I3W9F7 · AQP2_RHIIR
- ProteinAquaglyceroporin-2
- GeneAQPF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids316 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Water channel required to facilitate the transport of water across membranes (PubMed:23157494).
Stimulates plant drought tolerance by facilitating the transport of water from the arbuscular mycorrhiza fungus to host plants (PubMed:23157494).
Stimulates plant drought tolerance by facilitating the transport of water from the arbuscular mycorrhiza fungus to host plants (PubMed:23157494).
Catalytic activity
- H2O(in) = H2O(out)
- glycerol(in) = glycerol(out)
Activity regulation
Polyethylene glycol (PEG) stimulates whereas glycerol inhibits the aquaporin activity.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | glycerol channel activity | |
Molecular Function | water channel activity |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAquaglyceroporin-2
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Glomeromycotina > Glomeromycetes > Glomerales > Glomeraceae > Rhizophagus
Accessions
- Primary accessionI3W9F7
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Note: Shows a clear localization to the plasma membrane as well as intracellular membranes.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-59 | Cytoplasmic | ||||
Sequence: MADERGPINKSGPSSTYGATENNGESGGTRGAPATEDVIVIQDSGWYYIKFRFKEPFAE | ||||||
Transmembrane | 60-80 | Helical | ||||
Sequence: FLGTFILVAFGVGAIAQTVLS | ||||||
Topological domain | 81-86 | Extracellular | ||||
Sequence: KGATGN | ||||||
Transmembrane | 87-107 | Helical | ||||
Sequence: WITIALGFGLGLALGIAVSGH | ||||||
Topological domain | 108-131 | Cytoplasmic | ||||
Sequence: YSGGHLNPAVTITLAIYRKFPWVK | ||||||
Transmembrane | 132-152 | Helical | ||||
Sequence: VPVYITAQVLGAFVAAAVIYL | ||||||
Topological domain | 153-187 | Extracellular | ||||
Sequence: NYLPAIYNFAGDKRDVIGANATAGIFATYPQPFMS | ||||||
Transmembrane | 188-208 | Helical | ||||
Sequence: IGGAFFSEALGTFFLLFVILA | ||||||
Topological domain | 209-219 | Cytoplasmic | ||||
Sequence: MTDERNVPTTR | ||||||
Transmembrane | 220-240 | Helical | ||||
Sequence: IVAPITIGLTLTAIAISLGFE | ||||||
Topological domain | 241-271 | Extracellular | ||||
Sequence: TGFSLNAARDFGPRLFTFFIGYGVEVFTAYK | ||||||
Transmembrane | 272-292 | Helical | ||||
Sequence: FYFWIPLVAPIVGGLVAGFVY | ||||||
Topological domain | 293-316 | Cytoplasmic | ||||
Sequence: DSLLYWGEKSFLNKNVHHEHRAVA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457437 | 1-316 | Aquaglyceroporin-2 | |||
Sequence: MADERGPINKSGPSSTYGATENNGESGGTRGAPATEDVIVIQDSGWYYIKFRFKEPFAEFLGTFILVAFGVGAIAQTVLSKGATGNWITIALGFGLGLALGIAVSGHYSGGHLNPAVTITLAIYRKFPWVKVPVYITAQVLGAFVAAAVIYLNYLPAIYNFAGDKRDVIGANATAGIFATYPQPFMSIGGAFFSEALGTFFLLFVILAMTDERNVPTTRIVAPITIGLTLTAIAISLGFETGFSLNAARDFGPRLFTFFIGYGVEVFTAYKFYFWIPLVAPIVGGLVAGFVYDSLLYWGEKSFLNKNVHHEHRAVA | ||||||
Glycosylation | 172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Induction
Expression is increased significantly in arbuscule-enriched cortical cells and extraradical mycelia of maize roots under drought stress.
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MADERGPINKSGPSSTYGATENNGESGGTRG | ||||||
Compositional bias | 9-29 | Polar residues | ||||
Sequence: NKSGPSSTYGATENNGESGGT | ||||||
Motif | 114-116 | NPA 1 | ||||
Sequence: NPA | ||||||
Motif | 246-248 | NPA 2 | ||||
Sequence: NAA |
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) (Probable). AQFP2 has NPA/NAA motifs which is in accordance with the fungal aquaporins (NPx and NxA) (Probable).
Sequence similarities
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length316
- Mass (Da)33,968
- Last updated2012-09-05 v1
- Checksum8237070B83F8E7AD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-29 | Polar residues | ||||
Sequence: NKSGPSSTYGATENNGESGGT |