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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_MOUSE              Reviewed;         271 AA.
P56402; Q8VCG5; Q9R232;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
12-SEP-2018, entry version 146.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, TISSUE
SPECIFICITY, AND CHARACTERISTICS OF AN ANIMAL MODEL OF ANDI.
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=10191086; DOI=10.1006/geno.1999.5759;
Yang B., Ma T., Xu Z., Verkman A.S.;
"cDNA and genomic cloning of mouse aquaporin-2: functional analysis of
an orthologous mutant causing nephrogenic diabetes insipidus.";
Genomics 57:79-83(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=12426236; DOI=10.1152/ajprenal.00224.2001;
Zharkikh L., Zhu X., Stricklett P.K., Kohan D.E., Chipman G.,
Breton S., Brown D., Nelson R.D.;
"Renal principal cell-specific expression of green fluorescent protein
in transgenic mice.";
Am. J. Physiol. 283:F1351-F1364(2002).
[3]
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000250}. Basolateral cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Golgi apparatus, trans-Golgi network
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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 (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in kidney. Expressed in a radial
pattern from the cortex through the outer medulla into the inner
medulla. Higher levels in the inner medulla. Located in tubules
suggestive of collecting ducts. {ECO:0000269|PubMed:10191086,
ECO:0000269|PubMed:12426236}.
-!- INDUCTION: Increased levels on water deprivation.
{ECO:0000269|PubMed:10191086}.
-!- 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}.
-!- MISCELLANEOUS: In an animal model of nephrogenic diabetes
insipidis autosomal (ANDI-AQP2-T126M), AQP2 is fully functional
but is retained in the endoplasmic reticulum (ER).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF020519; AAB71414.1; -; mRNA.
EMBL; AF105336; AAD21017.1; -; Genomic_DNA.
EMBL; AY055468; AAL15462.1; -; Genomic_DNA.
EMBL; BC019966; AAH19966.1; -; mRNA.
CCDS; CCDS27822.1; -.
RefSeq; NP_033829.3; NM_009699.3.
UniGene; Mm.20206; -.
ProteinModelPortal; P56402; -.
SMR; P56402; -.
BioGrid; 198171; 3.
DIP; DIP-58509N; -.
IntAct; P56402; 2.
STRING; 10090.ENSMUSP00000023752; -.
iPTMnet; P56402; -.
PhosphoSitePlus; P56402; -.
PaxDb; P56402; -.
PRIDE; P56402; -.
Ensembl; ENSMUST00000023752; ENSMUSP00000023752; ENSMUSG00000023013.
GeneID; 11827; -.
KEGG; mmu:11827; -.
UCSC; uc007xps.2; mouse.
CTD; 359; -.
MGI; MGI:1096865; Aqp2.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P56402; -.
KO; K09865; -.
OMA; LLGIHYT; -.
OrthoDB; EOG091G166T; -.
PhylomeDB; P56402; -.
TreeFam; TF312940; -.
Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-MMU-432047; Passive transport by Aquaporins.
ChiTaRS; Aqp2; mouse.
PRO; PR:P56402; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023013; Expressed in 32 organ(s), highest expression level in cortex of kidney.
CleanEx; MM_AQP2; -.
ExpressionAtlas; P56402; baseline and differential.
Genevisible; P56402; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031303; C:integral component of endosome membrane; IC:MGI.
GO; GO:0016021; C:integral component of membrane; ISM:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0055038; C:recycling endosome membrane; IC:MGI.
GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0030133; C:transport vesicle; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0015168; F:glycerol transmembrane transporter activity; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0015250; F:water channel activity; IDA:MGI.
GO; GO:0005372; F:water transmembrane transporter activity; ISO:MGI.
GO; GO:0030042; P:actin filament depolymerization; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0006884; P:cell volume homeostasis; ISO:MGI.
GO; GO:0071280; P:cellular response to copper ion; ISO:MGI.
GO; GO:0071288; P:cellular response to mercury ion; ISO:MGI.
GO; GO:0042631; P:cellular response to water deprivation; IDA:MGI.
GO; GO:0015793; P:glycerol transport; ISO:MGI.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0072205; P:metanephric collecting duct development; IEP:UniProtKB.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
GO; GO:0003097; P:renal water transport; IMP:MGI.
GO; GO:0006833; P:water transport; IDA:MGI.
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_0000063936.
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:21183079}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 9 10 FS -> YC (in Ref. 1; AAB71414).
{ECO:0000305}.
CONFLICT 213 213 V -> I (in Ref. 1; AAB71414 and 3;
AAH19966). {ECO:0000305}.
SEQUENCE 271 AA; 28965 MW; 41601C37BFD11CBA CRC64;
MWELRSIAFS RAVLAEFLAT LLFVFFGLGS ALQWASSPPS VLQIAVAFGL GIGTLVQALG
HVSGAHINPA VTVACLVGCH VSFLRAAFYV AAQLLGAVAG AAILHEITPV EIRGDLAVNA
LHNNATAGQA VTVELFLTMQ LVLCIFASTD ERRSDNLGSP ALSIGFSVTL GHLLGIYFTG
CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAVIGSLLYN YLLFPSTKSL QERLAVLKGL
EPDTDWEERE VRRRQSVELH SPQSLPRGSK A


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