Q9BUI4 · RPC3_HUMAN
- ProteinDNA-directed RNA polymerase III subunit RPC3
- GenePOLR3C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids534 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:33558764, PubMed:33558766, PubMed:34675218, PubMed:35637192).
Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:20413673, PubMed:33558764, PubMed:33558766, PubMed:35637192).
Part of POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer, coordinates the dynamics of Pol III stalk and clamp modules during the transition from apo to elongation state (PubMed:33558764, PubMed:33558766).
Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a 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 (PubMed:19609254, PubMed:19631370).
Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner (PubMed:21358628).
Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:20413673, PubMed:33558764, PubMed:33558766, PubMed:35637192).
Part of POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer, coordinates the dynamics of Pol III stalk and clamp modules during the transition from apo to elongation state (PubMed:33558764, PubMed:33558766).
Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a 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 (PubMed:19609254, PubMed:19631370).
Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner (PubMed:21358628).
Miscellaneous
Antibodies against POLR3C have been found in the sera of patients with systemic sclerosis (SSc).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | RNA polymerase III complex | |
Molecular Function | DNA-directed 5'-3' RNA polymerase activity | |
Molecular Function | single-stranded DNA binding | |
Biological Process | defense response to virus | |
Biological Process | DNA-templated transcription | |
Biological Process | innate immune response | |
Biological Process | positive regulation of innate immune response | |
Biological Process | positive regulation of interferon-beta production | |
Biological Process | regulation of transcription by RNA polymerase III |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed RNA polymerase III subunit RPC3
- Short namesRNA polymerase III subunit C3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BUI4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 51-52 | Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: KK → EE | ||||||
Natural variant | VAR_019083 | 243 | in dbSNP:rs1044697 | |||
Sequence: H → R | ||||||
Mutagenesis | 312 | Loss of interaction with POLR3G and POLR3GL. No effect on interaction with POLR3F. | ||||
Sequence: L → K | ||||||
Mutagenesis | 357 | Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: R → E | ||||||
Mutagenesis | 364-367 | Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: RIFR → EIFE | ||||||
Mutagenesis | 389 | Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: K → E | ||||||
Mutagenesis | 445-449 | Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: NLIER → ALIEE | ||||||
Mutagenesis | 466-470 | Mild decrease in ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL. | ||||
Sequence: RVEAI → EVEAF |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 569 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000073963 | 1-534 | UniProt | DNA-directed RNA polymerase III subunit RPC3 | |||
Sequence: MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLESVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQEIPKTPDHAPSRTFYLYTVNILSAARMLLHRCYKSIANLIERRQFETKENKRLLEKSQRVEAIIASMQATGAEEAQLQEIEEMITAPERQQLETLKRNVNKLDASEIQVDETIFLLESYIECTMKRQ | |||||||
Modified residue | 194 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the RNA polymerase III complex consisting of 17 subunits: a ten-subunit horseshoe-shaped catalytic core composed of POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and CRCP/RPC9, protruding from the core and functioning primarily in transcription initiation; and additional subunits homologous to general transcription factors of the RNA polymerase II machinery, POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both transcription initiation and termination (PubMed:12391170, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218, PubMed:35637192, PubMed:9171375).
Directly interacts with POLR3G/RPC7 and POLR3GL (PubMed:21358628, PubMed:24107381, PubMed:26394183).
Directly interacts with POLR3F/RPC6 (PubMed:26394183).
Interacts with GTF3C4 (PubMed:10523658).
As part of the RNA polymerase III complex, interacts with PKP2 (PubMed:11416169).
Directly interacts with POLR3G/RPC7 and POLR3GL (PubMed:21358628, PubMed:24107381, PubMed:26394183).
Directly interacts with POLR3F/RPC6 (PubMed:26394183).
Interacts with GTF3C4 (PubMed:10523658).
As part of the RNA polymerase III complex, interacts with PKP2 (PubMed:11416169).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 161-181 | Disordered | ||||
Sequence: PSVPTTENSDPGPPPPAPTLV | ||||||
Region | 197-228 | Disordered | ||||
Sequence: GKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPI | ||||||
Compositional bias | 199-226 | Basic and acidic residues | ||||
Sequence: GKRRRSSDEDAAGEPKAKRPKYTTDNKE |
Sequence similarities
Belongs to the eukaryotic RPC3/POLR3C RNA polymerase subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length534
- Mass (Da)60,612
- Last updated2001-06-01 v1
- Checksum0E4CFEE295EE1A55
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PHH9 | E9PHH9_HUMAN | POLR3C | 411 | ||
A0A8V8TNN2 | A0A8V8TNN2_HUMAN | POLR3C | 323 | ||
A0A8V8TM54 | A0A8V8TM54_HUMAN | POLR3C | 450 | ||
A0A8V8TM82 | A0A8V8TM82_HUMAN | POLR3C | 62 | ||
A0A8V8TMN9 | A0A8V8TMN9_HUMAN | POLR3C | 325 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 85-86 | in Ref. 1; AAB63675 | ||||
Sequence: ML → IV | ||||||
Sequence conflict | 119-120 | in Ref. 1; AAB63675 | ||||
Sequence: SA → CT | ||||||
Compositional bias | 199-226 | Basic and acidic residues | ||||
Sequence: GKRRRSSDEDAAGEPKAKRPKYTTDNKE | ||||||
Sequence conflict | 216-237 | in Ref. 1; AAB63675 | ||||
Sequence: KRPKYTTDNKEPIPDDGIYWQA → RDQNILQITRXPFQMMGFIGRP | ||||||
Sequence conflict | 289 | in Ref. 1; AAB63675 | ||||
Sequence: S → F | ||||||
Sequence conflict | 343 | in Ref. 1; AAB63675 | ||||
Sequence: A → R | ||||||
Sequence conflict | 366 | in Ref. 1; AAB63675 | ||||
Sequence: F → C | ||||||
Sequence conflict | 387-389 | in Ref. 1; AAB63675 | ||||
Sequence: PAK → LQ | ||||||
Sequence conflict | 401 | in Ref. 1; AAB63675 | ||||
Sequence: E → G | ||||||
Sequence conflict | 436-437 | in Ref. 1; AAB63675 | ||||
Sequence: LH → FD | ||||||
Sequence conflict | 517 | in Ref. 3; CAB41919 | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U93867 EMBL· GenBank· DDBJ | AAB63675.1 EMBL· GenBank· DDBJ | mRNA | ||
AY091463 EMBL· GenBank· DDBJ | AAM12033.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ238221 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238222 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238223 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238224 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238225 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238226 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238227 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238228 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238229 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238230 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238231 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238232 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238233 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ238234 EMBL· GenBank· DDBJ | CAB41919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002586 EMBL· GenBank· DDBJ | AAH02586.1 EMBL· GenBank· DDBJ | mRNA |