ID   AQP10_HUMAN             Reviewed;         301 AA.
AC   Q96PS8; Q5VYD3; Q5VYD4; Q8NG70;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   02-SEP-2026, entry version 180.
DE   RecName: Full=Aquaporin-10 {ECO:0000305|PubMed:11573934, ECO:0000305|PubMed:12084581};
DE            Short=AQP-10;
DE   AltName: Full=Aquaglyceroporin-10 {ECO:0000303|PubMed:12084581};
DE   AltName: Full=Small intestine aquaporin {ECO:0000303|PubMed:11573934};
GN   Name=AQP10 {ECO:0000312|HGNC:HGNC:16029};
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] (ISOFORM 2), FUNCTION, TRANSPORTER ACTIVITY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CAUTION (ISOFORM 2).
RC   TISSUE=Jejunum;
RX   PubMed=11573934; DOI=10.1006/bbrc.2001.5661;
RA   Hatakeyama S., Yoshida Y., Tani T., Koyama Y., Nihei K., Ohshiro K.,
RA   Kamiie J., Yaoita E., Suda T., Hatakeyama K., Yamamoto T.;
RT   "Cloning of a new aquaporin (AQP10) abundantly expressed in duodenum and
RT   jejunum.";
RL   Biochem. Biophys. Res. Commun. 287:814-819(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12084581; DOI=10.1016/s0167-4781(02)00393-7;
RA   Ishibashi K., Morinaga T., Kuwahara M., Sasaki S., Imai M.;
RT   "Cloning and identification of a new member of water channel (AQP10) as an
RT   aquaglyceroporin.";
RL   Biochim. Biophys. Acta 1576:335-340(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15221416; DOI=10.1007/s00418-004-0657-1;
RA   Mobasheri A., Shakibaei M., Marples D.;
RT   "Immunohistochemical localization of aquaporin 10 in the apical membranes
RT   of the human ileum: a potential pathway for luminal water and small solute
RT   absorption.";
RL   Histochem. Cell Biol. 121:463-471(2004).
RN   [6]
RP   FUNCTION, TRANSPORTER ACTIVITY, GLYCOSYLATION AT ASN-133, MISCELLANEOUS,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF ASN-133.
RX   PubMed=21733844; DOI=10.1074/jbc.m111.242677;
RA   Oeberg F., Sjoehamn J., Fischer G., Moberg A., Pedersen A., Neutze R.,
RA   Hedfalk K.;
RT   "Glycosylation increases the thermostability of human aquaporin 10
RT   protein.";
RL   J. Biol. Chem. 286:31915-31923(2011).
RN   [7]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=23382902; DOI=10.1371/journal.pone.0054474;
RA   Laforenza U., Scaffino M.F., Gastaldi G.;
RT   "Aquaporin-10 represents an alternative pathway for glycerol efflux from
RT   human adipocytes.";
RL   PLoS ONE 8:E54474-E54474(2013).
RN   [8] {ECO:0007744|PDB:6F7H}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, TRANSPORTER ACTIVITY,
RP   ACTIVITY REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DOMAIN, SITE,
RP   AND MUTAGENESIS OF GLU-27; GLY-73; SER-77; HIS-80; PHE-85 AND ARG-94.
RX   PubMed=30420639; DOI=10.1038/s41467-018-07176-z;
RA   Gotfryd K., Mosca A.F., Missel J.W., Truelsen S.F., Wang K., Spulber M.,
RA   Krabbe S., Helix-Nielsen C., Laforenza U., Soveral G., Pedersen P.A.,
RA   Gourdon P.;
RT   "Human adipose glycerol flux is regulated by a pH gate in AQP10.";
RL   Nat. Commun. 9:4749-4749(2018).
CC   -!- FUNCTION: Aquaglyceroporins form homotetrameric transmembrane channels,
CC       with each monomer independently mediating glycerol and water transport
CC       across the plasma membrane along their osmotic gradient
CC       (PubMed:11573934, PubMed:12084581, PubMed:21733844, PubMed:23382902,
CC       PubMed:30420639). Could also be permeable to urea (PubMed:12084581).
CC       Among aquaglyceroporins, it exhibits a unique pH-gated glycerol
CC       transport activity, being more active at acidic pH. It most likely
CC       plays a central role in the efflux of glycerol formed during
CC       triglyceride hydrolysis in adipocytes and in glycerol uptake by
CC       enterocytes, as both processes occur and are stimulated at acidic pH
CC       (PubMed:11573934, PubMed:23382902, PubMed:30420639).
CC       {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581,
CC       ECO:0000269|PubMed:21733844, ECO:0000269|PubMed:23382902,
CC       ECO:0000269|PubMed:30420639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC         ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:12084581,
CC         ECO:0000269|PubMed:21733844, ECO:0000269|PubMed:23382902,
CC         ECO:0000269|PubMed:30420639};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC         Evidence={ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581,
CC         ECO:0000269|PubMed:21733844, ECO:0000269|PubMed:23382902,
CC         ECO:0000269|PubMed:30420639};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC         Evidence={ECO:0000305|PubMed:12084581};
CC   -!- ACTIVITY REGULATION: Glycerol transport is regulated by pH, with the
CC       porin being permeable to glycerol at pH 5.5 but not at pH 7.4
CC       (PubMed:30420639). Water permeability, however, is not influenced by
CC       pH. {ECO:0000269|PubMed:30420639}.
CC   -!- SUBUNIT: Homotetramer; each monomer provides an independent
CC       glycerol/water pore. {ECO:0000269|PubMed:30420639}.
CC   -!- INTERACTION:
CC       Q96PS8; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12820279, EBI-11343438;
CC       Q96PS8; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12820279, EBI-1045797;
CC       Q96PS8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12820279, EBI-6942903;
CC       Q96PS8; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-12820279, EBI-2680384;
CC       Q96PS8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12820279, EBI-781551;
CC       Q96PS8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12820279, EBI-13345167;
CC       Q96PS8; O60883: GPR37L1; NbExp=3; IntAct=EBI-12820279, EBI-2927498;
CC       Q96PS8; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12820279, EBI-8632435;
CC       Q96PS8; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-12820279, EBI-10329546;
CC       Q96PS8; O14880: MGST3; NbExp=3; IntAct=EBI-12820279, EBI-724754;
CC       Q96PS8; O14524-2: NEMP1; NbExp=3; IntAct=EBI-12820279, EBI-10969203;
CC       Q96PS8; O15173: PGRMC2; NbExp=3; IntAct=EBI-12820279, EBI-1050125;
CC       Q96PS8; P60201-2: PLP1; NbExp=3; IntAct=EBI-12820279, EBI-12188331;
CC       Q96PS8; P15151: PVR; NbExp=3; IntAct=EBI-12820279, EBI-3919694;
CC       Q96PS8; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-12820279, EBI-3920694;
CC       Q96PS8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12820279, EBI-17247926;
CC       Q96PS8; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12820279, EBI-17280858;
CC       Q96PS8; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-12820279, EBI-8032987;
CC       Q96PS8; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-12820279, EBI-17684533;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:15221416}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:30420639}. Cell membrane
CC       {ECO:0000269|PubMed:11573934, ECO:0000269|PubMed:12084581,
CC       ECO:0000269|PubMed:23382902, ECO:0000269|PubMed:30420639}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:30420639}. Lipid droplet
CC       {ECO:0000269|PubMed:23382902}. Note=Detected around lipid droplets.
CC       {ECO:0000269|PubMed:23382902}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96PS8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96PS8-2; Sequence=VSP_010211;
CC   -!- TISSUE SPECIFICITY: Detected in epithelial cells on villi in the ileum,
CC       and also in stomach, jejunum, colon, rectum, white adipose tissue and
CC       placenta (at protein level) (PubMed:15221416, PubMed:23382902).
CC       Expressed in duodenum and jejunum. Highest expression in absorptive
CC       epithelial cells at the tips of villi in the jejunum (PubMed:11573934,
CC       PubMed:12084581). Detected in subcutaneous adipose tissue
CC       (PubMed:23382902). {ECO:0000269|PubMed:11573934,
CC       ECO:0000269|PubMed:12084581, ECO:0000269|PubMed:15221416,
CC       ECO:0000269|PubMed:23382902}.
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). {ECO:0000269|PubMed:30420639}.
CC   -!- PTM: N-glycosylation at Asn-133 increases the stability of the protein
CC       but has no effect on its activity. {ECO:0000269|PubMed:21733844}.
CC   -!- MISCELLANEOUS: In vitro, it can transport the dietary compounds
CC       erythritol and xylitol. {ECO:0000269|PubMed:21733844}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: [Isoform 2]: Initial experiments showed that it is permeable
CC       to water but not to glycerol. However, this could be due to the pH
CC       conditions under which it was assessed rather than isoform specificity
CC       (PubMed:11573934). {ECO:0000269|PubMed:11573934}.
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DR   EMBL; AF159174; AAL25998.1; -; mRNA.
DR   EMBL; AB066105; BAB91223.1; -; mRNA.
DR   EMBL; AL354980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069607; AAH69607.1; -; mRNA.
DR   EMBL; BC074896; AAH74896.1; -; mRNA.
DR   EMBL; BC074897; AAH74897.1; -; mRNA.
DR   CCDS; CCDS1065.1; -. [Q96PS8-1]
DR   PIR; JC7772; JC7772.
DR   RefSeq; NP_536354.2; NM_080429.3. [Q96PS8-1]
DR   PDB; 6F7H; X-ray; 2.30 A; A/B/C/D=1-301.
DR   AlphaFoldDB; Q96PS8; -.
DR   SMR; Q96PS8; -.
DR   BioGRID; 124627; 21.
DR   FunCoup; Q96PS8; 50.
DR   IntAct; Q96PS8; 20.
DR   STRING; 9606.ENSP00000318355; -.
DR   TCDB; 1.A.8.9.5; the major intrinsic protein (mip) family.
DR   GlyCosmos; Q96PS8; 2 sites, No reported glycans.
DR   GlyGen; Q96PS8; 2 sites.
DR   iPTMnet; Q96PS8; -.
DR   BioMuta; AQP10; -.
DR   DMDM; 47117905; -.
DR   MassIVE; Q96PS8; -.
DR   PaxDb; 9606-ENSP00000318355; -.
DR   PeptideAtlas; Q96PS8; -.
DR   Antibodypedia; 34151; 146 antibodies from 24 providers.
DR   DNASU; 89872; -.
DR   Ensembl; ENST00000324978.8; ENSP00000318355.3; ENSG00000143595.14. [Q96PS8-1]
DR   Ensembl; ENST00000484864.1; ENSP00000420341.1; ENSG00000143595.14. [Q96PS8-2]
DR   GeneID; 89872; -.
DR   KEGG; hsa:89872; -.
DR   MANE-Select; ENST00000324978.8; ENSP00000318355.3; NM_080429.3; NP_536354.2.
DR   UCSC; uc001feu.3; human. [Q96PS8-1]
DR   AGR; HGNC:16029; -.
DR   ClinPGx; PA24919; -.
DR   CTD; 89872; -.
DR   DisGeNET; 89872; -.
DR   GeneCards; AQP10; -.
DR   HGNC; HGNC:16029; AQP10.
DR   HPA; ENSG00000143595; Tissue enriched (intestine).
DR   MIM; 606578; gene.
DR   OpenTargets; ENSG00000143595; -.
DR   VEuPathDB; HostDB:ENSG00000143595; -.
DR   eggNOG; KOG0224; Eukaryota.
DR   GeneTree; ENSGT00940000162648; -.
DR   HOGENOM; CLU_020019_9_1_1; -.
DR   InParanoid; Q96PS8; -.
DR   OMA; KAWDPEY; -.
DR   OrthoDB; 3222at2759; -.
DR   PAN-GO; Q96PS8; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q96PS8; -.
DR   PathwayCommons; Q96PS8; -.
DR   Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR   SignaLink; Q96PS8; -.
DR   Agora; ENSG00000143595; -.
DR   BioGRID-ORCS; 89872; 17 hits in 1159 CRISPR screens.
DR   GenomeRNAi; 89872; -.
DR   Pharos; Q96PS8; Tbio.
DR   PRO; PR:Q96PS8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96PS8; protein.
DR   Bgee; ENSG00000143595; Expressed in jejunal mucosa and 44 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; EXP:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015254; F:glycerol channel activity; IDA:UniProtKB.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR   GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR   GO; GO:0006833; P:water transport; IDA:UniProtKB.
DR   CDD; cd00333; MIP; 1.
DR   FunFam; 1.20.1080.10:FF:000005; Aquaporin 3; 1.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR026252; Aquaporin_10.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR050363; MIP/Aquaporin.
DR   InterPro; IPR022357; MIP_CS.
DR   NCBIfam; TIGR00861; MIP; 1.
DR   PANTHER; PTHR43829; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR   PANTHER; PTHR43829:SF13; AQUAPORIN-10; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02022; AQUAPORIN10M.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   PROSITE; PS00221; MIP; 1.
DR   PDBsum; 6F7H; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Glycoprotein;
KW   Lipid droplet; Membrane; Proteomics identification; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..301
FT                   /note="Aquaporin-10"
FT                   /id="PRO_0000063967"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        23..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        42..55
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        56..75
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        76..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   INTRAMEM        78..90
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        91..96
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        97..121
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        122..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        159..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        177..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        189..205
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        206..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   INTRAMEM        209..223
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        224..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   TRANSMEM        242..262
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:30420639,
FT                   ECO:0007744|PDB:6F7H"
FT   TOPO_DOM        263..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MOTIF           82..84
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000305|PubMed:30420639"
FT   MOTIF           214..216
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000305|PubMed:30420639"
FT   SITE            80
FT                   /note="pH-sensor"
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21733844"
FT   VAR_SEQ         236..301
FT                   /note="SAGNGWWWVPVVAPLVGATVGTATYQLLVALHHPEGPEPAQDLVSAQHKASE
FT                   LETPASAQMLECKL -> RWETDSPGAGLHSPSSAKGSVPGSTALCL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:11573934"
FT                   /id="VSP_010211"
FT   VARIANT         15
FT                   /note="R -> Q (in dbSNP:rs6668968)"
FT                   /id="VAR_033519"
FT   VARIANT         123
FT                   /note="H -> Y (in dbSNP:rs6685323)"
FT                   /id="VAR_050063"
FT   MUTAGEN         27
FT                   /note="E->Q: Loss of glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         73
FT                   /note="G->A: Increased glycerol channel activity at acidic
FT                   pH."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         73
FT                   /note="G->F: Loss of glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         77
FT                   /note="S->A,D: Decreased glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         80
FT                   /note="H->A: Loss of glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         85
FT                   /note="F->A: Decreased glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         94
FT                   /note="R->A: Loss of glycerol channel activity."
FT                   /evidence="ECO:0000269|PubMed:30420639"
FT   MUTAGEN         133
FT                   /note="N->Q: Abolishes N-glycosylation."
FT                   /evidence="ECO:0000269|PubMed:21733844"
FT   HELIX           19..47
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           55..72
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           100..121
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           123..130
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           156..178
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           190..205
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           215..225
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           226..230
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           233..240
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:6F7H"
FT   HELIX           244..267
FT                   /evidence="ECO:0007829|PDB:6F7H"
SQ   SEQUENCE   301 AA;  31763 MW;  CB2A7AB680548987 CRC64;
     MVFTQAPAEI MGHLRIRSLL ARQCLAEFLG VFVLMLLTQG AVAQAVTSGE TKGNFFTMFL
     AGSLAVTIAI YVGGNVSGAH LNPAFSLAMC IVGRLPWVKL PIYILVQLLS AFCASGATYV
     LYHDALQNYT GGNLTVTGPK ETASIFATYP APYLSLNNGF LDQVLGTGML IVGLLAILDR
     RNKGVPAGLE PVVVGMLILA LGLSMGANCG IPLNPARDLG PRLFTYVAGW GPEVFSAGNG
     WWWVPVVAPL VGATVGTATY QLLVALHHPE GPEPAQDLVS AQHKASELET PASAQMLECK
     L
//