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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_HUMAN              Reviewed;         271 AA.
P41181; Q9UD68;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 173.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8140421; DOI=10.1126/science.8140421;
Deen P.M.T., Verdijk M.A.J., Knoers V.V.A.M., Wieringa B.,
Monnens L.A.H., van Os C.H., van Oost B.A.;
"Requirement of human renal water channel aquaporin-2 for vasopressin-
dependent concentration of urine.";
Science 264:92-94(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7522228;
Uchida S., Sasaki S., Fushimi K., Marumo F.;
"Isolation of human aquaporin-CD gene.";
J. Biol. Chem. 269:23451-23455(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ANDI ARG-64; CYS-187 AND
PRO-216.
PubMed=7524315;
van Lieburg A.F., Verdijk M.A.J., Knoers V.V.A.M., van Essen A.J.,
Proesmans W., Mallmann R., Monnens L.A.H., van Oost B.A., van Os C.H.,
Deen P.M.T.;
"Patients with autosomal nephrogenic diabetes insipidus homozygous for
mutations in the aquaporin 2 water-channel gene.";
Am. J. Hum. Genet. 55:648-652(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Kidney;
PubMed=7510718; DOI=10.1172/JCI117079;
Sasaki S., Fushimi K., Saito H., Saito F., Uchida S., Ishibashi K.,
Kuwahara M., Ikeuchi T., Inui K., Nakajima K.;
"Cloning, characterization, and chromosomal mapping of human aquaporin
of collecting duct.";
J. Clin. Invest. 93:1250-1256(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Kidney;
PubMed=11929850; DOI=10.1093/hmg/11.7.779;
Marr N., Bichet D.G., Lonergan M., Arthus M.-F., Jeck N.,
Seyberth H.W., Rosenthal W., van Os C.H., Oksche A., Deen P.M.T.;
"Heteroligomerization of an aquaporin-2 mutant with wild-type
aquaporin-2 and their misrouting to late endosomes/lysosomes explains
dominant nephrogenic diabetes insipidus.";
Hum. Mol. Genet. 11:779-789(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
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).
[7]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-256, AND MUTAGENESIS OF
SER-148; SER-229; SER-231; THR-244 AND SER-256.
PubMed=12194985; DOI=10.1074/jbc.M207525200;
van Balkom B.W.M., Savelkoul P.J.M., Markovich D., Hofman E.,
Nielsen S., van der Sluijs P., Deen P.M.T.;
"The role of putative phosphorylation sites in the targeting and
shuttling of the aquaporin-2 water channel.";
J. Biol. Chem. 277:41473-41479(2002).
[8]
VARIANT ANDI CYS-202.
PubMed=8882880; DOI=10.1007/s004390050264;
Oksche A., Moeller A., Dickson J., Rosendahl W., Rascher W.,
Bichet D.G., Rosenthal W.;
"Two novel mutations in the aquaporin-2 and the vasopressin V2
receptor genes in patients with congenital nephrogenic diabetes
insipidus.";
Hum. Genet. 98:587-589(1996).
[9]
VARIANTS ANDI VAL-22 AND TRP-181.
PubMed=9302264; DOI=10.1093/hmg/6.11.1865;
Canfield M.C., Tamarappoo B.K., Moses A.M., Verkman A.S.,
Holtzman E.J.;
"Identification and characterization of aquaporin-2 water channel
mutations causing nephrogenic diabetes insipidus with partial
vasopressin response.";
Hum. Mol. Genet. 6:1865-1871(1997).
[10]
VARIANTS ANDI SER-68; MET-126 AND THR-147.
PubMed=9048343;
Mulders S.M., Knoers N.V., Van Lieburg A.F., Monnens L.A., Leumann E.,
Wuhl E., Schober E., Rijss J.P.L., Van Os C.H., Deen P.M.T.;
"New mutations in the AQP2 gene in nephrogenic diabetes insipidus
resulting in functional but misrouted water channels.";
J. Am. Soc. Nephrol. 8:242-248(1997).
[11]
VARIANTS ANDI MET-168 AND PRO-216.
PubMed=9402087;
Vargas-Poussou R., Forestier L., Dautzenberg M.D., Niaudet P.,
Dechaux M., Antignac C.;
"Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12
families with congenital nephrogenic diabetes insipidus.";
J. Am. Soc. Nephrol. 8:1855-1862(1997).
[12]
VARIANTS ANDI MET-125; ARG-175; THR-190 AND LEU-262.
PubMed=9550615;
Kuwahara M.;
"Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic
diabetes insipidus.";
Intern. Med. 37:215-217(1998).
[13]
VARIANT ANDI LYS-258.
PubMed=9649557; DOI=10.1172/JCI2605;
Mulders S.M., Bichet D.G., Rijss J.P.L., Kamsteeg E.-J., Arthus M.-F.,
Lonergan M., Fujiwara M., Morgan K., Leijendekker R.,
van der Sluijs P., van Os C.H., Deen P.M.T.;
"An aquaporin-2 water channel mutant which causes autosomal dominant
nephrogenic diabetes insipidus is retained in the Golgi complex.";
J. Clin. Invest. 102:57-66(1998).
[14]
VARIANTS ANDI MET-125 AND ARG-175.
PubMed=9745427; DOI=10.1210/jcem.83.9.5074;
Goji K., Kuwahara M., Gu Y., Matsuo M., Marumo F., Sasaki S.;
"Novel mutations in aquaporin-2 gene in female siblings with
nephrogenic diabetes insipidus: evidence of disrupted water channel
function.";
J. Clin. Endocrinol. Metab. 83:3205-3209(1998).
[15]
VARIANTS ANDI PRO-28; VAL-47; MET-71; MET-125; ARG-175 AND ALA-185,
AND VARIANT ILE-194.
PubMed=12191971; DOI=10.1097/01.ASN.0000027355.41663.14;
Marr N., Bichet D.G., Hoefs S., Savelkoul P.J.M., Konings I.B.,
De Mattia F., Graat M.P., Arthus M.-F., Lonergan M., Fujiwara T.M.,
Knoers N.V., Landau D., Balfe W.J., Oksche A., Rosenthal W.,
Muller D., Van Os C.H., Deen P.M.;
"Cell-biologic and functional analyses of five new Aquaporin-2
missense mutations that cause recessive nephrogenic diabetes
insipidus.";
J. Am. Soc. Nephrol. 13:2267-2277(2002).
[16]
VARIANTS ANDI PRO-57 AND VAL-100.
PubMed=12050236; DOI=10.1210/jcem.87.6.8617;
Lin S.H., Bichet D.G., Sasaki S., Kuwahara M., Arthus M.-F.,
Lonergan M., Lin Y.-F.;
"Two novel aquaporin-2 mutations responsible for congenital
nephrogenic diabetes insipidus in Chinese families.";
J. Clin. Endocrinol. Metab. 87:2694-2700(2002).
[17]
VARIANTS ANDI CYS-187; THR-190 AND LEU-262, AND CHARACTERIZATION OF
VARIANTS ANDI CYS-187; THR-190 AND LEU-262.
PubMed=15509592; DOI=10.1093/hmg/ddh339;
de Mattia F., Savelkoul P.J.M., Bichet D.G., Kamsteeg E.-J.,
Konings I.B.M., Marr N., Arthus M.-F., Lonergan M., van Os C.H.,
van der Sluijs P., Robertson G., Deen P.M.T.;
"A novel mechanism in recessive nephrogenic diabetes insipidus: wild-
type aquaporin-2 rescues the apical membrane expression of
intracellularly retained AQP2-P262L.";
Hum. Mol. Genet. 13:3045-3056(2004).
[18]
VARIANT ANDI LEU-254, AND CHARACTERIZATION OF VARIANT ANDI LEU-254.
PubMed=16120822; DOI=10.1681/ASN.2005010104;
de Mattia F., Savelkoul P.J.M., Kamsteeg E.-J., Konings I.B.M.,
van der Sluijs P., Mallmann R., Oksche A., Deen P.M.T.;
"Lack of arginine vasopressin-induced phosphorylation of aquaporin-2
mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus.";
J. Am. Soc. Nephrol. 16:2872-2880(2005).
[19]
VARIANTS ANDI ASP-70 AND HIS-187.
PubMed=16361827; DOI=10.3346/jkms.2005.20.6.1076;
Cheong H.I., Cho S.J., Zheng S.H., Cho H.Y., Ha I.S., Choi Y.;
"Two novel mutations in the aquaporin 2 gene in a girl with congenital
nephrogenic diabetes insipidus.";
J. Korean Med. Sci. 20:1076-1078(2005).
[20]
VARIANTS ANDI ARG-100 AND SER-180.
PubMed=16845277; DOI=10.1097/01.gim.0000223554.46981.7a;
Carroll P., Al-Mojalli H., Al-Abbad A., Al-Hassoun I., Al-Hamed M.,
Al-Amr R., Butt A.I., Meyer B.F.;
"Novel mutations underlying nephrogenic diabetes insipidus in Arab
families.";
Genet. Med. 8:443-447(2006).
[21]
INVOLVEMENT IN ANDI, VARIANT ANDI GLN-254, AND CHARACTERIZATION OF
VARIANT ANDI GLN-254.
PubMed=19585583; DOI=10.1002/humu.21082;
Savelkoul P.J.M., De Mattia F., Li Y., Kamsteeg E.-J., Konings I.B.M.,
van der Sluijs P., Deen P.M.T.;
"p.R254Q mutation in the aquaporin-2 water channel causing dominant
nephrogenic diabetes insipidus is due to a lack of arginine
vasopressin-induced phosphorylation.";
Hum. Mutat. 30:E891-E903(2009).
[22]
MISSORTING MOTIF OF VARIANT ANDI LYS-258.
PubMed=19701945; DOI=10.1002/humu.21068;
Kamsteeg E.-J., Stoffels M., Tamma G., Konings I.B.M., Deen P.M.T.;
"Repulsion between Lys258 and upstream arginines explains the
missorting of the AQP2 mutant p.Glu258Lys in nephrogenic diabetes
insipidus.";
Hum. Mutat. 30:1387-1396(2009).
[23]
VARIANT ANDI MET-108.
PubMed=24944815; DOI=10.3892/br.2014.283;
Park Y.J., Baik H.W., Cheong H.I., Kang J.H.;
"Congenital nephrogenic diabetes insipidus with a novel mutation in
the aquaporin 2 gene.";
Biomed. Rep. 2:596-598(2014).
-!- 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.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-12701138, EBI-625022;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:12194985}; Multi-pass membrane protein
{ECO:0000269|PubMed:12194985}. Basolateral cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12194985}; Multi-
pass membrane protein {ECO:0000269|PubMed:12194985}. Golgi
apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:12194985}; Multi-pass membrane protein
{ECO:0000269|PubMed:12194985}. 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. {ECO:0000269|PubMed:12194985}.
-!- DISEASE: Diabetes insipidus, nephrogenic, autosomal (ANDI)
[MIM:125800]: A disorder caused by the inability of the renal
collecting ducts to absorb water in response to arginine
vasopressin. Characterized by excessive water drinking
(polydipsia), excessive urine excretion (polyuria), persistent
hypotonic urine, and hypokalemia. Inheritance can be autosomal
dominant or recessive. {ECO:0000269|PubMed:12050236,
ECO:0000269|PubMed:12191971, ECO:0000269|PubMed:15509592,
ECO:0000269|PubMed:16120822, ECO:0000269|PubMed:16361827,
ECO:0000269|PubMed:16845277, ECO:0000269|PubMed:19585583,
ECO:0000269|PubMed:19701945, ECO:0000269|PubMed:24944815,
ECO:0000269|PubMed:7524315, ECO:0000269|PubMed:8882880,
ECO:0000269|PubMed:9048343, ECO:0000269|PubMed:9302264,
ECO:0000269|PubMed:9402087, ECO:0000269|PubMed:9550615,
ECO:0000269|PubMed:9649557, ECO:0000269|PubMed:9745427}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
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EMBL; Z29491; CAA82627.1; -; Genomic_DNA.
EMBL; D31846; BAA06632.1; -; Genomic_DNA.
EMBL; S73196; AAB31999.1; -; mRNA.
EMBL; S73197; AAB31998.1; -; mRNA.
EMBL; AF147093; AAD38692.1; -; Genomic_DNA.
EMBL; AF147092; AAD38692.1; JOINED; Genomic_DNA.
EMBL; BC042496; AAH42496.1; -; mRNA.
CCDS; CCDS8792.1; -.
PIR; A53442; A53442.
PIR; I64818; I64818.
RefSeq; NP_000477.1; NM_000486.5.
UniGene; Hs.130730; -.
PDB; 4NEF; X-ray; 2.75 A; A/B/C/D=3-241.
PDB; 4OJ2; X-ray; 3.05 A; X=1-271.
PDBsum; 4NEF; -.
PDBsum; 4OJ2; -.
ProteinModelPortal; P41181; -.
SMR; P41181; -.
BioGrid; 106855; 1.
IntAct; P41181; 3.
STRING; 9606.ENSP00000199280; -.
TCDB; 1.A.8.8.8; the major intrinsic protein (mip) family.
iPTMnet; P41181; -.
PhosphoSitePlus; P41181; -.
BioMuta; AQP2; -.
DMDM; 728874; -.
PaxDb; P41181; -.
PeptideAtlas; P41181; -.
PRIDE; P41181; -.
DNASU; 359; -.
Ensembl; ENST00000199280; ENSP00000199280; ENSG00000167580.
GeneID; 359; -.
KEGG; hsa:359; -.
UCSC; uc001rvn.4; human.
CTD; 359; -.
DisGeNET; 359; -.
EuPathDB; HostDB:ENSG00000167580.7; -.
GeneCards; AQP2; -.
GeneReviews; AQP2; -.
HGNC; HGNC:634; AQP2.
HPA; HPA046834; -.
MalaCards; AQP2; -.
MIM; 107777; gene.
MIM; 125800; phenotype.
neXtProt; NX_P41181; -.
OpenTargets; ENSG00000167580; -.
Orphanet; 223; Nephrogenic diabetes insipidus.
PharmGKB; PA24920; -.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P41181; -.
KO; K09865; -.
OMA; LLGIHYT; -.
OrthoDB; EOG091G166T; -.
PhylomeDB; P41181; -.
TreeFam; TF312940; -.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-432047; Passive transport by Aquaporins.
GeneWiki; Aquaporin_2; -.
GenomeRNAi; 359; -.
PRO; PR:P41181; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167580; -.
CleanEx; HS_AQP2; -.
ExpressionAtlas; P41181; baseline and differential.
Genevisible; P41181; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015250; F:water channel activity; EXP:Reactome.
GO; GO:0005372; F:water transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB.
GO; GO:0042631; P:cellular response to water deprivation; IEA:Ensembl.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0015793; P:glycerol transport; IDA:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0003097; P:renal water transport; IEA:Ensembl.
GO; GO:0006833; P:water transport; IDA: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;
3D-structure; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Diabetes insipidus; Disease mutation; Glycoprotein; Golgi apparatus;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 271 Aquaporin-2.
/FTId=PRO_0000063934.
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; by PKA.
{ECO:0000269|PubMed:12194985}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 22 22 L -> V (in ANDI; dbSNP:rs104894336).
{ECO:0000269|PubMed:9302264}.
/FTId=VAR_015239.
VARIANT 28 28 L -> P (in ANDI).
{ECO:0000269|PubMed:12191971}.
/FTId=VAR_015240.
VARIANT 47 47 A -> V (in ANDI).
{ECO:0000269|PubMed:12191971}.
/FTId=VAR_015241.
VARIANT 57 57 Q -> P (in ANDI; dbSNP:rs28931580).
{ECO:0000269|PubMed:12050236}.
/FTId=VAR_015256.
VARIANT 64 64 G -> R (in ANDI; dbSNP:rs104894326).
{ECO:0000269|PubMed:7524315}.
/FTId=VAR_004401.
VARIANT 68 68 N -> S (in ANDI; dbSNP:rs104894331).
{ECO:0000269|PubMed:9048343}.
/FTId=VAR_015242.
VARIANT 70 70 A -> D (in ANDI).
{ECO:0000269|PubMed:16361827}.
/FTId=VAR_062585.
VARIANT 71 71 V -> M (in ANDI; dbSNP:rs149659001).
{ECO:0000269|PubMed:12191971}.
/FTId=VAR_015243.
VARIANT 100 100 G -> R (in ANDI).
{ECO:0000269|PubMed:16845277}.
/FTId=VAR_062586.
VARIANT 100 100 G -> V (in ANDI; dbSNP:rs104894338).
{ECO:0000269|PubMed:12050236}.
/FTId=VAR_015257.
VARIANT 108 108 T -> M (in ANDI).
{ECO:0000269|PubMed:24944815}.
/FTId=VAR_071370.
VARIANT 121 121 L -> F (in dbSNP:rs11169226).
/FTId=VAR_037577.
VARIANT 125 125 T -> M (in ANDI; dbSNP:rs104894333).
{ECO:0000269|PubMed:12191971,
ECO:0000269|PubMed:9550615,
ECO:0000269|PubMed:9745427}.
/FTId=VAR_015244.
VARIANT 126 126 T -> M (in ANDI; dbSNP:rs104894330).
{ECO:0000269|PubMed:9048343}.
/FTId=VAR_015245.
VARIANT 147 147 A -> T (in ANDI; dbSNP:rs104894334).
{ECO:0000269|PubMed:9048343}.
/FTId=VAR_015246.
VARIANT 168 168 V -> M (in ANDI; dbSNP:rs755694590).
{ECO:0000269|PubMed:9402087}.
/FTId=VAR_015247.
VARIANT 175 175 G -> R (in ANDI; dbSNP:rs104894335).
{ECO:0000269|PubMed:12191971,
ECO:0000269|PubMed:9550615,
ECO:0000269|PubMed:9745427}.
/FTId=VAR_015248.
VARIANT 180 180 G -> S (in ANDI; dbSNP:rs147039983).
{ECO:0000269|PubMed:16845277}.
/FTId=VAR_062587.
VARIANT 181 181 C -> W (in ANDI; dbSNP:rs104894337).
{ECO:0000269|PubMed:9302264}.
/FTId=VAR_015249.
VARIANT 185 185 P -> A (in ANDI; dbSNP:rs761713751).
{ECO:0000269|PubMed:12191971}.
/FTId=VAR_015250.
VARIANT 187 187 R -> C (in ANDI; mutant protein does not
fold properly and is not functional;
dbSNP:rs104894328).
{ECO:0000269|PubMed:15509592,
ECO:0000269|PubMed:7524315}.
/FTId=VAR_004402.
VARIANT 187 187 R -> H (in ANDI; dbSNP:rs193922495).
{ECO:0000269|PubMed:16361827}.
/FTId=VAR_062588.
VARIANT 190 190 A -> T (in ANDI; mutant protein does not
fold properly and is not functional;
dbSNP:rs104894341).
{ECO:0000269|PubMed:15509592,
ECO:0000269|PubMed:9550615}.
/FTId=VAR_015251.
VARIANT 194 194 V -> I (in dbSNP:rs772051028).
{ECO:0000269|PubMed:12191971}.
/FTId=VAR_015252.
VARIANT 202 202 W -> C (in ANDI).
{ECO:0000269|PubMed:8882880}.
/FTId=VAR_015253.
VARIANT 216 216 S -> P (in ANDI; dbSNP:rs104894329).
{ECO:0000269|PubMed:7524315,
ECO:0000269|PubMed:9402087}.
/FTId=VAR_004403.
VARIANT 254 254 R -> L (in ANDI; results in the loss of
arginine vasopressin-mediated
phosphorylation at S-256).
{ECO:0000269|PubMed:16120822}.
/FTId=VAR_062589.
VARIANT 254 254 R -> Q (in ANDI; exerts a dominant-
negative effect on wild-type-AQP2 in that
it interferes with its trafficking to the
apical membrane; is a loss of function
instead of a gain of function mutation on
dominant nephrogenic diabetes insipidus).
{ECO:0000269|PubMed:19585583}.
/FTId=VAR_062590.
VARIANT 258 258 E -> K (in ANDI; retained in the Golgi
compartment; dbSNP:rs104894332).
{ECO:0000269|PubMed:19701945,
ECO:0000269|PubMed:9649557}.
/FTId=VAR_015254.
VARIANT 262 262 P -> L (in ANDI; mutant protein folds
properly and is functional but is
retained in intracellular vesicles and
does not localize to the ER; upon
coexpression with wild-type AQP2 mutant
protein interacts with wild-type AQP2 and
the resulting heterotetramer properly
localizes to the apical membrane;
dbSNP:rs104894339).
{ECO:0000269|PubMed:15509592,
ECO:0000269|PubMed:9550615}.
/FTId=VAR_015255.
MUTAGEN 148 148 S->A: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 148 148 S->D: Retained in the endoplasmic
reticulum. {ECO:0000269|PubMed:12194985}.
MUTAGEN 229 229 S->A: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 229 229 S->D: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 231 231 S->A: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 231 231 S->D: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 244 244 T->A: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 244 244 T->E: No effect on sorting from the ER to
the vesicles, redistribution to apical
membrane, or endocytosis.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 256 256 S->A: Retained in vesicles.
{ECO:0000269|PubMed:12194985}.
MUTAGEN 256 256 S->D: Expressed in the apical membrane.
{ECO:0000269|PubMed:12194985}.
CONFLICT 35 38 PQAL -> ATAP (in Ref. 4). {ECO:0000305}.
CONFLICT 83 83 V -> F (in Ref. 4). {ECO:0000305}.
HELIX 7 32 {ECO:0000244|PDB:4NEF}.
STRAND 35 37 {ECO:0000244|PDB:4NEF}.
HELIX 41 63 {ECO:0000244|PDB:4NEF}.
HELIX 69 77 {ECO:0000244|PDB:4NEF}.
HELIX 83 107 {ECO:0000244|PDB:4NEF}.
HELIX 110 113 {ECO:0000244|PDB:4NEF}.
HELIX 127 148 {ECO:0000244|PDB:4NEF}.
HELIX 159 179 {ECO:0000244|PDB:4NEF}.
HELIX 185 195 {ECO:0000244|PDB:4NEF}.
TURN 199 202 {ECO:0000244|PDB:4NEF}.
HELIX 203 221 {ECO:0000244|PDB:4NEF}.
HELIX 232 237 {ECO:0000244|PDB:4NEF}.
SEQUENCE 271 AA; 28837 MW; C2DDE2AF4DDD192A CRC64;
MWELRSIAFS RAVFAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL GIGTLVQALG
HISGAHINPA VTVACLVGCH VSVLRAAFYV AAQLLGAVAG AALLHEITPA DIRGDLAVNA
LSNSTTAGQA VTVELFLTLQ LVLCIFASTD ERRGENPGTP ALSIGFSVAL GHLLGIHYTG
CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAILGSLLYN YVLFPPAKSL SERLAVLKGL
EPDTDWEERE VRRRQSVELH SPQSLPRGTK A


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