Reviewed, UniProtKB/Swiss-Prot O43315 (AQP9_HUMAN)

Names and origin

Protein names

Recommended name:
    Aquaporin-9
      Short name=AQP-9
Alternative name(s):
    Small solute channel 1

Gene names

Name:	AQP9
Synonyms:	SSC1

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	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Forms a channel with a broad specificity. Mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na(+), K(+), Cl(-), and deprotonated monocarboxylates are excluded. Also permeable to urea but not to glycerol.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Highly expressed in peripheral leukocytes. Also expressed in liver, lung, and spleen.
Domain	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 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
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	amine transport Inferred from direct assay. Source: UniProtKB carboxylic acid transport Traceable author statement. Source: UniProtKB excretion Traceable author statement. Source: UniProtKB immune response Ref.1 Traceable author statement. Source: ProtInc metabolic process Traceable author statement. Source: UniProtKB polyol transport Inferred from direct assay. Source: UniProtKB purine transport Inferred from direct assay. Source: UniProtKB pyrimidine transport Inferred from direct assay. Source: UniProtKB response to mercury ion Inferred from direct assay. Source: UniProtKB response to organic substance Inferred from direct assay. Source: UniProtKB response to osmotic stress Traceable author statement. Source: UniProtKB water homeostasis Non-traceable author statement. Source: UniProtKB water transport Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	amine transmembrane transporter activity Traceable author statement. Source: UniProtKB carboxylic acid transmembrane transporter activity Traceable author statement. Source: UniProtKB polyol transmembrane transporter activity Traceable author statement. Source: UniProtKB porin activity Non-traceable author statement. Source: UniProtKB purine transmembrane transporter activity Inferred from direct assay. Source: UniProtKB pyrimidine transmembrane transporter activity Inferred from direct assay. Source: UniProtKB water channel activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 295	295	Aquaporin-9
Regions
	Topological domain	1 – 29	29	Cytoplasmic Potential
	Transmembrane	30 – 50	21	Potential
	Topological domain	51 – 54	4	Extracellular Potential
	Transmembrane	55 – 75	21	Potential
	Topological domain	76 – 110	35	Cytoplasmic Potential
	Transmembrane	111 – 131	21	Potential
	Topological domain	132 – 158	27	Extracellular Potential
	Transmembrane	159 – 179	21	Potential
	Topological domain	180 – 189	10	Cytoplasmic Potential
	Transmembrane	190 – 210	21	Potential
	Topological domain	211 – 245	35	Extracellular Potential
	Transmembrane	246 – 266	21	Potential
	Topological domain	267 – 295	29	Cytoplasmic Potential
	Motif	84 – 86	3	NPA 1
	Motif	216 – 218	3	NPA 2
Amino acid modifications
	Modified residue	222	1	Phosphoserine
Natural variations
	Natural variant	279	1	A → T: dbSNP rs1867380.

Sequences

	Sequence		Length	Mass (Da)
	O43315-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: A8B5A6CD9F1F9CAF	FASTA	295	31,401
	10 20 30 40 50 60 MQPEGAEKGK SFKQRLVLKS SLAKETLSEF LGTFILIVLG CGCVAQAILS RGRFGGVITI 70 80 90 100 110 120 NVGFSMAVAM AIYVAGGVSG GHINPAVSLA MCLFGRMKWF KLPFYVGAQF LGAFVGAATV 130 140 150 160 170 180 FGIYYDGLMS FAGGKLLIVG ENATAHIFAT YPAPYLSLAN AFADQVVATM ILLIIVFAIF 190 200 210 220 230 240 DSRNLGAPRG LEPIAIGLLI IVIASSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFRAG 250 260 270 280 290 NNFWWIPVVG PLVGAVIGGL IYVLVIEIHH PEPDSVFKAE QSEDKPEKYE LSVIM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol." Ishibashi K., Kuwahara M., Gu Y., Tanaka Y., Marumo F., Sasaki S. Biochem. Biophys. Res. Commun. 244:268-274(1998) [PubMed: 9514918] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Functional and molecular characterization of the human neutral solute channel aquaporin-9." Tsukaguchi H., Weremowicz S., Morton C.C., Hediger M.A. Am. J. Physiol. 277:F685-F696(1999) [PubMed: 10564231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY. Tissue: Epithelium.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB008775 mRNA. Translation: BAA24864.1. AF016495 mRNA. Translation: AAF16677.1. AF102870 Genomic DNA. Translation: AAF27983.1. BC026258 mRNA. Translation: AAH26258.1.
PIR	JC5973.
RefSeq	NP_066190.2.
UniGene	Hs.104624
3D structure databases
HSSP	HSSP built from PDB template 1FX8 based on UniProtKB P11244.
ModBase	Search...
PTM databases
PhosphoSite	O43315.
Genome annotation databases
Ensembl	ENSG00000103569. Homo sapiens. [Contig view]
GeneID	366.
KEGG	hsa:366.
Organism-specific databases
H-InvDB	HIX0012281.
HGNC	HGNC:643. AQP9.
MIM	602914. gene+phenotype.
PharmGKB	PA24927.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	O43315.
HOVERGEN	O43315.
Gene expression databases
ArrayExpress	O43315.
CleanEx	HS_AQP9.
Family and domain databases
InterPro	IPR012269. Aquaporin. IPR015685. Aquaporin_9. IPR000425. MIP. [Graphical view]
Gene3D	G3DSA:1.20.1080.10. MIP. 1 hit.
PANTHER	PTHR19139:SF15. AQP9. 1 hit. PTHR19139. MIP. 1 hit.
Pfam	PF00230. MIP. 1 hit. [Graphical view]
PRINTS	PR00783. MINTRINSICP.
ProDom	PD000295. MIP. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00861. MIP. 1 hit.
PROSITE	PS00221. MIP. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

AQP9_HUMAN

Accession

Primary (citable) accession number: O43315
Secondary accession number(s): Q9NP32

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	July 22, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)