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Protein

DNA-directed RNA polymerase III subunit RPC6

Gene

Polr3f

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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. May direct RNA Pol III binding to the TFIIIB-DNA complex. 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 induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Enzyme and pathway databases

ReactomeiR-MMU-1834949. Cytosolic sensors of pathogen-associated DNA.
R-MMU-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-MMU-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-MMU-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase III subunit RPC6
Short name:
RNA polymerase III subunit C6
Alternative name(s):
DNA-directed RNA polymerase III subunit F
Gene namesi
Name:Polr3f
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1924086. Polr3f.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 316315DNA-directed RNA polymerase III subunit RPC6PRO_0000073973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ921X6.
MaxQBiQ921X6.
PaxDbiQ921X6.
PRIDEiQ921X6.

PTM databases

iPTMnetiQ921X6.
PhosphoSiteiQ921X6.

Expressioni

Gene expression databases

BgeeiQ921X6.
CleanExiMM_POLR3F.
ExpressionAtlasiQ921X6. baseline and differential.
GenevisibleiQ921X6. MM.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex. Interacts with TBP and TFIIIB90 and GTF3C4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi214030. 3 interactions.
STRINGi10090.ENSMUSP00000028914.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Helixi15 – 2814Combined sources
Helixi35 – 417Combined sources
Helixi47 – 6014Combined sources
Beta strandi62 – 676Combined sources
Beta strandi69 – 768Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK8NMR-A11-78[»]
ProteinModelPortaliQ921X6.
SMRiQ921X6. Positions 11-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ921X6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3233. Eukaryota.
COG5111. LUCA.
GeneTreeiENSGT00390000009679.
HOGENOMiHOG000231688.
HOVERGENiHBG006817.
InParanoidiQ921X6.
KOiK03025.
OMAiATSHEVW.
OrthoDBiEOG7FV3R3.
PhylomeDBiQ921X6.
TreeFamiTF103051.

Family and domain databases

InterProiIPR007832. RNA_pol_Rpc34.
IPR016049. RNA_pol_Rpc34-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12780. PTHR12780. 1 hit.
PfamiPF05158. RNA_pol_Rpc34. 1 hit.
[Graphical view]
PIRSFiPIRSF028763. RNA_pol_Rpc34. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q921X6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR
60 70 80 90 100
AVAINRLLSM GQLDLLRSNT GLLYRIKDSQ NAGKMKGSDN QEKLVYQIIE
110 120 130 140 150
DAGNKGIWSR DIRYKSNLPL TEINKILKNL ESKKLIKAVK SVAASKKKVY
160 170 180 190 200
MLYNLQPDRS VTGGAWYSDQ DFESEFVEVL NQQCFKFLQS KAETARESKQ
210 220 230 240 250
NPVIQRNSSF ASSHEVWKYI CELGISKVEL SMEDIETILN TLIYDGKVEM
260 270 280 290 300
TIIAAKEGTV GSVDGHMKLY RAVNPILPPT GVVRAPCGLC PVFEDCHEGG
310
EISPSNCIYM TEWLEF
Length:316
Mass (Da):35,652
Last modified:December 1, 2001 - v1
Checksum:i0CEB63A5B3536421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036166 mRNA. Translation: BAC29327.1.
AK076538 mRNA. Translation: BAC36385.1.
AK144679 mRNA. Translation: BAE26008.1.
BC009159 mRNA. Translation: AAH09159.1.
CCDSiCCDS16820.1.
RefSeqiNP_084039.2. NM_029763.3.
UniGeneiMm.389351.

Genome annotation databases

EnsembliENSMUST00000028914; ENSMUSP00000028914; ENSMUSG00000027427.
GeneIDi70408.
KEGGimmu:70408.
UCSCiuc008mrg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036166 mRNA. Translation: BAC29327.1.
AK076538 mRNA. Translation: BAC36385.1.
AK144679 mRNA. Translation: BAE26008.1.
BC009159 mRNA. Translation: AAH09159.1.
CCDSiCCDS16820.1.
RefSeqiNP_084039.2. NM_029763.3.
UniGeneiMm.389351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK8NMR-A11-78[»]
ProteinModelPortaliQ921X6.
SMRiQ921X6. Positions 11-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214030. 3 interactions.
STRINGi10090.ENSMUSP00000028914.

PTM databases

iPTMnetiQ921X6.
PhosphoSiteiQ921X6.

Proteomic databases

EPDiQ921X6.
MaxQBiQ921X6.
PaxDbiQ921X6.
PRIDEiQ921X6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028914; ENSMUSP00000028914; ENSMUSG00000027427.
GeneIDi70408.
KEGGimmu:70408.
UCSCiuc008mrg.1. mouse.

Organism-specific databases

CTDi10621.
MGIiMGI:1924086. Polr3f.

Phylogenomic databases

eggNOGiKOG3233. Eukaryota.
COG5111. LUCA.
GeneTreeiENSGT00390000009679.
HOGENOMiHOG000231688.
HOVERGENiHBG006817.
InParanoidiQ921X6.
KOiK03025.
OMAiATSHEVW.
OrthoDBiEOG7FV3R3.
PhylomeDBiQ921X6.
TreeFamiTF103051.

Enzyme and pathway databases

ReactomeiR-MMU-1834949. Cytosolic sensors of pathogen-associated DNA.
R-MMU-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-MMU-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-MMU-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

EvolutionaryTraceiQ921X6.
PROiQ921X6.
SOURCEiSearch...

Gene expression databases

BgeeiQ921X6.
CleanExiMM_POLR3F.
ExpressionAtlasiQ921X6. baseline and differential.
GenevisibleiQ921X6. MM.

Family and domain databases

InterProiIPR007832. RNA_pol_Rpc34.
IPR016049. RNA_pol_Rpc34-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12780. PTHR12780. 1 hit.
PfamiPF05158. RNA_pol_Rpc34. 1 hit.
[Graphical view]
PIRSFiPIRSF028763. RNA_pol_Rpc34. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Head and Lung.
  2. "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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  4. "Solution structure of RPC34 subunit in RNA polymerase III from mouse."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 11-79.

Entry informationi

Entry nameiRPC6_MOUSE
AccessioniPrimary (citable) accession number: Q921X6
Secondary accession number(s): Q544K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.