AQP11_HORSE
ID AQP11_HORSE Reviewed; 272 AA.
AC F6S3G9;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Aquaporin-11 {ECO:0000250|UniProtKB:Q8NBQ7};
GN Name=AQP11 {ECO:0000250|UniProtKB:Q8NBQ7};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred;
RX PubMed=19892987; DOI=10.1126/science.1178158;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
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).
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. In situation of stress, participates in endoplasmic
CC reticulum (ER) homeostasis by regulating redox homeostasis through the
CC transport of hydrogen peroxide across the endoplasmic reticulum
CC membrane thereby regulating the oxidative stress through the NADPH
CC oxidase 2 pathway (By similarity). Plays a role by maintaining an
CC environment suitable for translation or protein foldings in the ER
CC lumen namely by participating in the PKD1 glycosylation processing
CC resulting in regulation of PKD1 membrane trafficking thereby preventing
CC the accumulation of unfolding protein in ER. Plays a role in the
CC proximal tubule function by regulating its endosomal acidification. May
CC play a role in postnatal kidney development (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotrimer (By similarity). Can
CC also form homomultimer (By similarity). {ECO:0000250|UniProtKB:Q8BHH1,
CC ECO:0000250|UniProtKB:Q8NBQ7}.
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:0000250|UniProtKB:Q8NBQ7}; 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:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8BHH1}. 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: Expressed in retina specifically at retinal Mueller
CC glial cells. {ECO:0000269|PubMed:27107718}.
CC -!- DOMAIN: The NPC motif is essential for oligomerization and water
CC permeability function. {ECO:0000250|UniProtKB:Q8BHH1}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; F6S3G9; -.
DR SMR; F6S3G9; -.
DR STRING; 9796.ENSECAP00000015158; -.
DR PaxDb; F6S3G9; -.
DR Ensembl; ENSECAT00000018577; ENSECAP00000015158; ENSECAG00000017607.
DR VGNC; VGNC:55782; AQP11.
DR GeneTree; ENSGT00530000063816; -.
DR HOGENOM; CLU_074449_0_0_1; -.
DR InParanoid; F6S3G9; -.
DR TreeFam; TF320251; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000017607; Expressed in retina and 22 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS: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; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; IEA:Ensembl.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0032364; P:oxygen homeostasis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0072014; P:proximal tubule development; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..272
FT /note="Aquaporin-11"
FT /id="PRO_0000448835"
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..47
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..167
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..235
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT MOTIF 100..102
FT /note="NPC"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 217..219
FT /note="NPA"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
SQ SEQUENCE 272 AA; 30293 MW; DA3A2C4979FF9947 CRC64;
MTALRALWSE MQDTCTSLGL MLSVVLLAGL ARVVARQQQL HRPMAHAFVL EFLATLQLCC
CTHELLLLSE QEPAHPTWPL TLIYFFTLVH GLTLVGTSSN PCGVMMQMML GGMSPEMGAV
RLLAQLIGAL GSRYCIGALW SLGLTKYHVS ERSFACKNPI QVDLPKAVIV EALCSFIFHS
ALLNFQEVRP KLRIHLLAAL ITFLVYAGGS LTGAVFNPAL ALSLHFKCFD EAFLQFFIVY
WLAPSLGILL MILMFSFFLP WLYNNHTINK KE
