Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q02013

- AQP1_MOUSE

UniProt

Q02013 - AQP1_MOUSE

Protein

Aquaporin-1

Gene

Aqp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Sites

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

    GO - Biological processi

    1. ammonium transmembrane transport Source: GOC
    2. ammonium transport Source: UniProtKB
    3. camera-type eye morphogenesis Source: MGI
    4. carbon dioxide transmembrane transport Source: UniProtKB
    5. carbon dioxide transport Source: UniProtKB
    6. cellular homeostasis Source: UniProtKB
    7. cellular hyperosmotic response Source: UniProtKB
    8. cellular response to cAMP Source: UniProtKB
    9. cellular response to copper ion Source: UniProtKB
    10. cellular response to dexamethasone stimulus Source: UniProtKB
    11. cellular response to hydrogen peroxide Source: UniProtKB
    12. cellular response to hypoxia Source: UniProtKB
    13. cellular response to inorganic substance Source: UniProtKB
    14. cellular response to mechanical stimulus Source: UniProtKB
    15. cellular response to mercury ion Source: UniProtKB
    16. cellular response to retinoic acid Source: UniProtKB
    17. cellular response to salt stress Source: UniProtKB
    18. cellular response to stress Source: UniProtKB
    19. cellular response to UV Source: UniProtKB
    20. cell volume homeostasis Source: UniProtKB
    21. cGMP biosynthetic process 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

    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

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    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

    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 Aqp1.1 Publication

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    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.1 Publication

    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.By similarity1 Publication

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ02013.
    SMRiQ02013. Positions 9-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 76CytoplasmicBy similarity
    Topological domaini37 – 4812ExtracellularBy similarityAdd
    BLAST
    Topological domaini67 – 704CytoplasmicBy similarity
    Topological domaini85 – 9410CytoplasmicBy similarity
    Topological domaini116 – 13621ExtracellularBy similarityAdd
    BLAST
    Topological domaini156 – 16611CytoplasmicBy similarityAdd
    BLAST
    Topological domaini184 – 1863ExtracellularBy similarity
    Topological domaini201 – 2077ExtracellularBy similarity
    Topological domaini229 – 26941CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei71 – 766By similarity
    Intramembranei77 – 848Helical; Name=Helix BBy similarity
    Intramembranei187 – 1926By similarity
    Intramembranei193 – 2008Helical; Name=Helix EBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 3629Helical; Name=Helix 1By similarityAdd
    BLAST
    Transmembranei49 – 6618Helical; Name=Helix 2By similarityAdd
    BLAST
    Transmembranei95 – 11521Helical; Name=Helix 3By similarityAdd
    BLAST
    Transmembranei137 – 15519Helical; Name=Helix 4By similarityAdd
    BLAST
    Transmembranei167 – 18317Helical; Name=Helix 5By similarityAdd
    BLAST
    Transmembranei208 – 22821Helical; Name=Helix 6By similarityAdd
    BLAST

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901G → S in AAH07125. (PubMed:15489334)Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 130 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