AQP7
entrez
364
canonical
uniprot
O14520
canonical
ensembl
ENSG00000165269
resolver
ensp
ENSP00000297988
resolver
ensp
ENSP00000368820
resolver
ensp
ENSP00000396111
resolver
ensp
ENSP00000485332
resolver
ensp
ENSP00000568454
resolver
ensp
ENSP00000664663
resolver
ensp
ENSP00000664667
resolver
enst
ENST00000377425
resolver
enst
ENST00000379506
resolver
enst
ENST00000624075
resolver
genesymbol
AQP7
resolver
genesymbol_syn
AQP7L
resolver
genesymbol_syn
AQP9
resolver
hgnc
HGNC:640
resolver
uniprot
A0A096LP09
resolver
uniprot
B7Z4U2
resolver
uniprot
B7Z4V0
resolver
uniprot
F6RZE9
resolver
uniprot
Q08E94
resolver
uniprot
Q5T5L9
resolver
uniprot
Q5T5M0
resolver
uniprot
Q6P5T0
resolver
uniprot
Q8NHM3
resolver
uniprot_entry
A0A096LP09_HUMAN
resolver
uniprot_entry
AQP7_HUMAN
resolver
uniprot_entry
B7Z4U2_HUMAN
resolver
uniprot_entry
B7Z4V0_HUMAN
resolver
uniprot_entry
F6RZE9_HUMAN
resolver
uniprot_entry
Q5T5M0_HUMAN
resolver
uniprot_entry
Q6P5T0_HUMAN
resolver
uniprot_sec
Q08E94
resolver
uniprot_sec
Q5T5L9
resolver
uniprot_sec
Q8NHM3
resolver
activity_regulation
ACTIVITY REGULATION: Glycerol transport is regulated by pH, with the porin being permeable to glycerol at pH 7.4 but not at pH 5.5 (PubMed:30420639, PubMed:30423801). Water permeability, however, is not influenced by pH (PubMed:30420639, PubMed:30423801). Inhibited by mercury ions (PubMed:9405233). {ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:9405233}.
uniprot
proteins
amino_acid_sequence
MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF
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:11952783, PubMed:30420639, PubMed:30423801, PubMed:36737436, PubMed:9405233). Could also be permeable to urea (PubMed:9405233). Mediates the efflux of glycerol, formed upon triglyceride hydrolysis, to avoid its accumulation in adipocytes and to make it available to other tissues. In the kidney, mediates the reabsorption of glycerol, preventing its loss in urine, again participating to energy homeostasis. In pancreatic beta cells, it also mediates the efflux of glycerol, regulating its intracellular levels (By similarity). {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:11952783, ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:36737436, ECO:0000269|PubMed:9405233}.
uniprot
proteins
mass_dalton
37232
uniprot
proteins
mutagenesis
MUTAGEN 10..11; /note="ST->AA: Loss of phosphorylation by PKA. Increased interaction with PLIN1."; /evidence="ECO:0000269|PubMed:27832861"; MUTAGEN 67; /note="Y->A: No effect on glycerol channel activity. No effect on water channel activity."; /evidence="ECO:0000269|PubMed:32695023"; MUTAGEN 74; /note="F->W: No effect on glycerol channel activity. No effect on water channel activity. Decreased glycerol channel activity; when associated with F-233."; /evidence="ECO:0000269|PubMed:32695023"; MUTAGEN 135; /note="Y->A: Strongly decreased glycerol channel activity. Mildly decreased water channel activity."; /evidence="ECO:0000269|PubMed:30423801"; MUTAGEN 165; /note="H->A: Decreased glycerol channel activity. Mildly decreased water channel activity."; /evidence="ECO:0000269|PubMed:30423801"; MUTAGEN 223; /note="Y->F: No effect on glycerol channel activity. No effect on water channel activity. Decreased glycerol channel activity; when associated with W-74."; /evidence="ECO:0000269|PubMed:32695023
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA could prevent the interaction with PLIN1. {ECO:0000269|PubMed:27832861}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
11952783
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17566090
uniprot
proteins
pubmed
27832861
uniprot
proteins
pubmed
28042826
uniprot
proteins
pubmed
30420639
uniprot
proteins
pubmed
30423801
uniprot
proteins
pubmed
32695023
uniprot
proteins
pubmed
36737436
uniprot
proteins
pubmed
9405233
uniprot
proteins
sequence_length
342
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11952783, ECO:0000269|PubMed:28042826, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:9405233}; Multi-pass membrane protein {ECO:0000269|PubMed:36737436}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:27832861}; Multi-pass membrane protein {ECO:0000269|PubMed:36737436}. Lipid droplet {ECO:0000305|PubMed:27832861}. Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (By similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (PubMed:27832861). {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:27832861}.
uniprot
proteins
transmembrane_region
TRANSMEM 37..54; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX"; TRANSMEM 68..85; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX"; TRANSMEM 112..132; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX"; TRANSMEM 171..188; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX"; TRANSMEM 201..217; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX"; TRANSMEM 254..275; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
uniprot
proteins