ID AQP2_RHIIR Reviewed; 316 AA. AC I3W9F7; DT 22-FEB-2023, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 1. DT 22-FEB-2023, entry version 27. DE RecName: Full=Aquaglyceroporin-2 {ECO:0000303|PubMed:23157494}; GN Name=AQPF2 {ECO:0000303|PubMed:23157494}; OS Rhizophagus irregularis (Arbuscular mycorrhizal fungus) (Glomus OS intraradices). OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina; OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus. OX NCBI_TaxID=4876; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, TOPOLOGY, SUBCELLULAR RP LOCATION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND INDUCTION. RX PubMed=23157494; DOI=10.1111/nph.12011; RA Li T., Hu Y.J., Hao Z.P., Li H., Wang Y.S., Chen B.D.; RT "First cloning and characterization of two functional aquaporin genes from RT an arbuscular mycorrhizal fungus Glomus intraradices."; RL New Phytol. 197:617-630(2013). CC -!- FUNCTION: Water channel required to facilitate the transport of water CC across membranes (PubMed:23157494). Stimulates plant drought tolerance CC by facilitating the transport of water from the arbuscular mycorrhiza CC fungus to host plants (PubMed:23157494). {ECO:0000269|PubMed:23157494}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; CC Evidence={ECO:0000269|PubMed:23157494}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675, CC ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:23157494}; CC -!- ACTIVITY REGULATION: Polyethylene glycol (PEG) stimulates whereas CC glycerol inhibits the aquaporin activity. CC {ECO:0000269|PubMed:23157494}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23157494}; CC Multi-pass membrane protein {ECO:0000255}. Membrane CC {ECO:0000269|PubMed:23157494}; Multi-pass membrane protein CC {ECO:0000255}. Note=Shows a clear localization to the plasma membrane CC as well as intracellular membranes. {ECO:0000269|PubMed:23157494}. CC -!- INDUCTION: Expression is increased significantly in arbuscule-enriched CC cortical cells and extraradical mycelia of maize roots under drought CC stress. {ECO:0000269|PubMed:23157494}. CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three CC membrane-spanning domains and a pore-forming loop with the signature CC motif Asn-Pro-Ala (NPA) (Probable). AQFP2 has NPA/NAA motifs which is CC in accordance with the fungal aquaporins (NPx and NxA) (Probable). CC {ECO:0000305|PubMed:23157494}. CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JQ412060; AFK93203.1; -; mRNA. DR AlphaFoldDB; I3W9F7; -. DR VEuPathDB; FungiDB:FUN_024007; -. DR VEuPathDB; FungiDB:GLOIN_2v1742988; -. DR VEuPathDB; FungiDB:RhiirA1_419484; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015267; F:channel activity; IEA:InterPro. DR CDD; cd00333; MIP; 1. DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000425; MIP. DR InterPro; IPR022357; MIP_CS. DR PANTHER; PTHR43829; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1. DR PANTHER; PTHR43829:SF9; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; Aquaporin-like; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. PE 1: Evidence at protein level; KW Cell membrane; Glycoprotein; Membrane; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..316 FT /note="Aquaglyceroporin-2" FT /id="PRO_0000457437" FT TOPO_DOM 1..59 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 81..86 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 108..131 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 153..187 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 188..208 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 209..219 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 220..240 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 241..271 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:23157494" FT TRANSMEM 272..292 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 293..316 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:23157494" FT MOTIF 114..116 FT /note="NPA 1" FT /evidence="ECO:0000305|PubMed:23157494" FT MOTIF 246..248 FT /note="NPA 2" FT /evidence="ECO:0000305|PubMed:23157494" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 316 AA; 33968 MW; 8237070B83F8E7AD CRC64; MADERGPINK SGPSSTYGAT ENNGESGGTR GAPATEDVIV IQDSGWYYIK FRFKEPFAEF LGTFILVAFG VGAIAQTVLS KGATGNWITI ALGFGLGLAL GIAVSGHYSG GHLNPAVTIT LAIYRKFPWV KVPVYITAQV LGAFVAAAVI YLNYLPAIYN FAGDKRDVIG ANATAGIFAT YPQPFMSIGG AFFSEALGTF FLLFVILAMT DERNVPTTRI VAPITIGLTL TAIAISLGFE TGFSLNAARD FGPRLFTFFI GYGVEVFTAY KFYFWIPLVA PIVGGLVAGF VYDSLLYWGE KSFLNKNVHH EHRAVA //