AQP11_HUMAN
ID AQP11_HUMAN Reviewed; 271 AA.
AC Q8NBQ7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aquaporin-11 {ECO:0000305|Ref.1};
DE Short=AQP-11 {ECO:0000305|Ref.1};
GN Name=AQP11 {ECO:0000312|HGNC:HGNC:19940}; Synonyms=AQPX1;
GN ORFNames=PSEC0027;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 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 [5]
RP SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND MUTAGENESIS OF CYS-227.
RX PubMed=24918044; DOI=10.1016/j.fob.2014.03.005;
RA Takahashi S., Muta K., Sonoda H., Kato A., Abdeen A., Ikeda M.;
RT "The role of Cysteine 227 in subcellular localization, water permeability,
RT and multimerization of aquaporin-11.";
RL FEBS Open Bio 4:315-320(2014).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24845055; DOI=10.1002/oby.20792;
RA Madeira A., Fernandez-Veledo S., Camps M., Zorzano A., Moura T.F.,
RA Ceperuelo-Mallafre V., Vendrell J., Soveral G.;
RT "Human aquaporin-11 is a water and glycerol channel and localizes in the
RT vicinity of lipid droplets in human adipocytes.";
RL Obesity 22:2010-2017(2014).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28042826; DOI=10.3390/ijms18010066;
RA Laforenza U., Pellavio G., Marchetti A.L., Omes C., Todaro F., Gastaldi G.;
RT "Aquaporin-Mediated Water and Hydrogen Peroxide Transport Is Involved in
RT Normal Human Spermatozoa Functioning.";
RL Int. J. Mol. Sci. 18:0-0(2016).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, FUNCTION, AND NOT GLYCOSYLATED.
RX PubMed=31546170; DOI=10.1016/j.redox.2019.101326;
RA Bestetti S., Galli M., Sorrentino I., Pinton P., Rimessi A., Sitia R.,
RA Medrano-Fernandez I.;
RT "Human aquaporin-11 guarantees efficient transport of H2O2 across the
RT endoplasmic reticulum membrane.";
RL Redox Biol. 28:101326-101326(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:24845055, PubMed:24918044, PubMed:31546170).
CC In situation of stress, participates in endoplasmic reticulum (ER)
CC homeostasis by regulating redox homeostasis through the transport of
CC hydrogen peroxide across the endoplasmic reticulum membrane thereby
CC regulating the oxidative stress through the NADPH oxidase 2 pathway
CC (PubMed:31546170). 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 (By similarity). Plays a role
CC in the proximal tubule function by regulating its endosomal
CC acidification (By similarity). May play a role in postnatal kidney
CC development (By similarity). {ECO:0000250|UniProtKB:Q8BHH1,
CC ECO:0000269|PubMed:24845055, ECO:0000269|PubMed:24918044,
CC ECO:0000269|PubMed:31546170}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Can also form
CC homomultimer (PubMed:24918044, PubMed:31546170).
CC {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000269|PubMed:24918044,
CC ECO:0000269|PubMed:31546170}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:28042826}; Multi-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24918044, ECO:0000269|PubMed:31546170}; Multi-pass
CC membrane protein. Cell membrane; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24918044}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery
CC of lipid droplets (PubMed:24845055). it accumulates partly in
CC mitochondrial-associated endoplasmic reticulum membranes
CC (PubMed:31546170). {ECO:0000269|PubMed:24845055,
CC ECO:0000269|PubMed:31546170}.
CC -!- TISSUE SPECIFICITY: Detected in the sperm head and tail (at protein
CC level) (PubMed:28042826). Expressed in subcutaneous adipocytes
CC (PubMed:24845055). Expressed in testis, kidney and ejaculated
CC spermatozoa (PubMed:19812234). {ECO:0000269|PubMed:19812234,
CC ECO:0000269|PubMed:24845055, ECO:0000269|PubMed:28042826}.
CC -!- DOMAIN: The NPC motif is essential for oligomerization and water
CC permeability function. {ECO:0000250|UniProtKB:Q8BHH1}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:31546170}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12
CC subfamily. {ECO:0000305}.
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DR EMBL; AB028147; BAC45004.1; -; mRNA.
DR EMBL; AK075346; BAC11558.1; -; mRNA.
DR EMBL; BC040443; AAH40443.1; -; mRNA.
DR CCDS; CCDS8251.1; -.
DR RefSeq; NP_766627.1; NM_173039.2.
DR AlphaFoldDB; Q8NBQ7; -.
DR SMR; Q8NBQ7; -.
DR BioGRID; 129399; 1.
DR IntAct; Q8NBQ7; 1.
DR STRING; 9606.ENSP00000318770; -.
DR TCDB; 1.A.8.4.1; the major intrinsic protein (mip) family.
DR BioMuta; AQP11; -.
DR DMDM; 47115841; -.
DR MassIVE; Q8NBQ7; -.
DR MaxQB; Q8NBQ7; -.
DR PaxDb; Q8NBQ7; -.
DR PeptideAtlas; Q8NBQ7; -.
DR PRIDE; Q8NBQ7; -.
DR ProteomicsDB; 72810; -.
DR Antibodypedia; 48098; 111 antibodies from 26 providers.
DR DNASU; 282679; -.
DR Ensembl; ENST00000313578.4; ENSP00000318770.3; ENSG00000178301.4.
DR GeneID; 282679; -.
DR KEGG; hsa:282679; -.
DR MANE-Select; ENST00000313578.4; ENSP00000318770.3; NM_173039.3; NP_766627.1.
DR UCSC; uc001oyj.4; human.
DR CTD; 282679; -.
DR DisGeNET; 282679; -.
DR GeneCards; AQP11; -.
DR HGNC; HGNC:19940; AQP11.
DR HPA; ENSG00000178301; Tissue enhanced (intestine, liver).
DR MIM; 609914; gene.
DR neXtProt; NX_Q8NBQ7; -.
DR OpenTargets; ENSG00000178301; -.
DR PharmGKB; PA134949682; -.
DR VEuPathDB; HostDB:ENSG00000178301; -.
DR eggNOG; ENOG502S15B; Eukaryota.
DR GeneTree; ENSGT00530000063816; -.
DR HOGENOM; CLU_074449_0_0_1; -.
DR InParanoid; Q8NBQ7; -.
DR OMA; CTNELSL; -.
DR OrthoDB; 1086803at2759; -.
DR PhylomeDB; Q8NBQ7; -.
DR TreeFam; TF320251; -.
DR PathwayCommons; Q8NBQ7; -.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; Q8NBQ7; -.
DR BioGRID-ORCS; 282679; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; AQP11; human.
DR GenomeRNAi; 282679; -.
DR Pharos; Q8NBQ7; Tbio.
DR PRO; PR:Q8NBQ7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NBQ7; protein.
DR Bgee; ENSG00000178301; Expressed in jejunal mucosa and 105 other tissues.
DR Genevisible; Q8NBQ7; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
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; 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; ISS: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; IMP:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; IEA:Ensembl.
DR GO; GO:0015793; P:glycerol transmembrane transport; IMP:UniProtKB.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IMP:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0072014; P:proximal tubule development; ISS:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; IDA:UniProtKB.
DR GO; GO:0006833; P:water transport; IMP: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 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_0000063968"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 15..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..41
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 75..95
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..163
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 195..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..234
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31546170"
FT TRANSMEM 235..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31546170"
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 VARIANT 102
FT /note="G -> S (in dbSNP:rs2276415)"
FT /id="VAR_020446"
FT MUTAGEN 227
FT /note="C->A: Does not affect endoplasmic reticulum
FT localization. Does not affect trafficking to the plasma
FT membrane. Increases osmotic water permeability. Decreases
FT homomultimerization."
FT /evidence="ECO:0000269|PubMed:24918044"
FT MUTAGEN 227
FT /note="C->S: Does not affect endoplasmic reticulum
FT localization. Does not affect trafficking to the plasma
FT membrane. Reduces protein expression. Increases osmotic
FT water permeability."
FT /evidence="ECO:0000269|PubMed:24918044"
SQ SEQUENCE 271 AA; 30203 MW; C4CB292B544C5A40 CRC64;
MSPLLGLRSE LQDTCTSLGL MLSVVLLMGL ARVVARQQLH RPVAHAFVLE FLATFQLCCC
THELQLLSEQ HPAHPTWTLT LVYFFSLVHG LTLVGTSSNP CGVMMQMMLG GMSPETGAVR
LLAQLVSALC SRYCTSALWS LGLTQYHVSE RSFACKNPIR VDLLKAVITE AVCSFLFHSA
LLHFQEVRTK LRIHLLAALI TFLVYAGGSL TGAVFNPALA LSLHFMCFDE AFPQFFIVYW
LAPSLGILLM ILMFSFFLPW LHNNHTINKK E
