AQP5_SHEEP
ID AQP5_SHEEP Reviewed; 265 AA.
AC Q866S3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Aquaporin-5;
DE Short=AQP-5;
GN Name=AQP5;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Coghlan M.W., Koukoulas I., Armugam A., Jeyaseelan K.;
RT "Aquaporin 4 and 5 from sheep.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a water-specific channel (By similarity). 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:P55064,
CC ECO:0000250|UniProtKB:Q9WTY4}.
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:0000250|UniProtKB:P55064}; 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 -!- 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; AY177613; AAO21367.1; -; mRNA.
DR RefSeq; NP_001009273.1; NM_001009273.2.
DR AlphaFoldDB; Q866S3; -.
DR SMR; Q866S3; -.
DR STRING; 9940.ENSOARP00000019504; -.
DR GeneID; 443251; -.
DR KEGG; oas:443251; -.
DR CTD; 362; -.
DR eggNOG; KOG0223; Eukaryota.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0071476; P:cellular hypotonic response; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; 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; 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_0000063954"
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"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 28139 MW; BAE4EFC6F530ADB7 CRC64;
MKKEVCSAAF LKAVFAEFLA TLIFVFFGLG SALKWPSAMP SVLQISLAFG LAIGTMAQAL
GPVSGGHMNP AITLALLVGN QISLLRAVFY LVAQLVGAIA GAAILYGLAP YNARSNLAVN
ALNNNTTAGQ AVVAEMILTF QLALCVFSST DSRRTSPVGS PALSIGLSVT LGHLVGIYFT
GCSMNPARSF GPAVIMSRFS SAHWVFWVGP IVGAATAAII YFYLLFPHSL SLSDRVAILK
GTYEPDEDWE ESQEERKKTM ELTAH
