AQP1_PIG
ID AQP1_PIG Reviewed; 271 AA.
AC Q6PQZ1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Aquaporin-1;
DE Short=AQP-1;
DE AltName: Full=Aquaporin-CHIP;
DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN Name=AQP1;
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].
RC TISSUE=Kidney;
RA Jin S., Liu Y., Wang Y., Yang H., Gao H., He C., Ma T.;
RT "Cloning and expression of porcine aquaporin-1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC membranes of red cells and kidney proximal tubules with high
CC permeability to water, thereby permitting water to move in the
CC direction of an osmotic gradient. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with EPHB2; involved
CC in endolymph production in the inner ear. Identified in a complex with
CC STOM (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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).
CC -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC concentrations of mercury. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AY585335; AAS98212.1; -; mRNA.
DR RefSeq; NP_999619.1; NM_214454.1.
DR AlphaFoldDB; Q6PQZ1; -.
DR SMR; Q6PQZ1; -.
DR PeptideAtlas; Q6PQZ1; -.
DR PRIDE; Q6PQZ1; -.
DR GeneID; 407773; -.
DR KEGG; ssc:407773; -.
DR CTD; 358; -.
DR InParanoid; Q6PQZ1; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; ISS:UniProtKB.
DR GO; GO:0030184; F:nitric oxide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
DR GO; GO:0035378; P:carbon dioxide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; ISS:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; ISS:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0071474; P:cellular hyperosmotic response; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0071288; P:cellular response to mercury ion; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0021670; P:lateral ventricle development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030185; P:nitric oxide transport; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0046878; P:positive regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0003097; P:renal water transport; ISS:UniProtKB.
DR GO; GO:0035377; P:transepithelial water 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; IPR023274; Aquaporin_1.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02013; AQUAPORIN1.
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; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Aquaporin-1"
FT /id="PRO_0000063922"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..34
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 35..50
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 51..68
FT /note="Helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 69..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 74..78
FT /evidence="ECO:0000250"
FT INTRAMEM 79..88
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..117
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 118..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..158
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 159..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 170..187
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 190..193
FT /evidence="ECO:0000250"
FT INTRAMEM 194..204
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 205..215
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 216..230
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 231..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 78..80
FT /note="NPA 1"
FT MOTIF 194..196
FT /note="NPA 2"
FT SITE 58
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 182
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Hg(2+)-sensitive residue"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 255
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 28679 MW; A03DFD4112F0579B CRC64;
MASEFKKKIF WRAVVAEFLA MTLFIFISIG SALGFQYPVR NNQTSGAAQD NVKVSLAFGL
SIATLAQSVG HISGAHLNPA VTLGLLLSCQ ISVLRAVMYI IAQCVGAIVA TAILSGITSS
LPGNSLGLNS LAPGVDSGQG LGIEIIGTLQ LVLCVLATTD RRRRDLGGSA PLAIGFSVAL
GHLLAIDYTG CGINPARSFG SAVITHNFQD HWVFWVGPFI GGALAVLIYD FILAPRSSDL
TDRVKVWTSG QVEEYDLDGD DINSRVEMKP K
