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   27-MAR-2024, entry version 155.
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; 9606-ENSP00000318770; -.
DR   PeptideAtlas; Q8NBQ7; -.
DR   ProteomicsDB; 72810; -.
DR   Antibodypedia; 48098; 122 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   AGR; HGNC:19940; -.
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; YCLAPSL; -.
DR   OrthoDB; 2875321at2759; -.
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; 12 hits in 1154 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 107 other cell types or tissues.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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: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:0032364; P:intracellular oxygen homeostasis; IEA:Ensembl.
DR   GO; GO:0009992; P:intracellular water homeostasis; IDA: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: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:0006833; P:water transport; IMP:UniProtKB.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023266; Aquaporin_11.
DR   InterPro; IPR016697; Aquaporin_11/12.
DR   InterPro; IPR000425; MIP.
DR   PANTHER; PTHR21191; AQUAPORIN; 1.
DR   PANTHER; PTHR21191:SF7; AQUAPORIN-11; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PIRSF; PIRSF017529; Aquaporin_11/12; 1.
DR   PRINTS; PR02024; AQUAPORIN11.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   Genevisible; Q8NBQ7; HS.
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
//