ID RPC8_HUMAN Reviewed; 204 AA.
AC Q9Y535; B0QYH9; Q5M7Y8; Q96AE3; Q9BY95;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 178.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC8;
DE Short=RNA polymerase III subunit C8;
DE AltName: Full=DNA-directed RNA polymerase III subunit H;
DE AltName: Full=RNA polymerase III subunit 22.9 kDa subunit;
DE Short=RPC22.9;
GN Name=POLR3H {ECO:0000312|HGNC:HGNC:30349}; Synonyms=KIAA1665, RPC8;
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 (ISOFORM 1), IDENTIFICATION IN THE RNA POL III COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RPC9.
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] (ISOFORM 1).
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pituitary;
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 [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 OF POL III.
RX PubMed=20413673; DOI=10.1101/gr.101337.109;
RA Canella D., Praz V., Reina J.H., Cousin P., Hernandez N.;
RT "Defining the RNA polymerase III transcriptome: Genome-wide localization of
RT the RNA polymerase III transcription machinery in human cells.";
RL Genome Res. 20:710-721(2010).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=33335104; DOI=10.1038/s41467-020-20262-5;
RA Ramsay E.P., Abascal-Palacios G., Daiss J.L., King H., Gouge J., Pilsl M.,
RA Beuron F., Morris E., Gunkel P., Engel C., Vannini A.;
RT "Structure of human RNA polymerase III.";
RL Nat. Commun. 11:6409-6421(2020).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS), AND SUBUNIT.
RX PubMed=33674783; DOI=10.1038/s41422-021-00472-2;
RA Li L., Yu Z., Zhao D., Ren Y., Hou H., Xu Y.;
RT "Structure of human RNA polymerase III elongation complex.";
RL Cell Res. 31:791-800(2021).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=34675218; DOI=10.1038/s41467-021-26402-9;
RA Hou H., Li Y., Wang M., Liu A., Yu Z., Chen K., Zhao D., Xu Y.;
RT "Structural insights into RNA polymerase III-mediated transcription
RT termination through trapping poly-deoxythymidine.";
RL Nat. Commun. 12:6135-6146(2021).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=33558764; DOI=10.1038/s41594-020-00555-5;
RA Girbig M., Misiaszek A.D., Vorlander M.K., Lafita A., Grotsch H.,
RA Baudin F., Bateman A., Muller C.W.;
RT "Cryo-EM structures of human RNA polymerase III in its unbound and
RT transcribing states.";
RL Nat. Struct. Mol. Biol. 28:210-219(2021).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=33558766; DOI=10.1038/s41594-021-00557-x;
RA Wang Q., Li S., Wan F., Xu Y., Wu Z., Cao M., Lan P., Lei M., Wu J.;
RT "Structural insights into transcriptional regulation of human RNA
RT polymerase III.";
RL Nat. Struct. Mol. Biol. 28:220-227(2021).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates
CC (PubMed:20413673, PubMed:34675218, PubMed:33558764). Specific
CC peripheric component of RNA polymerase III (Pol III) which synthesizes
CC small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from
CC at least 500 distinct genomic loci. With CRCP/RPC9 forms a mobile stalk
CC that protrudes from Pol III core and functions primarily in
CC transcription initiation (PubMed:34675218, PubMed:33558764) (By
CC similarity). Pol III 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, such as Epstein-Barr virus-
CC encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through
CC the RIG-I pathway (PubMed:19609254, PubMed:19631370). {ECO:0000250,
CC ECO:0000250|UniProtKB:O94285, ECO:0000269|PubMed:19609254,
CC ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20413673,
CC ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218}.
CC -!- SUBUNIT: Component of the RNA polymerase III complex consisting of 17
CC subunits: a ten-subunit horseshoe-shaped catalytic core composed of
CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10,
CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and
CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and
CC CRCP/RPC9, protruding from the core and functioning primarily in
CC transcription initiation; and additional subunits homologous to general
CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3-
CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription
CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both
CC transcription initiation and termination (PubMed:12391170,
CC PubMed:33335104, PubMed:33674783, PubMed:34675218, PubMed:33558764,
CC PubMed:33558766). Interacts with CRCP/RPC9. POLR3H/RPC8 and CRCP/RPC9
CC probably form a Pol III subcomplex. {ECO:0000269|PubMed:12391170,
CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764,
CC ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783,
CC ECO:0000269|PubMed:34675218}.
CC -!- INTERACTION:
CC Q9Y535; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-2515065, EBI-1166928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y535-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y535-2; Sequence=VSP_007067;
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB33335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY092087; AAM18217.1; -; mRNA.
DR EMBL; AB051452; BAB33335.1; ALT_INIT; mRNA.
DR EMBL; CR456459; CAG30345.1; -; mRNA.
DR EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60438.1; -; Genomic_DNA.
DR EMBL; BC017248; AAH17248.1; -; mRNA.
DR EMBL; BC088367; AAH88367.1; -; mRNA.
DR CCDS; CCDS14018.1; -. [Q9Y535-1]
DR CCDS; CCDS33651.1; -. [Q9Y535-2]
DR RefSeq; NP_001018060.1; NM_001018050.3. [Q9Y535-1]
DR RefSeq; NP_001018062.1; NM_001018052.3. [Q9Y535-2]
DR RefSeq; NP_001269813.1; NM_001282884.1. [Q9Y535-1]
DR RefSeq; NP_001269814.1; NM_001282885.1. [Q9Y535-1]
DR RefSeq; NP_612211.1; NM_138338.4. [Q9Y535-1]
DR PDB; 7A6H; EM; 3.30 A; G=1-204.
DR PDB; 7AE1; EM; 2.80 A; G=1-204.
DR PDB; 7AE3; EM; 3.10 A; G=1-204.
DR PDB; 7AEA; EM; 3.40 A; G=1-204.
DR PDB; 7AST; EM; 4.00 A; J=1-204.
DR PDB; 7D58; EM; 2.90 A; G=1-204.
DR PDB; 7D59; EM; 3.10 A; G=1-204.
DR PDB; 7DN3; EM; 3.50 A; G=1-204.
DR PDB; 7DU2; EM; 3.35 A; G=1-204.
DR PDB; 7FJI; EM; 3.60 A; G=1-204.
DR PDB; 7FJJ; EM; 3.60 A; G=1-204.
DR PDB; 8ITY; EM; 3.90 A; G=1-204.
DR PDB; 8IUE; EM; 4.10 A; G=1-204.
DR PDB; 8IUH; EM; 3.40 A; G=1-204.
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; Q9Y535; -.
DR EMDB; EMD-11673; -.
DR EMDB; EMD-11736; -.
DR EMDB; EMD-11738; -.
DR EMDB; EMD-11742; -.
DR EMDB; EMD-11904; -.
DR EMDB; EMD-30577; -.
DR EMDB; EMD-30578; -.
DR EMDB; EMD-30779; -.
DR EMDB; EMD-30865; -.
DR EMDB; EMD-31621; -.
DR EMDB; EMD-31622; -.
DR EMDB; EMD-35712; -.
DR EMDB; EMD-35719; -.
DR EMDB; EMD-35722; -.
DR SMR; Q9Y535; -.
DR BioGRID; 128147; 93.
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 IntAct; Q9Y535; 13.
DR MINT; Q9Y535; -.
DR STRING; 9606.ENSP00000347345; -.
DR iPTMnet; Q9Y535; -.
DR PhosphoSitePlus; Q9Y535; -.
DR BioMuta; POLR3H; -.
DR DMDM; 29428071; -.
DR EPD; Q9Y535; -.
DR jPOST; Q9Y535; -.
DR MassIVE; Q9Y535; -.
DR MaxQB; Q9Y535; -.
DR PaxDb; 9606-ENSP00000347345; -.
DR PeptideAtlas; Q9Y535; -.
DR ProteomicsDB; 86282; -. [Q9Y535-1]
DR ProteomicsDB; 86283; -. [Q9Y535-2]
DR Pumba; Q9Y535; -.
DR Antibodypedia; 26963; 183 antibodies from 25 providers.
DR DNASU; 171568; -.
DR Ensembl; ENST00000337566.9; ENSP00000337627.5; ENSG00000100413.17. [Q9Y535-2]
DR Ensembl; ENST00000355209.9; ENSP00000347345.4; ENSG00000100413.17. [Q9Y535-1]
DR Ensembl; ENST00000396504.6; ENSP00000379761.2; ENSG00000100413.17. [Q9Y535-1]
DR Ensembl; ENST00000407461.5; ENSP00000385315.1; ENSG00000100413.17. [Q9Y535-1]
DR GeneID; 171568; -.
DR KEGG; hsa:171568; -.
DR MANE-Select; ENST00000355209.9; ENSP00000347345.4; NM_001018050.4; NP_001018060.1.
DR UCSC; uc003baf.5; human. [Q9Y535-1]
DR AGR; HGNC:30349; -.
DR CTD; 171568; -.
DR DisGeNET; 171568; -.
DR GeneCards; POLR3H; -.
DR HGNC; HGNC:30349; POLR3H.
DR HPA; ENSG00000100413; Low tissue specificity.
DR MalaCards; POLR3H; -.
DR MIM; 619801; gene.
DR neXtProt; NX_Q9Y535; -.
DR OpenTargets; ENSG00000100413; -.
DR Orphanet; 243; 46,XX gonadal dysgenesis.
DR PharmGKB; PA134994174; -.
DR VEuPathDB; HostDB:ENSG00000100413; -.
DR eggNOG; KOG3297; Eukaryota.
DR GeneTree; ENSGT00390000004383; -.
DR HOGENOM; CLU_073901_1_0_1; -.
DR InParanoid; Q9Y535; -.
DR OMA; LGPTLWW; -.
DR OrthoDB; 35529at2759; -.
DR PhylomeDB; Q9Y535; -.
DR TreeFam; TF103053; -.
DR PathwayCommons; Q9Y535; -.
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; Q9Y535; -.
DR SIGNOR; Q9Y535; -.
DR BioGRID-ORCS; 171568; 701 hits in 1153 CRISPR screens.
DR ChiTaRS; POLR3H; human.
DR GenomeRNAi; 171568; -.
DR Pharos; Q9Y535; Tbio.
DR PRO; PR:Q9Y535; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y535; Protein.
DR Bgee; ENSG00000100413; Expressed in prefrontal cortex and 167 other cell types or tissues.
DR ExpressionAtlas; Q9Y535; baseline and differential.
DR Genevisible; Q9Y535; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
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:0006139; P:nucleobase-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:UniProtKB.
DR GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IBA:GO_Central.
DR CDD; cd04330; RNAP_III_Rpc25_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.30.1490.120; RNA polymerase Rpb7-like, N-terminal domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013238; RNA_pol_III_Rbc25.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR004519; RNAP_E/RPC8.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR NCBIfam; TIGR00448; rpoE; 1.
DR PANTHER; PTHR12709; DNA-DIRECTED RNA POLYMERASE II, III; 1.
DR PANTHER; PTHR12709:SF1; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC8; 1.
DR Pfam; PF08292; RNA_pol_Rbc25; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SUPFAM; SSF88798; N-terminal, heterodimerisation domain of RBP7 (RpoE); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1..204
FT /note="DNA-directed RNA polymerase III subunit RPC8"
FT /id="PRO_0000073994"
FT REGION 158..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 70..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007067"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:8IUH"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7D59"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 204 AA; 22918 MW; DE85D44A5770C5D9 CRC64;
MFVLVEMVDT VRIPPWQFER KLNDSIAEEL NKKLANKVVY NVGLCICLFD ITKLEDAYVF
PGDGASHTKV HFRCVVFHPF LDEILIGKIK GCSPEGVHVS LGFFDDILIP PESLQQPAKF
DEAEQVWVWE YETEEGAHDL YMDTGEEIRF RVVDESFVDT SPTGPSSADA TTSSEELPKK
EAPYTLVGSI SEPGLGLLSW WTSN
//
