O14520 (AQP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aquaporin-7
Short name=AQP-7

Alternative name(s):
Aquaglyceroporin-7
Aquaporin adipose
Short name=AQPap
Aquaporin-7-like

Gene names

Name:	AQP7
Synonyms:	AQP7L, AQP9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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]

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	excretion Traceable author statement. Source: ProtInc generation of precursor metabolites and energy Traceable author statement. Source: ProtInc
Cellular component	cell-cell junction Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from direct assay. Source: UniProtKB integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	glycerol channel activity Inferred from experiment. Source: Reactome water channel activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 342	342	Aquaporin-7		PRO_0000063958
Regions
	Topological domain	1 – 36	36	Cytoplasmic Potential
	Transmembrane	37 – 57	21	Helical; Potential
	Topological domain	58 – 65	8	Extracellular Potential
	Transmembrane	66 – 86	21	Helical; Potential
	Topological domain	87 – 113	27	Cytoplasmic Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Topological domain	135 – 170	36	Extracellular Potential
	Transmembrane	171 – 191	21	Helical; Potential
	Topological domain	192 – 196	5	Cytoplasmic Potential
	Transmembrane	197 – 217	21	Helical; Potential
	Topological domain	218 – 255	38	Extracellular Potential
	Transmembrane	256 – 276	21	Helical; Potential
	Topological domain	277 – 342	66	Cytoplasmic Potential
	Motif	94 – 96	3	NPA 1
	Motif	226 – 228	3	NPA 2
Natural variations
	Natural variant	38	1	L → V. Corresponds to variant rs2381003 [ dbSNP | Ensembl ].		VAR_061343
	Natural variant	63	1	K → T. Corresponds to variant rs4008658 [ dbSNP | Ensembl ].		VAR_061344
Experimental info
	Sequence conflict	264	1	G → V in BAC05693. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O14520 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 8A05F92B977D2F93	FASTA	342	37,232
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB006190 mRNA. Translation: BAA21745.1. AB052626 Genomic DNA. Translation: BAC05693.1. AL356218 Genomic DNA. Translation: CAI13309.1.
IPI	IPI00022359.
PIR	JC5791.
RefSeq	NP_001161.1. NM_001170.1.
UniGene	Hs.455323.
3D structure databases
ProteinModelPortal	O14520.
SMR	O14520. Positions 32-280.
ModBase	Search...
Protein-protein interaction databases
STRING	O14520.
Proteomic databases
PRIDE	O14520.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297988; ENSP00000297988; ENSG00000165269.
GeneID	364.
KEGG	hsa:364.
UCSC	uc003zst.1. human.
Organism-specific databases
CTD	364.
GeneCards	GC09M033384.
H-InvDB	HIX0034738. HIX0034865.
HGNC	HGNC:640. AQP7.
MIM	602974. gene.
neXtProt	NX_O14520.
PharmGKB	PA24925.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17389.
HOVERGEN	HBG106057.
InParanoid	O14520.
OMA	LFACFDG.
PhylomeDB	O14520.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	O14520.
Bgee	O14520.
CleanEx	HS_AQP7. HS_AQP9.
Genevestigator	O14520.
GermOnline	ENSG00000165269. Homo sapiens.
Family and domain databases
InterPro	IPR012269. Aquaporin. IPR023271. Aquaporin-like. IPR015686. Aquaporin_7. IPR000425. MIP. [Graphical view]
Gene3D	G3DSA:1.20.1080.10. MIP. 1 hit.
KO	K08771.
PANTHER	PTHR19139:SF16. AQP7. 1 hit. PTHR19139. MIP. 1 hit.
Pfam	PF00230. MIP. 1 hit. [Graphical view]
PRINTS	PR00783. MINTRINSICP.
SUPFAM	SSF81338. MIP. 1 hit.
TIGRFAMs	TIGR00861. MIP. 1 hit.
PROSITE	PS00221. MIP. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	1523.
SOURCE	Search...

Entry information

Entry name

AQP7_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.