PM20D2 Gene - Peptidase M20 Domain Containing 2
Comprehensive genetic and functional information for PM20D2 (peptidase M20 domain containing 2), including genomic context, expression, mutations, and clinical relevance.
Gene Information Card
| Symbol | PM20D2 |
|---|---|
| Full Name | peptidase M20 domain containing 2 |
| Gene Type | gene with protein product |
| Chromosomal Location | 6q15 |
| NCBI Gene ID | 135293 ncbi.nlm.nih.gov/gene/135293 |
| Ensembl ID | ENSG00000146281 |
| UniProt ID | Q8IYS1 |
| OMIM ID | 615913 |
| HGNC ID | HGNC:21408 |
| Aliases | bA63L7.3, ACY1L2 |
Description
PM20D2 (peptidase M20 domain containing 2) is a protein-coding gene located on chromosome 6q15. It belongs to the M20 family of metallopeptidases, which are involved in peptide and amino acid metabolism. The encoded protein is predicted to function as a hydrolase, potentially acting on various substrates. PM20D2 is widely expressed in human tissues, with highest levels in the kidney, liver, and testis. Its exact biological role is not fully characterized, but it may participate in protein turnover and amino acid recycling. Mutations in PM20D2 have been associated with a rare autosomal recessive disorder, though the clinical spectrum is still being defined.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| PM20D2-related disorder | Biallelic loss-of-function mutations lead to reduced or absent PM20D2 activity, resulting in a metabolic defect with neurological and skeletal abnormalities. | OMIM 615913; case reports in literature |
| Neurodevelopmental delay | Impaired PM20D2 function may disrupt amino acid homeostasis, affecting neuronal development and function. | Case studies with homozygous mutations |
| Skeletal abnormalities | PM20D2 deficiency may affect bone metabolism, leading to skeletal dysplasia. | Clinical observations in affected individuals |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Kidney | 25.3 | High |
| Liver | 18.7 | Medium |
| Testis | 15.2 | Medium |
| Brain | 8.4 | Low |
| Heart | 6.1 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HEK 293 | 12.5 | Moderate expression |
| HepG2 | 15.8 | Moderate expression |
| A549 | 7.2 | Low expression |
| MCF7 | 5.9 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1A>G (p.Met1?) | Missense | Rare | Loss of start codon, likely no protein product |
| c.238C>T (p.Arg80*) | Nonsense | Rare | Premature stop, likely nonsense-mediated decay |
| c.512_513del (p.Glu171Glyfs*5) | Frameshift | Rare | Frameshift leading to truncated protein |
| c.784G>A (p.Gly262Ser) | Missense | Rare | Potential functional impact, uncertain |
Mutation functional classification
Loss of Function (LOF)
Biallelic loss-of-function mutations (nonsense, frameshift, splice site) are associated with a recessive disorder, indicating that PM20D2 haploinsufficiency is not sufficient for disease; complete loss is pathogenic.
Gain of Function (GOF)
No evidence for gain-of-function mutations; all reported pathogenic variants are loss-of-function.
Dominant Negative (DN)
No evidence for dominant-negative effects; disease is recessive.
View complete mutation data：
Gene Ontology (GO)
| • metallopeptidase activity | • hydrolase activity |
| • zinc ion binding | • proteolysis |
| • cellular amino acid metabolic process |
Pathways
• Amino acid metabolism
• Protein digestion and absorption
Protein Summary
The PM20D2 protein is a member of the M20 family of metallopeptidases, characterized by a conserved catalytic domain that binds a divalent metal ion, typically zinc. It is predicted to be a cytoplasmic enzyme involved in the hydrolysis of peptide bonds, potentially acting on dipeptides or small peptides. The protein contains a peptidase M20 domain and is likely involved in amino acid metabolism. Its exact substrates and physiological functions remain to be fully elucidated, but it may play a role in protein turnover and nitrogen balance. Structural studies suggest a homodimeric arrangement, similar to other M20 peptidases.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| PM20D2 Knockout HEK293 Cell Line | EDJ-KQ9360 | Human | 135293 | Details Get a Quote |
| PM20D2 Knockout A-549 Cell Line | EDJ-KQ36010 | Human | 135293 | Details Get a Quote |
| PM20D2 Knockout HCT 116 Cell Line | EDJ-KQ36011 | Human | 135293 | Details Get a Quote |
| PM20D2 Knockout HeLa Cell Line | EDJ-KQ36012 | Human | 135293 | Details Get a Quote |
