P41181 (AQP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aquaporin-2
Short name=AQP-2

Alternative name(s):
ADH water channel
Aquaporin-CD
Short name=AQP-CD
Collecting duct water channel protein
WCH-CD
Water channel protein for renal collecting duct

Gene names

Name:

AQP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein. 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. Ref.7
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).
Post-translational modification	Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent.
Involvement in 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 (polydypsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Sequence similarities	Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell membrane Cytoplasmic vesicle Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Diabetes insipidus Disease mutation
Domain	Repeat Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament depolymerization Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara cell volume homeostasis Inferred from electronic annotation. Source: Compara cellular response to copper ion Inferred from direct assay PubMed 8584435. Source: UniProtKB cellular response to mercury ion Inferred from direct assay PubMed 8584435. Source: UniProtKB cellular response to water deprivation Inferred from electronic annotation. Source: Compara excretion Traceable author statement PubMed 7532304. Source: ProtInc female pregnancy Inferred from electronic annotation. Source: Compara hyperosmotic response Inferred from electronic annotation. Source: Compara metanephric collecting duct development Inferred from electronic annotation. Source: Compara positive regulation of calcium ion transport Inferred from electronic annotation. Source: Compara renal water transport Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from electronic annotation. Source: Compara response to glucagon stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to lithium ion Inferred from electronic annotation. Source: Compara response to salt stress Inferred from electronic annotation. Source: Compara response to starvation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell apical plasma membrane Inferred from direct assay PubMed 16928804. Source: UniProtKB basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell clathrin-coated vesicle Inferred from electronic annotation. Source: Compara early endosome Inferred from electronic annotation. Source: Compara exocytic vesicle Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosome Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara recycling endosome Inferred from electronic annotation. Source: Compara rough endoplasmic reticulum Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from electronic annotation. Source: Compara transport vesicle membrane Traceable author statement. Source: Reactome
Molecular_function	glycerol transmembrane transporter activity Inferred from direct assay PubMed 8584435. Source: UniProtKB water channel activity Inferred from experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 271	271	Aquaporin-2		PRO_0000063934
Regions
	Topological domain	1 – 16	16	Cytoplasmic Potential
	Transmembrane	17 – 34	18	Helical; Potential
	Topological domain	35 – 40	6	Extracellular Potential
	Transmembrane	41 – 59	19	Helical; Potential
	Topological domain	60 – 85	26	Cytoplasmic Potential
	Transmembrane	86 – 107	22	Helical; Potential
	Topological domain	108 – 127	20	Extracellular Potential
	Transmembrane	128 – 148	21	Helical; Potential
	Topological domain	149 – 156	8	Cytoplasmic Potential
	Transmembrane	157 – 176	20	Helical; Potential
	Topological domain	177 – 202	26	Extracellular Potential
	Transmembrane	203 – 224	22	Helical; Potential
	Topological domain	225 – 271	47	Cytoplasmic Potential
	Motif	68 – 70	3	NPA 1
	Motif	184 – 186	3	NPA 2
Amino acid modifications
	Modified residue	256	1	Phosphoserine; by PKA Ref.7
	Modified residue	261	1	Phosphoserine By similarity
	Modified residue	264	1	Phosphoserine By similarity
	Glycosylation	123	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	22	1	L → V in ANDI. Ref.9		VAR_015239
	Natural variant	28	1	L → P in ANDI. Ref.15		VAR_015240
	Natural variant	47	1	A → V in ANDI. Ref.15		VAR_015241
	Natural variant	57	1	Q → P in ANDI. Ref.16 Corresponds to variant rs28931580 [ dbSNP | Ensembl ].		VAR_015256
	Natural variant	64	1	G → R in ANDI. Ref.3		VAR_004401
	Natural variant	68	1	N → S in ANDI. Ref.10		VAR_015242
	Natural variant	70	1	A → D in ANDI. Ref.19		VAR_062585
	Natural variant	71	1	V → M in ANDI. Ref.15		VAR_015243
	Natural variant	100	1	G → R in ANDI. Ref.20		VAR_062586
	Natural variant	100	1	G → V in ANDI. Ref.16 Corresponds to variant rs28929477 [ dbSNP | Ensembl ].		VAR_015257
	Natural variant	121	1	L → F. Corresponds to variant rs11169226 [ dbSNP | Ensembl ].		VAR_037577
	Natural variant	125	1	T → M in ANDI. Ref.12 Ref.14 Ref.15		VAR_015244
	Natural variant	126	1	T → M in ANDI. Ref.10		VAR_015245
	Natural variant	147	1	A → T in ANDI. Ref.10		VAR_015246
	Natural variant	168	1	V → M in ANDI. Ref.11		VAR_015247
	Natural variant	175	1	G → R in ANDI. Ref.12 Ref.14 Ref.15		VAR_015248
	Natural variant	180	1	G → S in ANDI. Ref.20		VAR_062587
	Natural variant	181	1	C → W in ANDI. Ref.9		VAR_015249
	Natural variant	185	1	P → A in ANDI. Ref.15		VAR_015250
	Natural variant	187	1	R → C in ANDI; mutant protein does not fold properly and is not functional. Ref.3 Ref.17		VAR_004402
	Natural variant	187	1	R → H in ANDI. Ref.19		VAR_062588
	Natural variant	190	1	A → T in ANDI; mutant protein does not fold properly and is not functional. Ref.12 Ref.17		VAR_015251
	Natural variant	194	1	V → I. Ref.15		VAR_015252
	Natural variant	202	1	W → C in ANDI. Ref.8		VAR_015253
	Natural variant	216	1	S → P in ANDI. Ref.3 Ref.11		VAR_004403
	Natural variant	254	1	R → L in ANDI; results in the loss of arginine vasopressin-mediated phosphorylation at S-256. Ref.18		VAR_062589
	Natural variant	254	1	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. Ref.21		VAR_062590
	Natural variant	258	1	E → K in ANDI; retained in the Golgi compartment. Ref.13 Ref.22		VAR_015254
	Natural variant	262	1	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. Ref.12 Ref.17		VAR_015255
Experimental info
	Mutagenesis	148	1	S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	148	1	S → D: Retained in the endoplasmic reticulum. Ref.7
	Mutagenesis	229	1	S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	229	1	S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	231	1	S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	231	1	S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	244	1	T → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	244	1	T → E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
	Mutagenesis	256	1	S → A: Retained in vesicles. Ref.7
	Mutagenesis	256	1	S → D: Expressed in the apical membrane. Ref.7
	Sequence conflict	35 – 38	4	PQAL → ATAP Ref.4
	Sequence conflict	83	1	V → F Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P41181 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C2DDE2AF4DDD192A	FASTA	271	28,837
	10 20 30 40 50 60 MWELRSIAFS RAVFAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL GIGTLVQALG 70 80 90 100 110 120 HISGAHINPA VTVACLVGCH VSVLRAAFYV AAQLLGAVAG AALLHEITPA DIRGDLAVNA 130 140 150 160 170 180 LSNSTTAGQA VTVELFLTLQ LVLCIFASTD ERRGENPGTP ALSIGFSVAL GHLLGIHYTG 190 200 210 220 230 240 CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAILGSLLYN YVLFPPAKSL SERLAVLKGL 250 260 270 EPDTDWEERE VRRRQSVELH SPQSLPRGTK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine." 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. Science 264:92-94(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation of human aquaporin-CD gene." Uchida S., Sasaki S., Fushimi K., Marumo F. J. Biol. Chem. 269:23451-23455(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene." 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. Am. J. Hum. Genet. 55:648-652(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ANDI ARG-64; CYS-187 AND PRO-216.
[4]	"Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct." Sasaki S., Fushimi K., Saito H., Saito F., Uchida S., Ishibashi K., Kuwahara M., Ikeuchi T., Inui K., Nakajima K. J. Clin. Invest. 93:1250-1256(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney.
[5]	"Heteroligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus." 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. Hum. Mol. Genet. 11:779-789(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[7]	"The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel." van Balkom B.W.M., Savelkoul P.J.M., Markovich D., Hofman E., Nielsen S., van der Sluijs P., Deen P.M.T. J. Biol. Chem. 277:41473-41479(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-256, MUTAGENESIS OF SER-148; SER-229; SER-231; THR-244 AND SER-256.
[8]	"Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus." Oksche A., Moeller A., Dickson J., Rosendahl W., Rascher W., Bichet D.G., Rosenthal W. Hum. Genet. 98:587-589(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ANDI CYS-202.
[9]	"Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response." Canfield M.C., Tamarappoo B.K., Moses A.M., Verkman A.S., Holtzman E.J. Hum. Mol. Genet. 6:1865-1871(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI VAL-22 AND TRP-181.
[10]	"New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels." 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. J. Am. Soc. Nephrol. 8:242-248(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI SER-68; MET-126 AND THR-147.
[11]	"Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus." Vargas-Poussou R., Forestier L., Dautzenberg M.D., Niaudet P., Dechaux M., Antignac C. J. Am. Soc. Nephrol. 8:1855-1862(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI MET-168 AND PRO-216.
[12]	"Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus." Kuwahara M. Intern. Med. 37:215-217(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI MET-125; ARG-175; THR-190 AND LEU-262.
[13]	"An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex." 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. J. Clin. Invest. 102:57-66(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ANDI LYS-258.
[14]	"Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function." Goji K., Kuwahara M., Gu Y., Matsuo M., Marumo F., Sasaki S. J. Clin. Endocrinol. Metab. 83:3205-3209(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI MET-125 AND ARG-175.
[15]	"Cell-biologic and functional analyses of five new Aquaporin-2 missense mutations that cause recessive nephrogenic diabetes insipidus." 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. J. Am. Soc. Nephrol. 13:2267-2277(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI PRO-28; VAL-47; MET-71; MET-125; ARG-175 AND ALA-185, VARIANT ILE-194.
[16]	"Two novel aquaporin-2 mutations responsible for congenital nephrogenic diabetes insipidus in Chinese families." Lin S.H., Bichet D.G., Sasaki S., Kuwahara M., Arthus M.-F., Lonergan M., Lin Y.-F. J. Clin. Endocrinol. Metab. 87:2694-2700(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI PRO-57 AND VAL-100.
[17]	"A novel mechanism in recessive nephrogenic diabetes insipidus: wild-type aquaporin-2 rescues the apical membrane expression of intracellularly retained AQP2-P262L." 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. Hum. Mol. Genet. 13:3045-3056(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI CYS-187; THR-190 AND LEU-262, CHARACTERIZATION OF VARIANTS ANDI CYS-187; THR-190 AND LEU-262.
[18]	"Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus." 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. J. Am. Soc. Nephrol. 16:2872-2880(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ANDI LEU-254, CHARACTERIZATION OF VARIANT ANDI LEU-254.
[19]	"Two novel mutations in the aquaporin 2 gene in a girl with congenital nephrogenic diabetes insipidus." Cheong H.I., Cho S.J., Zheng S.H., Cho H.Y., Ha I.S., Choi Y. J. Korean Med. Sci. 20:1076-1078(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI ASP-70 AND HIS-187.
[20]	"Novel mutations underlying nephrogenic diabetes insipidus in Arab families." Carroll P., Al-Mojalli H., Al-Abbad A., Al-Hassoun I., Al-Hamed M., Al-Amr R., Butt A.I., Meyer B.F. Genet. Med. 8:443-447(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANDI ARG-100 AND SER-180.
[21]	"p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation." Savelkoul P.J.M., De Mattia F., Li Y., Kamsteeg E.-J., Konings I.B.M., van der Sluijs P., Deen P.M.T. Hum. Mutat. 30:E891-E903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ANDI GLN-254, CHARACTERIZATION OF VARIANT ANDI GLN-254.
[22]	"Repulsion between Lys258 and upstream arginines explains the missorting of the AQP2 mutant p.Glu258Lys in nephrogenic diabetes insipidus." Kamsteeg E.-J., Stoffels M., Tamma G., Konings I.B.M., Deen P.M.T. Hum. Mutat. 30:1387-1396(2009) [PubMed] [Europe PMC] [Abstract] Cited for: MISSORTING MOTIF OF VARIANT ANDI LYS-258.
+	Additional computationally mapped references.

Web resources

Nephrogenic and neurogenic Diabetes Insipidus

AQP2 pages

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z29491 Genomic DNA. Translation: CAA82627.1. D31846 Genomic DNA. Translation: BAA06632.1. S73196 mRNA. Translation: AAB31999.1. S73197 mRNA. Translation: AAB31998.1. AF147093, AF147092 Genomic DNA. Translation: AAD38692.1. BC042496 mRNA. Translation: AAH42496.1.
IPI	IPI00012818.
PIR	A53442. I64818.
RefSeq	NP_000477.1. NM_000486.5.
UniGene	Hs.130730.
3D structure databases
ProteinModelPortal	P41181.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000199280.
Protein family/group databases
TCDB	1.A.8.8.8. major intrinsic protein (MIP) family.
PTM databases
PhosphoSite	P41181.
Polymorphism databases
DMDM	728874.
Proteomic databases
PaxDb	P41181.
PRIDE	P41181.
Protocols and materials databases
DNASU	359.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000199280; ENSP00000199280; ENSG00000167580.
GeneID	359.
KEGG	hsa:359.
UCSC	uc001rvn.3. human.
Organism-specific databases
CTD	359.
GeneCards	GC12P050400.
HGNC	HGNC:634. AQP2.
HPA	CAB009866.
MIM	107777. gene. 125800. phenotype.
neXtProt	NX_P41181.
Orphanet	223. Nephrogenic diabetes insipidus.
PharmGKB	PA24920.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0580.
HOGENOM	HOG000288286.
HOVERGEN	HBG000312.
InParanoid	P41181.
KO	K09865.
OMA	ADWEERE.
OrthoDB	EOG4FJ89M.
PhylomeDB	P41181.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P41181.
Bgee	P41181.
CleanEx	HS_AQP2.
Genevestigator	P41181.
GermOnline	ENSG00000167580. Homo sapiens.
Family and domain databases
Gene3D	1.20.1080.10. 1 hit.
InterPro	IPR023271. Aquaporin-like. IPR000425. MIP. IPR022357. MIP_CS. [Graphical view]
PANTHER	PTHR19139. PTHR19139. 1 hit.
Pfam	PF00230. MIP. 1 hit. [Graphical view]
PRINTS	PR00783. MINTRINSICP.
SUPFAM	SSF81338. MIP. 1 hit.
TIGRFAMs	TIGR00861. MIP. 1 hit.
PROSITE	PS00221. MIP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	359.
NextBio	1501.
SOURCE	Search...

Entry information

Entry name

AQP2_HUMAN

Accession

Primary (citable) accession number: P41181
Secondary accession number(s): Q9UD68

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.