR PharmGKB; PA134870963; -. DR VEuPathDB; HostDB:ENSG00000186141; -. DR eggNOG; KOG2587; Eukaryota. DR GeneTree; ENSGT00390000002799; -. DR HOGENOM; CLU_023294_1_1_1; -. DR InParanoid; Q9BUI4; -. DR OMA; QHNLLWH; -. DR OrthoDB; 2875034at2759; -. DR PhylomeDB; Q9BUI4; -. DR TreeFam; TF103048; -. DR PathwayCommons; Q9BUI4; -. 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; Q9BUI4; -. DR SIGNOR; Q9BUI4; -. DR BioGRID-ORCS; 10623; 749 hits in 1180 CRISPR screens. DR ChiTaRS; POLR3C; human. DR EvolutionaryTrace; Q9BUI4; -. DR GeneWiki; POLR3C; -. DR GenomeRNAi; 10623; -. DR Pharos; Q9BUI4; Tbio. DR PRO; PR:Q9BUI4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BUI4; Protein. DR Bgee; ENSG00000186141; Expressed in calcaneal tendon and 177 other tissues. DR ExpressionAtlas; Q9BUI4; baseline and differential. DR Genevisible; Q9BUI4; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. 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 Gene3D; 6.10.140.1450; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 4. DR InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH. DR InterPro; IPR008806; RNA_pol_III_Rpc82_C. DR InterPro; IPR039748; RPC3. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR12949:SF0; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3; 1. DR PANTHER; PTHR12949; RNA POLYMERASE III DNA DIRECTED -RELATED; 1. DR Pfam; PF08221; HTH_9; 1. DR Pfam; PF05645; RNA_pol_Rpc82; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; DNA-binding; DNA-directed RNA polymerase; KW Immunity; Innate immunity; Nucleus; Phosphoprotein; Reference proteome; KW Transcription. FT CHAIN 1..534 FT /note="DNA-directed RNA polymerase III subunit RPC3" FT /id="PRO_0000073963" FT REGION 161..181 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VARIANT 243 FT /note="H -> R (in dbSNP:rs1044697)" FT /evidence="ECO:0000269|PubMed:9171375" FT /id="VAR_019083" FT MUTAGEN 51..52 FT /note="KK->EE: Strongly decreased ssDNA-binding. No effect FT on interaction with POLR3F, POLR3G, nor with POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 312 FT /note="L->K: Loss of interaction with POLR3G and POLR3GL. FT No effect on interaction with POLR3F." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 357 FT /note="R->E: Strongly decreased ssDNA-binding. No effect on FT interaction with POLR3F, POLR3G, nor with POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 364..367 FT /note="RIFR->EIFE: Strongly decreased ssDNA-binding. No FT effect on interaction with POLR3F, POLR3G, nor with FT POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 389 FT /note="K->E: Strongly decreased ssDNA-binding. No effect on FT interaction with POLR3F, POLR3G, nor with POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 445..449 FT /note="NLIER->ALIEE: Strongly decreased ssDNA-binding. No FT effect on interaction with POLR3F, POLR3G, nor with FT POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT MUTAGEN 466..470 FT /note="RVEAI->EVEAF: Mild decrease in ssDNA-binding. No FT effect on interaction with POLR3F, POLR3G, nor with FT POLR3GL." FT /evidence="ECO:0000269|PubMed:21358628" FT CONFLICT 85..86 FT /note="ML -> IV (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 119..120 FT /note="SA -> CT (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 216..237 FT /note="KRPKYTTDNKEPIPDDGIYWQA -> RDQNILQITRXPFQMMGFIGRP (in FT Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 289 FT /note="S -> F (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="A -> R (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="F -> C (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 387..389 FT /note="PAK -> LQ (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="E -> G (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 436..437 FT /note="LH -> FD (in Ref. 1; AAB63675)" FT /evidence="ECO:0000305" FT CONFLICT 517 FT /note="D -> E (in Ref. 3; CAB41919)" FT /evidence="ECO:0000305" FT HELIX 3..31 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 36..43 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 47..59 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 62..68 FT /evidence="ECO:0007829|PDB:2XUB" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 79..83 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 88..113 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:7D58" FT HELIX 118..131 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 141..153 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:2XUB" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:7DU2" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 229..232 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 239..258 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 261..272 FT /evidence="ECO:0007829|PDB:2XUB" FT TURN 273..277 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 290..295 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 305..316 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:7DU2" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 333..337 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 338..358 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 360..371 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 377..384 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 388..400 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 417..419 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 421..425 FT /evidence="ECO:0007829|PDB:7D59" FT HELIX 428..456 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 458..472 FT /evidence="ECO:0007829|PDB:2XUB" FT STRAND 473..476 FT /evidence="ECO:0007829|PDB:7AE3" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 485..488 FT /evidence="ECO:0007829|PDB:2XUB" FT HELIX 493..529 FT /evidence="ECO:0007829|PDB:2XUB" SQ SEQUENCE 534 AA; 60612 MW; 0E4CFEE295EE1A55 CRC64; MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH NLVSYQVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYS DTGELIVEEL LLNGKLTMSA VVKKVADRLT ETMEDGKTMD YAEVSNTFVR LADTHFVQRC PSVPTTENSD PGPPPPAPTL VINEKDMYLV PKLSLIGKGK RRRSSDEDAA GEPKAKRPKY TTDNKEPIPD DGIYWQANLD RFHQHFRDQA IVSAVANRMD QTSSEIVRTM LRMSEITTSS SAPFTQPLSS NEIFRSLPVG YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINLHK ALASLATATL ESVVQERFGS RCARIFRLVL QKKHIEQKQV EDFAMIPAKE AKDMLYKMLS ENFMSLQEIP KTPDHAPSRT FYLYTVNILS AARMLLHRCY KSIANLIERR QFETKENKRL LEKSQRVEAI IASMQATGAE EAQLQEIEEM ITAPERQQLE TLKRNVNKLD ASEIQVDETI FLLESYIECT MKRQ //