ID AQP1_BOVIN Reviewed; 271 AA.
AC P47865; Q2HJE2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 170.
DE RecName: Full=Aquaporin-1 {ECO:0000250|UniProtKB:P29972};
DE Short=AQP-1;
DE AltName: Full=Aquaporin-CHIP;
DE AltName: Full=Water channel protein CHIP29;
DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN Name=AQP1 {ECO:0000250|UniProtKB:P29972};
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 [MRNA].
RC TISSUE=Ocular ciliary epithelium;
RX PubMed=7526855; DOI=10.1006/bbrc.1994.2539;
RA Patil R.V., Yang X., Saito I., Coca-Prados M., Wax M.B.;
RT "Cloning of a novel cDNA homologous to CHIP28 water channel from ocular
RT ciliary epithelium.";
RL Biochem. Biophys. Res. Commun. 204:861-866(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RA Joshi S., Recinos A., Jap B.K.;
RT "Nucleotide sequence of an aquaporin cDNA from bovine bone marrow.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=10957645; DOI=10.1107/s0907444900008143;
RA Sui H., Walian P.J., Tang G., Oh A., Jap B.K.;
RT "Crystallization and preliminary X-ray crystallographic analysis of water
RT channel AQP1.";
RL Acta Crystallogr. D 56:1198-1200(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11780053; DOI=10.1038/414872a;
RA Sui H., Han B.-G., Lee J.K., Walian P., Jap B.K.;
RT "Structural basis of water-specific transport through the AQP1 water
RT channel.";
RL Nature 414:872-878(2001).
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. Component of the ankyrin-1 complex, a
CC multiprotein complex involved in the stability and shape of the
CC erythrocyte membrane. {ECO:0000250|UniProtKB:P29972}.
CC -!- SUBUNIT: Homotetramer. Component of the ankyrin-1 complex in the
CC erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB
CC and AQP1 (By similarity). Interacts with EPHB2; involved in endolymph
CC production in the inner ear (By similarity). Identified in a complex
CC with STOM. Interacts (via the N-terminal) with ANK1 (via ANK 1-5
CC repeats). Interacts (via the C-terminal) with EPB42 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P29972,
CC ECO:0000250|UniProtKB:Q02013}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; S74759; AAB32365.1; -; mRNA.
DR EMBL; AF028005; AAB84190.1; -; mRNA.
DR EMBL; BT025412; ABF57368.1; -; mRNA.
DR EMBL; BC105525; AAI05526.1; -; mRNA.
DR PIR; JC2348; JC2348.
DR RefSeq; NP_777127.1; NM_174702.3.
DR PDB; 1J4N; X-ray; 2.20 A; A=1-271.
DR PDBsum; 1J4N; -.
DR AlphaFoldDB; P47865; -.
DR SMR; P47865; -.
DR STRING; 9913.ENSBTAP00000000993; -.
DR GlyCosmos; P47865; 1 site, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000000993; -.
DR Ensembl; ENSBTAT00000000993.6; ENSBTAP00000000993.5; ENSBTAG00000000745.6.
DR GeneID; 282653; -.
DR KEGG; bta:282653; -.
DR CTD; 358; -.
DR VEuPathDB; HostDB:ENSBTAG00000000745; -.
DR VGNC; VGNC:107216; AQP1.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000157015; -.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; P47865; -.
DR OMA; KMFWRAV; -.
DR OrthoDB; 3236018at2759; -.
DR TreeFam; TF312940; -.
DR Reactome; R-BTA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-BTA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-BTA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-BTA-432047; Passive transport by Aquaporins.
DR EvolutionaryTrace; P47865; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000000745; Expressed in cortex of kidney and 99 other cell types or tissues.
DR GO; GO:0170014; C:ankyrin-1 complex; ISS:UniProtKB.
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:0032127; C:dense core granule membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
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:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
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:0033326; P:cerebrospinal fluid secretion; IEA:Ensembl.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
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:0006972; P:hyperosmotic response; IBA:GO_Central.
DR GO; GO:0009992; P:intracellular water homeostasis; 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:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0030157; P:pancreatic juice secretion; IEA:Ensembl.
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; Glycerol uptake facilitator protein; 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 NCBIfam; TIGR00861; MIP; 1.
DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR PANTHER; PTHR19139:SF161; AQUAPORIN-1; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02013; AQUAPORIN1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Aquaporin-1"
FT /id="PRO_0000063918"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT TRANSMEM 10..34
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 35..50
FT /note="Extracellular"
FT TRANSMEM 51..68
FT /note="Helical; Name=Helix 2"
FT TOPO_DOM 69..73
FT /note="Cytoplasmic"
FT INTRAMEM 74..78
FT INTRAMEM 79..88
FT /note="Helical; Name=Helix B"
FT TOPO_DOM 89..92
FT /note="Cytoplasmic"
FT TRANSMEM 93..117
FT /note="Helical; Name=Helix 3"
FT TOPO_DOM 118..142
FT /note="Extracellular"
FT TRANSMEM 143..158
FT /note="Helical; Name=Helix 4"
FT TOPO_DOM 159..169
FT /note="Cytoplasmic"
FT TRANSMEM 170..187
FT /note="Helical; Name=Helix 5"
FT TOPO_DOM 188..189
FT /note="Extracellular"
FT INTRAMEM 190..193
FT INTRAMEM 194..204
FT /note="Helical; Name=Helix E"
FT TOPO_DOM 205..215
FT /note="Extracellular"
FT TRANSMEM 216..230
FT /note="Helical; Name=Helix 6"
FT TOPO_DOM 231..271
FT /note="Cytoplasmic"
FT MOTIF 78..80
FT /note="NPA 1"
FT MOTIF 194..196
FT /note="NPA 2"
FT SITE 58
FT /note="Substrate discrimination"
FT SITE 182
FT /note="Substrate discrimination"
FT SITE 191
FT /note="Hg(2+)-sensitive residue"
FT SITE 197
FT /note="Substrate discrimination"
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"
FT HELIX 6..33
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 51..73
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 93..117
FT /evidence="ECO:0007829|PDB:1J4N"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 170..189
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:1J4N"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:1J4N"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:1J4N"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1J4N"
SQ SEQUENCE 271 AA; 28800 MW; 3A1C9A2071CDA5E4 CRC64;
MASEFKKKLF WRAVVAEFLA MILFIFISIG SALGFHYPIK SNQTTGAVQD NVKVSLAFGL
SIATLAQSVG HISGAHLNPA VTLGLLLSCQ ISVLRAIMYI IAQCVGAIVA TAILSGITSS
LPDNSLGLNA LAPGVNSGQG LGIEIIGTLQ LVLCVLATTD RRRRDLGGSG PLAIGFSVAL
GHLLAIDYTG CGINPARSFG SSVITHNFQD HWIFWVGPFI GAALAVLIYD FILAPRSSDL
TDRVKVWTSG QVEEYDLDAD DINSRVEMKP K
//
