AQP7_MOUSE
ID AQP7_MOUSE Reviewed; 303 AA.
AC O54794; Q8C630;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aquaporin-7;
DE Short=AQP-7;
DE AltName: Full=Aquaglyceroporin-7;
GN Name=Aqp7;
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=Testis;
RA Ishibashi K.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15591341; DOI=10.1073/pnas.0406230101;
RA Maeda N., Funahashi T., Hibuse T., Nagasawa A., Kishida K., Kuriyama H.,
RA Nakamura T., Kihara S., Shimomura I., Matsuzawa Y.;
RT "Adaptation to fasting by glycerol transport through aquaporin 7 in adipose
RT tissue.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17801-17806(2004).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15746100; DOI=10.1074/jbc.c500028200;
RA Hara-Chikuma M., Sohara E., Rai T., Ikawa M., Okabe M., Sasaki S.,
RA Uchida S., Verkman A.S.;
RT "Progressive adipocyte hypertrophy in aquaporin-7-deficient mice: adipocyte
RT glycerol permeability as a novel regulator of fat accumulation.";
RL J. Biol. Chem. 280:15493-15496(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15998844; DOI=10.1152/ajprenal.00133.2005;
RA Sohara E., Rai T., Miyazaki J., Verkman A.S., Sasaki S., Uchida S.;
RT "Defective water and glycerol transport in the proximal tubules of AQP7
RT knockout mice.";
RL Am. J. Physiol. 289:F1195-F1200(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16009937; DOI=10.1073/pnas.0503291102;
RA Hibuse T., Maeda N., Funahashi T., Yamamoto K., Nagasawa A., Mizunoya W.,
RA Kishida K., Inoue K., Kuriyama H., Nakamura T., Fushiki T., Kihara S.,
RA Shimomura I.;
RT "Aquaporin 7 deficiency is associated with development of obesity through
RT activation of adipose glycerol kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10993-10998(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17077387; DOI=10.1152/ajprenal.00314.2006;
RA Skowronski M.T., Lebeck J., Rojek A., Praetorius J., Fuechtbauer E.M.,
RA Froekiaer J., Nielsen S.;
RT "AQP7 is localized in capillaries of adipose tissue, cardiac and striated
RT muscle: implications in glycerol metabolism.";
RL Am. J. Physiol. 292:F956-F965(2007).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25643985; DOI=10.1016/j.febslet.2015.01.025;
RA Miyauchi T., Yamamoto H., Abe Y., Yoshida G.J., Rojek A., Sohara E.,
RA Uchida S., Nielsen S., Yasui M.;
RT "Dynamic subcellular localization of aquaporin-7 in white adipocytes.";
RL FEBS Lett. 589:608-614(2015).
CC -!- FUNCTION: Forms a channel that mediates water and glycerol transport
CC across cell membranes at neutral pH (PubMed:15591341, PubMed:15746100,
CC PubMed:16009937). The channel is also permeable to urea (By
CC similarity). Plays an important role in body energy homeostasis under
CC conditions that promote lipid catabolism, giving rise to glycerol and
CC free fatty acids (PubMed:15591341, PubMed:16009937). Mediates glycerol
CC export from adipocytes (PubMed:15591341, PubMed:15746100,
CC PubMed:16009937). After release into the blood stream, glycerol is used
CC for gluconeogenesis in the liver to maintain normal blood glucose
CC levels and prevent fasting hypoglycemia (PubMed:15591341). Required for
CC normal glycerol reabsorption in the kidney (PubMed:15998844,
CC PubMed:17077387). {ECO:0000250|UniProtKB:O14520,
CC ECO:0000269|PubMed:15591341, ECO:0000269|PubMed:15746100,
CC ECO:0000269|PubMed:15998844, ECO:0000269|PubMed:16009937,
CC ECO:0000269|PubMed:17077387}.
CC -!- SUBUNIT: Homotetramer. Interacts (via N-terminus) with PLIN1.
CC {ECO:0000250|UniProtKB:O14520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15746100,
CC ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:25643985}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:25643985}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25643985}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55087}. Lipid droplet
CC {ECO:0000269|PubMed:25643985}. Note=Internalized from the cell membrane
CC in response to catecholamine-induced activation of PKA; detected on
CC intracellular membranes and colocalizes with lipid droplets
CC (PubMed:25643985). Colocalizes with PLIN1 in adipocytes, probably on
CC lipid droplets (By similarity). {ECO:0000250|UniProtKB:O14520,
CC ECO:0000269|PubMed:25643985}.
CC -!- TISSUE SPECIFICITY: Detected in proximal tubules in kidney
CC (PubMed:15998844, PubMed:17077387). Detected in the capillary network
CC between muscle fibers in skeletal muscle and heart, and in spermatids
CC and on spermatozoa tails in testis and epididymis (PubMed:17077387).
CC Detected in white and brown adipose tissue, especially on small blood
CC vessels (at protein level) (PubMed:15591341, PubMed:17077387,
CC PubMed:25643985). Detected in kidney and white adipose tissue
CC (PubMed:15746100). {ECO:0000269|PubMed:15591341,
CC ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:15998844,
CC ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:25643985}.
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-Ala/Ser (NPA). {ECO:0000250|UniProtKB:P55064}.
CC -!- DISRUPTION PHENOTYPE: Young mutant mice appear normal and are fertile
CC (PubMed:16009937, PubMed:17077387). However, they start to become obese
CC after about 12 weeks and display enlarged adipocytes (PubMed:15746100,
CC PubMed:16009937). The effects on plasma glycerol levels vary between
CC experiments; some reports find no significant difference in plasma
CC glycerol levels in fed animals (PubMed:15746100, PubMed:15998844,
CC PubMed:17077387). Others report decreased plasma glycerol levels in fed
CC animals (PubMed:15591341). After fasting, mutant mice display lower
CC plasma glycerol levels than wild-type, and increased glycerol content
CC in their adipose tissue (PubMed:15591341, PubMed:16009937). After
CC fasting, mutant mice display lower blood glucose levels than wild-type
CC (PubMed:15591341). Mutant mice display strongly increased glycerol
CC levels in urine (PubMed:15998844, PubMed:17077387). Water permeability
CC of brush border membranes is slightly reduced, but urinary
CC concentrating ability is not altered (PubMed:15998844).
CC {ECO:0000269|PubMed:15591341, ECO:0000269|PubMed:15746100,
CC ECO:0000269|PubMed:15998844, ECO:0000269|PubMed:16009937,
CC ECO:0000269|PubMed:17077387}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB010100; BAA24537.1; -; mRNA.
DR EMBL; AK076642; BAC36431.1; -; mRNA.
DR EMBL; BC022223; AAH22223.1; -; mRNA.
DR CCDS; CCDS18055.1; -.
DR RefSeq; NP_031499.1; NM_007473.4.
DR RefSeq; XP_006537623.2; XM_006537560.3.
DR AlphaFoldDB; O54794; -.
DR SMR; O54794; -.
DR STRING; 10090.ENSMUSP00000030136; -.
DR iPTMnet; O54794; -.
DR PhosphoSitePlus; O54794; -.
DR jPOST; O54794; -.
DR PaxDb; O54794; -.
DR PRIDE; O54794; -.
DR ProteomicsDB; 273914; -.
DR DNASU; 11832; -.
DR Ensembl; ENSMUST00000030136; ENSMUSP00000030136; ENSMUSG00000028427.
DR Ensembl; ENSMUST00000054945; ENSMUSP00000093007; ENSMUSG00000028427.
DR GeneID; 11832; -.
DR KEGG; mmu:11832; -.
DR UCSC; uc008sif.1; mouse.
DR CTD; 364; -.
DR MGI; MGI:1314647; Aqp7.
DR VEuPathDB; HostDB:ENSMUSG00000028427; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000159054; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; O54794; -.
DR OMA; ACFPGRK; -.
DR OrthoDB; 1246320at2759; -.
DR PhylomeDB; O54794; -.
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; 11832; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Aqp7; mouse.
DR PRO; PR:O54794; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O54794; protein.
DR Bgee; ENSMUSG00000028427; Expressed in spermatid and 73 other tissues.
DR ExpressionAtlas; O54794; baseline and differential.
DR Genevisible; O54794; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; ISO:MGI.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; IMP:MGI.
DR GO; GO:0070295; P:renal water absorption; IGI:MGI.
DR GO; GO:0015840; P:urea transport; ISO:MGI.
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; IPR015686; Aquaporin_7.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR43829:SF15; PTHR43829:SF15; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Aquaporin-7"
FT /id="PRO_0000063959"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 42..51
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 72..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 76..83
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 84..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..133
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 134..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 174..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..204
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 205..206
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 207..220
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 221..303
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOTIF 79..81
FT /note="NPA 1"
FT MOTIF 211..213
FT /note="NPA 2"
FT SITE 120
FT /note="Important for permeability to glycerol"
FT /evidence="ECO:0000250|UniProtKB:O14520"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56403"
FT CONFLICT 180
FT /note="S -> R (in Ref. 2; BAC36431)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="D -> Y (in Ref. 2; BAC36431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 32667 MW; DC4C0A57FC61E575 CRC64;
MAPRSVLETI QSVLQKNMVR EFLAEFLSTY VMMVFGLGSV AHMVLGENSG SYLGVNLGFG
FGVTMGVHVA GGISGAHMNA AVTFTNCALG RMTWKKFPVY VLGQFLGSFS AAATTYLIFY
GAINHFAGGD LLVTGSKATA NIFATYLPEY MTLWRGFLDE AFVTGMLQLC LFAITDKKNS
PALQGTEPLV IGILVTVLGV SLGMNSGYAI NPSRDLPPRL FTFIAGWGKQ VFRAGNNWWW
VPVVAPLLGA YLGGIVYLGL IHPSIPQDPQ RLENFTARDQ KVTASYKNAA SANISGSVPL
EHF
