AQP3_PIG
ID AQP3_PIG Reviewed; 290 AA.
AC A9Y006; A8IF63;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Aquaporin-3;
DE AltName: Full=Aquaglyceroporin-3;
GN Name=AQP3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=18249020; DOI=10.1016/j.cbpb.2007.11.014;
RA Li X., Lei T., Xia T., Chen X., Feng S., Chen H., Chen Z., Peng Y.,
RA Yang Z.;
RT "Molecular characterization, chromosomal and expression patterns of three
RT aquaglyceroporins (AQP3, 7, 9) from pig.";
RL Comp. Biochem. Physiol. 149B:468-476(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Z.-Q., Wang Y.-L., Yang G.-Y., Wang W.-J., Tai Y.-L., Han L.-Q.;
RT "Molecular cloning and expression of porcine aquaporin 3.";
RL Submitted (SEP-2007) 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 -!- TISSUE SPECIFICITY: Highly expressed in stomach and spleen, with lower
CC expression in kidney and lung. {ECO:0000269|PubMed:18249020}.
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; EU024115; ABW06528.1; -; Genomic_DNA.
DR EMBL; EU161094; ABW06862.1; -; mRNA.
DR RefSeq; NP_001103642.1; NM_001110172.1.
DR AlphaFoldDB; A9Y006; -.
DR SMR; A9Y006; -.
DR STRING; 9823.ENSSSCP00000011724; -.
DR PaxDb; A9Y006; -.
DR PeptideAtlas; A9Y006; -.
DR GeneID; 100126235; -.
DR KEGG; ssc:100126235; -.
DR CTD; 360; -.
DR eggNOG; KOG0224; Eukaryota.
DR InParanoid; A9Y006; -.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
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:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015791; P:polyol 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; 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..290
FT /note="Aquaporin-3"
FT /id="PRO_0000394026"
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..290
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"
FT CONFLICT 248
FT /note="A -> V (in Ref. 2; ABW06862)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31145 MW; 12312C8A983F2D27 CRC64;
MGRQKELVTR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN
LAFGFAVTLG ILVAGQVSGA HLNPAVTFAM CFLAREPWIK LPVYTLAQTL GAFLGAGIIF
GLYYDAIWAF ANNQLIVSGP NGTAGIFATY PSGHLDMVNG FFDQFIGTAS LIVCVLAIVD
PNNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTAIAG WGSEVFTTGR
HWWWVPIASP LLGSIAGVFV YQLMIGCHLE PPPPSTDEEN VKLSQVKHKE
