PITRM1

Chr 10p15.2

pitrilysin metallopeptidase 1

Aliases:: MP1, KIAA1104, hMP1, PreP
MANE:: ENST00000224949.9

OMIM: 618211 ↗NCBI: 10531 ↗Ensembl ↗

Annotations refreshed 10 hours ago.

Predicted protein structure

AlphaFold predicted structure

PITRM1 · Q5JRX3

v62025-08-01

Predicted Aligned Error matrix for PITRM1 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

94.3/ 100

Very high

1,037 residues

Confidence breakdown

Very high(≥ 90)93%
Confident(70–90)3%
Low(50–70)1%
Very low(< 50)4%

Open interactive 3D viewer

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

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

Ataxia and cerebellar anomalies - narrow panel
BIALLELIC, autosomal or pseudoautosomal
Intellectual disability
BIALLELIC, autosomal or pseudoautosomal
Likely inborn error of metabolism
BIALLELIC, autosomal or pseudoautosomal
Mitochondrial disorders
BIALLELIC, autosomal or pseudoautosomal
Possible mitochondrial disorder - nuclear genes
Unknown

Disease associations (Open Targets)

spinocerebellar ataxia, autosomal recessive 30
0.72
mitochondrial DNA depletion syndrome 7 (hepatocerebral type)
0.33
thyroid gland disorder
0.22
skin disorder
0.21
alcohol drinking
0.18
synovium disorder
0.17
hyperpituitarism
0.17
colorectal carcinoma
0.15
generalized dystonia
0.13
digestive system disorder
0.13

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

Protein function (UniProt)

Presequence protease, mitochondrial

Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing (PubMed:10360838, PubMed:16849325, PubMed:19196155, PubMed:24931469). Has an ATP-independent activity (PubMed:16849325). Specifically cleaves peptides in the range of 5 to 65 residues (PubMed:19196155). Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference (PubMed:10360838, PubMed:19196155, PubMed:24931469). Degrades the transit peptides of mitochondrial proteins after their cleavage (PubMed:19196155). Also degrades other unstructured peptides (PubMed:19196155). It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion (PubMed:16849325, PubMed:24931469, PubMed:26697887). It is a highly efficient protease, at least toward amyloid-beta protein 40 (PubMed:24931469, PubMed:29383861, PubMed:29764912). Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently (PubMed:24931469). It is also able to degrade amyloid-beta protein 42 (PubMed:29764912)