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Protein

Aquaporin-9

Gene

AQP9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 and glycerol.1 Publication

GO - Molecular functioni

  1. amine transmembrane transporter activity Source: UniProtKB
  2. carboxylic acid transmembrane transporter activity Source: UniProtKB
  3. glycerol channel activity Source: Reactome
  4. polyol transmembrane transporter activity Source: UniProtKB
  5. porin activity Source: UniProtKB
  6. purine nucleobase transmembrane transporter activity Source: UniProtKB
  7. pyrimidine nucleobase transmembrane transporter activity Source: UniProtKB
  8. urea transmembrane transporter activity Source: GO_Central
  9. water channel activity Source: UniProtKB
  10. water transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. amine transport Source: UniProtKB
  2. canalicular bile acid transport Source: Ensembl
  3. carboxylic acid transport Source: UniProtKB
  4. cellular response to cAMP Source: UniProtKB
  5. cellular water homeostasis Source: GO_Central
  6. excretion Source: UniProtKB
  7. glycerol transport Source: Reactome
  8. immune response Source: ProtInc
  9. ion transmembrane transport Source: GO_Central
  10. metabolic process Source: UniProtKB
  11. polyol transport Source: UniProtKB
  12. purine nucleobase transport Source: UniProtKB
  13. pyrimidine-containing compound transmembrane transport Source: GOC
  14. pyrimidine nucleobase transport Source: UniProtKB
  15. response to mercury ion Source: UniProtKB
  16. response to organic substance Source: UniProtKB
  17. response to osmotic stress Source: UniProtKB
  18. transmembrane transport Source: Reactome
  19. transport Source: UniProtKB
  20. urea transmembrane transport Source: GO_Central
  21. water homeostasis Source: UniProtKB
  22. water transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_23809. Transport of glycerol from adipocytes to the liver by Aquaporins.
REACT_23826. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin-9
Short name:
AQP-9
Alternative name(s):
Aquaglyceroporin-9
Small solute channel 1
Gene namesi
Name:AQP9
Synonyms:SSC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:643. AQP9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei30 – 5021HelicalSequence AnalysisAdd
BLAST
Topological domaini51 – 544ExtracellularSequence Analysis
Transmembranei55 – 7521HelicalSequence AnalysisAdd
BLAST
Topological domaini76 – 11035CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei111 – 13121HelicalSequence AnalysisAdd
BLAST
Topological domaini132 – 15827ExtracellularSequence AnalysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 18910CytoplasmicSequence Analysis
Transmembranei190 – 21021HelicalSequence AnalysisAdd
BLAST
Topological domaini211 – 24535ExtracellularSequence AnalysisAdd
BLAST
Transmembranei246 – 26621HelicalSequence AnalysisAdd
BLAST
Topological domaini267 – 29529CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. integral component of membrane Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
  4. intracellular membrane-bounded organelle Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

MIMi602914. gene+phenotype.
PharmGKBiPA24927.

Polymorphism and mutation databases

BioMutaiAQP9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Aquaporin-9PRO_0000063964Add
BLAST

Proteomic databases

PaxDbiO43315.
PRIDEiO43315.

PTM databases

PhosphoSiteiO43315.

Expressioni

Tissue specificityi

Highly expressed in peripheral leukocytes. Also expressed in liver, lung, and spleen.

Gene expression databases

BgeeiO43315.
CleanExiHS_AQP9.
ExpressionAtlasiO43315. baseline and differential.
GenevestigatoriO43315.

Interactioni

Protein-protein interaction databases

BioGridi106861. 2 interactions.
STRINGi9606.ENSP00000219919.

Structurei

3D structure databases

ProteinModelPortaliO43315.
SMRiO43315. Positions 21-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 863NPA 1
Motifi216 – 2183NPA 2

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.
GeneTreeiENSGT00510000046311.
HOGENOMiHOG000288287.
HOVERGENiHBG106057.
InParanoidiO43315.
KOiK09877.
OMAiINVGFSM.
PhylomeDBiO43315.
TreeFamiTF313173.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR015685. Aquaporin_9.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PTHR19139:SF15. PTHR19139:SF15. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02021. AQUAPORIN9.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPEGAEKGK SFKQRLVLKS SLAKETLSEF LGTFILIVLG CGCVAQAILS
60 70 80 90 100
RGRFGGVITI NVGFSMAVAM AIYVAGGVSG GHINPAVSLA MCLFGRMKWF
110 120 130 140 150
KLPFYVGAQF LGAFVGAATV FGIYYDGLMS FAGGKLLIVG ENATAHIFAT
160 170 180 190 200
YPAPYLSLAN AFADQVVATM ILLIIVFAIF DSRNLGAPRG LEPIAIGLLI
210 220 230 240 250
IVIASSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFRAG NNFWWIPVVG
260 270 280 290
PLVGAVIGGL IYVLVIEIHH PEPDSVFKTE QSEDKPEKYE LSVIM
Length:295
Mass (Da):31,431
Last modified:January 11, 2011 - v2
Checksum:iB3B416CD9F1F9CAF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti279 – 2791T → A.3 Publications
Corresponds to variant rs1867380 [ dbSNP | Ensembl ].
VAR_024538

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008775 mRNA. Translation: BAA24864.1.
AF016495 mRNA. Translation: AAF16677.1.
AF102870 Genomic DNA. Translation: AAF27983.1.
AC025431 Genomic DNA. No translation available.
AC066616 Genomic DNA. No translation available.
BC026258 mRNA. Translation: AAH26258.1.
CCDSiCCDS10165.1.
PIRiJC5973.
RefSeqiNP_066190.2. NM_020980.3.
UniGeneiHs.104624.

Genome annotation databases

EnsembliENST00000219919; ENSP00000219919; ENSG00000103569.
ENST00000536493; ENSP00000441390; ENSG00000103569.
GeneIDi366.
KEGGihsa:366.
UCSCiuc002aez.2. human.

Polymorphism and mutation databases

BioMutaiAQP9.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008775 mRNA. Translation: BAA24864.1.
AF016495 mRNA. Translation: AAF16677.1.
AF102870 Genomic DNA. Translation: AAF27983.1.
AC025431 Genomic DNA. No translation available.
AC066616 Genomic DNA. No translation available.
BC026258 mRNA. Translation: AAH26258.1.
CCDSiCCDS10165.1.
PIRiJC5973.
RefSeqiNP_066190.2. NM_020980.3.
UniGeneiHs.104624.

3D structure databases

ProteinModelPortaliO43315.
SMRiO43315. Positions 21-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106861. 2 interactions.
STRINGi9606.ENSP00000219919.

Chemistry

GuidetoPHARMACOLOGYi696.

PTM databases

PhosphoSiteiO43315.

Polymorphism and mutation databases

BioMutaiAQP9.

Proteomic databases

PaxDbiO43315.
PRIDEiO43315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219919; ENSP00000219919; ENSG00000103569.
ENST00000536493; ENSP00000441390; ENSG00000103569.
GeneIDi366.
KEGGihsa:366.
UCSCiuc002aez.2. human.

Organism-specific databases

CTDi366.
GeneCardsiGC15P058430.
H-InvDBHIX0012281.
HGNCiHGNC:643. AQP9.
MIMi602914. gene+phenotype.
neXtProtiNX_O43315.
PharmGKBiPA24927.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0580.
GeneTreeiENSGT00510000046311.
HOGENOMiHOG000288287.
HOVERGENiHBG106057.
InParanoidiO43315.
KOiK09877.
OMAiINVGFSM.
PhylomeDBiO43315.
TreeFamiTF313173.

Enzyme and pathway databases

ReactomeiREACT_23809. Transport of glycerol from adipocytes to the liver by Aquaporins.
REACT_23826. Passive transport by Aquaporins.

Miscellaneous databases

GeneWikiiAQP9.
GenomeRNAii366.
NextBioi1527.
PROiO43315.
SOURCEiSearch...

Gene expression databases

BgeeiO43315.
CleanExiHS_AQP9.
ExpressionAtlasiO43315. baseline and differential.
GenevestigatoriO43315.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR015685. Aquaporin_9.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PTHR19139:SF15. PTHR19139:SF15. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02021. AQUAPORIN9.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-279.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANT ALA-279.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ALA-279.
    Tissue: Liver.

Entry informationi

Entry nameiAQP9_HUMAN
AccessioniPrimary (citable) accession number: O43315
Secondary accession number(s): Q9NP32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 11, 2011
Last modified: April 29, 2015
This is version 130 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.