AQP7_MACFA
ID AQP7_MACFA Reviewed; 342 AA.
AC Q4R691;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Aquaporin-7;
DE Short=AQP-7;
DE AltName: Full=Aquaglyceroporin-7;
GN Name=AQP7; ORFNames=QtsA-18739;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a channel that mediates water and glycerol transport
CC across cell membranes at neutral pH (By similarity). The channel is
CC also permeable to urea (By similarity). Plays an important role in body
CC energy homeostasis under conditions that promote lipid catabolism,
CC giving rise to glycerol and free fatty acids. Mediates glycerol export
CC from adipocytes. After release into the blood stream, glycerol is used
CC for gluconeogenesis in the liver to maintain normal blood glucose
CC levels and prevent fasting hypoglycemia. Required for normal glycerol
CC reabsorption in the kidney (By similarity).
CC {ECO:0000250|UniProtKB:O14520, ECO:0000250|UniProtKB:O54794}.
CC -!- SUBUNIT: Homotetramer. Interacts (via N-terminus) with PLIN1.
CC {ECO:0000250|UniProtKB:O14520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O54794};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasm,
CC cell cortex {ECO:0000250|UniProtKB:O54794}. Cytoplasmic vesicle
CC membrane {ECO:0000250|UniProtKB:O54794}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55087}. Lipid droplet
CC {ECO:0000250|UniProtKB:O54794}. Note=Internalized from the cell
CC membrane in response to catecholamine-induced activation of PKA;
CC detected on intracellular membranes and colocalizes with lipid droplets
CC (By similarity). Colocalizes with PLIN1 in adipocytes, probably on
CC lipid droplets (By similarity). {ECO:0000250|UniProtKB:O14520,
CC ECO:0000250|UniProtKB:O54794}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB169297; BAE01384.1; -; mRNA.
DR RefSeq; NP_001270808.1; NM_001283879.1.
DR AlphaFoldDB; Q4R691; -.
DR SMR; Q4R691; -.
DR STRING; 9541.XP_005581576.1; -.
DR GeneID; 101925995; -.
DR CTD; 364; -.
DR eggNOG; KOG0224; Eukaryota.
DR OrthoDB; 1246320at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; ISS: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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..342
FT /note="Aquaporin-7"
FT /id="PRO_0000286052"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 58..65
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 87..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 91..99
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 100..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 135..170
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 192..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 218..221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 222..232
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 233..255
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 277..342
FT /note="Cytoplasmic"
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:0000250|UniProtKB:O14520"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56403"
SQ SEQUENCE 342 AA; 37196 MW; D68330F936620DB8 CRC64;
MVQTSRHRRS TRGSKMVSWS VMAKIQEILQ KKMVREFLAE FMSTYVMMVF GLGSVAHMVL
NKKYGSYLGV NLGFGFGVTM GVHVAGHISG AHMNAAVTFA NCALGRVPWR KFPVYVLGQF
LGSFLAAATI YTLFYTAILH FSGGQLMVTG PVATAGIFAT YLPDHMTLWR GFLNEAWLTG
MLQLCLFAIT DQENNAALPG TQALVIGILV VIIGVSLGMN TGYAINPSRD LPPRVFTFIA
GWGKEVFSEG ENWWWVPVVA PLLGACLGGI IYLVFIGSTT PREPLKLEDS VAYEDHGITV
LPKMGSHEPT ISPLTPVSVS PANRSSVRPA PPLHESMALG HF
