AQP2_PROHA
ID AQP2_PROHA Reviewed; 109 AA.
AC P79229;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Aquaporin-2;
DE Short=AQP-2;
DE AltName: Full=ADH water channel;
DE AltName: Full=Aquaporin-CD;
DE Short=AQP-CD;
DE AltName: Full=Collecting duct water channel protein;
DE AltName: Full=WCH-CD;
DE AltName: Full=Water channel protein for renal collecting duct;
DE Flags: Fragment;
GN Name=AQP2;
OS Procavia capensis habessinica (Abyssinian hyrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Hyracoidea; Procaviidae; Procavia.
OX NCBI_TaxID=9814;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9100366; DOI=10.1093/oxfordjournals.molbev.a025772;
RA Madsen O.J., Deen P.M.T., Pesole G., Saccone C., de Jong W.W.;
RT "Molecular evolution of mammalian aquaporin-2: further evidence that
RT elephant shrew and aardvark join the paenungulate clade.";
RL Mol. Biol. Evol. 14:363-371(1997).
CC -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC membranes of renal collecting duct with high permeability to water,
CC thereby permitting water to move in the direction of an osmotic
CC gradient. {ECO:0000250|UniProtKB:P41181}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41181}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P41181}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P34080}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Cell membrane
CC {ECO:0000250|UniProtKB:P41181}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P41181}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:P41181}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Note=Shuttles from vesicles to the
CC apical membrane. Vasopressin-regulated phosphorylation is required for
CC translocation to the apical cell membrane. PLEKHA8/FAPP2 is required to
CC transport AQP2 from the TGN to sites where AQP2 is phosphorylated.
CC {ECO:0000250|UniProtKB:P41181}.
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). {ECO:0000250|UniProtKB:P41181}.
CC -!- PTM: Serine phosphorylation is necessary and sufficient for expression
CC at the apical membrane. Endocytosis is not phosphorylation-dependent.
CC {ECO:0000250|UniProtKB:P41181}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41181}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; Y10631; CAA71656.1; -; Genomic_DNA.
DR AlphaFoldDB; P79229; -.
DR SMR; P79229; -.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; ISS:UniProtKB.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..>109
FT /note="Aquaporin-2"
FT /id="PRO_0000063938"
FT TOPO_DOM <1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 28..35
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 55..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 60..69
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 70..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 103..>109
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOTIF 63..65
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT NON_TER 1
FT NON_TER 109
SQ SEQUENCE 109 AA; 11312 MW; 3BB4A9A3D636AA2A CRC64;
SIAFSRAVLS EFLATLLFVF FGLGSALNWP QALPSVLQIA MAFGLAIGTL VQTLGHISGA
HINPAVTIAC LVGCHVSFLR ALFYLAAQLL GAVAGAALLH ELTPPDIRG
