AQP1_RAT
ID AQP1_RAT Reviewed; 269 AA.
AC P29975; Q5EB50; Q7TN36;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
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; Synonyms=Chip28;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1280133; DOI=10.1016/0006-291x(92)91368-z;
RA Deen P.M.T., Dempster J.A., Wieringa B., van Os C.H.;
RT "Isolation of a cDNA for rat CHIP28 water channel: high mRNA expression in
RT kidney cortex and inner medulla.";
RL Biochem. Biophys. Res. Commun. 188:1267-1273(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Parotid gland;
RX PubMed=7530838; DOI=10.1007/bf00374565;
RA Li J., Nielsen S., Dai Y., Lazowski K.W., Christensen E.I., Tabak L.A.,
RA Baum B.J.;
RT "Examination of rat salivary glands for the presence of the aquaporin
RT CHIP.";
RL Pflugers Arch. 428:455-460(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8421053; DOI=10.1083/jcb.120.2.359;
RA Zhang R., Skach W., Hasegawa H., van Hoek A.N., Verkman A.S.;
RT "Cloning, functional analysis and cell localization of a kidney proximal
RT tubule water transporter homologous to CHIP28.";
RL J. Cell Biol. 120:359-369(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Aortic smooth muscle;
RX PubMed=8508530; DOI=10.1161/01.res.73.1.193;
RA Shanahan C.M., Weissberg P.L., Metcalfe J.C.;
RT "Isolation of gene markers of differentiated and proliferating vascular
RT smooth muscle cells.";
RL Circ. Res. 73:193-204(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Erythrocytes and renal tubules.
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.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; X67948; CAA48134.1; -; mRNA.
DR EMBL; L07268; AAB46624.1; -; mRNA.
DR EMBL; X70257; CAA49761.1; -; mRNA.
DR EMBL; X71069; CAA50395.1; -; mRNA.
DR EMBL; BC090068; AAH90068.1; -; mRNA.
DR PIR; JC1320; JC1320.
DR RefSeq; NP_036910.1; NM_012778.1.
DR AlphaFoldDB; P29975; -.
DR SMR; P29975; -.
DR CORUM; P29975; -.
DR STRING; 10116.ENSRNOP00000015692; -.
DR GlyGen; P29975; 2 sites.
DR iPTMnet; P29975; -.
DR PhosphoSitePlus; P29975; -.
DR SwissPalm; P29975; -.
DR PaxDb; P29975; -.
DR PRIDE; P29975; -.
DR Ensembl; ENSRNOT00000015692; ENSRNOP00000015692; ENSRNOG00000011648.
DR GeneID; 25240; -.
DR KEGG; rno:25240; -.
DR UCSC; RGD:2141; rat.
DR CTD; 358; -.
DR RGD; 2141; Aqp1.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000157015; -.
DR InParanoid; P29975; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P29975; -.
DR TreeFam; TF312940; -.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P29975; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011648; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P29975; baseline and differential.
DR Genevisible; P29975; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
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:0005901; C:caveola; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0015079; F:potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015250; F:water channel activity; IMP:RGD.
DR GO; GO:0005372; F:water transmembrane transporter activity; ISO:RGD.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
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:0071732; P:cellular response to nitric oxide; ISO:RGD.
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:0033326; P:cerebrospinal fluid secretion; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0051458; P:corticotropin secretion; ISO:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; ISO:RGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEP:RGD.
DR GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB.
DR GO; GO:0044241; P:lipid digestion; ISO:RGD.
DR GO; GO:0072220; P:metanephric descending thin limb development; ISO:RGD.
DR GO; GO:0072239; P:metanephric glomerulus vasculature development; ISO:RGD.
DR GO; GO:0072232; P:metanephric proximal convoluted tubule segment 2 development; ISO:RGD.
DR GO; GO:0072230; P:metanephric proximal straight tubule development; ISO:RGD.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0030185; P:nitric oxide transport; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:0046878; P:positive regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0070295; P:renal water absorption; ISO:RGD.
DR GO; GO:0003097; P:renal water transport; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0032940; P:secretion by cell; ISO:RGD.
DR GO; GO:0033363; P:secretory granule organization; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; ISO:RGD.
DR GO; GO:0006833; P:water transport; IMP:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
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..269
FT /note="Aquaporin-1"
FT /id="PRO_0000063924"
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..48
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..66
FT /note="Helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 67..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 71..76
FT /evidence="ECO:0000250"
FT INTRAMEM 77..84
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..115
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..136
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 137..155
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 156..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 167..183
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..186
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 187..192
FT /evidence="ECO:0000250"
FT INTRAMEM 193..200
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 201..207
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..228
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 229..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 76..78
FT /note="NPA 1"
FT MOTIF 192..194
FT /note="NPA 2"
FT SITE 56
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Hg(2+)-sensitive residue"
FT SITE 195
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="S -> T (in Ref. 4; CAA50395)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="I -> F (in Ref. 3; CAA49761)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="L -> S (in Ref. 2; AAB46624)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> Q (in Ref. 4; CAA50395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28857 MW; 69BE16F65212AAB6 CRC64;
MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV KVSLAFGLSI
ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA QCVGAIVASA ILSGITSSLL
ENSLGRNDLA RGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
LLAIDYTGCG INPARSFGSA VLTRNFSNHW IFWVGPFIGS ALAVLIYDFI LAPRSSDFTD
RMKVWTSGQV EEYDLDADDI NSRVEMKPK
