AQP5_RAT
ID AQP5_RAT Reviewed; 265 AA.
AC P47864; Q2YDV0; Q569C5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Aquaporin-5;
DE Short=AQP-5;
GN Name=Aqp5;
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, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Submandibular gland;
RX PubMed=7530250; DOI=10.1074/jbc.270.4.1908;
RA Raina S., Preston G.M., Guggino W.B., Agre P.;
RT "Molecular cloning and characterization of an aquaporin cDNA from salivary,
RT lacrimal, and respiratory tissues.";
RL J. Biol. Chem. 270:1908-1912(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Forms a water-specific channel (PubMed:7530250). Plays an
CC important role in fluid secretion in salivary glands. Required for
CC TRPV4 activation by hypotonicity. Together with TRPV4, controls
CC regulatory volume decrease in salivary epithelial cells. Seems to play
CC a redundant role in water transport in the eye, lung and in sweat
CC glands (By similarity). {ECO:0000250|UniProtKB:Q9WTY4,
CC ECO:0000269|PubMed:7530250}.
CC -!- SUBUNIT: Homotetramer. Interacts with TRPV4; the interaction is
CC probably indirect and regulates TRPV4 activation by hypotonicity.
CC {ECO:0000250|UniProtKB:P55064}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9WTY4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Cell membrane
CC {ECO:0000269|PubMed:7530250}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P55064}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Note=Hypotonicity increases location at
CC the cell membrane. Phosphorylation decreases location at the cell
CC membrane. {ECO:0000250|UniProtKB:P55064}.
CC -!- TISSUE SPECIFICITY: Salivary glands, lacrimal glands, corneal
CC epithelium in eye, trachea and lung. {ECO:0000269|PubMed:7530250}.
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:0000250|UniProtKB:P55064}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; U16245; AAA66221.1; -; mRNA.
DR EMBL; BC092572; AAH92572.2; -; mRNA.
DR EMBL; BC110045; AAI10046.1; -; mRNA.
DR PIR; A55630; A55630.
DR RefSeq; NP_036911.1; NM_012779.1.
DR AlphaFoldDB; P47864; -.
DR SMR; P47864; -.
DR STRING; 10116.ENSRNOP00000024102; -.
DR GlyGen; P47864; 1 site.
DR iPTMnet; P47864; -.
DR PhosphoSitePlus; P47864; -.
DR PaxDb; P47864; -.
DR GeneID; 25241; -.
DR KEGG; rno:25241; -.
DR UCSC; RGD:2144; rat.
DR CTD; 362; -.
DR RGD; 2144; Aqp5.
DR VEuPathDB; HostDB:ENSRNOG00000051970; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; P47864; -.
DR OMA; KKEVCSA; -.
DR OrthoDB; 1152704at2759; -.
DR TreeFam; TF312940; -.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P47864; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000051970; Expressed in lung and 7 other tissues.
DR Genevisible; P47864; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
DR GO; GO:0071476; P:cellular hypotonic response; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0046541; P:saliva secretion; ISO:RGD.
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; IPR023276; Aquaporin_5.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR PANTHER; PTHR19139:SF38; PTHR19139:SF38; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02017; AQUAPORIN5.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="Aquaporin-5"
FT /id="PRO_0000063953"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 34..39
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 61..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 66..74
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 109..126
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 148..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 180
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 181..191
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 192..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 225..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 69..71
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT MOTIF 185..187
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 28421 MW; DE0F1BED9D2C0600 CRC64;
MKKEVCSLAF FKAVFAEFLA TLIFVFFGLG SALKWPSALP TILQISIAFG LAIGTLAQAL
GPVSGGHINP AITLALLIGN QISLLRAVFY VAAQLVGAIA GAGILYWLAP LNARGNLAVN
ALNNNTTPGK AMVVELILTF QLALCIFSST DSRRTSPVGS PALSIGLSVT LGHLVGIYFT
GCSMNPARSF GPAVVMNRFS PSHWVFWVGP IVGAMLAAIL YFYLLFPSSL SLHDRVAVVK
GTYEPEEDWE DHREERKKTI ELTAH
