P3H1 (Prolyl 3-Hydroxylase 1)
Gene encoding a collagen-modifying enzyme critical for bone development and connective tissue integrity
Gene Information Card
| Symbol | P3H1 |
|---|---|
| Full Name | Prolyl 3-Hydroxylase 1 |
| Gene Type | Protein coding |
| Chromosomal Location | 1p34.2 |
| NCBI Gene ID | 64175 ncbi.nlm.nih.gov/gene/64175 |
| Ensembl ID | ENSG00000117385 |
| UniProt ID | Q32P28 |
| OMIM ID | 610339 |
| HGNC ID | 19316 |
| Aliases | LEPRE1, LEPR1, P3H1 |
Description
P3H1 encodes prolyl 3-hydroxylase 1, an enzyme that hydroxylates proline residues in collagen chains, specifically at the Pro-986 position of type I collagen. This modification is essential for proper collagen folding, stability, and extracellular matrix assembly. Mutations in P3H1 cause autosomal recessive osteogenesis imperfecta type VIII, characterized by severe bone fragility and growth deficiency.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Osteogenesis imperfecta type VIII | Loss-of-function mutations in P3H1 impair collagen prolyl 3-hydroxylation, leading to misfolded collagen and defective bone mineralization | OMIM #610915; ClinVar pathogenic variants |
| Ehlers-Danlos syndrome (rare) | Potential digenic or modifier effects; limited evidence | Case reports in literature |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Bone | 12.5 | Medium |
| Cartilage | 9.8 | Medium |
| Skin | 7.2 | Low |
| Lung | 6.1 | Low |
| Heart | 4.3 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| Osteoblasts | 15.0 | High expression in bone-forming cells |
| Chondrocytes | 11.2 | Moderate expression |
| Fibroblasts | 8.5 | Moderate expression |
| HEK 293 | 2.1 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1080+1G>A | Splice donor | Rare | Loss of function; causes OI type VIII |
| p.Arg319* | Nonsense | Rare | Premature truncation; loss of enzyme activity |
| p.Gly557Val | Missense | Rare | Reduced hydroxylation activity |
Mutation functional classification
Loss of Function (LOF)
Most P3H1 mutations are loss-of-function, leading to reduced or absent prolyl 3-hydroxylase activity and severe osteogenesis imperfecta.
Gain of Function (GOF)
No gain-of-function mutations reported.
Dominant Negative (DN)
No dominant-negative effects documented; disease is autosomal recessive.
View complete mutation data：
Gene Ontology (GO)
| • prolyl 3-hydroxylase activity | • collagen binding |
| • L-ascorbic acid binding | • endoplasmic reticulum lumen |
| • protein hydroxylation | • collagen fibril organization |
Pathways
• Collagen biosynthesis and modifying enzymes
• Endoplasmic reticulum protein processing
• Extracellular matrix organization
Protein Summary
Prolyl 3-hydroxylase 1 is a 736-amino acid protein localized to the endoplasmic reticulum. It forms a complex with cartilage-associated protein (CRTAP) and prolyl 3-hydroxylase 2 (P3H2) to hydroxylate proline residues in collagen triple helices. This modification is critical for collagen folding and secretion. Deficiency leads to severe bone fragility.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| P3H1 Knockout HEK293 Cell Line | EDJ-KQ11360 | Human | 64175 | Details Get a Quote |
| P3H1 Knockout A-549 Cell Line | EDJ-KQ40794 | Human | 64175 | Details Get a Quote |
| P3H1 Knockout HCT 116 Cell Line | EDJ-KQ40795 | Human | 64175 | Details Get a Quote |
| P3H1 Knockout HeLa Cell Line | EDJ-KQ40796 | Human | 64175 | Details Get a Quote |
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