AQP10
Domain
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Function
Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient (PubMed:11573934, PubMed:12084581, PubMed:21733844, PubMed:23382902, PubMed:30420639). Could also be permeable to urea (PubMed:12084581). Among aquaglyceroporins, it exhibits a unique pH-gated glycerol transport activity, being more active at acidic pH. It most likely plays a central role in the efflux of glycerol formed during triglyceride hydrolysis in adipocytes and in glycerol uptake by enterocytes, as both processes occur and are stimulated at acidic pH (PubMed:11573934, PubMed:23382902, PubMed:30420639).
Post-translational modifications
N-glycosylation at Asn-133 increases the stability of the protein but has no effect on its activity.
Sequence Similarities
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Tissue Specificity
Detected in epithelial cells on villi in the ileum, and also in stomach, jejunum, colon, rectum, white adipose tissue and placenta (at protein level) (PubMed:15221416, PubMed:23382902). Expressed in duodenum and jejunum. Highest expression in absorptive epithelial cells at the tips of villi in the jejunum (PubMed:11573934, PubMed:12084581). Detected in subcutaneous adipose tissue (PubMed:23382902).
Cellular localization
- Apical cell membrane
- Multi-pass membrane protein
- Cell membrane
- Multi-pass membrane protein
- Lipid droplet
- Detected around lipid droplets.
Alternative names
Aquaporin-10, AQP-10, Aquaglyceroporin-10, Small intestine aquaporin, AQP10