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P56402 (AQP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Apical cell membrane; Multi-pass membrane protein By similarity. Basolateral cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein By similarity. Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein By similarity. 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.

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. Ref.1 Ref.2

Induction

Increased levels on water deprivation. Ref.1

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 By similarity.

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).

Sequence similarities

Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Cytoplasmic vesicle
Golgi apparatus
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament depolymerization

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell volume homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to copper ion

Inferred from electronic annotation. Source: Ensembl

cellular response to mercury ion

Inferred from electronic annotation. Source: Ensembl

cellular response to water deprivation

Inferred from direct assay Ref.1. Source: MGI

female pregnancy

Inferred from electronic annotation. Source: Ensembl

hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

metanephric collecting duct development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

positive regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

renal water transport

Inferred from mutant phenotype PubMed 3184310. Source: MGI

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to lithium ion

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

water transport

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin-coated vesicle

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from direct assay PubMed 18505797. Source: MGI

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome

Inferred from electronic annotation. Source: Ensembl

exocytic vesicle

Inferred from electronic annotation. Source: Ensembl

integral component of endosome membrane

Inferred by curator Ref.1. Source: MGI

integral component of membrane

Inferred from sequence model Ref.1. Source: MGI

integral component of plasma membrane

Inferred by curator Ref.1. Source: MGI

lysosome

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 15632412. Source: MGI

plasma membrane

Inferred from direct assay Ref.1. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

recycling endosome

Inferred from direct assay Ref.1. Source: MGI

recycling endosome membrane

Inferred by curator Ref.1. Source: MGI

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionglycerol transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

water channel activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Aquaporin-2
PRO_0000063936

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3418Helical; Potential
Topological domain35 – 406Extracellular Potential
Transmembrane41 – 5919Helical; Potential
Topological domain60 – 8526Cytoplasmic Potential
Transmembrane86 – 10722Helical; Potential
Topological domain108 – 12720Extracellular Potential
Transmembrane128 – 14821Helical; Potential
Topological domain149 – 1568Cytoplasmic Potential
Transmembrane157 – 17620Helical; Potential
Topological domain177 – 20226Extracellular Potential
Transmembrane203 – 22422Helical; Potential
Topological domain225 – 27147Cytoplasmic Potential
Motif68 – 703NPA 1
Motif184 – 1863NPA 2

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict9 – 102FS → YC in AAB71414. Ref.1
Sequence conflict2131V → I in AAB71414. Ref.1
Sequence conflict2131V → I in AAH19966. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P56402 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 41601C37BFD11CBA

FASTA27128,965
        10         20         30         40         50         60 
MWELRSIAFS RAVLAEFLAT LLFVFFGLGS ALQWASSPPS VLQIAVAFGL GIGTLVQALG 

        70         80         90        100        110        120 
HVSGAHINPA VTVACLVGCH VSFLRAAFYV AAQLLGAVAG AAILHEITPV EIRGDLAVNA 

       130        140        150        160        170        180 
LHNNATAGQA VTVELFLTMQ LVLCIFASTD ERRSDNLGSP ALSIGFSVTL GHLLGIYFTG 

       190        200        210        220        230        240 
CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAVIGSLLYN YLLFPSTKSL QERLAVLKGL 

       250        260        270 
EPDTDWEERE VRRRQSVELH SPQSLPRGSK A 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and genomic cloning of mouse aquaporin-2: functional analysis of an orthologous mutant causing nephrogenic diabetes insipidus."
Yang B., Ma T., Xu Z., Verkman A.S.
Genomics 57:79-83(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, TISSUE SPECIFICITY, CHARACTERISTICS OF AN ANIMAL MODEL OF ANDI.
Strain: C57BL/6J.
Tissue: Kidney.
[2]"Renal principal cell-specific expression of green fluorescent protein in transgenic mice."
Zharkikh L., Zhu X., Stricklett P.K., Kohan D.E., Chipman G., Breton S., Brown D., Nelson R.D.
Am. J. Physiol. 283:F1351-F1364(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/SvJ.
[3]"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: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF020519 mRNA. Translation: AAB71414.1.
AF105336 Genomic DNA. Translation: AAD21017.1.
AY055468 Genomic DNA. Translation: AAL15462.1.
BC019966 mRNA. Translation: AAH19966.1.
RefSeqNP_033829.3. NM_009699.3.
UniGeneMm.20206.

3D structure databases

ProteinModelPortalP56402.
SMRP56402. Positions 3-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198171. 2 interactions.
DIPDIP-58509N.

PTM databases

PhosphoSiteP56402.

Proteomic databases

PaxDbP56402.
PRIDEP56402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023752; ENSMUSP00000023752; ENSMUSG00000023013.
GeneID11827.
KEGGmmu:11827.
UCSCuc007xps.2. mouse.

Organism-specific databases

CTD359.
MGIMGI:1096865. Aqp2.

Phylogenomic databases

eggNOGCOG0580.
HOGENOMHOG000288286.
HOVERGENHBG000312.
InParanoidP56402.
KOK09865.
OMAPEGFQTR.
OrthoDBEOG7N8ZWD.
PhylomeDBP56402.
TreeFamTF312940.

Gene expression databases

BgeeP56402.
CleanExMM_AQP2.
GenevestigatorP56402.

Family and domain databases

Gene3D1.20.1080.10. 1 hit.
InterProIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERPTHR19139. PTHR19139. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR00783. MINTRINSICP.
SUPFAMSSF81338. SSF81338. 1 hit.
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAQP2. mouse.
NextBio279731.
PROP56402.
SOURCESearch...

Entry information

Entry nameAQP2_MOUSE
AccessionPrimary (citable) accession number: P56402
Secondary accession number(s): Q8VCG5, Q9R232
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 19, 2002
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot