AQP6_MOUSE
ID AQP6_MOUSE Reviewed; 293 AA.
AC Q8C4A0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Aquaporin-6;
DE Short=AQP-6;
GN Name=Aqp6;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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-specific channel that participates in distinct
CC physiological functions such as glomerular filtration, tubular
CC endocytosis and acid-base metabolism. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AK082699; BAC38576.1; -; mRNA.
DR CCDS; CCDS27824.1; -.
DR RefSeq; NP_780296.1; NM_175087.4.
DR AlphaFoldDB; Q8C4A0; -.
DR SMR; Q8C4A0; -.
DR STRING; 10090.ENSMUSP00000023754; -.
DR GlyGen; Q8C4A0; 1 site.
DR PhosphoSitePlus; Q8C4A0; -.
DR PaxDb; Q8C4A0; -.
DR PRIDE; Q8C4A0; -.
DR ProteomicsDB; 296274; -.
DR Antibodypedia; 26099; 90 antibodies from 23 providers.
DR DNASU; 11831; -.
DR Ensembl; ENSMUST00000023754; ENSMUSP00000023754; ENSMUSG00000043144.
DR GeneID; 11831; -.
DR KEGG; mmu:11831; -.
DR UCSC; uc007xpw.1; mouse.
DR CTD; 363; -.
DR MGI; MGI:1341204; Aqp6.
DR VEuPathDB; HostDB:ENSMUSG00000043144; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000161949; -.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; Q8C4A0; -.
DR OMA; MAIQVTW; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q8C4A0; -.
DR TreeFam; TF312940; -.
DR BioGRID-ORCS; 11831; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q8C4A0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C4A0; protein.
DR Bgee; ENSMUSG00000043144; Expressed in cerebellar vermis and 57 other tissues.
DR ExpressionAtlas; Q8C4A0; baseline and differential.
DR Genevisible; Q8C4A0; MM.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IBA:GO_Central.
DR GO; GO:0015706; P:nitrate transmembrane transport; ISO:MGI.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0003097; P:renal water transport; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; IBA:GO_Central.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023254; Aquaporin_6.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR PANTHER; PTHR19139:SF113; PTHR19139:SF113; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02018; AQUAPORIN6.
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 Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..293
FT /note="Aquaporin-6"
FT /id="PRO_0000063956"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 79..81
FT /note="NPA 1"
FT MOTIF 193..195
FT /note="NPA 2"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 293 AA; 30709 MW; A48282992451ECEE CRC64;
MEPGLCSRAY LLVGGLWTAI SKALFAEFLA TGLYVFFGVG SVLPWPVALP SVLQIAITFN
LATATAVQIS WKTSGAHANP AVTLAYLVGS HISLPRAMAY IAAQLAGATA GAALLYGVTP
GGIRETLGVN VVHNSTSTGQ AVAVELVLTL QLVLCVFASM DGRQTLASPA AMIGTSVALG
HLIGIYFTGC SMNPARSFGP AVIVGKFAVH WIFWVGPLTG AVLASLIYNF ILFPDTKTVA
QRLAILVGTT KVEKVVDLEP QKKESQTNSE DTECLTSPCE EAVRSFSFTL GLC
