AQP10
entrez
89872
canonical
uniprot
Q96PS8
canonical
ensembl
ENSG00000143595
resolver
ensp
ENSP00000318355
resolver
ensp
ENSP00000578348
resolver
genesymbol
AQP10
resolver
hgnc
HGNC:16029
resolver
uniprot
Q5VYD3
resolver
uniprot
Q5VYD4
resolver
uniprot
Q8NG70
resolver
uniprot_entry
AQP10_HUMAN
resolver
uniprot_sec
Q5VYD3
resolver
uniprot_sec
Q5VYD4
resolver
uniprot_sec
Q8NG70
resolver
activity_regulation
ACTIVITY REGULATION: Glycerol transport is regulated by pH, with the porin being permeable to glycerol at pH 5.5 but not at pH 7.4 (PubMed:30420639). Water permeability, however, is not influenced by pH. {ECO:0000269|PubMed:30420639}.
uniprot
proteins
amino_acid_sequence
MVFTQAPAEIMGHLRIRSLLARQCLAEFLGVFVLMLLTQGAVAQAVTSGETKGNFFTMFLAGSLAVTIAIYVGGNVSGAHLNPAFSLAMCIVGRLPWVKLPIYILVQLLSAFCASGATYVLYHDALQNYTGGNLTVTGPKETASIFATYPAPYLSLNNGFLDQVLGTGMLIVGLLAILDRRNKGVPAGLEPVVVGMLILALGLSMGANCGIPLNPARDLGPRLFTYVAGWGPEVFSAGNGWWWVPVVAPLVGATVGTATYQLLVALHHPEGPEPAQDLVSAQHKASELETPASAQMLECKL
uniprot
proteins
function
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). {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581, ECO:0000269|PubMed:21733844, ECO:0000269|PubMed:23382902, ECO:0000269|PubMed:30420639}.
uniprot
proteins
mass_dalton
31763
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="E->Q: Loss of glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 73; /note="G->A: Increased glycerol channel activity at acidic pH."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 73; /note="G->F: Loss of glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 77; /note="S->A,D: Decreased glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 80; /note="H->A: Loss of glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 85; /note="F->A: Decreased glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 94; /note="R->A: Loss of glycerol channel activity."; /evidence="ECO:0000269|PubMed:30420639"; MUTAGEN 133; /note="N->Q: Abolishes N-glycosylation."; /evidence="ECO:0000269|PubMed:21733844
uniprot
proteins
post_translational_modification
PTM: N-glycosylation at Asn-133 increases the stability of the protein but has no effect on its activity. {ECO:0000269|PubMed:21733844}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
11573934
uniprot
proteins
pubmed
12084581
uniprot
proteins
pubmed
15221416
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
21733844
uniprot
proteins
pubmed
23382902
uniprot
proteins
pubmed
30420639
uniprot
proteins
sequence_length
301
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15221416}; Multi-pass membrane protein {ECO:0000269|PubMed:30420639}. Cell membrane {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581, ECO:0000269|PubMed:23382902, ECO:0000269|PubMed:30420639}; Multi-pass membrane protein {ECO:0000269|PubMed:30420639}. Lipid droplet {ECO:0000269|PubMed:23382902}. Note=Detected around lipid droplets. {ECO:0000269|PubMed:23382902}.
uniprot
proteins
transmembrane_region
TRANSMEM 23..41; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H"; TRANSMEM 56..75; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H"; TRANSMEM 97..121; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H"; TRANSMEM 159..176; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H"; TRANSMEM 189..205; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H"; TRANSMEM 242..262; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:30420639, ECO:0007744|PDB:6F7H
uniprot
proteins