Aqp7
entrez
11832
canonical
uniprot
O54794
canonical
ensembl
ENSMUSG00000028427
resolver
ensp
ENSMUSP00000030136
resolver
ensp
ENSMUSP00000093007
resolver
ensp
ENSMUSP00000306180
resolver
ensp
ENSMUSP00000306183
resolver
ensp
ENSMUSP00000306187
resolver
ensp
ENSMUSP00000306200
resolver
ensp
ENSMUSP00000362944
resolver
enst
ENSMUST00000030136
resolver
enst
ENSMUST00000054945
resolver
genesymbol
Aqp7
resolver
uniprot
Q5DX24
resolver
uniprot
Q8C630
resolver
uniprot_entry
AQP7_MOUSE
resolver
uniprot_entry
Q5DX24_MOUSE
resolver
uniprot_sec
Q8C630
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. Water permeability, however, is not influenced by pH. {ECO:0000250|UniProtKB:O14520}.
uniprot
proteins
amino_acid_sequence
MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF
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. Could also be permeable to urea (By similarity). Mediates the efflux of glycerol, formed upon triglyceride hydrolysis, to avoid its accumulation in adipocytes and to make it available to other tissues (PubMed:15591341, PubMed:15746100, PubMed:16009937). In the kidney, mediates the reabsorption of glycerol, preventing its loss in urine, again participating to energy homeostasis (PubMed:15998844, PubMed:17077387). In pancreatic beta cells, it also mediates the efflux of glycerol, regulating its intracellular levels (PubMed:17576812). {ECO:0000250|UniProtKB:O14520, ECO:0000269|PubMed:15591341, ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:15998844, ECO:0000269|PubMed:16009937, ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:17576812}.
uniprot
proteins
mass_dalton
32667
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA could prevent the interaction with PLIN1. {ECO:0000250|UniProtKB:O14520}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15591341
uniprot
proteins
pubmed
15746100
uniprot
proteins
pubmed
15998844
uniprot
proteins
pubmed
16009937
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17077387
uniprot
proteins
pubmed
17576812
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25643985
uniprot
proteins
sequence_length
303
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:25643985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25643985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Lipid droplet {ECO:0000269|PubMed:25643985}. Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (PubMed:25643985). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (By similarity). {ECO:0000250|UniProtKB:O14520, ECO:0000269|PubMed:25643985}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..39; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:O14520"; TRANSMEM 53..70; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:O14520"; TRANSMEM 97..117; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:O14520"; TRANSMEM 153..173; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:O14520"; TRANSMEM 186..202; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:O14520"; TRANSMEM 239..260; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:O14520
uniprot
proteins