AQP9_HUMAN
ID AQP9_HUMAN Reviewed; 295 AA.
AC O43315; Q9NP32;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Aquaporin-9;
DE Short=AQP-9;
DE AltName: Full=Aquaglyceroporin-9;
DE AltName: Full=Small solute channel 1;
GN Name=AQP9; Synonyms=SSC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANT ALA-279.
RC TISSUE=Liver;
RX PubMed=9514918; DOI=10.1006/bbrc.1998.8252;
RA Ishibashi K., Kuwahara M., Gu Y., Tanaka Y., Marumo F., Sasaki S.;
RT "Cloning and functional expression of a new aquaporin (AQP9) abundantly
RT expressed in the peripheral leukocytes permeable to water and urea, but not
RT to glycerol.";
RL Biochem. Biophys. Res. Commun. 244:268-274(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANT ALA-279.
RX PubMed=10564231; DOI=10.1152/ajprenal.1999.277.5.f685;
RA Tsukaguchi H., Weremowicz S., Morton C.C., Hediger M.A.;
RT "Functional and molecular characterization of the human neutral solute
RT channel aquaporin-9.";
RL Am. J. Physiol. 277:F685-F696(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-279.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=30420639; DOI=10.1038/s41467-018-07176-z;
RA Gotfryd K., Mosca A.F., Missel J.W., Truelsen S.F., Wang K., Spulber M.,
RA Krabbe S., Helix-Nielsen C., Laforenza U., Soveral G., Pedersen P.A.,
RA Gourdon P.;
RT "Human adipose glycerol flux is regulated by a pH gate in AQP10.";
RL Nat. Commun. 9:4749-4749(2018).
CC -!- FUNCTION: Forms a water channel with a broad specificity. Also
CC permeable glycerol and urea. Mediates passage of a wide variety of
CC small, non-charged solutes including carbamides, polyols, purines, and
CC pyrimidines. {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:30420639,
CC ECO:0000269|PubMed:9514918}.
CC -!- INTERACTION:
CC O43315; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-17444777, EBI-10225815;
CC O43315; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-17444777, EBI-11957045;
CC O43315; P05090: APOD; NbExp=3; IntAct=EBI-17444777, EBI-715495;
CC O43315; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-17444777, EBI-9083477;
CC O43315; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17444777, EBI-12256978;
CC O43315; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-17444777, EBI-18013275;
CC O43315; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-17444777, EBI-12019274;
CC O43315; Q9BV81: EMC6; NbExp=3; IntAct=EBI-17444777, EBI-2820492;
CC O43315; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-17444777, EBI-12175685;
CC O43315; O75084: FZD7; NbExp=3; IntAct=EBI-17444777, EBI-746917;
CC O43315; P01350: GAST; NbExp=3; IntAct=EBI-17444777, EBI-3436637;
CC O43315; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-17444777, EBI-2867874;
CC O43315; P24593: IGFBP5; NbExp=3; IntAct=EBI-17444777, EBI-720480;
CC O43315; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-17444777, EBI-2820517;
CC O43315; P30301: MIP; NbExp=3; IntAct=EBI-17444777, EBI-8449636;
CC O43315; P09466: PAEP; NbExp=3; IntAct=EBI-17444777, EBI-465167;
CC O43315; Q9NRX5: SERINC1; NbExp=3; IntAct=EBI-17444777, EBI-2683145;
CC O43315; O95470: SGPL1; NbExp=3; IntAct=EBI-17444777, EBI-1046170;
CC O43315; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-17444777, EBI-10314552;
CC O43315; P02787: TF; NbExp=3; IntAct=EBI-17444777, EBI-714319;
CC O43315; Q9BVK6: TMED9; NbExp=3; IntAct=EBI-17444777, EBI-1056827;
CC O43315; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-17444777, EBI-1057733;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10564231,
CC ECO:0000269|PubMed:9514918}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral leukocytes. Also
CC expressed in liver, lung, and spleen. {ECO:0000269|PubMed:10564231,
CC ECO:0000269|PubMed:9514918}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). {ECO:0000250|UniProtKB:Q96PS8}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB008775; BAA24864.1; -; mRNA.
DR EMBL; AF016495; AAF16677.1; -; mRNA.
DR EMBL; AF102870; AAF27983.1; -; Genomic_DNA.
DR EMBL; AC025431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC066616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026258; AAH26258.1; -; mRNA.
DR CCDS; CCDS10165.1; -.
DR PIR; JC5973; JC5973.
DR RefSeq; NP_066190.2; NM_020980.4.
DR AlphaFoldDB; O43315; -.
DR SMR; O43315; -.
DR BioGRID; 106861; 42.
DR IntAct; O43315; 22.
DR STRING; 9606.ENSP00000219919; -.
DR BindingDB; O43315; -.
DR DrugBank; DB09462; Glycerin.
DR TCDB; 1.A.8.9.14; the major intrinsic protein (mip) family.
DR iPTMnet; O43315; -.
DR PhosphoSitePlus; O43315; -.
DR BioMuta; AQP9; -.
DR MassIVE; O43315; -.
DR PaxDb; O43315; -.
DR PeptideAtlas; O43315; -.
DR PRIDE; O43315; -.
DR ProteomicsDB; 48894; -.
DR Antibodypedia; 53183; 146 antibodies from 26 providers.
DR DNASU; 366; -.
DR Ensembl; ENST00000219919.9; ENSP00000219919.4; ENSG00000103569.10.
DR Ensembl; ENST00000536493.1; ENSP00000441390.1; ENSG00000103569.10.
DR GeneID; 366; -.
DR KEGG; hsa:366; -.
DR MANE-Select; ENST00000219919.9; ENSP00000219919.4; NM_020980.5; NP_066190.2.
DR UCSC; uc002aez.3; human.
DR CTD; 366; -.
DR DisGeNET; 366; -.
DR GeneCards; AQP9; -.
DR HGNC; HGNC:643; AQP9.
DR HPA; ENSG00000103569; Tissue enriched (liver).
DR MIM; 602914; gene+phenotype.
DR neXtProt; NX_O43315; -.
DR OpenTargets; ENSG00000103569; -.
DR PharmGKB; PA24927; -.
DR VEuPathDB; HostDB:ENSG00000103569; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000160582; -.
DR InParanoid; O43315; -.
DR OMA; MTRTGMF; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; O43315; -.
DR TreeFam; TF313173; -.
DR BioCyc; MetaCyc:ENSG00000103569-MON; -.
DR PathwayCommons; O43315; -.
DR Reactome; R-HSA-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; O43315; -.
DR SIGNOR; O43315; -.
DR BioGRID-ORCS; 366; 9 hits in 1061 CRISPR screens.
DR GeneWiki; AQP9; -.
DR GenomeRNAi; 366; -.
DR Pharos; O43315; Tbio.
DR PRO; PR:O43315; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O43315; protein.
DR Bgee; ENSG00000103569; Expressed in blood and 114 other tissues.
DR ExpressionAtlas; O43315; baseline and differential.
DR Genevisible; O43315; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; IDA:UniProtKB.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; IMP:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0015837; P:amine transport; ISS:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006863; P:purine nucleobase transport; ISS:UniProtKB.
DR GO; GO:0015855; P:pyrimidine nucleobase transport; ISS:UniProtKB.
DR GO; GO:0071918; P:urea transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006833; P:water transport; IDA:UniProtKB.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR015685; Aquaporin_9.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR43829:SF6; PTHR43829:SF6; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02021; AQUAPORIN9.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="Aquaporin-9"
FT /id="PRO_0000063964"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 49..54
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 76..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 80..93
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 94..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..124
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 125..158
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 180..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT INTRAMEM 210..228
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 229..245
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 267..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 84..86
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 216..218
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT VARIANT 279
FT /note="T -> A (in dbSNP:rs1867380)"
FT /evidence="ECO:0000269|PubMed:10564231,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9514918"
FT /id="VAR_024538"
SQ SEQUENCE 295 AA; 31431 MW; B3B416CD9F1F9CAF CRC64;
MQPEGAEKGK SFKQRLVLKS SLAKETLSEF LGTFILIVLG CGCVAQAILS RGRFGGVITI
NVGFSMAVAM AIYVAGGVSG GHINPAVSLA MCLFGRMKWF KLPFYVGAQF LGAFVGAATV
FGIYYDGLMS FAGGKLLIVG ENATAHIFAT YPAPYLSLAN AFADQVVATM ILLIIVFAIF
DSRNLGAPRG LEPIAIGLLI IVIASSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFRAG
NNFWWIPVVG PLVGAVIGGL IYVLVIEIHH PEPDSVFKTE QSEDKPEKYE LSVIM
