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Q02013

- AQP1_MOUSE

UniProt

Q02013 - AQP1_MOUSE

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Protein
Aquaporin-1
Gene
Aqp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Substrate discrimination By similarity
Sitei180 – 1801Substrate discrimination By similarity
Sitei189 – 1891Hg(2+)-sensitive residue By similarity
Sitei195 – 1951Substrate discrimination By similarity

GO - Molecular functioni

  1. ammonium transmembrane transporter activity Source: UniProtKB
  2. carbon dioxide transmembrane transporter activity Source: UniProtKB
  3. ephrin receptor binding Source: UniProtKB
  4. glycerol transmembrane transporter activity Source: UniProtKB
  5. intracellular cGMP activated cation channel activity Source: UniProtKB
  6. nitric oxide transmembrane transporter activity Source: UniProtKB
  7. potassium channel activity Source: UniProtKB
  8. potassium ion transmembrane transporter activity Source: UniProtKB
  9. water channel activity Source: UniProtKB
  10. water transmembrane transporter activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. ammonium transmembrane transport Source: GOC
  2. ammonium transport Source: UniProtKB
  3. cGMP biosynthetic process Source: UniProtKB
  4. camera-type eye morphogenesis Source: MGI
  5. carbon dioxide transmembrane transport Source: UniProtKB
  6. carbon dioxide transport Source: UniProtKB
  7. cell volume homeostasis Source: UniProtKB
  8. cellular homeostasis Source: UniProtKB
  9. cellular hyperosmotic response Source: UniProtKB
  10. cellular response to UV Source: UniProtKB
  11. cellular response to cAMP Source: UniProtKB
  12. cellular response to copper ion Source: UniProtKB
  13. cellular response to dexamethasone stimulus Source: UniProtKB
  14. cellular response to hydrogen peroxide Source: UniProtKB
  15. cellular response to hypoxia Source: UniProtKB
  16. cellular response to inorganic substance Source: UniProtKB
  17. cellular response to mechanical stimulus Source: UniProtKB
  18. cellular response to mercury ion Source: UniProtKB
  19. cellular response to retinoic acid Source: UniProtKB
  20. cellular response to salt stress Source: UniProtKB
  21. cellular response to stress Source: UniProtKB
  22. corticotropin secretion Source: MGI
  23. establishment or maintenance of actin cytoskeleton polarity Source: UniProtKB
  24. glomerular filtration Source: MGI
  25. glycerol transport Source: UniProtKB
  26. hyperosmotic salinity response Source: Ensembl
  27. lateral ventricle development Source: UniProtKB
  28. lipid digestion Source: MGI
  29. maintenance of symbiont-containing vacuole by host Source: UniProtKB
  30. metanephric descending thin limb development Source: UniProtKB
  31. metanephric glomerulus vasculature development Source: UniProtKB
  32. metanephric proximal convoluted tubule segment 2 development Source: UniProtKB
  33. metanephric proximal straight tubule development Source: UniProtKB
  34. negative regulation of apoptotic process Source: UniProtKB
  35. nitric oxide transport Source: UniProtKB
  36. positive regulation of angiogenesis Source: UniProtKB
  37. positive regulation of cell migration Source: MGI
  38. positive regulation of epithelial cell migration Source: Ensembl
  39. positive regulation of fibroblast proliferation Source: UniProtKB
  40. positive regulation of lamellipodium assembly Source: Ensembl
  41. positive regulation of saliva secretion Source: UniProtKB
  42. potassium ion transmembrane transport Source: GOC
  43. potassium ion transport Source: UniProtKB
  44. renal water absorption Source: MGI
  45. response to drug Source: UniProtKB
  46. response to estrogen Source: Ensembl
  47. secretion by cell Source: MGI
  48. secretory granule organization Source: MGI
  49. sensory perception of pain Source: MGI
  50. transepithelial water transport Source: UniProtKB
  51. water homeostasis Source: MGI
  52. water transport Source: MGI
  53. wound healing Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.
REACT_213947. Regulation of water balance by renal Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Aqp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:103201. Aqp1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76Cytoplasmic By similarity
Transmembranei8 – 3629Helical; Name=Helix 1; By similarity
Add
BLAST
Topological domaini37 – 4812Extracellular By similarity
Add
BLAST
Transmembranei49 – 6618Helical; Name=Helix 2; By similarity
Add
BLAST
Topological domaini67 – 704Cytoplasmic By similarity
Intramembranei71 – 766 By similarity
Intramembranei77 – 848Helical; Name=Helix B; By similarity
Topological domaini85 – 9410Cytoplasmic By similarity
Transmembranei95 – 11521Helical; Name=Helix 3; By similarity
Add
BLAST
Topological domaini116 – 13621Extracellular By similarity
Add
BLAST
Transmembranei137 – 15519Helical; Name=Helix 4; By similarity
Add
BLAST
Topological domaini156 – 16611Cytoplasmic By similarity
Add
BLAST
Transmembranei167 – 18317Helical; Name=Helix 5; By similarity
Add
BLAST
Topological domaini184 – 1863Extracellular By similarity
Intramembranei187 – 1926 By similarity
Intramembranei193 – 2008Helical; Name=Helix E; By similarity
Topological domaini201 – 2077Extracellular By similarity
Transmembranei208 – 22821Helical; Name=Helix 6; By similarity
Add
BLAST
Topological domaini229 – 26941Cytoplasmic By similarity
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. axon Source: MGI
  3. axon terminus Source: Ensembl
  4. basal plasma membrane Source: UniProtKB
  5. basolateral plasma membrane Source: UniProtKB
  6. brush border Source: UniProtKB
  7. brush border membrane Source: UniProtKB
  8. cytoplasm Source: UniProtKB
  9. extracellular vesicular exosome Source: MGI
  10. integral component of membrane Source: MGI
  11. integral component of plasma membrane Source: MGI
  12. membrane Source: MGI
  13. neuronal cell body membrane Source: Ensembl
  14. nuclear membrane Source: UniProtKB
  15. nucleus Source: UniProtKB
  16. plasma membrane Source: MGI
  17. sarcolemma Source: UniProtKB
  18. symbiont-containing vacuole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate and appear healthy and normal, but display strongly reduced urine osmolality. Besides, their erythrocytes show reduced water permeability. Mice lacking both Aqp1 and Slc14a1 are born at the expected Mendelian ratio, but do not thrive; half of them die within ten days after birth and none are alive after two weeks. Urine osmolality is somewhat lower than that observed with mice lacking only Aqp1. Besides, erythrocyte water permeability is significantly lower than in mice lacking only Aqp1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 269268Aquaporin-1
PRO_0000063921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi205 – 2051N-linked (GlcNAc...) Reviewed prediction
Modified residuei262 – 2621Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ02013.
PaxDbiQ02013.
PRIDEiQ02013.

PTM databases

PhosphoSiteiQ02013.

Expressioni

Tissue specificityi

Detected in erythrocytes (at protein level). Erythrocytes and renal tubules.

Gene expression databases

BgeeiQ02013.
CleanExiMM_AQP1.
GenevestigatoriQ02013.

Interactioni

Subunit structurei

Homotetramer. Identified in a complex with STOM By similarity. Interacts with EPHB2; involved in endolymph production in the inner ear.1 Publication

Protein-protein interaction databases

BioGridi198170. 1 interaction.
IntActiQ02013. 2 interactions.
MINTiMINT-4088080.

Structurei

3D structure databases

ProteinModelPortaliQ02013.
SMRiQ02013. Positions 9-233.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi76 – 783NPA 1
Motifi192 – 1943NPA 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 1624Poly-Arg

Domaini

Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0580.
GeneTreeiENSGT00740000115105.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiQ02013.
KOiK09864.
OMAiITHNFKD.
OrthoDBiEOG7N8ZWD.
PhylomeDBiQ02013.
TreeFamiTF312940.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02013-1 [UniParc]FASTAAdd to Basket

« Hide

MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV    50
KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA 100
QCVGAIVATA ILSGITSSLV DNSLGRNDLA HGVNSGQGLG IEIIGTLQLV 150
LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA 200
VLTRNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDFTD RMKVWTSGQV 250
EEYDLDADDI NSRVEMKPK 269
Length:269
Mass (Da):28,793
Last modified:January 23, 2007 - v3
Checksum:iF0499724AD4AB5F6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901G → S in AAH07125. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS20164.1.
PIRiB44499.
RefSeqiNP_031498.1. NM_007472.2.
UniGeneiMm.18625.

Genome annotation databases

EnsembliENSMUST00000004774; ENSMUSP00000004774; ENSMUSG00000004655.
GeneIDi11826.
KEGGimmu:11826.
UCSCiuc009caq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS20164.1.
PIRi B44499.
RefSeqi NP_031498.1. NM_007472.2.
UniGenei Mm.18625.

3D structure databases

ProteinModelPortali Q02013.
SMRi Q02013. Positions 9-233.
ModBasei Search...

Protein-protein interaction databases

BioGridi 198170. 1 interaction.
IntActi Q02013. 2 interactions.
MINTi MINT-4088080.

PTM databases

PhosphoSitei Q02013.

Proteomic databases

MaxQBi Q02013.
PaxDbi Q02013.
PRIDEi Q02013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004774 ; ENSMUSP00000004774 ; ENSMUSG00000004655 .
GeneIDi 11826.
KEGGi mmu:11826.
UCSCi uc009caq.1. mouse.

Organism-specific databases

CTDi 358.
MGIi MGI:103201. Aqp1.

Phylogenomic databases

eggNOGi COG0580.
GeneTreei ENSGT00740000115105.
HOGENOMi HOG000288286.
HOVERGENi HBG000312.
InParanoidi Q02013.
KOi K09864.
OMAi ITHNFKD.
OrthoDBi EOG7N8ZWD.
PhylomeDBi Q02013.
TreeFami TF312940.

Enzyme and pathway databases

Reactomei REACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.
REACT_213947. Regulation of water balance by renal Aquaporins.

Miscellaneous databases

ChiTaRSi AQP1. mouse.
NextBioi 279727.
PROi Q02013.
SOURCEi Search...

Gene expression databases

Bgeei Q02013.
CleanExi MM_AQP1.
Genevestigatori Q02013.

Family and domain databases

Gene3Di 1.20.1080.10. 1 hit.
InterProi IPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view ]
PANTHERi PTHR19139. PTHR19139. 1 hit.
Pfami PF00230. MIP. 1 hit.
[Graphical view ]
PRINTSi PR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMi SSF81338. SSF81338. 1 hit.
TIGRFAMsi TIGR00861. MIP. 1 hit.
PROSITEi PS00221. MIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence for UT-B-facilitated water transport in erythrocytes."
    Yang B., Verkman A.S.
    J. Biol. Chem. 277:36782-36786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAQP1_MOUSE
AccessioniPrimary (citable) accession number: Q02013
Secondary accession number(s): Q542P1, Q91VY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi