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P29972

- AQP1_HUMAN

UniProt

P29972 - AQP1_HUMAN

Protein

Aquaporin-1

Gene

AQP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 discrimination
    Sitei180 – 1801Substrate discrimination
    Sitei189 – 1891Hg(2+)-sensitive residue
    Sitei195 – 1951Substrate discrimination

    GO - Molecular functioni

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

    GO - Biological processi

    1. ammonium transmembrane transport Source: GOC
    2. ammonium transport Source: UniProtKB
    3. bicarbonate transport Source: Reactome
    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 nitric oxide Source: UniProtKB
    17. cellular response to retinoic acid Source: UniProtKB
    18. cellular response to salt stress Source: UniProtKB
    19. cellular response to stress Source: UniProtKB
    20. cellular response to UV Source: UniProtKB
    21. cell volume homeostasis Source: UniProtKB
    22. cerebrospinal fluid secretion Source: UniProtKB
    23. cGMP biosynthetic process Source: UniProtKB
    24. establishment or maintenance of actin cytoskeleton polarity Source: UniProtKB
    25. glycerol transport Source: UniProtKB
    26. lateral ventricle development Source: UniProtKB
    27. maintenance of symbiont-containing vacuole by host Source: UniProtKB
    28. multicellular organismal water homeostasis Source: UniProtKB
    29. negative regulation of apoptotic process Source: UniProtKB
    30. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    31. nitric oxide transport Source: UniProtKB
    32. odontogenesis Source: UniProtKB
    33. pancreatic juice secretion Source: UniProtKB
    34. positive regulation of angiogenesis Source: UniProtKB
    35. positive regulation of fibroblast proliferation Source: UniProtKB
    36. positive regulation of saliva secretion Source: UniProtKB
    37. potassium ion transmembrane transport Source: GOC
    38. potassium ion transport Source: UniProtKB
    39. renal water transport Source: UniProtKB
    40. response to drug Source: UniProtKB
    41. small molecule metabolic process Source: Reactome
    42. transepithelial water transport Source: UniProtKB
    43. transmembrane transport Source: Reactome
    44. water transport Source: UniProtKB

    Keywords - Molecular functioni

    Blood group antigen

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_23826. Passive transport by Aquaporins.
    REACT_24023. Regulation of water balance by renal Aquaporins.

    Protein family/group databases

    TCDBi1.A.8.8.1. the major intrinsic protein (mip) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aquaporin-1
    Short name:
    AQP-1
    Alternative name(s):
    Aquaporin-CHIP
    Urine water channel
    Water channel protein for red blood cells and kidney proximal tubule
    Gene namesi
    Name:AQP1
    Synonyms:CHIP28
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:633. AQP1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical part of cell Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB
    3. basal plasma membrane Source: UniProtKB
    4. basolateral plasma membrane Source: UniProtKB
    5. brush border Source: UniProtKB
    6. brush border membrane Source: UniProtKB
    7. cytoplasm Source: UniProtKB
    8. extracellular vesicular exosome Source: UniProt
    9. integral component of plasma membrane Source: ProtInc
    10. nuclear membrane Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. plasma membrane Source: UniProtKB
    13. sarcolemma Source: UniProtKB
    14. symbiont-containing vacuole Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi110450. phenotype.
    PharmGKBiPA24918.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 269268Aquaporin-1PRO_0000063920Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Modified residuei262 – 2621PhosphoserineBy similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP29972.
    PRIDEiP29972.

    PTM databases

    PhosphoSiteiP29972.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver.1 Publication

    Gene expression databases

    ArrayExpressiP29972.
    BgeeiP29972.
    CleanExiHS_AQP1.
    GenevestigatoriP29972.

    Organism-specific databases

    HPAiCAB001707.
    HPA019206.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with EPHB2; involved in endolymph production in the inner ear By similarity. Identified in a complex with STOM.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDFIQ997504EBI-745213,EBI-724076

    Protein-protein interaction databases

    BioGridi106854. 7 interactions.
    DIPiDIP-29607N.
    IntActiP29972. 8 interactions.
    MINTiMINT-1439356.
    STRINGi9606.ENSP00000311165.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 3528
    Beta strandi37 – 426
    Helixi48 – 6518
    Beta strandi68 – 714
    Helixi76 – 838
    Helixi94 – 11421
    Turni119 – 1224
    Beta strandi132 – 1354
    Helixi136 – 15419
    Helixi166 – 18217
    Turni183 – 1853
    Helixi192 – 1998
    Helixi207 – 22721

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FQYX-ray3.80A1-269[»]
    1H6IX-ray3.54A1-269[»]
    1IH5X-ray3.70A1-269[»]
    ProteinModelPortaliP29972.
    SMRiP29972. Positions 9-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29972.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 76Cytoplasmic1 Publication
    Topological domaini37 – 4812Extracellular1 PublicationAdd
    BLAST
    Topological domaini67 – 704Cytoplasmic1 Publication
    Topological domaini85 – 9410Cytoplasmic1 Publication
    Topological domaini116 – 13621Extracellular1 PublicationAdd
    BLAST
    Topological domaini156 – 16611Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini184 – 1863Extracellular1 Publication
    Topological domaini201 – 2077Extracellular1 Publication
    Topological domaini229 – 26941Cytoplasmic1 PublicationAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei71 – 766
    Intramembranei77 – 848Helical; Name=Helix B
    Intramembranei187 – 1926
    Intramembranei193 – 2008Helical; Name=Helix E

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 3629Helical; Name=Helix 1Add
    BLAST
    Transmembranei49 – 6618Helical; Name=Helix 2Add
    BLAST
    Transmembranei95 – 11521Helical; Name=Helix 3Add
    BLAST
    Transmembranei137 – 15519Helical; Name=Helix 4Add
    BLAST
    Transmembranei167 – 18317Helical; Name=Helix 5Add
    BLAST
    Transmembranei208 – 22821Helical; Name=Helix 6Add
    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.
    HOGENOMiHOG000288286.
    HOVERGENiHBG000312.
    InParanoidiP29972.
    KOiK09864.
    OMAiITHNFKD.
    OrthoDBiEOG7N8ZWD.
    PhylomeDBiP29972.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P29972-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV    50
    KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA 100
    QCVGAIVATA ILSGITSSLT GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV 150
    LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA 200
    VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD RVKVWTSGQV 250
    EEYDLDADDI NSRVEMKPK 269
    Length:269
    Mass (Da):28,526
    Last modified:January 23, 2007 - v3
    Checksum:iBA204D82FB26352E
    GO
    Isoform 2 (identifier: P29972-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: MASEFKKKLF...KYPVGNNQTA → MPGARPLPLV...LGRVGPGSRQ
         46-128: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:186
    Mass (Da):19,956
    Checksum:i5C132B4A21FCC8BC
    GO
    Isoform 3 (identifier: P29972-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-128: MASEFKKKLF...LTGNSLGRND → MFWTFGYEAV...LGRVGPGSRQ

    Note: Gene prediction based on EST data.

    Show »
    Length:218
    Mass (Da):23,425
    Checksum:i409D14C5A0F352CE
    GO
    Isoform 4 (identifier: P29972-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MASEFKKKLFWRA → MQSGMGWNVLDFW
         14-128: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:154
    Mass (Da):16,677
    Checksum:i764FA0B49CB3B1FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451A → T in AAH22486. (PubMed:15489334)Curated

    Polymorphismi

    AQP1 is responsible for the Colton blood group system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46), approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-46). Co(A-B-) which is very rare, is due to a complete absence of AQP1.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381P → L in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability. 1 Publication
    VAR_013279
    Natural varianti45 – 451A → V in Co(A-B+) antigen. 2 Publications
    Corresponds to variant rs28362692 [ dbSNP | Ensembl ].
    VAR_004400
    Natural varianti165 – 1651G → D.1 Publication
    Corresponds to variant rs28362731 [ dbSNP | Ensembl ].
    VAR_022318

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 128128MASEF…LGRND → MFWTFGYEAVSPAGPSHLFA SLLLGVLLTITFMPGARPLP LVLVPQNTLAWMQLDAKAPA HPRPLQLLGRVGPGSRQ in isoform 3. CuratedVSP_046679Add
    BLAST
    Alternative sequencei1 – 4545MASEF…NNQTA → MPGARPLPLVLVPQNTLAWM QLDAKAPAHPRPLQLLGRVG PGSRQ in isoform 2. 1 PublicationVSP_046109Add
    BLAST
    Alternative sequencei1 – 1313MASEF…LFWRA → MQSGMGWNVLDFW in isoform 4. CuratedVSP_046680Add
    BLAST
    Alternative sequencei14 – 128115Missing in isoform 4. CuratedVSP_046681Add
    BLAST
    Alternative sequencei46 – 12883Missing in isoform 2. 1 PublicationVSP_046110Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77829 mRNA. Translation: AAA58425.1.
    U41517 mRNA. Translation: AAC50648.1.
    U41518 mRNA. Translation: AAC50649.1.
    S73482 mRNA. Translation: AAB31193.1.
    AK309608 mRNA. No translation available.
    AY953319 Genomic DNA. Translation: AAX24129.1.
    AC004691 Genomic DNA. Translation: AAC16481.1.
    AC005155 Genomic DNA. Translation: AAC23788.1.
    AB451275 mRNA. Translation: BAG70089.1.
    AB451402 mRNA. Translation: BAG70216.1.
    CH471073 Genomic DNA. Translation: EAW93971.1.
    BC022486 mRNA. Translation: AAH22486.1.
    AF480415 Genomic DNA. Translation: AAL87136.1.
    CCDSiCCDS5431.1. [P29972-1]
    CCDS55096.1. [P29972-4]
    CCDS55097.1. [P29972-3]
    CCDS55098.1. [P29972-2]
    PIRiA41616.
    I52366.
    RefSeqiNP_001171989.1. NM_001185060.1. [P29972-2]
    NP_001171990.1. NM_001185061.1. [P29972-3]
    NP_001171991.1. NM_001185062.1. [P29972-4]
    NP_932766.1. NM_198098.2. [P29972-1]
    UniGeneiHs.76152.

    Genome annotation databases

    EnsembliENST00000311813; ENSP00000311165; ENSG00000240583. [P29972-1]
    ENST00000409611; ENSP00000387178; ENSG00000240583. [P29972-3]
    ENST00000409899; ENSP00000386712; ENSG00000240583. [P29972-4]
    ENST00000441328; ENSP00000405698; ENSG00000240583. [P29972-2]
    GeneIDi358.
    KEGGihsa:358.
    UCSCiuc003tbv.2. human. [P29972-1]

    Polymorphism databases

    DMDMi267412.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    dbRBC/BGMUT

    Blood group antigen gene mutation database

    SeattleSNPs
    Protein Spotlight

    Liquid states - Issue 36 of July 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77829 mRNA. Translation: AAA58425.1 .
    U41517 mRNA. Translation: AAC50648.1 .
    U41518 mRNA. Translation: AAC50649.1 .
    S73482 mRNA. Translation: AAB31193.1 .
    AK309608 mRNA. No translation available.
    AY953319 Genomic DNA. Translation: AAX24129.1 .
    AC004691 Genomic DNA. Translation: AAC16481.1 .
    AC005155 Genomic DNA. Translation: AAC23788.1 .
    AB451275 mRNA. Translation: BAG70089.1 .
    AB451402 mRNA. Translation: BAG70216.1 .
    CH471073 Genomic DNA. Translation: EAW93971.1 .
    BC022486 mRNA. Translation: AAH22486.1 .
    AF480415 Genomic DNA. Translation: AAL87136.1 .
    CCDSi CCDS5431.1. [P29972-1 ]
    CCDS55096.1. [P29972-4 ]
    CCDS55097.1. [P29972-3 ]
    CCDS55098.1. [P29972-2 ]
    PIRi A41616.
    I52366.
    RefSeqi NP_001171989.1. NM_001185060.1. [P29972-2 ]
    NP_001171990.1. NM_001185061.1. [P29972-3 ]
    NP_001171991.1. NM_001185062.1. [P29972-4 ]
    NP_932766.1. NM_198098.2. [P29972-1 ]
    UniGenei Hs.76152.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FQY X-ray 3.80 A 1-269 [» ]
    1H6I X-ray 3.54 A 1-269 [» ]
    1IH5 X-ray 3.70 A 1-269 [» ]
    ProteinModelPortali P29972.
    SMRi P29972. Positions 9-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106854. 7 interactions.
    DIPi DIP-29607N.
    IntActi P29972. 8 interactions.
    MINTi MINT-1439356.
    STRINGi 9606.ENSP00000311165.

    Chemistry

    DrugBanki DB00819. Acetazolamide.
    GuidetoPHARMACOLOGYi 688.

    Protein family/group databases

    TCDBi 1.A.8.8.1. the major intrinsic protein (mip) family.

    PTM databases

    PhosphoSitei P29972.

    Polymorphism databases

    DMDMi 267412.

    Proteomic databases

    PaxDbi P29972.
    PRIDEi P29972.

    Protocols and materials databases

    DNASUi 358.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311813 ; ENSP00000311165 ; ENSG00000240583 . [P29972-1 ]
    ENST00000409611 ; ENSP00000387178 ; ENSG00000240583 . [P29972-3 ]
    ENST00000409899 ; ENSP00000386712 ; ENSG00000240583 . [P29972-4 ]
    ENST00000441328 ; ENSP00000405698 ; ENSG00000240583 . [P29972-2 ]
    GeneIDi 358.
    KEGGi hsa:358.
    UCSCi uc003tbv.2. human. [P29972-1 ]

    Organism-specific databases

    CTDi 358.
    GeneCardsi GC07P030894.
    HGNCi HGNC:633. AQP1.
    HPAi CAB001707.
    HPA019206.
    MIMi 107776. gene.
    110450. phenotype.
    neXtProti NX_P29972.
    PharmGKBi PA24918.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0580.
    HOGENOMi HOG000288286.
    HOVERGENi HBG000312.
    InParanoidi P29972.
    KOi K09864.
    OMAi ITHNFKD.
    OrthoDBi EOG7N8ZWD.
    PhylomeDBi P29972.
    TreeFami TF312940.

    Enzyme and pathway databases

    Reactomei REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_23826. Passive transport by Aquaporins.
    REACT_24023. Regulation of water balance by renal Aquaporins.

    Miscellaneous databases

    EvolutionaryTracei P29972.
    GeneWikii Aquaporin_1.
    GenomeRNAii 358.
    NextBioi 1497.
    PROi P29972.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29972.
    Bgeei P29972.
    CleanExi HS_AQP1.
    Genevestigatori P29972.

    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. "Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family."
      Preston G.M., Agre P.
      Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization."
      Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.
      J. Biol. Chem. 268:15772-15778(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium."
      Ruiz A.C., Bok D.
      Biochim. Biophys. Acta 1282:174-178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retinal pigment epithelium.
    4. "The water channel gene in human uterus."
      Li X., Yu H., Koide S.S.
      Biochem. Mol. Biol. Int. 32:371-377(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Uterus.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Mesangial cell.
    6. SeattleSNPs variation discovery resource
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-45 AND ASP-165.
    7. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 1).
      Tissue: Brain.
    11. "Human chondrocytes in situ express aquaporin water channels: changes in AQP1 abundance in pathologies of articular cartilage."
      Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
      Tissue: Articular cartilage.
    12. "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins."
      Smith B.L., Agre P.
      J. Biol. Chem. 266:6407-6415(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-36.
    13. "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein."
      Preston G.M., Carroll T.P., Guggino W.B., Agre P.
      Science 256:385-387(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel."
      Preston G.M., Jung J.S., Guggino W.B., Agre P.
      J. Biol. Chem. 268:17-20(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TARGET OF MERCURY INHIBITION.
    15. "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis."
      Preston G.M., Jung J.S., Guggino W.B., Agre P.
      J. Biol. Chem. 269:1668-1673(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    16. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
      Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
      Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH STOM, SUBUNIT.
    17. "The three-dimensional structure of human erythrocyte aquaporin CHIP."
      Walz T., Smith B.L., Agre P., Engel A.
      EMBO J. 13:2985-2993(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
    18. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
    19. "Structural determinants of water permeation through aquaporin-1."
      Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y.
      Nature 407:599-605(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
    20. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
    21. "Visualization of a water-selective pore by electron crystallography in vitreous ice."
      Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
    22. "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens."
      Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.
      J. Clin. Invest. 94:1043-1049(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP COLTON VAL-45.
    23. "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels."
      Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.
      Science 265:1585-1587(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-38.

    Entry informationi

    Entry nameiAQP1_HUMAN
    AccessioniPrimary (citable) accession number: P29972
    Secondary accession number(s): B5BU39
    , E7EM69, E9PC21, F5GY19, Q8TBI5, Q8TDC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Miscellaneous

    Pharmacologically inhibited by submillimolar concentrations of mercury.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Blood group antigen proteins
      Nomenclature of blood group antigens and list of entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3