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Aquaporin-2 (AQP-2) (ADH water channel) (Aquaporin-CD) (AQP-CD) (Collecting duct water channel protein) (WCH-CD) (Water channel protein for renal collecting duct)

 AQP2_RAT                Reviewed;         271 AA.
P34080; A1A5L4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Aquaporin-2;
Short=AQP-2;
AltName: Full=ADH water channel;
AltName: Full=Aquaporin-CD;
Short=AQP-CD;
AltName: Full=Collecting duct water channel protein;
AltName: Full=WCH-CD;
AltName: Full=Water channel protein for renal collecting duct;
Name=Aqp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=8429910; DOI=10.1038/361549a0;
Fushimi K., Uchida S., Hara Y., Hirata Y., Marumo F., Sasaki S.;
"Cloning and expression of apical membrane water channel of rat kidney
collecting tubule.";
Nature 361:549-552(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=7505572; DOI=10.1006/bbrc.1993.2529;
Ma T., Frigeri A., Skach W., Verkman A.S.;
"Cloning of a novel rat kidney cDNA homologous to CHIP28 and WCH-CD
water channels.";
Biochem. Biophys. Res. Commun. 197:654-659(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=7508187;
Ma T., Hasegawa H., Skach W., Frigeri A., Verkman A.S.;
"Expression, functional analysis, and in situ hybridization of a
cloned rat kidney collecting duct water channel.";
Am. J. Physiol. 266:C189-C197(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-261; SER-264
AND SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[6]
SUBCELLULAR LOCATION.
PubMed=19794145; DOI=10.1152/ajpcell.00098.2009;
Yui N., Okutsu R., Sohara E., Rai T., Ohta A., Noda Y., Sasaki S.,
Uchida S.;
"FAPP2 is required for aquaporin-2 apical sorting at trans-Golgi
network in polarized MDCK cells.";
Am. J. Physiol. 297:C1389-C1396(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Forms a water-specific channel that provides the plasma
membranes of renal collecting duct with high permeability to
water, thereby permitting water to move in the direction of an
osmotic gradient.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:19794145}; Multi-pass membrane protein
{ECO:0000269|PubMed:19794145}. Basolateral cell membrane
{ECO:0000269|PubMed:19794145}; Multi-pass membrane protein
{ECO:0000269|PubMed:19794145}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:19794145}; Multi-pass membrane protein
{ECO:0000269|PubMed:19794145}. Golgi apparatus, trans-Golgi
network membrane {ECO:0000269|PubMed:19794145}; Multi-pass
membrane protein {ECO:0000269|PubMed:19794145}. Note=Shuttles from
vesicles to the apical membrane. Vasopressin-regulated
phosphorylation is required for translocation to the apical cell
membrane. PLEKHA8/FAPP2 is required to transport AQP2 from the TGN
to sites where AQP2 is phosphorylated.
-!- TISSUE SPECIFICITY: Expressed in renal collecting tubules.
-!- 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).
-!- PTM: Ser-256 phosphorylation is necessary and sufficient for
expression at the apical membrane. Endocytosis is not
phosphorylation-dependent (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA41478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D13906; BAA03006.1; -; mRNA.
EMBL; L28112; AAA41478.1; ALT_INIT; mRNA.
EMBL; BC128705; AAI28706.1; -; mRNA.
PIR; JT0750; JT0750.
RefSeq; NP_037041.2; NM_012909.2.
UniGene; Rn.90076; -.
ProteinModelPortal; P34080; -.
CORUM; P34080; -.
DIP; DIP-46223N; -.
IntAct; P34080; 4.
STRING; 10116.ENSRNOP00000000324; -.
iPTMnet; P34080; -.
PhosphoSitePlus; P34080; -.
PaxDb; P34080; -.
GeneID; 25386; -.
KEGG; rno:25386; -.
UCSC; RGD:2142; rat.
CTD; 359; -.
RGD; 2142; Aqp2.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P34080; -.
KO; K09865; -.
PhylomeDB; P34080; -.
TreeFam; TF312940; -.
PRO; PR:P34080; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IDA:RGD.
GO; GO:0070382; C:exocytic vesicle; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0055037; C:recycling endosome; ISO:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
GO; GO:0030133; C:transport vesicle; IDA:RGD.
GO; GO:0003779; F:actin binding; IDA:RGD.
GO; GO:0015168; F:glycerol transmembrane transporter activity; ISO:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0015250; F:water channel activity; ISO:RGD.
GO; GO:0005372; F:water transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0030042; P:actin filament depolymerization; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0006884; P:cell volume homeostasis; IMP:RGD.
GO; GO:0071280; P:cellular response to copper ion; ISO:RGD.
GO; GO:0071288; P:cellular response to mercury ion; ISO:RGD.
GO; GO:0042631; P:cellular response to water deprivation; IDA:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0015793; P:glycerol transport; ISO:RGD.
GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0072205; P:metanephric collecting duct development; ISO:RGD.
GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
GO; GO:0003097; P:renal water transport; ISO:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0033762; P:response to glucagon; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0042594; P:response to starvation; IEP:RGD.
GO; GO:0009414; P:response to water deprivation; IEP:RGD.
GO; GO:0030104; P:water homeostasis; TAS:RGD.
GO; GO:0006833; P:water transport; IMP:UniProtKB.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Glycoprotein;
Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 271 Aquaporin-2.
/FTId=PRO_0000063940.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 34 Helical. {ECO:0000255}.
TOPO_DOM 35 40 Extracellular. {ECO:0000255}.
TRANSMEM 41 59 Helical. {ECO:0000255}.
TOPO_DOM 60 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 107 Helical. {ECO:0000255}.
TOPO_DOM 108 127 Extracellular. {ECO:0000255}.
TRANSMEM 128 148 Helical. {ECO:0000255}.
TOPO_DOM 149 156 Cytoplasmic. {ECO:0000255}.
TRANSMEM 157 176 Helical. {ECO:0000255}.
TOPO_DOM 177 202 Extracellular. {ECO:0000255}.
TRANSMEM 203 224 Helical. {ECO:0000255}.
TOPO_DOM 225 271 Cytoplasmic. {ECO:0000255}.
MOTIF 68 70 NPA 1.
MOTIF 184 186 NPA 2.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 54 54 I -> T (in Ref. 4; AAI28706).
{ECO:0000305}.
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


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