AQP1_SHEEP
ID AQP1_SHEEP Reviewed; 272 AA.
AC P56401;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
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 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], AND TISSUE SPECIFICITY.
RX PubMed=9761352; DOI=10.1007/s004670050502;
RA Wintour E.M., Earnest L., Alcorn D., Butkus A., Shandley L., Jeyaseelan K.;
RT "Ovine AQP1: cDNA cloning, ontogeny, and control of renal gene
RT expression.";
RL Pediatr. Nephrol. 12:545-553(1998).
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 -!- TISSUE SPECIFICITY: Detected in fetal kidney (at protein level).
CC Detected in fetal kidney. {ECO:0000269|PubMed:9761352}.
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; AF009037; AAB63463.1; -; mRNA.
DR RefSeq; NP_001009194.1; NM_001009194.1.
DR AlphaFoldDB; P56401; -.
DR SMR; P56401; -.
DR STRING; 9940.ENSOARP00000008340; -.
DR GeneID; 442999; -.
DR KEGG; oas:442999; -.
DR CTD; 358; -.
DR eggNOG; KOG0223; Eukaryota.
DR eggNOG; KOG2871; Eukaryota.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA: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: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; IEP: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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..272
FT /note="Aquaporin-1"
FT /id="PRO_0000063925"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..36
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..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..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 73..78
FT /evidence="ECO:0000250"
FT INTRAMEM 79..86
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..117
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 118..138
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..157
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 158..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 170..186
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 190..195
FT /evidence="ECO:0000250"
FT INTRAMEM 196..203
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 204..210
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 211..231
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 232..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 78..80
FT /note="NPA 1"
FT MOTIF 195..197
FT /note="NPA 2"
FT SITE 58
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Hg(2+)-sensitive residue"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 256
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 272 AA; 29057 MW; F8515FBDCCD361FC CRC64;
MASEFKKKLF WRAVVAEFLA MILFIFISIG SALGFHYPIK SNQTTGAVQD NVKVSLAFGL
SIATLAQSVG HISGAHLNPA VTLGLLLSCQ ISILRAIMYI IAQCVGAIVA TVILSGITSS
LPDNSLGLNA LAPGVNSGQG LGIEIIGTLQ LVLCVLATTD RRRRRDLGDS GPLAIGFSVA
LGHLLAIDYT GCGINPARSF GSSVITHNFQ DHWIFWVGPF IGAALAVLIY DFILAPRSSD
LTDRVKVWTS GQVEEYDLDA DDINSRVEMK PK
