UniProt-reviewed human alpha-carbonic-anhydrase scope record. Ten experimental structure mappings, two direct assay activities, and one reaction assignment retain membrane attachment and construct boundaries. This release links 13 source records to this accession, a selection rather than every record the upstream databases hold.
Normalized identity
- Gene
- CA4
- UniProt accession
P22748- Catalytic status
- Catalytic
- Review state
- UniProt-reviewed
- Taxon
- 9606
- Entry version
- 232, updated 2026-06-10
- Sequence identity
- v2, CRC64
EF5F182474ABE9B0 - Sequence length
- 312 residues
- Selected structures
- 10
- Selected activities
- 2
- Reaction assignments
- 1
- ChEMBL targets
- CHEMBL3729
Where the identity data came from
Each row is a UniProt snapshot used to build this release: when it was retrieved, its SHA-256 digest and the exact request. The snapshot files stay with the build and are not served here.
| Retrieved | Build-input snapshot | SHA-256 | Upstream request |
|---|---|---|---|
| 2026-07-14T09:21:32Z | raw/uniprot/entries/P22748.json | 28fa76c5a216b9356479d42199f709dd46e662172f2872078a5491cfe2c618f1 | Open exact source |
Source-reported location comments
- Cell membrane · Lipid-anchor, GPI-anchor
UniProt function text
Catalyzes the reversible hydration of carbon dioxide into bicarbonate and protons and thus is essential to maintaining intracellular and extracellular pH (PubMed:15563508, PubMed:16686544, PubMed:16807956, PubMed:17127057, PubMed:17314045, PubMed:17652713, PubMed:17705204, PubMed:18618712, PubMed:19186056, PubMed:19206230, PubMed:7625839). May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis (PubMed:15563508). It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid (PubMed:15563508)