AQP2_SHEEP
ID AQP2_SHEEP Reviewed; 271 AA.
AC O62735;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 99.
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;
GN Name=AQP2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10412857; DOI=10.1007/s004670050627;
RA Butkus A., Earnest L., Jeyaseelan K., Moritz K., Johnston H., Tenis N.,
RA Wintour E.M.;
RT "Ovine aquaporin-2: cDNA cloning, ontogeny and control of renal gene
RT expression.";
RL Pediatr. Nephrol. 13:379-390(1999).
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 -!- TISSUE SPECIFICITY: Expressed in renal collecting tubules.
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: Ser-256 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}.
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; AF050152; AAC05745.1; -; mRNA.
DR AlphaFoldDB; O62735; -.
DR SMR; O62735; -.
DR STRING; 9940.ENSOARP00000019510; -.
DR eggNOG; KOG0223; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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 CDD; cd00333; MIP; 1.
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 TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Aquaporin-2"
FT /id="PRO_0000063941"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 33..40
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 60..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 65..74
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 75..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 108..127
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 149..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 177..180
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 181..193
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 194..201
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT TOPO_DOM 223..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 249..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 68..70
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT MOTIF 184..186
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41181"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 29006 MW; 486BED73AC42916B CRC64;
MWELRSIAFS RAVLAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL AIGTLVQALG
HVSGAHINPA VTVACLVGCH VSFLRAVFYV AAQLLGAVAG AALLHEITPP AIRGDLAVNA
LNNNSTAGQA VTVELFLTLQ LVLCIFPSTD KRRGKQLGHP ALSIGFSVAL GHLLGIHYTG
CSMNPARSLA PAIVTGKFDD HWVFWIGPLV GAIVASLLYN YVLFPPAKSL SERLAVLKGL
EPDTDWEERE VRRRQSVELH SPQSLPRGTK A
