Reviewed, UniProtKB/Swiss-Prot O14802 (RPC1_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase III subunit RPC1
      Short name=RNA polymerase III subunit C1
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase III subunit A
    DNA-directed RNA polymerase III largest subunit
    RPC155
    RNA polymerase III subunit C160

Gene names

Name:

POLR3A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1390 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. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition By similarity. 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. Ref.8 Ref.9
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the RNA polymerase beta' chain family.

Ontologies

Keywords
Biological process	Antiviral defense Immune response Innate immunity Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	innate immune response Ref.9 Inferred from mutant phenotype. Source: UniProtKB positive regulation of interferon-beta production Ref.9 Inferred from mutant phenotype. Source: UniProtKB response to virus Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	DNA-directed RNA polymerase III complex Non-traceable author statement. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Ref.1 Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1390	1390	DNA-directed RNA polymerase III subunit RPC1		PRO_0000073947
Regions
	Region	844 – 856	13	Bridging helix By similarity
Sites
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	72	1	Zinc 1 By similarity
	Metal binding	79	1	Zinc 1 By similarity
	Metal binding	82	1	Zinc 1 By similarity
	Metal binding	109	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 2 By similarity
	Metal binding	156	1	Zinc 2 By similarity
	Metal binding	499	1	Magnesium; catalytic By similarity
	Metal binding	501	1	Magnesium; catalytic By similarity
	Metal binding	503	1	Magnesium; catalytic By similarity
Amino acid modifications
	Modified residue	445	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	582	1	R → L: dbSNP rs34588967.		VAR_051873
	Natural variant	713	1	K → N: dbSNP rs35354908.		VAR_051874
Experimental info
	Sequence conflict	15	1	I → T in AAB86536. Ref.1
	Sequence conflict	262	1	I → F in AAB86536. Ref.1
	Sequence conflict	283	1	L → P in AAM12029. Ref.5
	Sequence conflict	1056	1	A → G in AAB86536. Ref.1
	Sequence conflict	1275	1	M → MV in AAB86536. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O14802-1 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 56F30900848E3DB9	FASTA	1,390	155,641
	10 20 30 40 50 60 MVKEQFRETD VAKKISHICF GMKSPEEMRQ QAHIQVVSKN LYSQDNQHAP LLYGVLDHRM 70 80 90 100 110 120 GTSEKDRPCE TCGKNLADCL GHYGYIDLEL PCFHVGYFRA VIGILQMICK TCCHIMLSQE 130 140 150 160 170 180 EKKQFLDYLK RPGLTYLQKR GLKKKISDKC RKKNICHHCG AFNGTVKKCG LLKIIHEKYK 190 200 210 220 230 240 TNKKVVDPIV SNFLQSFETA IEHNKEVEPL LGRAQENLNP LVVLNLFKRI PAEDVPLLLM 250 260 270 280 290 300 NPEAGKPSDL ILTRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRISG 310 320 330 340 350 360 AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG RFRGNLSGKR 370 380 390 400 410 420 VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TFPEKVNKAN INFLRKLVQN GPEVHPGANF 430 440 450 460 470 480 IQQRHTQMKR FLKYGNREKM AQELKYGDIV ERHLIDGDVV LFNRQPSLHK LSIMAHLARV 490 500 510 520 530 540 KPHRTFRFNE CVCTPYNADF DGDEMNLHLP QTEEAKAEAL VLMGTKANLV TPRNGEPLIA 550 560 570 580 590 600 AIQDFLTGAY LLTLKDTFFD RAKACQIIAS ILVGKDEKIK VRLPPPTILK PVTLWTGKQI 610 620 630 640 650 660 FSVILRPSDD NPVRANLRTK GKQYCGKGED LCANDSYVTI QNSELMSGSM DKGTLGSGSK 670 680 690 700 710 720 NNIFYILLRD WGQNEAADAM SRLARLAPVY LSNRGFSIGI GDVTPGQGLL KAKYELLNAG 730 740 750 760 770 780 YKKCDEYIEA LNTGKLQQQP GCTAEETLEA LILKELSVIR DHAGSACLRE LDKSNSPLTM 790 800 810 820 830 840 ALCGSKGSFI NISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVANSFYS 850 860 870 880 890 900 GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF 910 920 930 940 950 960 IYGGDGLDPA AMEGKDEPLE FKRVLDNIKA VFPCPSEPAL SKNELILTTE SIMKKSEFLC 970 980 990 1000 1010 1020 CQDSFLQEIK KFIKGVSEKI KKTRDKYGIN DNGTTEPRVL YQLDRITPTQ VEKFLETCRD 1030 1040 1050 1060 1070 1080 KYMRAQMEPG SAVGALCAQS IGEPGTQMTL KTFHFAGVAS MNITLGVPRI KEIINASKAI 1090 1100 1110 1120 1130 1140 STPIITAQLD KDDDADYARL VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL 1150 1160 1170 1180 1190 1200 RLEVNAETVR YSICTSKLRV KPGDVAVHGE AVVCVTPREN SKSSMYYVLQ FLKEDLPKVV 1210 1220 1230 1240 1250 1260 VQGIPEVSRA VIHIDEQSGK EKYKLLVEGD NLRAVMATHG VKGTRTTSNN TYEVEKTLGI 1270 1280 1290 1300 1310 1320 EAARTTIINE IQYTMVNHGM SIDRRHVMLL SDLMTYKGEV LGITRFGLAK MKESVLMLAS 1330 1340 1350 1360 1370 1380 FEKTADHLFD AAYFGQKDSV CGVSECIIMG IPMNIGTGLF KLLHKADRDP NPPKRPLIFD 1390 TNEFHIPLVT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III." Sepehri S., Hernandez N. Genome Res. 7:1006-1019(1997) [PubMed: 9331371] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[5]	"Identification of an immunodominant epitope on RNA polymerase III recognized by systemic sclerosis sera: application to enzyme-linked immunosorbent assay." Kuwana M., Kimura K., Kawakami Y. Arthritis Rheum. 46:2742-2747(2002) [PubMed: 12384934] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-374.
[6]	"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: 12391170] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL III COMPLEX, MASS SPECTROMETRY.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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: 19631370] [Abstract] Cited for: FUNCTION.
[9]	"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: 19609254] [Abstract] Cited for: FUNCTION.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-445, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF021351 mRNA. Translation: AAB86536.1. AL512628 Genomic DNA. Translation: CAI16466.1. CH471083 Genomic DNA. Translation: EAW54617.1. BC041089 mRNA. Translation: AAH41089.1. AY091459 mRNA. Translation: AAM12029.1.
IPI	IPI00024163.
RefSeq	NP_008986.2.
UniGene	Hs.436896
3D structure databases
SMR	O14802. Positions 2-1363.
ModBase	Search...
Protein-protein interaction databases
STRING	O14802.
Proteomic databases
PRIDE	O14802.
Genome annotation databases
Ensembl	ENST00000372371; ENSP00000361446; ENSG00000148606; Homo sapiens. [Genome view]
GeneID	11128.
KEGG	hsa:11128.
Organism-specific databases
CTD	11128.
GeneCards	GC10M079405.
H-InvDB	HIX0008960.
HGNC	HGNC:30074. POLR3A.
PharmGKB	PA134900426.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15151.
HOGENOM	HBG499785.
HOVERGEN	O14802.
InParanoid	O14802.
OMA	LCVNDSY.
OrthoDB	EOG9B8N0M.
PhylomeDB	O14802.
Enzyme and pathway databases
BRENDA	2.7.7.6. 247.
Reactome	REACT_1788. Transcription.
Gene expression databases
ArrayExpress	O14802.
Bgee	O14802.
CleanEx	HS_POLR3A.
Genevestigator	O14802.
GermOnline	ENSG00000148606. Homo sapiens.
Family and domain databases
InterPro	IPR000722. RNA_pol_asu. IPR006592. RNA_pol_N. IPR007080. RNA_pol_Rpb1_1. IPR007066. RNA_pol_Rpb1_3. IPR007083. RNA_pol_Rpb1_4. IPR007081. RNA_pol_Rpb1_5. [Graphical view]
Gene3D	G3DSA:2.40.40.30. RNA_pol_A. 1 hit. G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit.
Pfam	PF04997. RNA_pol_Rpb1_1. 1 hit. PF00623. RNA_pol_Rpb1_2. 1 hit. PF04983. RNA_pol_Rpb1_3. 1 hit. PF05000. RNA_pol_Rpb1_4. 1 hit. PF04998. RNA_pol_Rpb1_5. 1 hit. [Graphical view]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPC1_HUMAN

Accession

Primary (citable) accession number: O14802
Secondary accession number(s): Q8IW34, Q8TCW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 23, 2008
Last modified:	January 19, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.