AQP7_RAT
ID AQP7_RAT Reviewed; 269 AA.
AC P56403; Q8K3F5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Aquaporin-7;
DE Short=AQP-7;
DE AltName: Full=Aquaglyceroporin-7;
GN Name=Aqp7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9252401; DOI=10.1074/jbc.272.33.20782;
RA Ishibashi K., Kuwahara M., Gu Y., Kageyama Y., Tohsaka A., Suzuki F.,
RA Marumo F., Sasaki S.;
RT "Cloning and functional expression of a new water channel abundantly
RT expressed in the testis permeable to water, glycerol, and urea.";
RL J. Biol. Chem. 272:20782-20786(1997).
RN [2]
RP SEQUENCE REVISION TO 27; 79; 93-94 AND 128-129.
RA Ishibashi K.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=12192003; DOI=10.1074/jbc.m206157200;
RA Virkki L.V., Franke C., Somieski P., Boron W.F.;
RT "Cloning and functional characterization of a novel aquaporin from Xenopus
RT laevis oocytes.";
RL J. Biol. Chem. 277:40610-40616(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA Yang K., Yang B., Zhao X.;
RT "Expression of aquaporin 7 in the testis of rats.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Forms a channel that mediates water and glycerol transport
CC across cell membranes at neutral pH (PubMed:9252401). The channel is
CC also permeable to urea (PubMed:9252401). Plays an important role in
CC body 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:O54794, ECO:0000269|PubMed:9252401}.
CC -!- ACTIVITY REGULATION: Not inhibited by mercury ions.
CC {ECO:0000269|PubMed:9252401}.
CC -!- SUBUNIT: Homotetramer. Interacts (via N-terminus) with PLIN1.
CC {ECO:0000250|UniProtKB:O14520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9252401};
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 -!- TISSUE SPECIFICITY: Detected in heart, kidney and testis.
CC {ECO:0000269|PubMed:9252401}.
CC -!- DEVELOPMENTAL STAGE: Expressed at late stages of spermatogenesis, from
CC late to maturing spermatids (at protein level).
CC {ECO:0000269|PubMed:9252401}.
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; AB000507; BAA22053.2; -; mRNA.
DR EMBL; AY120935; AAM81581.1; -; mRNA.
DR EMBL; AY157737; AAN52930.1; -; mRNA.
DR EMBL; BC072695; AAH72695.1; -; mRNA.
DR RefSeq; NP_062030.2; NM_019157.2.
DR RefSeq; XP_017448684.1; XM_017593195.1.
DR AlphaFoldDB; P56403; -.
DR SMR; P56403; -.
DR STRING; 10116.ENSRNOP00000012974; -.
DR iPTMnet; P56403; -.
DR PhosphoSitePlus; P56403; -.
DR PaxDb; P56403; -.
DR Ensembl; ENSRNOT00000012975; ENSRNOP00000012974; ENSRNOG00000009686.
DR GeneID; 29171; -.
DR KEGG; rno:29171; -.
DR UCSC; RGD:2145; rat.
DR CTD; 364; -.
DR RGD; 2145; Aqp7.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000159054; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; P56403; -.
DR OMA; ACFPGRK; -.
DR OrthoDB; 1246320at2759; -.
DR PhylomeDB; P56403; -.
DR TreeFam; TF313173; -.
DR Reactome; R-RNO-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P56403; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009686; Expressed in testis and 15 other tissues.
DR Genevisible; P56403; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0015254; F:glycerol channel activity; IDA:RGD.
DR GO; GO:0015265; F:urea channel activity; IDA:RGD.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; IDA:RGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:RGD.
DR GO; GO:0070295; P:renal water absorption; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0015840; P:urea transport; IDA:RGD.
DR GO; GO:0006833; P:water transport; IDA:RGD.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR015686; Aquaporin_7.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR43829:SF15; PTHR43829:SF15; 1.
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 Cell membrane; Cytoplasm; Cytoplasmic vesicle; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..269
FT /note="Aquaporin-7"
FT /id="PRO_0000063960"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 41..50
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 71..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 75..82
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 83..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..132
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 133..151
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 173..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 204..205
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 206..219
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55087"
FT TOPO_DOM 220..269
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOTIF 78..80
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT MOTIF 210..212
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT SITE 119
FT /note="Important for permeability to glycerol"
FT /evidence="ECO:0000250|UniProtKB:O14520"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 269 AA; 28882 MW; A2F4B8BB5E775745 CRC64;
MAGSVLENIQ SVLQKTWVRE FLAEFLSTYV LMVFGLGSVA HMVLGERLGS YLGVNLGFGF
GVTMGIHVAG GISGAHMNAA VTFTNCALGR MAWKKFPIYV LGQFLGSFLA AATTYLIFYG
AINHYAGGEL LVTGPKSTAN IFATYLPEHM TLWRGFVDEV FVTGMLQLCI FAITDKLNSP
ALQGTEPLMI GILVCVLGVS LGMNTGYAIN PSRDLPPRFF TFIAGWGKKV FSAGNNWWWV
PVVAPLLGAY LGGIVYLGLI HAGIPPQGS
