POLRMT

Chr 19p13.3

RNA polymerase mitochondrial

Aliases:: h-mtRPOL, APOLMT, MTRNAP, MTRPOL
MANE:: ENST00000588649.7

OMIM: 601778 ↗NCBI: 5442 ↗Ensembl ↗

Annotations refreshed 9 hours ago.

Predicted protein structure

AlphaFold predicted structure

POLRMT · O00411

v62025-08-01

Predicted Aligned Error matrix for POLRMT — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

83.4/ 100

Confident

1,230 residues

Confidence breakdown

Very high(≥ 90)64%
Confident(70–90)17%
Low(50–70)8%
Very low(< 50)12%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

Intellectual disability
BOTH monoallelic and biallelic, autosomal or pseudoautosomal
Likely inborn error of metabolism
BOTH monoallelic and biallelic, autosomal or pseudoautosomal
Mitochondrial disorders
BOTH monoallelic and biallelic, autosomal or pseudoautosomal
Possible mitochondrial disorder - nuclear genes
BOTH monoallelic and biallelic, autosomal or pseudoautosomal

Disease associations (Open Targets)

combined oxidative phosphorylation deficiency 55
0.80
neurodegenerative disease
0.47
neurodevelopmental disorder
0.34
substance-related disorder
0.15
Alpers syndrome
0.12
mitochondrial DNA depletion syndrome 4a
0.12
autosomal dominant progressive external ophthalmoplegia
0.12
non-small cell lung carcinoma
0.08
prostate cancer
0.08
Familial prostate cancer
0.08

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

DNA-directed RNA polymerase, mitochondrial

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)