AQP9_MOUSE
ID AQP9_MOUSE Reviewed; 295 AA.
AC Q9JJJ3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aquaporin-9;
DE Short=AQP-9;
DE AltName: Full=Aquaglyceroporin-9;
GN Name=Aqp9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10777495; DOI=10.1074/jbc.m001119200;
RA Kishida K., Kuriyama H., Funahashi T., Shimomura I., Kihara S., Ouchi N.,
RA Nishida M., Nishizawa H., Masuda M., Takahashi M., Hotta K., Nakamura T.,
RA Yamashita S., Tochino Y., Matsuzawa Y.;
RT "Aquaporin adipose, a putative glycerol channel in adipocytes.";
RL J. Biol. Chem. 275:20896-20902(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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:0000250|UniProtKB:P56627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P56627};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P56627}.
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; AB037180; BAB03271.1; -; mRNA.
DR EMBL; AK050042; BAC34044.1; -; mRNA.
DR EMBL; AK050325; BAC34190.1; -; mRNA.
DR CCDS; CCDS23325.1; -.
DR RefSeq; NP_071309.1; NM_022026.3.
DR RefSeq; XP_006511394.1; XM_006511331.2.
DR RefSeq; XP_006511395.1; XM_006511332.3.
DR RefSeq; XP_011241084.1; XM_011242782.2.
DR RefSeq; XP_011241085.1; XM_011242783.1.
DR AlphaFoldDB; Q9JJJ3; -.
DR SMR; Q9JJJ3; -.
DR STRING; 10090.ENSMUSP00000074063; -.
DR iPTMnet; Q9JJJ3; -.
DR PhosphoSitePlus; Q9JJJ3; -.
DR jPOST; Q9JJJ3; -.
DR MaxQB; Q9JJJ3; -.
DR PaxDb; Q9JJJ3; -.
DR PRIDE; Q9JJJ3; -.
DR ProteomicsDB; 273915; -.
DR Antibodypedia; 53183; 146 antibodies from 26 providers.
DR DNASU; 64008; -.
DR Ensembl; ENSMUST00000074465; ENSMUSP00000074063; ENSMUSG00000032204.
DR Ensembl; ENSMUST00000113570; ENSMUSP00000109200; ENSMUSG00000032204.
DR GeneID; 64008; -.
DR KEGG; mmu:64008; -.
DR UCSC; uc009qov.2; mouse.
DR CTD; 366; -.
DR MGI; MGI:1891066; Aqp9.
DR VEuPathDB; HostDB:ENSMUSG00000032204; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000160582; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; Q9JJJ3; -.
DR OMA; MTRTGMF; -.
DR PhylomeDB; Q9JJJ3; -.
DR TreeFam; TF313173; -.
DR Reactome; R-MMU-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR BioGRID-ORCS; 64008; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Aqp9; mouse.
DR PRO; PR:Q9JJJ3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JJJ3; protein.
DR Bgee; ENSMUSG00000032204; Expressed in left lobe of liver and 73 other tissues.
DR ExpressionAtlas; Q9JJJ3; baseline and differential.
DR Genevisible; Q9JJJ3; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0015166; F:polyol transmembrane transporter activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0015837; P:amine transport; ISS:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; ISO:MGI.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015791; P:polyol transmembrane transport; ISS: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; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; ISS: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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="Aquaporin-9"
FT /id="PRO_0000063965"
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"
SQ SEQUENCE 295 AA; 31764 MW; E2C75A6DD45C35FD CRC64;
MPSEKDRAKK NLVQRLALKS CLAKETLSEF LGTFIMIVLG CGSIAQAVLS REKAGGIITI
NIGFATAVVM ALYATFGVSG GHINPAVSFA MCTFGRMEWF KFPFYVGAQL LGAFVGAATV
FGIYYDGLMA FADGKLLITG ENGTAFIFAT YPKPFVSVPG AFVDQVVSTM FLLLIVFAIF
DSRNLGVPRG LEPIVIGLLI IVISCSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFTFG
NNFWWIPVVG PMIGAVLGGL IYVLFIQMHH SNPDPEVKAE PAENNLEKHE LSVIM
