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Q02013 (AQP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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-1

Short name=AQP-1
Alternative name(s):
Aquaporin-CHIP
Delayed early response protein 2
Short name=DER2
Water channel protein for red blood cells and kidney proximal tubule
Gene names
Name:Aqp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.

Subunit structure

Homotetramer. Identified in a complex with STOM By similarity. Interacts with EPHB2; involved in endolymph production in the inner ear. Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Erythrocytes and renal 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).

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Sequence similarities

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

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processammonium transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

ammonium transport

Inferred from sequence or structural similarity. Source: UniProtKB

cGMP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

camera-type eye morphogenesis

Inferred from mutant phenotype PubMed 11891232. Source: MGI

carbon dioxide transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

carbon dioxide transport

Inferred from sequence or structural similarity. Source: UniProtKB

cell volume homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular hyperosmotic response

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to UV

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to copper ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to dexamethasone stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to inorganic substance

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mercury ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to salt stress

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

corticotropin secretion

Inferred from mutant phenotype PubMed 18511498. Source: MGI

establishment or maintenance of actin cytoskeleton polarity

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular filtration

Inferred from mutant phenotype PubMed 15283758. Source: MGI

glycerol transport

Inferred from sequence or structural similarity. Source: UniProtKB

hyperosmotic salinity response

Inferred from electronic annotation. Source: Ensembl

lateral ventricle development

Inferred from expression pattern PubMed 16133142. Source: UniProtKB

lipid digestion

Inferred from mutant phenotype PubMed 11121384. Source: MGI

maintenance of symbiont-containing vacuole by host

Inferred from mutant phenotype PubMed 18665841. Source: UniProtKB

metanephric descending thin limb development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

metanephric glomerulus vasculature development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

metanephric proximal convoluted tubule segment 2 development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

metanephric proximal straight tubule development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

nitric oxide transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype PubMed 19298815. Source: MGI

positive regulation of epithelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of saliva secretion

Inferred from sequence or structural similarity. Source: UniProtKB

potassium ion transmembrane transport

Inferred from direct assay PubMed 18665841. Source: GOC

potassium ion transport

Inferred from direct assay PubMed 18665841. Source: UniProtKB

renal water absorption

Inferred from mutant phenotype PubMed 10021457PubMed 10662735PubMed 10724035PubMed 10795927PubMed 11035042PubMed 12133842PubMed 16525162PubMed 9468475. Source: MGI

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from electronic annotation. Source: Ensembl

secretion by cell

Inferred from mutant phenotype PubMed 18511498. Source: MGI

secretory granule organization

Inferred from mutant phenotype PubMed 18511498. Source: MGI

sensory perception of pain

Inferred from mutant phenotype PubMed 16476579. Source: MGI

transepithelial water transport

Inferred from sequence or structural similarity. Source: UniProtKB

water homeostasis

Inferred from mutant phenotype PubMed 12034763. Source: MGI

water transport

Inferred from direct assay PubMed 10644730. Source: MGI

wound healing

Inferred from mutant phenotype PubMed 19298815. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 16133142. Source: UniProtKB

axon

Inferred from direct assay PubMed 17257750. Source: MGI

axon terminus

Inferred from electronic annotation. Source: Ensembl

basal plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 16133142. Source: UniProtKB

brush border

Inferred from direct assay PubMed 16133142. Source: UniProtKB

brush border membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19724054. Source: MGI

integral component of membrane

Inferred from direct assay PubMed 12181190. Source: MGI

integral component of plasma membrane

Traceable author statement PubMed 11066060. Source: MGI

membrane

Inferred from direct assay PubMed 15952169PubMed 18511498. Source: MGI

neuronal cell body membrane

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 11078688PubMed 11891232PubMed 12133842PubMed 16508653PubMed 17257750PubMed 17377981. Source: MGI

sarcolemma

Inferred from sequence or structural similarity. Source: UniProtKB

symbiont-containing vacuole

Inferred from direct assay PubMed 18665841. Source: UniProtKB

   Molecular_functionammonium transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

carbon dioxide transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor binding

Inferred from physical interaction Ref.4. Source: UniProtKB

glycerol transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular cGMP activated cation channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

nitric oxide transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

potassium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

potassium ion transmembrane transporter activity

Inferred from direct assay PubMed 18665841. Source: UniProtKB

water channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

water transmembrane transporter activity

Inferred from direct assay PubMed 10644730. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 269268Aquaporin-1
PRO_0000063921

Regions

Topological domain2 – 76Cytoplasmic By similarity
Transmembrane8 – 3629Helical; Name=Helix 1; By similarity
Topological domain37 – 4812Extracellular By similarity
Transmembrane49 – 6618Helical; Name=Helix 2; By similarity
Topological domain67 – 704Cytoplasmic By similarity
Intramembrane71 – 766 By similarity
Intramembrane77 – 848Helical; Name=Helix B; By similarity
Topological domain85 – 9410Cytoplasmic By similarity
Transmembrane95 – 11521Helical; Name=Helix 3; By similarity
Topological domain116 – 13621Extracellular By similarity
Transmembrane137 – 15519Helical; Name=Helix 4; By similarity
Topological domain156 – 16611Cytoplasmic By similarity
Transmembrane167 – 18317Helical; Name=Helix 5; By similarity
Topological domain184 – 1863Extracellular By similarity
Intramembrane187 – 1926 By similarity
Intramembrane193 – 2008Helical; Name=Helix E; By similarity
Topological domain201 – 2077Extracellular By similarity
Transmembrane208 – 22821Helical; Name=Helix 6; By similarity
Topological domain229 – 26941Cytoplasmic By similarity
Motif76 – 783NPA 1
Motif192 – 1943NPA 2
Compositional bias159 – 1624Poly-Arg

Sites

Site561Substrate discrimination By similarity
Site1801Substrate discrimination By similarity
Site1891Hg(2+)-sensitive residue By similarity
Site1951Substrate discrimination By similarity

Amino acid modifications

Modified residue2621Phosphoserine Ref.5
Glycosylation2051N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1901G → S in AAH07125. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q02013 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F0499724AD4AB5F6

FASTA26928,793
        10         20         30         40         50         60 
MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV KVSLAFGLSI 

        70         80         90        100        110        120 
ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA QCVGAIVATA ILSGITSSLV 

       130        140        150        160        170        180 
DNSLGRNDLA HGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 

       190        200        210        220        230        240 
LLAIDYTGCG INPARSFGSA VLTRNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDFTD 

       250        260 
RMKVWTSGQV EEYDLDADDI NSRVEMKPK 

« Hide

References

« Hide 'large scale' references
[1]"Growth factor-induced delayed early response genes."
Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.
Mol. Cell. Biol. 12:3919-3929(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Inner ear and Spleen.
[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: Mammary tumor.
[4]"EphB2 guides axons at the midline and is necessary for normal vestibular function."
Cowan C.A., Yokoyama N., Bianchi L.M., Henkemeyer M., Fritzsch B.
Neuron 26:417-430(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHB2.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02914 mRNA. Translation: AAB53928.1.
AK081886 mRNA. Translation: BAC38360.1.
AK086688 mRNA. Translation: BAC39719.1.
AK157333 mRNA. Translation: BAE34051.1.
AK158226 mRNA. Translation: BAE34412.1.
AK158389 mRNA. Translation: BAE34482.1.
AK171627 mRNA. Translation: BAE42573.1.
AK172361 mRNA. Translation: BAE42966.1.
BC007125 mRNA. Translation: AAH07125.1.
CCDSCCDS20164.1.
PIRB44499.
RefSeqNP_031498.1. NM_007472.2.
UniGeneMm.18625.

3D structure databases

ProteinModelPortalQ02013.
SMRQ02013. Positions 9-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198170. 1 interaction.
IntActQ02013. 2 interactions.
MINTMINT-4088080.

PTM databases

PhosphoSiteQ02013.

Proteomic databases

MaxQBQ02013.
PaxDbQ02013.
PRIDEQ02013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004774; ENSMUSP00000004774; ENSMUSG00000004655.
GeneID11826.
KEGGmmu:11826.
UCSCuc009caq.1. mouse.

Organism-specific databases

CTD358.
MGIMGI:103201. Aqp1.

Phylogenomic databases

eggNOGCOG0580.
GeneTreeENSGT00740000115105.
HOGENOMHOG000288286.
HOVERGENHBG000312.
InParanoidQ02013.
KOK09864.
OMAITHNFKD.
OrthoDBEOG7N8ZWD.
PhylomeDBQ02013.
TreeFamTF312940.

Gene expression databases

BgeeQ02013.
CleanExMM_AQP1.
GenevestigatorQ02013.

Family and domain databases

Gene3D1.20.1080.10. 1 hit.
InterProIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERPTHR19139. PTHR19139. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMSSF81338. SSF81338. 1 hit.
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAQP1. mouse.
NextBio279727.
PROQ02013.
SOURCESearch...

Entry information

Entry nameAQP1_MOUSE
AccessionPrimary (citable) accession number: Q02013
Secondary accession number(s): Q542P1, Q91VY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 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