CLPX: Caseinolytic Mitochondrial Matrix Peptidase Chaperone Subunit
A mitochondrial ATP-dependent protease chaperone involved in protein quality control and heme biosynthesis.
Gene Information Card
| Symbol | CLPX |
|---|---|
| Full Name | Caseinolytic Mitochondrial Matrix Peptidase Chaperone Subunit |
| Gene Type | Protein coding |
| Chromosomal Location | 15q22.31 |
| NCBI Gene ID | 10845 ncbi.nlm.nih.gov/gene/10845 |
| Ensembl ID | ENSG00000104067 |
| UniProt ID | O76031 |
| OMIM ID | 615824 |
| HGNC ID | 2088 |
| Aliases | CLPXP, hCLPX, FLJ11100 |
Description
CLPX encodes the ATP-dependent chaperone subunit of the mitochondrial matrix peptidase complex. It forms a hexameric ring that unfolds and translocates substrate proteins into the proteolytic chamber of CLPP for degradation. CLPX is essential for mitochondrial protein quality control and plays a role in heme biosynthesis by regulating the stability of 5-aminolevulinic acid synthase (ALAS1).
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Perrault syndrome 5 | Biallelic CLPX mutations impair mitochondrial protease function, leading to sensorineural hearing loss and ovarian dysfunction. | OMIM #619300 |
| Mitochondrial complex deficiency | CLPX dysfunction disrupts mitochondrial proteostasis, causing respiratory chain defects. | ClinVar |
| Heme biosynthesis disorders | CLPX regulates ALAS1 turnover; mutations may alter heme production. | UniProt |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 12.5 | Medium |
| Heart | 9.8 | Medium |
| Skeletal muscle | 8.2 | Medium |
| Kidney | 7.1 | Low |
| Brain | 5.3 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 | 14.2 | High expression |
| K-562 | 10.1 | Medium expression |
| HeLa | 8.5 | Medium expression |
| A549 | 6.3 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.814C>T (p.Arg272Trp) | Missense | Rare | Loss of ATPase activity; associated with Perrault syndrome 5 |
| c.1045G>A (p.Gly349Arg) | Missense | Rare | Impaired substrate binding; reported in ClinVar |
| c.1234_1235del (p.Lys412Glufs*3) | Frameshift | Very rare | Truncated protein; loss of function |
Mutation functional classification
Loss of Function (LOF)
Most CLPX disease-associated mutations are loss-of-function, reducing ATPase or chaperone activity, leading to mitochondrial protein aggregation and dysfunction.
Gain of Function (GOF)
No gain-of-function mutations have been reported for CLPX.
Dominant Negative (DN)
Heterozygous missense mutations may exert dominant-negative effects by disrupting hexamer assembly, though evidence is limited.
View complete mutation data：
Gene Ontology (GO)
| • ATP-dependent protein folding chaperone | • ATP hydrolysis activity |
| • mitochondrial matrix | • protein homooligomerization |
| • proteolysis | • response to stress |
Pathways
• Mitochondrial protein degradation (CLPXP complex)
• Heme biosynthesis (regulation of ALAS1)
Protein Summary
CLPX is a 633-amino acid mitochondrial chaperone that forms a hexameric ring structure. It uses ATP hydrolysis to unfold and translocate protein substrates into the CLPP protease chamber. CLPX is critical for mitochondrial proteostasis and heme pathway regulation. Mutations cause Perrault syndrome 5 and mitochondrial dysfunction.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| CLPX Knockout HEK293 Cell Line | EDJ-KQ3578 | Human | 10845 | Details Get a Quote |
| CLPX Knockout A-549 Cell Line | EDJ-KQ25463 | Human | 10845 | Details Get a Quote |
| CLPX Knockout HCT 116 Cell Line | EDJ-KQ25464 | Human | 10845 | Details Get a Quote |
| CLPX Knockout HeLa Cell Line | EDJ-KQ25465 | Human | 10845 | Details Get a Quote |
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