AQP7_HUMAN
ID AQP7_HUMAN Reviewed; 342 AA.
AC O14520; Q08E94; Q5T5L9; Q8NHM3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Aquaporin-7;
DE Short=AQP-7;
DE AltName: Full=Aquaglyceroporin-7;
DE AltName: Full=Aquaporin adipose {ECO:0000303|PubMed:11952783};
DE Short=AQPap {ECO:0000303|PubMed:11952783};
DE AltName: Full=Aquaporin-7-like;
GN Name=AQP7; Synonyms=AQP7L, AQP9 {ECO:0000303|PubMed:9405233};
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 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=9405233; DOI=10.1006/bbrc.1997.7769;
RA Kuriyama H., Kawamoto S., Ishida N., Ohno I., Mita S., Matsuzawa Y.,
RA Matsubara K., Okubo K.;
RT "Molecular cloning and expression of a novel human aquaporin from adipose
RT tissue with glycerol permeability.";
RL Biochem. Biophys. Res. Commun. 241:53-58(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN GLYCQTL, VARIANTS CYS-12;
RP LEU-59 AND VAL-264, CHARACTERIZATION OF VARIANT VAL-264, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11952783; DOI=10.1046/j.1432-1033.2002.02821.x;
RA Kondo H., Shimomura I., Kishida K., Kuriyama H., Makino Y., Nishizawa H.,
RA Matsuda M., Maeda N., Nagaretani H., Kihara S., Kurachi Y., Nakamura T.,
RA Funahashi T., Matsuzawa Y.;
RT "Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis
RT and functional mutation.";
RL Eur. J. Biochem. 269:1814-1826(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP SUBCELLULAR LOCATIONS, 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 [7]
RP INTERACTION WITH PLIN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-MET--LYS-32.
RX PubMed=27832861; DOI=10.1016/j.metabol.2016.09.004;
RA Hansen J.S., Krintel C., Hernebring M., Haataja T.J., de Mare S.,
RA Wasserstrom S., Kosinska-Eriksson U., Palmgren M., Holm C., Stenkula K.G.,
RA Jones H.A., Lindkvist-Petersson K.;
RT "Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its
RT mobility via protein kinase A mediated phosphorylation.";
RL Metabolism 65:1731-1742(2016).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP MUTAGENESIS OF TYR-135 AND HIS-165.
RX PubMed=30423801; DOI=10.3390/cells7110207;
RA Mosca A.F., de Almeida A., Wragg D., Martins A.P., Sabir F., Leoni S.,
RA Moura T.F., Prista C., Casini A., Soveral G.;
RT "Molecular Basis of Aquaporin-7 Permeability Regulation by pH.";
RL Cells 7:0-0(2018).
RN [9]
RP FUNCTION, AND ACTIVITY REGULATION.
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).
RN [10]
RP VARIANT VAL-264.
RX PubMed=17566090; DOI=10.1210/jc.2007-0531;
RA Ceperuelo-Mallafre V., Miranda M., Chacon M.R., Vilarrasa N., Megia A.,
RA Gutierrez C., Fernandez-Real J.M., Gomez J.M., Caubet E., Fruhbeck G.,
RA Vendrell J.;
RT "Adipose tissue expression of the glycerol channel aquaporin-7 gene is
RT altered in severe obesity but not in type 2 diabetes.";
RL J. Clin. Endocrinol. Metab. 92:3640-3645(2007).
CC -!- FUNCTION: Forms a channel that mediates water and glycerol transport
CC across cell membranes at neutral pH (PubMed:9405233, PubMed:11952783,
CC PubMed:30423801, PubMed:30420639). The channel is also permeable to
CC urea (PubMed:9405233). Plays an important role in body energy
CC homeostasis under conditions that promote lipid catabolism, giving rise
CC to glycerol and free fatty acids. Mediates glycerol export from
CC adipocytes. After release into the blood stream, glycerol is used for
CC gluconeogenesis in the liver to maintain normal blood glucose levels
CC and prevent fasting hypoglycemia. Required for normal glycerol
CC reabsorption in the kidney (By similarity).
CC {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:11952783,
CC ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:30423801,
CC ECO:0000269|PubMed:9405233}.
CC -!- ACTIVITY REGULATION: Inhibited by mercury ions (PubMed:9405233). Fully
CC active at pH 6.5 to 7.5. Activity decreases with decreasing pH.
CC Inactive at pH 5.5 (PubMed:30423801, PubMed:30420639).
CC {ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:30423801,
CC ECO:0000269|PubMed:9405233}.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts (via N-terminus) with PLIN1
CC (PubMed:27832861). {ECO:0000269|PubMed:27832861,
CC ECO:0000305|PubMed:30423801}.
CC -!- INTERACTION:
CC O14520; O60240: PLIN1; NbExp=4; IntAct=EBI-20765950, EBI-26906001;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11952783,
CC ECO:0000269|PubMed:28042826, ECO:0000269|PubMed:30423801,
CC ECO:0000269|PubMed:9405233}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55087}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O54794}. Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:27832861}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55087}. Lipid droplet
CC {ECO:0000305|PubMed:27832861}. Note=Internalized from the cell membrane
CC in response to catecholamine-induced activation of PKA; detected on
CC intracellular membranes and colocalizes with lipid droplets (By
CC similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid
CC droplets (PubMed:27832861). {ECO:0000250|UniProtKB:O54794,
CC ECO:0000269|PubMed:27832861}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14520-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14520-2; Sequence=VSP_056249, VSP_056250;
CC -!- TISSUE SPECIFICITY: Detected in the sperm head (at protein level)
CC (PubMed:28042826). Detected in white adipose tissue (PubMed:9405233).
CC {ECO:0000269|PubMed:28042826, ECO:0000269|PubMed:9405233}.
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-Ala/Ser (NPA). {ECO:0000250|UniProtKB:P55064}.
CC -!- POLYMORPHISM: Genetic variations in AQP7 are responsible for changes in
CC glycerol release during exercise and define the glycerol quantitative
CC trait locus (GLYCQTL) [MIM:614411].
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB006190; BAA21745.1; -; mRNA.
DR EMBL; AB052626; BAC05693.1; -; Genomic_DNA.
DR EMBL; AK300716; BAH13332.1; -; mRNA.
DR EMBL; AK315879; BAF98770.1; -; mRNA.
DR EMBL; AL356218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119672; AAI19673.1; -; mRNA.
DR EMBL; BC119673; AAI19674.1; -; mRNA.
DR CCDS; CCDS6541.1; -. [O14520-1]
DR PIR; JC5791; JC5791.
DR RefSeq; NP_001161.1; NM_001170.2. [O14520-1]
DR RefSeq; NP_001305086.1; NM_001318157.1.
DR RefSeq; NP_001305087.1; NM_001318158.1.
DR RefSeq; XP_005251510.1; XM_005251453.3.
DR RefSeq; XP_011516168.1; XM_011517866.2. [O14520-1]
DR PDB; 6KXW; X-ray; 3.70 A; A/B/C/D=1-342.
DR PDB; 6N1G; X-ray; 4.00 A; A/B/C/D=1-342.
DR PDB; 6QZI; X-ray; 1.90 A; A=33-279.
DR PDB; 6QZJ; X-ray; 2.20 A; A=33-279.
DR PDBsum; 6KXW; -.
DR PDBsum; 6N1G; -.
DR PDBsum; 6QZI; -.
DR PDBsum; 6QZJ; -.
DR AlphaFoldDB; O14520; -.
DR SMR; O14520; -.
DR BioGRID; 106860; 4.
DR IntAct; O14520; 7.
DR STRING; 9606.ENSP00000297988; -.
DR DrugBank; DB09462; Glycerin.
DR TCDB; 1.A.8.9.6; the major intrinsic protein (mip) family.
DR iPTMnet; O14520; -.
DR PhosphoSitePlus; O14520; -.
DR BioMuta; AQP7; -.
DR jPOST; O14520; -.
DR MassIVE; O14520; -.
DR PaxDb; O14520; -.
DR PeptideAtlas; O14520; -.
DR PRIDE; O14520; -.
DR ProteomicsDB; 48063; -. [O14520-1]
DR Antibodypedia; 10988; 140 antibodies from 24 providers.
DR DNASU; 364; -.
DR Ensembl; ENST00000297988.6; ENSP00000297988.1; ENSG00000165269.13. [O14520-1]
DR Ensembl; ENST00000447660.3; ENSP00000412868.2; ENSG00000165269.13. [O14520-2]
DR GeneID; 364; -.
DR KEGG; hsa:364; -.
DR MANE-Select; ENST00000297988.6; ENSP00000297988.1; NM_001170.3; NP_001161.1.
DR UCSC; uc003zst.3; human. [O14520-1]
DR CTD; 364; -.
DR DisGeNET; 364; -.
DR GeneCards; AQP7; -.
DR HGNC; HGNC:640; AQP7.
DR HPA; ENSG00000165269; Tissue enhanced (adipose tissue, breast, heart muscle).
DR MalaCards; AQP7; -.
DR MIM; 602974; gene.
DR MIM; 614411; phenotype.
DR neXtProt; NX_O14520; -.
DR OpenTargets; ENSG00000165269; -.
DR PharmGKB; PA24925; -.
DR VEuPathDB; HostDB:ENSG00000165269; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000159054; -.
DR InParanoid; O14520; -.
DR OMA; ACFPGRK; -.
DR OrthoDB; 1246320at2759; -.
DR PhylomeDB; O14520; -.
DR TreeFam; TF313173; -.
DR BioCyc; MetaCyc:ENSG00000165269-MON; -.
DR PathwayCommons; O14520; -.
DR Reactome; R-HSA-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; O14520; -.
DR BioGRID-ORCS; 364; 380 hits in 1005 CRISPR screens.
DR ChiTaRS; AQP7; human.
DR GeneWiki; AQP7; -.
DR GenomeRNAi; 364; -.
DR Pharos; O14520; Tbio.
DR PRO; PR:O14520; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O14520; protein.
DR Bgee; ENSG00000165269; Expressed in apex of heart and 95 other tissues.
DR ExpressionAtlas; O14520; baseline and differential.
DR Genevisible; O14520; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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:0006833; P:water transport; IDA:UniProtKB.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Lipid droplet; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..342
FT /note="Aquaporin-7"
FT /id="PRO_0000063958"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 57..66
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 87..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 91..98
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 99..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..148
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 149..167
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 189..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 220..221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 222..235
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 236..342
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOTIF 94..96
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT MOTIF 226..228
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT SITE 135
FT /note="Important for permeability to glycerol"
FT /evidence="ECO:0000269|PubMed:30423801"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56403"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056249"
FT VAR_SEQ 248..342
FT /note="SNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGIT
FT VLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF -> RYCPCPGPFL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056250"
FT VARIANT 12
FT /note="R -> C (in dbSNP:rs139297434)"
FT /evidence="ECO:0000269|PubMed:11952783"
FT /id="VAR_067253"
FT VARIANT 38
FT /note="L -> V (in dbSNP:rs2381003)"
FT /id="VAR_061343"
FT VARIANT 59
FT /note="V -> L (in dbSNP:rs4008659)"
FT /evidence="ECO:0000269|PubMed:11952783"
FT /id="VAR_067254"
FT VARIANT 63
FT /note="K -> T (in dbSNP:rs4008658)"
FT /id="VAR_061344"
FT VARIANT 264
FT /note="G -> V (affects water and glycerol transport;
FT dbSNP:rs62542743)"
FT /evidence="ECO:0000269|PubMed:11952783,
FT ECO:0000269|PubMed:17566090"
FT /id="VAR_067255"
FT MUTAGEN 1..32
FT /note="Missing: Decreased interaction with PLIN1."
FT /evidence="ECO:0000269|PubMed:27832861"
FT MUTAGEN 135
FT /note="Y->A: Strongly decreased permeability to glycerol.
FT Mildly decreased water permeability."
FT /evidence="ECO:0000269|PubMed:30423801"
FT MUTAGEN 165
FT /note="H->A: Decreased permeability to glycerol. Mildly
FT decreased water permeability."
FT /evidence="ECO:0000269|PubMed:30423801"
FT HELIX 34..60
FT /evidence="ECO:0007829|PDB:6QZI"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:6QZI"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 111..133
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:6QZI"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 168..190
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:6QZI"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6QZI"
FT HELIX 256..278
FT /evidence="ECO:0007829|PDB:6QZI"
SQ SEQUENCE 342 AA; 37232 MW; 8A05F92B977D2F93 CRC64;
MVQASGHRRS TRGSKMVSWS VIAKIQEILQ RKMVREFLAE FMSTYVMMVF GLGSVAHMVL
NKKYGSYLGV NLGFGFGVTM GVHVAGRISG AHMNAAVTFA NCALGRVPWR KFPVYVLGQF
LGSFLAAATI YSLFYTAILH FSGGQLMVTG PVATAGIFAT YLPDHMTLWR GFLNEAWLTG
MLQLCLFAIT DQENNPALPG TEALVIGILV VIIGVSLGMN TGYAINPSRD LPPRIFTFIA
GWGKQVFSNG ENWWWVPVVA PLLGAYLGGI IYLVFIGSTI PREPLKLEDS VAYEDHGITV
LPKMGSHEPT ISPLTPVSVS PANRSSVHPA PPLHESMALE HF
