Q9BUI4 (RPC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase III subunit RPC3
Short name=RNA polymerase III subunit C3

Alternative name(s):
DNA-directed RNA polymerase III subunit C
RNA polymerase III 62 kDa subunit
Short name=RPC62

Gene names

Name:

POLR3C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	534 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 core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. 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
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex. Interacts with GTF3C4 By similarity. Ref.1 Ref.5
Subcellular location	Nucleus By similarity.
Miscellaneous	Antibodies against POLR3C have been found in the sera of patients with systemic sclerosis (SSc).
Sequence similarities	Belongs to the eukaryotic RPC3/POLR3C RNA polymerase subunit family.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	innate immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of innate immune response Inferred from mutant phenotype Ref.9. Source: UniProtKB positive regulation of interferon-beta production Inferred from mutant phenotype Ref.9. Source: UniProtKB regulation of transcription from RNA polymerase III promoter Traceable author statement. Source: ProtInc response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	DNA-directed RNA polymerase III complex Traceable author statement. Source: ProtInc
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 534

534

DNA-directed RNA polymerase III subunit RPC3

PRO_0000073963

Amino acid modifications

Modified residue

194

1

Phosphoserine Ref.7

Natural variations

Natural variant

243

1

H → R. Ref.1
Corresponds to variant rs1044697 [ dbSNP | Ensembl ].

VAR_019083

Experimental info

Sequence conflict

85 – 86

2

ML → IV in AAB63675. Ref.1

Sequence conflict

119 – 120

2

SA → CT in AAB63675. Ref.1

Sequence conflict

216 – 237

22

KRPKY…IYWQA → RDQNILQITRXPFQMMGFIG RP in AAB63675. Ref.1

Sequence conflict

289

1

S → F in AAB63675. Ref.1

Sequence conflict

343

1

A → R in AAB63675. Ref.1

Sequence conflict

366

1

F → C in AAB63675. Ref.1

Sequence conflict

387 – 389

3

PAK → LQ in AAB63675. Ref.1

Sequence conflict

401

1

E → G in AAB63675. Ref.1

Sequence conflict

436 – 437

2

LH → FD in AAB63675. Ref.1

Sequence conflict

517

1

D → E in CAB41919. Ref.3

Secondary structure

1

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534

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

20 – 23

4

Helix

27 – 30

4

Helix

36 – 42

7

Helix

47 – 59

13

Beta strand

62 – 67

6

Beta strand

73 – 77

5

Helix

79 – 83

5

Helix

84 – 87

4

Helix

88 – 99

12

Helix

105 – 112

8

Helix

118 – 131

14

Helix

141 – 153

13

Beta strand

156 – 159

4

Beta strand

235 – 237

3

Helix

239 – 258

20

Helix

261 – 272

12

Turn

273 – 277

5

Helix

290 – 295

6

Helix

305 – 316

12

Helix

338 – 357

20

Helix

361 – 371

11

Helix

377 – 384

8

Helix

388 – 400

13

Helix

428 – 456

29

Helix

458 – 472

15

Helix

485 – 488

4

Helix

493 – 529

37

Sequences

	Sequence		Length	Mass (Da)
	Q9BUI4 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0E4CFEE295EE1A55	FASTA	534	60,612
	10 20 30 40 50 60 MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH 70 80 90 100 110 120 NLVSYQVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYS DTGELIVEEL LLNGKLTMSA 130 140 150 160 170 180 VVKKVADRLT ETMEDGKTMD YAEVSNTFVR LADTHFVQRC PSVPTTENSD PGPPPPAPTL 190 200 210 220 230 240 VINEKDMYLV PKLSLIGKGK RRRSSDEDAA GEPKAKRPKY TTDNKEPIPD DGIYWQANLD 250 260 270 280 290 300 RFHQHFRDQA IVSAVANRMD QTSSEIVRTM LRMSEITTSS SAPFTQPLSS NEIFRSLPVG 310 320 330 340 350 360 YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINLHK ALASLATATL ESVVQERFGS 370 380 390 400 410 420 RCARIFRLVL QKKHIEQKQV EDFAMIPAKE AKDMLYKMLS ENFMSLQEIP KTPDHAPSRT 430 440 450 460 470 480 FYLYTVNILS AARMLLHRCY KSIANLIERR QFETKENKRL LEKSQRVEAI IASMQATGAE 490 500 510 520 530 EAQLQEIEEM ITAPERQQLE TLKRNVNKLD ASEIQVDETI FLLESYIECT MKRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation." Wang Z., Roeder R.G. Genes Dev. 11:1315-1326(1997) [PubMed: 9171375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR3G AND POLR3F, VARIANT ARG-243. Tissue: Cervix carcinoma.
[2]	"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], IDENTIFICATION AS ANTIGEN IN SYSTEMIC SCLEROSIS.
[3]	"Genomic structure of human RNA polymerase III subunit (RPC62)." Totaro A. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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: Ovary.
[5]	"The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity." Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G. Mol. Cell. Biol. 19:7697-7704(1999) [PubMed: 10523658] [Abstract] Cited for: INTERACTION WITH GTF3C4.
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U93867 mRNA. Translation: AAB63675.1.
AY091463 mRNA. Translation: AAM12033.1.
AJ238221 , AJ238222, AJ238223, AJ238224, AJ238225, AJ238226, AJ238227, AJ238228, AJ238229, AJ238230, AJ238231, AJ238232, AJ238233, AJ238234 Genomic DNA. Translation: CAB41919.1.
BC002586 mRNA. Translation: AAH02586.1.

IPI

IPI00007948.

RefSeq

NP_006459.3. NM_006468.6.

UniGene

Hs.591457.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XUB	X-ray	2.80	A	1-534	[»]
2XV4	X-ray	2.95	S	1-534	[»]

ProteinModelPortal

Q9BUI4.

SMR

Q9BUI4. Positions 1-532.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59078N.

STRING

Q9BUI4.

PTM databases

PhosphoSite

Q9BUI4.

Polymorphism databases

DMDM

60393871.

Proteomic databases

PRIDE

Q9BUI4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334163; ENSP00000334564; ENSG00000186141.

GeneID

10623.

KEGG

hsa:10623.

UCSC

uc001eog.1. human.

Organism-specific databases

CTD

10623.

GeneCards

GC01M145592.

H-InvDB

HIX0000978.

HGNC

HGNC:30076. POLR3C.

HPA

HPA027508.
HPA027516.

neXtProt

NX_Q9BUI4.

PharmGKB

PA134870963.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000002799.

HOGENOM

HBG281216.

HOVERGEN

HBG059543.

InParanoid

Q9BUI4.

OMA

GKMTMSA.

OrthoDB

EOG4HQDJ8.

PhylomeDB

Q9BUI4.

Gene expression databases

ArrayExpress

Q9BUI4.

Bgee

Q9BUI4.

CleanEx

HS_POLR3C.

Genevestigator

Q9BUI4.

GermOnline

ENSG00000186141. Homo sapiens.

Family and domain databases

InterPro

IPR013197. RNA_pol_III_RPC82-rel_HTH.
IPR008806. RNA_pol_III_Rpc82_C.
[Graphical view]

KO

K03023.

Pfam

PF08221. HTH_9. 1 hit.
PF05645. RNA_pol_Rpc82. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

40364.

Entry information

Entry name

RPC3_HUMAN

Accession

Primary (citable) accession number: Q9BUI4
Secondary accession number(s): O15317, Q9Y3R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 80 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.