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Reviewed, UniProtKB/Swiss-Prot O14520 (AQP7_HUMAN)

Last modified December 16, 2008. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aquaporin-7
      Short name=AQP-7
Alternative name(s):
    Aquaporin-7-like
    Aquaporin adipose
      Short name=AQPap
Gene names
Name: AQP7
Synonyms: AQP7L, AQP9
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Forms a channel for water and glycerol.

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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

Sequence similarities

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Aquaporin-7
PRO_0000063958

Regions

Topological domain1 – 3636Cytoplasmic Potential
Transmembrane37 – 5721 Potential
Topological domain58 – 658Extracellular Potential
Transmembrane66 – 8621 Potential
Topological domain87 – 11327Cytoplasmic Potential
Transmembrane114 – 13421 Potential
Topological domain135 – 17036Extracellular Potential
Transmembrane171 – 19121 Potential
Topological domain192 – 1965Cytoplasmic Potential
Transmembrane197 – 21721 Potential
Topological domain218 – 25538Extracellular Potential
Transmembrane256 – 27621 Potential
Topological domain277 – 34266Cytoplasmic Potential
Motif94 – 963NPA 1
Motif226 – 2283NPA 2

Experimental info

Sequence conflict2641G → V in BAC05693. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
O14520-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8A05F92B977D2F93

FASTA34237,232
        10         20         30         40         50         60 
MVQASGHRRS TRGSKMVSWS VIAKIQEILQ RKMVREFLAE FMSTYVMMVF GLGSVAHMVL 

        70         80         90        100        110        120 
NKKYGSYLGV NLGFGFGVTM GVHVAGRISG AHMNAAVTFA NCALGRVPWR KFPVYVLGQF 

       130        140        150        160        170        180 
LGSFLAAATI YSLFYTAILH FSGGQLMVTG PVATAGIFAT YLPDHMTLWR GFLNEAWLTG 

       190        200        210        220        230        240 
MLQLCLFAIT DQENNPALPG TEALVIGILV VIIGVSLGMN TGYAINPSRD LPPRIFTFIA 

       250        260        270        280        290        300 
GWGKQVFSNG ENWWWVPVVA PLLGAYLGGI IYLVFIGSTI PREPLKLEDS VAYEDHGITV 

       310        320        330        340 
LPKMGSHEPT ISPLTPVSVS PANRSSVHPA PPLHESMALE HF

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability."
Kuriyama H., Kawamoto S., Ishida N., Ohno I., Mita S., Matsuzawa Y., Matsubara K., Okubo K.
Biochem. Biophys. Res. Commun. 241:53-58(1997) [PubMed: 9405233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adipose tissue.
[2]"Genomic structure and mutations in aquaporin adipose."
Kondo H., Kishida K., Kuriyama H., Matsukawa Y.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB006190 mRNA. Translation: BAA21745.1.
AB052626 Genomic DNA. Translation: BAC05693.1.
AL356218 Genomic DNA. Translation: CAI13309.1.
PIRJC5791.
RefSeqNP_001161.1.
UniGeneHs.455323

3D structure databases

HSSPHSSP built from PDB template 1FX8 based on UniProtKB P11244.
ModBaseSearch...

Proteomic databases

PRIDEO14520.

Genome annotation databases

EnsemblENSG00000165269. Homo sapiens. [Contig view]
GeneID364.
KEGGhsa:364.

Organism-specific databases

GeneCardsGC09M033374.
H-InvDBHIX0034738.
HGNCHGNC:640. AQP7.
MIM602974. gene.
PharmGKBPA24925.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO14520.
HOVERGENO14520.

Gene expression databases

CleanExHS_AQP7.
HS_AQP9.
GermOnlineENSG00000165269. Homo sapiens.

Family and domain databases

InterProIPR012269. Aquaporin.
IPR015686. Aquaporin_7.
IPR000425. MIP.
[Graphical view]
Gene3DG3DSA:1.20.1080.10. MIP. 1 hit.
PANTHERPTHR19139:SF16. AQP7. 1 hit.
PTHR19139. MIP. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR00783. MINTRINSICP.
ProDomPD000295. MIP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio1523.
SOURCESearch...

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Entry information

Entry nameAQP7_HUMAN
AccessionPrimary (citable) accession number: O14520
Secondary accession number(s): Q5T5L9, Q8NHM3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: December 16, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents