AQP11_MOUSE
ID AQP11_MOUSE Reviewed; 271 AA.
AC Q8BHH1; Q8JZU1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Aquaporin-11 {ECO:0000305|Ref.1};
DE Short=AQP-11 {ECO:0000305|Ref.1};
GN Name=Aqp11 {ECO:0000312|MGI:MGI:1913583};
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.;
RT "Cloning of a new superfamily of aquaporin.";
RL Submitted (MAY-1999) 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 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 [4]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16107722; DOI=10.1128/mcb.25.17.7770-7779.2005;
RA Morishita Y., Matsuzaki T., Hara-chikuma M., Andoo A., Shimono M.,
RA Matsuki A., Kobayashi K., Ikeda M., Yamamoto T., Verkman A., Kusano E.,
RA Ookawara S., Takata K., Sasaki S., Ishibashi K.;
RT "Disruption of aquaporin-11 produces polycystic kidneys following
RT vacuolization of the proximal tubule.";
RL Mol. Cell. Biol. 25:7770-7779(2005).
RN [5]
RP FUNCTION.
RX PubMed=18606867; DOI=10.1096/fj.08-111872;
RA Okada S., Misaka T., Tanaka Y., Matsumoto I., Ishibashi K., Sasaki S.,
RA Abe K.;
RT "Aquaporin-11 knockout mice and polycystic kidney disease animals share a
RT common mechanism of cyst formation.";
RL FASEB J. 22:3672-3684(2008).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND MUTAGENESIS OF CYS-227.
RX PubMed=18701606; DOI=10.1681/asn.2008030296;
RA Tchekneva E.E., Khuchua Z., Davis L.S., Kadkina V., Dunn S.R., Bachman S.,
RA Ishibashi K., Rinchik E.M., Harris R.C., Dikov M.M., Breyer M.D.;
RT "Single amino acid substitution in aquaporin 11 causes renal failure.";
RL J. Am. Soc. Nephrol. 19:1955-1964(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=19812234; DOI=10.1530/rep-09-0298;
RA Yeung C.H., Cooper T.G.;
RT "Aquaporin AQP11 in the testis: molecular identity and association with the
RT processing of residual cytoplasm of elongated spermatids.";
RL Reproduction 139:209-216(2010).
RN [9]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-101, SUBUNIT, AND FUNCTION.
RX PubMed=21118806; DOI=10.1074/jbc.m110.180968;
RA Ikeda M., Andoo A., Shimono M., Takamatsu N., Taki A., Muta K.,
RA Matsushita W., Uechi T., Matsuzaki T., Kenmochi N., Takata K., Sasaki S.,
RA Ito K., Ishibashi K.;
RT "The NPC motif of aquaporin-11, unlike the NPA motif of known aquaporins,
RT is essential for full expression of molecular function.";
RL J. Biol. Chem. 286:3342-3350(2011).
RN [10]
RP FUNCTION.
RX PubMed=21251984; DOI=10.1016/j.jsb.2011.01.003;
RA Yakata K., Tani K., Fujiyoshi Y.;
RT "Water permeability and characterization of aquaporin-11.";
RL J. Struct. Biol. 174:315-320(2011).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23275615; DOI=10.1152/ajpgi.00208.2012;
RA Rojek A., Fuechtbauer E.M., Fuechtbauer A., Jelen S., Malmendal A.,
RA Fenton R.A., Nielsen S.;
RT "Liver-specific Aquaporin 11 knockout mice show rapid vacuolization of the
RT rough endoplasmic reticulum in periportal hepatocytes after amino acid
RT feeding.";
RL Am. J. Physiol. 304:G501-G515(2013).
RN [12]
RP TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF ASN-99; GLY-102 AND CYS-227,
RP AND FUNCTION.
RX PubMed=23486012; DOI=10.1152/ajprenal.00344.2012;
RA Atochina-Vasserman E.N., Biktasova A., Abramova E., Cheng D.S.,
RA Polosukhin V.V., Tanjore H., Takahashi S., Sonoda H., Foye L., Venkov C.,
RA Ryzhov S.V., Novitskiy S., Shlonimskaya N., Ikeda M., Blackwell T.S.,
RA Lawson W.E., Gow A.J., Harris R.C., Dikov M.M., Tchekneva E.E.;
RT "Aquaporin 11 insufficiency modulates kidney susceptibility to oxidative
RT stress.";
RL Am. J. Physiol. 304:F1295-F1307(2013).
RN [13]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24854278; DOI=10.1681/asn.2013060614;
RA Inoue Y., Sohara E., Kobayashi K., Chiga M., Rai T., Ishibashi K.,
RA Horie S., Su X., Zhou J., Sasaki S., Uchida S.;
RT "Aberrant glycosylation and localization of polycystin-1 cause polycystic
RT kidney in an AQP11 knockout model.";
RL J. Am. Soc. Nephrol. 25:2789-2799(2014).
RN [14]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27258268; DOI=10.3390/ijms17060861;
RA Koike S., Tanaka Y., Matsuzaki T., Morishita Y., Ishibashi K.;
RT "Aquaporin-11 (AQP11) Expression in the Mouse Brain.";
RL Int. J. Mol. Sci. 17:0-0(2016).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=27107718; DOI=10.1186/s12974-016-0554-2;
RA Deeg C.A., Amann B., Lutz K., Hirmer S., Lutterberg K., Kremmer E.,
RA Hauck S.M.;
RT "Aquaporin 11, a regulator of water efflux at retinal Mueller glial cell
RT surface decreases concomitant with immune-mediated gliosis.";
RL J. Neuroinflamm. 13:89-89(2016).
RN [16]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27582095; DOI=10.1152/ajprenal.00065.2016;
RA Ruetzler M., Rojek A., Damgaard M.V., Andreasen A., Fenton R.A.,
RA Nielsen S.;
RT "Temporal deletion of Aqp11 in mice is linked to the severity of cyst-like
RT disease.";
RL Am. J. Physiol. 312:F343-F351(2017).
RN [17]
RP FUNCTION.
RX PubMed=30656220; DOI=10.1016/j.bbrep.2019.01.003;
RA Hoshino Y., Sonoda H., Nishimura R., Mori K., Ishibashi K., Ikeda M.;
RT "Involvement of the NADPH oxidase 2 pathway in renal oxidative stress in
RT Aqp11-/- mice.";
RL Biochem. Biophys. Rep. 17:169-176(2019).
CC -!- FUNCTION: Channel protein that facilitates the transport of water,
CC glycerol and hydrogen peroxide across membrane of cell or organelles
CC guaranteeing intracellular homeostasis in several organes like liver,
CC kidney and brain (PubMed:21118806, PubMed:21251984). In situation of
CC stress, participates in endoplasmic reticulum (ER) homeostasis by
CC regulating redox homeostasis through the transport of hydrogen peroxide
CC across the endoplasmic reticulum membrane thereby regulating the
CC oxidative stress through the NADPH oxidase 2 pathway (PubMed:23275615,
CC PubMed:30656220). Plays a role by maintaining an environment suitable
CC for translation or protein foldings in the ER lumen namely by
CC participating in the PKD1 glycosylation processing resulting in
CC regulation of PKD1 membrane trafficking thereby preventing the
CC accumulation of unfolding protein in ER (PubMed:24854278,
CC PubMed:18606867). Plays a role in the proximal tubule function by
CC regulating its endosomal acidification (PubMed:16107722). May play a
CC role in postnatal kidney development (PubMed:18701606, PubMed:23486012,
CC PubMed:27582095). {ECO:0000269|PubMed:16107722,
CC ECO:0000269|PubMed:18606867, ECO:0000269|PubMed:18701606,
CC ECO:0000269|PubMed:21118806, ECO:0000269|PubMed:21251984,
CC ECO:0000269|PubMed:23275615, ECO:0000269|PubMed:23486012,
CC ECO:0000269|PubMed:24854278, ECO:0000269|PubMed:27582095,
CC ECO:0000269|PubMed:30656220}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:16107722,
CC PubMed:21118806). Can also form homomultimer (PubMed:21118806).
CC {ECO:0000269|PubMed:16107722, ECO:0000269|PubMed:21118806}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16107722, ECO:0000269|PubMed:21118806,
CC ECO:0000269|PubMed:24854278}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm
CC {ECO:0000269|PubMed:16107722}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16107722}. Note=Localizes mainly to the periphery
CC of lipid droplets. it accumulates partly in mitochondrial-associated
CC endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the S1 proximal tubule segment,
CC (PubMed:23486012). Expressed in the testis, kidney, and liver. Weakly
CC expressed in the heart, brain, and muscle. Highly expressed in the
CC testis. Expressed in the proximal tubule of the cortex of 8-day-old
CC mouse kidney (PubMed:16107722). Expressed in retina specifically at
CC retinal Mueller glial cells (PubMed:27107718). Expressed in brain.
CC Expressed abundantly at the choroid plexus but also expressed weakly in
CC the parenchyma. Expressed at the capillary endothelium in the cerebral
CC white matter (PubMed:27258268). Expressed in adult testis, in the
CC elongated spermatids (ES) and in residual bodies inside Sertoli cells
CC (PubMed:19812234). {ECO:0000269|PubMed:16107722,
CC ECO:0000269|PubMed:19812234, ECO:0000269|PubMed:23486012,
CC ECO:0000269|PubMed:27107718, ECO:0000269|PubMed:27258268}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed at the brain surface with a
CC slight expression in the brain parenchyma at postnatal day 1, 7, and
CC 14. At the stage of postnatal day 28, mainly expressed in the
CC parenchyma. {ECO:0000269|PubMed:27258268}.
CC -!- INDUCTION: Increased by glucose (PubMed:23486012). Decreased by
CC phlorizin (PubMed:23486012). {ECO:0000269|PubMed:23486012}.
CC -!- DOMAIN: The NPC motif is essential for oligomerization and water
CC permeability function. {ECO:0000269|PubMed:21118806}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- DISRUPTION PHENOTYPE: Homozygous Aqp11 knockout mice are born normally
CC at the expected Mendelian frequency and are normal. However, after 15
CC days mice begin dying, and only 15% survive until day 60. Mice exhibit
CC severe renal dysfunction with a significant increase of blood urea
CC nitrogen (BUN) level. The kidneys are large and pale with rough texture
CC occupying the whole abdominal cavity. The kidneys are anemic and
CC polycystic following swelling and vacuolization of the proximal tubule
CC (PubMed:18701606, PubMed:16107722). Mice with conditional knockout of
CC Aqp11 in liver appear to have a normal life span of more than 1 year,
CC are fertile (both females and males), show a normal growth rate, and do
CC not show any behavioral abnormalities. Unchallenged mice have normal
CC longevity, their livers appear normal, and reveal only a minor defect
CC in lipid handling. In contrast, rough endoplasmic reticulum (RER)-
CC derived vacuoles develop rapidly in the periportal hepatocytes of
CC liver-specific following 24 h fasting and refeeding (PubMed:23275615).
CC Mice with temporal conditional knockout of Aqp11 between post natal
CC days (P) P2 and P12 exhibit apparently normal kidneys at birth and
CC within the first two postnatal weeks of life exhibit tubular dilations.
CC When conditional knockout of Aqp11 is induced until P8, proximal tubule
CC (PT) cell vacuolization and apparent tubular cysts are formed, whereas
CC no deficient renal development are observed if conditional knockout of
CC Aqp11 starts at P12 (PubMed:27582095). {ECO:0000269|PubMed:16107722,
CC ECO:0000269|PubMed:18701606, ECO:0000269|PubMed:23275615,
CC ECO:0000269|PubMed:27582095}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37088.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB028148; BAC45005.1; -; mRNA.
DR EMBL; AK075757; BAC35935.1; -; mRNA.
DR EMBL; BC037088; AAH37088.1; ALT_INIT; mRNA.
DR CCDS; CCDS21463.1; -.
DR RefSeq; NP_780314.1; NM_175105.3.
DR AlphaFoldDB; Q8BHH1; -.
DR SMR; Q8BHH1; -.
DR STRING; 10090.ENSMUSP00000082054; -.
DR SwissPalm; Q8BHH1; -.
DR jPOST; Q8BHH1; -.
DR PaxDb; Q8BHH1; -.
DR PRIDE; Q8BHH1; -.
DR ProteomicsDB; 282007; -.
DR Antibodypedia; 48098; 111 antibodies from 26 providers.
DR DNASU; 66333; -.
DR Ensembl; ENSMUST00000206389; ENSMUSP00000146215; ENSMUSG00000042797.
DR GeneID; 66333; -.
DR KEGG; mmu:66333; -.
DR UCSC; uc009ijs.1; mouse.
DR CTD; 282679; -.
DR MGI; MGI:1913583; Aqp11.
DR VEuPathDB; HostDB:ENSMUSG00000042797; -.
DR eggNOG; ENOG502S15B; Eukaryota.
DR GeneTree; ENSGT00530000063816; -.
DR HOGENOM; CLU_074449_0_0_1; -.
DR InParanoid; Q8BHH1; -.
DR OMA; CTNELSL; -.
DR OrthoDB; 1086803at2759; -.
DR PhylomeDB; Q8BHH1; -.
DR TreeFam; TF320251; -.
DR Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR BioGRID-ORCS; 66333; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Aqp11; mouse.
DR PRO; PR:Q8BHH1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BHH1; protein.
DR Bgee; ENSMUSG00000042797; Expressed in spermatid and 202 other tissues.
DR ExpressionAtlas; Q8BHH1; baseline and differential.
DR Genevisible; Q8BHH1; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015267; F:channel activity; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; IDA:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; IMP:MGI.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; IMP:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0072014; P:proximal tubule development; IMP:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; ISO:MGI.
DR GO; GO:0006833; P:water transport; IDA:MGI.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023266; Aquaporin_11.
DR InterPro; IPR016697; Aquaporin_11/12.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR21191:SF7; PTHR21191:SF7; 1.
DR Pfam; PF00230; MIP; 1.
DR PIRSF; PIRSF017529; Aquaporin_11/12; 1.
DR PRINTS; PR02024; AQUAPORIN11.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Aquaporin-11"
FT /id="PRO_0000063969"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..41
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..166
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT MOTIF 99..101
FT /note="NPC"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 216..218
FT /note="NPA"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MUTAGEN 99
FT /note="N->D: Reduces oligomerization."
FT /evidence="ECO:0000269|PubMed:23486012"
FT MUTAGEN 101
FT /note="C->A: Does not affect endoplasmic reticulum
FT localization. Does not affect plama membrane localization.
FT Reduces oligomerization. Impairs water permeability."
FT /evidence="ECO:0000269|PubMed:21118806"
FT MUTAGEN 102
FT /note="G->V: Does not affect oligomerization formation."
FT /evidence="ECO:0000269|PubMed:23486012"
FT MUTAGEN 227
FT /note="C->S: Homozygous sudden juvenile death syndrome
FT (sjds) mice die before 20 day of age and exhibit severe
FT proximal tubule injury and formation of giant vacuoles in
FT the renal cortex. Interfers with maintenance of AQP11
FT oligomeric structure. Aqp11 mutant mice developed proximal
FT tubule (PT)-specific mitochondrial injury. Heterozygous
FT sudden juvenile death syndrome (sjds) mice exhibit higher
FT AQP11 levels but are not further increased in response to
FT glucose. Upon glucose treatment, heterozygous Aqp11 mice
FT show increased blood urea nitrogen levels that are
FT prevented by the antioxidant sulforaphane or by phlorizin."
FT /evidence="ECO:0000269|PubMed:18701606"
SQ SEQUENCE 271 AA; 30481 MW; 1E88F989B3889226 CRC64;
MSALLGLRPE VQDTCISLGL MLLFVLFVGL ARVIARQQLH RPVVHAFVLE FLATFQLCCC
THELQVLSEQ DSAHPTWTLT LIYFFSLVHG LTLVGTASNP CGVMMQMILG GMSPEMGAVR
LLAQLVSALC SRYCISALWS LSLTKYHYDE RILACRNPIH TDMSKAIIIE AICSFIFHSA
LLHFQEVRTK LRIHLLAALI TFLAYAGGSL TGALFNPALA LSLHFPCFDE LFYKFFVVYW
LAPSVGVLMM ILMFSFFLPW LHNNQMTNKK E
