Q9Y535 (RPC8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase III subunit RPC8
Short name=RNA polymerase III subunit C8

Alternative name(s):
DNA-directed RNA polymerase III subunit H
RNA polymerase III subunit 22.9 kDa subunit
Short name=RPC22.9

Gene names

Name:	POLR3H
Synonyms:	KIAA1665, RPC8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway By similarity. Ref.7 Ref.8
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity. Interacts with CRCP/RPC9. POLR3H/RPC8 and CRCP/RPC9 probably form a Pol III subcomplex. Ref.1
Subcellular location	Nucleus.
Sequence similarities	Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Sequence caution	The sequence BAB33335.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Alternative splicing
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW termination of RNA polymerase III transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase III promoter Traceable author statement. Source: Reactome
Cellular_component	DNA-directed RNA polymerase III complex Inferred from direct assay Ref.1. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y535-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y535-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-98: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	DNA-directed RNA polymerase III subunit RPC8		PRO_0000073994
Natural variations
	Alternative sequence	70 – 98	29	Missing in isoform 2.		VSP_007067

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: DE85D44A5770C5D9	FASTA	204	22,918
	10 20 30 40 50 60 MFVLVEMVDT VRIPPWQFER KLNDSIAEEL NKKLANKVVY NVGLCICLFD ITKLEDAYVF 70 80 90 100 110 120 PGDGASHTKV HFRCVVFHPF LDEILIGKIK GCSPEGVHVS LGFFDDILIP PESLQQPAKF 130 140 150 160 170 180 DEAEQVWVWE YETEEGAHDL YMDTGEEIRF RVVDESFVDT SPTGPSSADA TTSSEELPKK 190 200 EAPYTLVGSI SEPGLGLLSW WTSN
	Isoform 2 [UniParc]. Checksum: 2213B9D553C5DEE9	FASTA	175	19,658
	10 20 30 40 50 60 MFVLVEMVDT VRIPPWQFER KLNDSIAEEL NKKLANKVVY NVGLCICLFD ITKLEDAYVF 70 80 90 100 110 120 PGDGASHTKV SLGFFDDILI PPESLQQPAK FDEAEQVWVW EYETEEGAHD LYMDTGEEIR 130 140 150 160 170 FRVVDESFVD TSPTGPSSAD ATTSSEELPK KEAPYTLVGS ISEPGLGLLS WWTSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits." Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N. Mol. Cell. Biol. 22:8044-8055(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), IDENTIFICATION IN THE RNA POL III COMPLEX, MASS SPECTROMETRY, INTERACTION WITH RPC9.
[2]	"Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping." Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O. DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Pituitary.
[7]	"RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway." Chiu Y.-H., Macmillan J.B., Chen Z.J. Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate." Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V. Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY092087 mRNA. Translation: AAM18217.1. AB051452 mRNA. Translation: BAB33335.1. Different initiation. CR456459 mRNA. Translation: CAG30345.1. AL023553 Genomic DNA. Translation: CAB46023.1. AL023553 Genomic DNA. Translation: CAQ10207.1. CH471095 Genomic DNA. Translation: EAW60438.1. BC017248 mRNA. Translation: AAH17248.1. BC088367 mRNA. Translation: AAH88367.1.
IPI	IPI00215871. IPI00289667.
RefSeq	NP_001018060.1. NM_001018050.2. NP_001018062.1. NM_001018052.2. NP_612211.1. NM_138338.3.
UniGene	Hs.712617.
3D structure databases
ProteinModelPortal	Q9Y535.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y535. 1 interaction.
STRING	9606.ENSP00000347345.
Polymorphism databases
DMDM	29428071.
Proteomic databases
PaxDb	Q9Y535.
PRIDE	Q9Y535.
Protocols and materials databases
DNASU	171568.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000337566; ENSP00000337627; ENSG00000100413. ENST00000355209; ENSP00000347345; ENSG00000100413. ENST00000396504; ENSP00000379761; ENSG00000100413. ENST00000407461; ENSP00000385315; ENSG00000100413.
GeneID	171568.
KEGG	hsa:171568.
UCSC	uc003baf.3. human. uc003bai.2. human.
Organism-specific databases
CTD	171568.
GeneCards	GC22M041921.
HGNC	HGNC:30349. POLR3H.
HPA	HPA046787.
neXtProt	NX_Q9Y535.
PharmGKB	PA134994174.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1095.
HOGENOM	HOG000157370.
HOVERGEN	HBG044510.
InParanoid	Q9Y535.
KO	K03022.
OMA	NVGLCIA.
OrthoDB	EOG434W70.
PhylomeDB	Q9Y535.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9Y535.
Bgee	Q9Y535.
CleanEx	HS_POLR3H.
Genevestigator	Q9Y535.
GermOnline	ENSG00000100413. Homo sapiens.
Family and domain databases
Gene3D	3.30.1490.120. 1 hit.
InterPro	IPR012340. NA-bd_OB-fold. IPR013238. RNA_pol_III_Rbc25. IPR005576. RNA_pol_Rpb7_N. IPR004519. RNAP_E/RPC8. [Graphical view]
Pfam	PF08292. RNA_pol_Rbc25. 1 hit. PF03876. SHS2_Rpb7-N. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF88798. RNA_pol_Rpb7_N. 1 hit.
TIGRFAMs	TIGR00448. rpoE. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	171568.
NextBio	89296.

Entry information

Entry name

RPC8_HUMAN

Accession

Primary (citable) accession number: Q9Y535
Secondary accession number(s): B0QYH9 , Q5M7Y8, Q96AE3, Q9BY95

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.