AQP2_RAT
ID AQP2_RAT Reviewed; 271 AA.
AC P34080; A1A5L4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 {ECO:0000303|PubMed:8429910};
DE AltName: Full=Water channel protein for renal collecting duct;
GN Name=Aqp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8429910; DOI=10.1038/361549a0;
RA Fushimi K., Uchida S., Hara Y., Hirata Y., Marumo F., Sasaki S.;
RT "Cloning and expression of apical membrane water channel of rat kidney
RT collecting tubule.";
RL Nature 361:549-552(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=7505572; DOI=10.1006/bbrc.1993.2529;
RA Ma T., Frigeri A., Skach W., Verkman A.S.;
RT "Cloning of a novel rat kidney cDNA homologous to CHIP28 and WCH-CD water
RT channels.";
RL Biochem. Biophys. Res. Commun. 197:654-659(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7508187; DOI=10.1152/ajpcell.1994.266.1.c189;
RA Ma T., Hasegawa H., Skach W., Frigeri A., Verkman A.S.;
RT "Expression, functional analysis, and in situ hybridization of a cloned rat
RT kidney collecting duct water channel.";
RL Am. J. Physiol. 266:C189-C197(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-261; SER-264 AND
RP SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19794145; DOI=10.1152/ajpcell.00098.2009;
RA Yui N., Okutsu R., Sohara E., Rai T., Ohta A., Noda Y., Sasaki S.,
RA Uchida S.;
RT "FAPP2 is required for aquaporin-2 apical sorting at trans-Golgi network in
RT polarized MDCK cells.";
RL Am. J. Physiol. 297:C1389-C1396(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:8429910, PubMed:7508187). Plays an essential role in
CC renal water homeostasis (By similarity). {ECO:0000250|UniProtKB:P41181,
CC ECO:0000269|PubMed:7508187, ECO:0000269|PubMed:8429910}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41181}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19794145, ECO:0000269|PubMed:8429910}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P41181}. Basolateral cell
CC membrane {ECO:0000269|PubMed:19794145}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Cell membrane
CC {ECO:0000269|PubMed:7508187}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:19794145}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P41181}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:19794145}; 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:0000269|PubMed:19794145}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, in cortical and the medullary
CC collecting tubules (at protein level) (PubMed:8429910). Detected in
CC kidney medulla and cortex (PubMed:8429910, PubMed:7508187).
CC {ECO:0000269|PubMed:7508187, ECO:0000269|PubMed:8429910}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA41478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13906; BAA03006.1; -; mRNA.
DR EMBL; L28112; AAA41478.1; ALT_INIT; mRNA.
DR EMBL; BC128705; AAI28706.1; -; mRNA.
DR PIR; JT0750; JT0750.
DR RefSeq; NP_037041.2; NM_012909.2.
DR AlphaFoldDB; P34080; -.
DR SMR; P34080; -.
DR CORUM; P34080; -.
DR DIP; DIP-46223N; -.
DR IntAct; P34080; 4.
DR STRING; 10116.ENSRNOP00000000324; -.
DR GlyGen; P34080; 1 site.
DR iPTMnet; P34080; -.
DR PhosphoSitePlus; P34080; -.
DR PaxDb; P34080; -.
DR DNASU; 25386; -.
DR GeneID; 25386; -.
DR KEGG; rno:25386; -.
DR UCSC; RGD:2142; rat.
DR CTD; 359; -.
DR RGD; 2142; Aqp2.
DR eggNOG; KOG0223; Eukaryota.
DR InParanoid; P34080; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P34080; -.
DR TreeFam; TF312940; -.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P34080; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0070382; C:exocytic vesicle; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098576; C:lumenal side of membrane; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; ISO:RGD.
DR GO; GO:0071288; P:cellular response to mercury ion; ISO:RGD.
DR GO; GO:0042631; P:cellular response to water deprivation; IDA:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISO:RGD.
DR GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
DR GO; GO:0072205; P:metanephric collecting duct development; ISO:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0003091; P:renal water homeostasis; ISS:UniProtKB.
DR GO; GO:0003097; P:renal water transport; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0033762; P:response to glucagon; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0009651; P:response to salt stress; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009414; P:response to water deprivation; IEP:RGD.
DR GO; GO:0030104; P:water homeostasis; TAS:RGD.
DR GO; GO:0006833; P:water transport; IMP: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 1: Evidence at protein 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_0000063940"
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 251..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:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 54
FT /note="I -> T (in Ref. 4; AAI28706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 28931 MW; 86722ED2BCE0B3E4 CRC64;
MWELRSIAFS RAVLAEFLAT LLFVFFGLGS ALQWASSPPS VLQIAVAFGL GIGILVQALG
HVSGAHINPA VTVACLVGCH VSFLRAAFYV AAQLLGAVAG AAILHEITPV EIRGDLAVNA
LHNNATAGQA VTVELFLTMQ LVLCIFASTD ERRGDNLGSP ALSIGFSVTL GHLLGIYFTG
CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAIIGSLLYN YLLFPSAKSL QERLAVLKGL
EPDTDWEERE VRRRQSVELH SPQSLPRGSK A
