RPC8_HUMAN
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 03-AUG-2022, entry version 171.
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; 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).
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. Plays a key role in sensing and
CC limiting infection by intracellular bacteria and DNA viruses. Acts as
CC nuclear and cytosolic DNA sensor involved in innate immune response.
CC Can sense non-self dsDNA that serves as template for transcription into
CC dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-
CC Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-
CC B through the RIG-I pathway (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). Interacts with CRCP/RPC9.
CC POLR3H/RPC8 and CRCP/RPC9 probably form a Pol III subcomplex.
CC {ECO:0000250, ECO:0000269|PubMed:12391170}.
CC -!- INTERACTION:
CC Q9Y535; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-2515065, EBI-1166928;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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 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; Q9Y535; -.
DR SMR; Q9Y535; -.
DR BioGRID; 128147; 79.
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; Q9Y535; -.
DR PeptideAtlas; Q9Y535; -.
DR PRIDE; Q9Y535; -.
DR ProteomicsDB; 86282; -. [Q9Y535-1]
DR ProteomicsDB; 86283; -. [Q9Y535-2]
DR Antibodypedia; 26963; 166 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 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 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; 661 hits in 1068 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 165 other 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:UniProtKB.
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 from RNA polymerase III promoter; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 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 PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF08292; RNA_pol_Rbc25; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
DR TIGRFAMs; TIGR00448; rpoE; 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 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
