O00411 · RPOM_HUMAN
- ProteinDNA-directed RNA polymerase, mitochondrial
- GenePOLRMT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1230 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:21278163, PubMed:33602924).
Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603).
In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603).
Has DNA primase activity (PubMed:18685103, PubMed:33602924).
Catalyzes the synthesis of short RNA primers that are necessary for the initiation of lagging-strand DNA synthesis from the origin of light-strand DNA replication (OriL) (PubMed:18685103, PubMed:33602924).
Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603).
In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603).
Has DNA primase activity (PubMed:18685103, PubMed:33602924).
Catalyzes the synthesis of short RNA primers that are necessary for the initiation of lagging-strand DNA synthesis from the origin of light-strand DNA replication (OriL) (PubMed:18685103, PubMed:33602924).
Catalytic activity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 922 | |||||
Sequence: D | ||||||
Active site | 991 | |||||
Sequence: K | ||||||
Active site | 1151 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial DNA-directed RNA polymerase complex | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrion | |
Cellular Component | protein-containing complex | |
Molecular Function | 3'-5'-RNA exonuclease activity | |
Molecular Function | DNA primase activity | |
Molecular Function | DNA-directed 5'-3' RNA polymerase activity | |
Molecular Function | mitochondrial promoter sequence-specific DNA binding | |
Molecular Function | RNA binding | |
Molecular Function | sequence-specific DNA binding | |
Biological Process | mitochondrial transcription | |
Biological Process | transcription initiation at mitochondrial promoter |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed RNA polymerase, mitochondrial
- EC number
- Short namesMtRPOL
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00411
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Combined oxidative phosphorylation deficiency 55 (COXPD55)
- Note
- DescriptionA mitochondrial disease characterized by global developmental delay, hypotonia, short stature, and impaired intellectual development with speech disabilities in childhood. Indolent progressive external ophthalmoplegia may be present in some patients. COXPD55 transmission pattern is consistent with autosomal dominant inheritance in some families, and with autosomal recessive inheritance in others.
- See alsoMIM:619743
Natural variants in COXPD55
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086918 | 149-1230 | missing | in COXPD55 | |
VAR_086919 | 250 | H>D | in COXPD55; results in mild reduction of transcription of mitochondrial DNA in an in vitro assay; dbSNP:rs137994680 | |
VAR_086920 | 566 | P>S | in COXPD55; when associated in cis with F-1193; dbSNP:rs41545023 | |
VAR_086921 | 611 | S>F | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro; reduced DNA primase activity; dbSNP:rs2144625053 | |
VAR_086922 | 641 | F>L | in COXPD55; results in mild reduction of transcription of mitochondrial DNA in vitro; reduced DNA primase activity; dbSNP:rs748687181 and dbSNP:rs1362809473 | |
VAR_086923 | 742-747 | missing | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro | |
VAR_086924 | 810 | P>S | in COXPD55; uncertain significance; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs201364510 | |
VAR_086925 | 870 | D>N | in COXPD55; uncertain significance; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs139383492 | |
VAR_086926 | 925-1230 | missing | in COXPD55 | |
VAR_086927 | 1013 | R>C | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs745348188 | |
VAR_086928 | 1193 | S>F | in COXPD55; when associated in cis with S-566; dbSNP:rs142850300 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_086918 | 149-1230 | in COXPD55 | |||
Sequence: Missing | ||||||
Natural variant | VAR_086919 | 250 | in COXPD55; results in mild reduction of transcription of mitochondrial DNA in an in vitro assay; dbSNP:rs137994680 | |||
Sequence: H → D | ||||||
Natural variant | VAR_019427 | 555 | in dbSNP:rs2238549 | |||
Sequence: E → A | ||||||
Natural variant | VAR_086920 | 566 | in COXPD55; when associated in cis with F-1193; dbSNP:rs41545023 | |||
Sequence: P → S | ||||||
Natural variant | VAR_086921 | 611 | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro; reduced DNA primase activity; dbSNP:rs2144625053 | |||
Sequence: S → F | ||||||
Natural variant | VAR_086922 | 641 | in COXPD55; results in mild reduction of transcription of mitochondrial DNA in vitro; reduced DNA primase activity; dbSNP:rs748687181 and dbSNP:rs1362809473 | |||
Sequence: F → L | ||||||
Natural variant | VAR_086923 | 742-747 | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro | |||
Sequence: Missing | ||||||
Natural variant | VAR_086924 | 810 | in COXPD55; uncertain significance; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs201364510 | |||
Sequence: P → S | ||||||
Natural variant | VAR_086925 | 870 | in COXPD55; uncertain significance; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs139383492 | |||
Sequence: D → N | ||||||
Natural variant | VAR_086926 | 925-1230 | in COXPD55 | |||
Sequence: Missing | ||||||
Natural variant | VAR_086927 | 1013 | in COXPD55; results in decreased transcription of mitochondrial DNA in vitro; dbSNP:rs745348188 | |||
Sequence: R → C | ||||||
Natural variant | VAR_086928 | 1193 | in COXPD55; when associated in cis with S-566; dbSNP:rs142850300 | |||
Sequence: S → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,065 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-41 | UniProt | Mitochondrion | ||||
Sequence: MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRS | |||||||
Chain | PRO_0000031068 | 42-1230 | UniProt | DNA-directed RNA polymerase, mitochondrial | |||
Sequence: SSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSLPPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKPTLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVVRMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASDAEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSSRLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHSGAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQLFQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEALYRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS | |||||||
Modified residue (large scale data) | 1184 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer (PubMed:29149603).
Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT (PubMed:29149603).
In this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603).
Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301).
Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (PubMed:29445193).
Interacts with TFB1M and TFB2M, leading to the stimulation of transcription (PubMed:12068295).
Interacts with TEFM (PubMed:21278163).
Interacts with MTRES1 (PubMed:31226201).
Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT (PubMed:29149603).
In this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603).
Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301).
Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (PubMed:29445193).
Interacts with TFB1M and TFB2M, leading to the stimulation of transcription (PubMed:12068295).
Interacts with TEFM (PubMed:21278163).
Interacts with MTRES1 (PubMed:31226201).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00411 | MRPL12 P52815 | 7 | EBI-355145, EBI-358272 | |
BINARY | O00411 | TEFM Q96QE5 | 6 | EBI-355145, EBI-725550 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-55 | Disordered | ||||
Sequence: RPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRK | ||||||
Region | 95-115 | Disordered | ||||
Sequence: GSGDGSLQPPRKVQMGAKDAT | ||||||
Region | 731-750 | Disordered | ||||
Sequence: VPAPPSEAPQPPEAHLPHSA | ||||||
Compositional bias | 732-746 | Pro residues | ||||
Sequence: PAPPSEAPQPPEAHL | ||||||
Region | 802-1230 | Mediates interaction with TEFM | ||||
Sequence: FRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS |
Sequence similarities
Belongs to the phage and mitochondrial RNA polymerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,230
- Mass (Da)138,620
- Last updated2004-07-19 v2
- Checksum47AFBF2E0884AEFA
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 399 | in Ref. 1; AAB58255 | ||||
Sequence: L → F | ||||||
Compositional bias | 732-746 | Pro residues | ||||
Sequence: PAPPSEAPQPPEAHL | ||||||
Sequence conflict | 983 | in Ref. 1; AAB58255 | ||||
Sequence: G → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U75370 EMBL· GenBank· DDBJ | AAB58255.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004449 EMBL· GenBank· DDBJ | AAC06147.1 EMBL· GenBank· DDBJ | Genomic DNA |