Lysosomal Pro-X carboxypeptidase
Named enzymes, including the metabolising cytochromes and the monoamine oxidases.
- Measurements
- 1
- Compounds
- 1
- Binding constants
- 0
- Median pX
- —
I · Identity
What this target is
Its function as UniProt states it, where in a cell the protein is found, and which cell types and tissues transcribe its gene.
Lysosomal Pro-X carboxypeptidase
Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH
Quoted from UniProt’s FUNCTION annotation for P42785 (reviewed).
What it acts with
STRING’s highest-confidence human functional partners. The combined score mixes several kinds of evidence, so each channel is shown separately — a partner supported by experiment is a different claim from one supported only by text mining, and for a receptor this is where its coupling appears as evidence rather than as assertion.
Where it sits in the cell
- Vesicles
Human Protein Atlas, by antibody immunofluorescence in cell lines — a different assay from the expression figures below, which are RNA.
UniProt, curated Lysosome
Expression by cell type
Single cell type RNA, the 5 highest of those the Human Protein Atlas reports for this gene. Transcript, not protein, and a cell type rather than a tissue.
- Kupffer cells375.1 nCPM
- Neutrophils328.4 nCPM
- Bergmann glia243.7 nCPM
- Vascular endothelial cells213.7 nCPM
- cDC210.4 nCPM
IV · Evidence
Every measurement at this target
Each row links to the ChEMBL assay it came from.
Functional readouts 1
IC₅₀, EC₅₀, AC₅₀ and potency. Assay-dependent, and not interchangeable with a binding constant.
| Target | Class | Type | Value (nM) | pX | Organism | Assay |
|---|---|---|---|---|---|---|
| Lysosomal Pro-X carboxypeptidase | Enzymes | IC50 | 20.00 | 7.70 | Homo sapiens | CHEMBL764432 |