AQP9_RAT
ID AQP9_RAT Reviewed; 295 AA.
AC P56627; O88815;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aquaporin-9;
DE Short=AQP-9;
DE AltName: Full=Aquaglyceroporin-9;
GN Name=Aqp9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=9733774; DOI=10.1074/jbc.273.38.24737;
RA Tsukaguchi H., Shayakul C., Berger U.V., MacKenzie B., Devidas S.,
RA Guggino W.B., van Hoek A.N., Hediger M.A.;
RT "Molecular characterization of a broad selectivity neutral solute
RT channel.";
RL J. Biol. Chem. 273:24737-24743(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10205677; DOI=10.1080/15216549900201333;
RA Ko S.B., Uchida S., Naruse S., Kuwahara M., Ishibashi K., Marumo F.,
RA Hayakawa T., Sasaki S.;
RT "Cloning and functional expression of rAQP9L a new member of aquaporin
RT family from rat liver.";
RL Biochem. Mol. Biol. Int. 47:309-318(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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:9733774}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by mercury ions and
CC phloretin. {ECO:0000269|PubMed:9733774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9733774};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in testis and liver. Detected in immature
CC spermatocytes and in interstitial Leydig cells.
CC {ECO:0000269|PubMed:9733774}.
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; AF016406; AAC36020.1; -; mRNA.
DR EMBL; AB013112; BAA33680.1; -; mRNA.
DR EMBL; BC085731; AAH85731.1; -; mRNA.
DR RefSeq; NP_075249.1; NM_022960.2.
DR RefSeq; XP_006243424.1; XM_006243362.1.
DR RefSeq; XP_008764558.1; XM_008766336.2.
DR AlphaFoldDB; P56627; -.
DR SMR; P56627; -.
DR STRING; 10116.ENSRNOP00000021442; -.
DR TCDB; 1.A.8.9.2; the major intrinsic protein (mip) family.
DR iPTMnet; P56627; -.
DR PhosphoSitePlus; P56627; -.
DR PaxDb; P56627; -.
DR Ensembl; ENSRNOT00000087980; ENSRNOP00000069377; ENSRNOG00000061883.
DR GeneID; 65054; -.
DR KEGG; rno:65054; -.
DR UCSC; RGD:68433; rat.
DR CTD; 366; -.
DR RGD; 68433; Aqp9.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000160582; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; P56627; -.
DR OMA; MTRTGMF; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P56627; -.
DR TreeFam; TF313173; -.
DR Reactome; R-RNO-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P56627; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000061883; Expressed in liver and 13 other tissues.
DR Genevisible; P56627; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:RGD.
DR GO; GO:0015837; P:amine transport; IDA:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; IDA:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015791; P:polyol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006863; P:purine nucleobase transport; IDA:UniProtKB.
DR GO; GO:0015855; P:pyrimidine nucleobase transport; IDA:UniProtKB.
DR GO; GO:0046689; P:response to mercury ion; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0006970; P:response to osmotic stress; TAS:UniProtKB.
DR GO; GO:0071918; P:urea transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; IDA:RGD.
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_0000063966"
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 CONFLICT 93
FT /note="A -> V (in Ref. 2; BAA33680)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="G -> S (in Ref. 2; BAA33680)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> P (in Ref. 2; BAA33680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 31871 MW; 09FD8B1DE936E61F CRC64;
MPSEKDGAKK SLMQRLALKS RIAKETLSEF LGTFIMIVLG CSSIAQAVLS RERFGGIITI
NIGFASAVVM ALYVTFGISG GHINPAVSFA MCAFGRMEWF KFPFYVGAQF LGAFVGAATV
FGIYYDGLMA FAGGKLLVVG ENATAFIFAT YPAPFISTPG AFVDQVVSTM FLLLIVFAMF
DSRNLGVPRG LEPVVIGLLI IVLSCSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFTVG
NNFWWIPVVG PMIGAFLGGL IYILFIQMHH SKLDPDMKAE PSENNLEKHE LSVIM
