AQP3_BOVIN
ID AQP3_BOVIN Reviewed; 292 AA.
AC Q08DE6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aquaporin-3;
DE Short=AQP-3;
DE AltName: Full=Aquaglyceroporin-3;
GN Name=AQP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Water channel required to promote glycerol permeability and
CC water transport across cell membranes. Acts as a glycerol transporter
CC in skin and plays an important role in regulating SC (stratum corneum)
CC and epidermal glycerol content. Involved in skin hydration, wound
CC healing, and tumorigenesis. Provides kidney medullary collecting duct
CC with high permeability to water, thereby permitting water to move in
CC the direction of an osmotic gradient. Slightly permeable to urea and
CC may function as a water and urea exit mechanism in antidiuresis in
CC collecting duct cells. It may play an important role in
CC gastrointestinal tract water transport and in glycerol metabolism.
CC {ECO:0000250|UniProtKB:Q8R2N1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47862};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47862}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:P47862}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P47862}.
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:Q96PS8}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; BC123791; AAI23792.1; -; mRNA.
DR RefSeq; NP_001073262.1; NM_001079794.1.
DR AlphaFoldDB; Q08DE6; -.
DR SMR; Q08DE6; -.
DR STRING; 9913.ENSBTAP00000011196; -.
DR PaxDb; Q08DE6; -.
DR Ensembl; ENSBTAT00000011196; ENSBTAP00000011196; ENSBTAG00000008493.
DR GeneID; 780866; -.
DR KEGG; bta:780866; -.
DR CTD; 360; -.
DR VEuPathDB; HostDB:ENSBTAG00000008493; -.
DR VGNC; VGNC:56935; AQP3.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000157242; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; Q08DE6; -.
DR OMA; GDLPWAS; -.
DR OrthoDB; 1152704at2759; -.
DR TreeFam; TF313173; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000008493; Expressed in surface of tongue and 92 other tissues.
DR ExpressionAtlas; Q08DE6; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0015166; F:polyol transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0015791; P:polyol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0002684; P:positive regulation of immune system process; IEA:Ensembl.
DR GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
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; IPR023275; Aquaporin_3.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02015; AQUAPORIN3.
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; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..292
FT /note="Aquaporin-3"
FT /id="PRO_0000282885"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 48..53
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 75..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 79..92
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 93..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..123
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 124..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 179..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT INTRAMEM 209..227
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 228..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 266..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 83..85
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 215..217
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 292 AA; 31518 MW; CD231DC9BA4BA6CC CRC64;
MGRQKELVNR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN
LAFGFAVTLG ILIAGQVSGA HLNPAVTFAM CFLAREPWIK LPVYTLAQTL GAFLGAGIIF
GLYYDAIWAF ANNQLIVSGP NGTAGIFATY PSGHLDMVNG FFDQFIGTAS LIVCVLAIVD
PYNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTAIAG WGSEVFTTGR
HWWWVPIVSP LLGSIAGVFV YQLMIGCHLE PPPPSTDEEN VKLSHVKHKE QM
