Search Results
Overview
| Uniprot ID | O75844 |
|---|---|
| Protein Name | CAAX prenyl protease 1 homolog |
| Gene Name | ZMPSTE24 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 429 | AKKLGKAKDLYSALI |
Function
Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum (PubMed:33293369, PubMed:33315887). Proteolytically removes the C-terminal three residues of farnesylated proteins (PubMed:33293369, PubMed:33315887). Also plays an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia (PubMed:28169297, PubMed:28246125). Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity (PubMed:35283811)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0031901 | early endosome membrane |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031902 | late endosome membrane |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005637 | nuclear inner membrane |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0004175 | endopeptidase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0004222 | metalloendopeptidase activity |
| Molecular Function | GO:0008235 | metalloexopeptidase activity |
| Biological Process | GO:0071586 | CAAX-box protein processing |
| Biological Process | GO:0006998 | nuclear envelope organization |
| Biological Process | GO:0051604 | protein maturation |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0050688 | regulation of defense response to virus |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.