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Aquaporin-4 (AQP-4) (Mercurial-insensitive water channel) (MIWC) (WCH4)

 AQP4_RAT                Reviewed;         323 AA.
P47863;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Aquaporin-4;
Short=AQP-4;
AltName: Full=Mercurial-insensitive water channel;
Short=MIWC;
AltName: Full=WCH4;
Name=Aqp4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF HIS-201.
TISSUE=Brain;
PubMed=7528931; DOI=10.1073/pnas.91.26.13052;
Jung J.S., Bhat R.V., Preston G.M., Guggino W.B., Baraban J.M.,
Agre P.;
"Molecular characterization of an aquaporin cDNA from brain: candidate
osmoreceptor and regulator of water balance.";
Proc. Natl. Acad. Sci. U.S.A. 91:13052-13056(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Chen D., Chen J., Jing K., Simon R.P., Graham S.H.;
"Isolation of an aquaporin-4 water channel (AQP4) gene induced
following cerebral ischemia from the rat brain using modified
subtractive hybridization and differential screening.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-323.
TISSUE=Lung;
PubMed=7509789;
Hasegawa H., Ma T., Skach W., Matthay M.A., Verkman A.S.;
"Molecular cloning of a mercurial-insensitive water channel expressed
in selected water-transporting tissues.";
J. Biol. Chem. 269:5497-5500(1994).
[4]
PHOSPHORYLATION AT SER-285.
PubMed=12692561; DOI=10.1038/nbt819;
Wu C.C., MacCoss M.J., Howell K.E., Yates J.R. III;
"A method for the comprehensive proteomic analysis of membrane
proteins.";
Nat. Biotechnol. 21:532-538(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[6]
PHOSPHORYLATION AT SER-111.
PubMed=18286643; DOI=10.1002/glia.20627;
Gunnarson E., Zelenina M., Axehult G., Song Y., Bondar A., Krieger P.,
Brismar H., Zelenin S., Aperia A.;
"Identification of a molecular target for glutamate regulation of
astrocyte water permeability.";
Glia 56:587-596(2008).
[7]
PHOSPHORYLATION AT SER-180.
PubMed=19800950; DOI=10.1016/j.neuroscience.2009.09.072;
Moeller H.B., Fenton R.A., Zeuthen T., Macaulay N.;
"Vasopressin-dependent short-term regulation of aquaporin 4 expressed
in Xenopus oocytes.";
Neuroscience 164:1674-1684(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-285, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[9]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-323, AND SUBUNIT.
PubMed=16325200; DOI=10.1016/j.jmb.2005.10.081;
Hiroaki Y., Tani K., Kamegawa A., Gyobu N., Nishikawa K., Suzuki H.,
Walz T., Sasaki S., Mitsuoka K., Kimura K., Mizoguchi A.,
Fujiyoshi Y.;
"Implications of the aquaporin-4 structure on array formation and cell
adhesion.";
J. Mol. Biol. 355:628-639(2006).
[10]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-323, AND SUBUNIT.
PubMed=19406128; DOI=10.1016/j.jmb.2009.04.049;
Tani K., Mitsuma T., Hiroaki Y., Kamegawa A., Nishikawa K.,
Tanimura Y., Fujiyoshi Y.;
"Mechanism of aquaporin-4's fast and highly selective water conduction
and proton exclusion.";
J. Mol. Biol. 389:694-706(2009).
-!- FUNCTION: Forms a water-specific channel. Osmoreceptor which
regulates body water balance and mediates water flow within the
central nervous system. It is expressed predominantly in the
ependymal cell lining the aqueductal system and over the space of
the brain in contact with the subarachnoid space, as cerebrospinal
fluid fills these structures it may facilitate water balance
between brain parenchyma and the fluid compartment. In the plasma
membranes of the neurons of the paraventricular and supraoptic
nuclei, it may mediate rapid changes in cell volume in response to
local shifts in extracellular osmolarity.
-!- SUBUNIT: Homotetramer. Part of a complex containing MLC1, TRPV4,
HEPACAM and ATP1B1 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9HBA0:TRPV4 (xeno); NbExp=2; IntAct=EBI-15907676, EBI-962786;
Q9ERZ8:Trpv4; NbExp=2; IntAct=EBI-15907676, EBI-10095418;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P47863-1; Sequence=Displayed;
Name=Short;
IsoId=P47863-2; Sequence=VSP_003235;
-!- TISSUE SPECIFICITY: Abundant in mature brain but only weakly
detectable in eye, kidney, intestine, and lung.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- PTM: Phosphorylation by PKC at Ser-180 reduces conductance by 50%.
Phosphorylation by PKG at Ser-111 in response to glutamats
increases conductance by 40%. {ECO:0000269|PubMed:12692561,
ECO:0000269|PubMed:18286643, ECO:0000269|PubMed:19800950}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U14007; AAC52152.1; -; mRNA.
EMBL; AF144082; AAD37965.1; -; mRNA.
EMBL; L27588; AAA17730.1; -; mRNA.
PIR; I59283; I59283.
RefSeq; NP_001257487.1; NM_001270558.2. [P47863-2]
RefSeq; NP_036957.1; NM_012825.4. [P47863-1]
UniGene; Rn.90091; -.
PDB; 2D57; X-ray; 3.20 A; A=23-323.
PDB; 2ZZ9; X-ray; 2.80 A; A=23-323.
PDB; 3IYZ; EM; 10.00 A; A=23-323.
PDBsum; 2D57; -.
PDBsum; 2ZZ9; -.
PDBsum; 3IYZ; -.
ProteinModelPortal; P47863; -.
SMR; P47863; -.
BioGrid; 247332; 2.
CORUM; P47863; -.
DIP; DIP-59601N; -.
IntAct; P47863; 2.
STRING; 10116.ENSRNOP00000063720; -.
iPTMnet; P47863; -.
PhosphoSitePlus; P47863; -.
SwissPalm; P47863; -.
PaxDb; P47863; -.
PRIDE; P47863; -.
Ensembl; ENSRNOT00000068150; ENSRNOP00000063720; ENSRNOG00000016043. [P47863-1]
GeneID; 25293; -.
KEGG; rno:25293; -.
CTD; 361; -.
RGD; 2143; Aqp4.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P47863; -.
KO; K09866; -.
PhylomeDB; P47863; -.
Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-RNO-432047; Passive transport by Aquaporins.
EvolutionaryTrace; P47863; -.
PRO; PR:P47863; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000016043; -.
ExpressionAtlas; P47863; baseline and differential.
Genevisible; P47863; RN.
GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0031253; C:cell projection membrane; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0030315; C:T-tubule; IDA:RGD.
GO; GO:0015288; F:porin activity; IDA:RGD.
GO; GO:0015250; F:water channel activity; IDA:RGD.
GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IMP:RGD.
GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0042538; P:hyperosmotic salinity response; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0050891; P:multicellular organismal water homeostasis; ISO:RGD.
GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IMP:RGD.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:RGD.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IMP:RGD.
GO; GO:0070295; P:renal water absorption; ISO:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
GO; GO:0030104; P:water homeostasis; ISO:RGD.
GO; GO:0006833; P:water transport; IDA:RGD.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Glycoprotein;
Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 323 Aquaporin-4.
/FTId=PRO_0000063950.
TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.
TRANSMEM 37 57 Helical. {ECO:0000255}.
TOPO_DOM 58 64 Extracellular. {ECO:0000255}.
TRANSMEM 65 85 Helical. {ECO:0000255}.
TOPO_DOM 86 115 Cytoplasmic. {ECO:0000255}.
TRANSMEM 116 136 Helical. {ECO:0000255}.
TOPO_DOM 137 155 Extracellular. {ECO:0000255}.
TRANSMEM 156 176 Helical. {ECO:0000255}.
TOPO_DOM 177 184 Cytoplasmic. {ECO:0000255}.
TRANSMEM 185 205 Helical. {ECO:0000255}.
TOPO_DOM 206 231 Extracellular. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TOPO_DOM 253 323 Cytoplasmic. {ECO:0000255}.
MOTIF 97 99 NPA 1.
MOTIF 213 215 NPA 2.
MOD_RES 111 111 Phosphoserine; by PKG.
{ECO:0000269|PubMed:18286643}.
MOD_RES 180 180 Phosphoserine; by PKC.
{ECO:0000269|PubMed:19800950}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:12692561}.
MOD_RES 289 289 Phosphothreonine.
{ECO:0000250|UniProtKB:P55088}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 150 204 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_003235.
MUTAGEN 201 201 H->P: Partial loss of transport activity.
{ECO:0000269|PubMed:7528931}.
CONFLICT 201 201 H -> P (in Ref. 3; AAA17730).
{ECO:0000305}.
HELIX 32 53 {ECO:0000244|PDB:2ZZ9}.
STRAND 60 63 {ECO:0000244|PDB:2D57}.
HELIX 70 88 {ECO:0000244|PDB:2ZZ9}.
HELIX 89 91 {ECO:0000244|PDB:2ZZ9}.
HELIX 98 106 {ECO:0000244|PDB:2ZZ9}.
STRAND 108 110 {ECO:0000244|PDB:2ZZ9}.
TURN 112 115 {ECO:0000244|PDB:2ZZ9}.
HELIX 116 134 {ECO:0000244|PDB:2ZZ9}.
TURN 138 140 {ECO:0000244|PDB:2D57}.
HELIX 141 143 {ECO:0000244|PDB:2ZZ9}.
HELIX 156 177 {ECO:0000244|PDB:2ZZ9}.
STRAND 180 183 {ECO:0000244|PDB:2ZZ9}.
HELIX 189 208 {ECO:0000244|PDB:2ZZ9}.
HELIX 214 224 {ECO:0000244|PDB:2ZZ9}.
TURN 228 231 {ECO:0000244|PDB:2ZZ9}.
HELIX 232 249 {ECO:0000244|PDB:2ZZ9}.
TURN 250 252 {ECO:0000244|PDB:2ZZ9}.
SEQUENCE 323 AA; 34480 MW; 6ADD24647713609D CRC64;
MSDGAAARRW GKCGPPCSRE SIMVAFKGVW TQAFWKAVTA EFLAMLIFVL LSVGSTINWG
GSENPLPVDM VLISLCFGLS IATMVQCFGH ISGGHINPAV TVAMVCTRKI SIAKSVFYIT
AQCLGAIIGA GILYLVTPPS VVGGLGVTTV HGNLTAGHGL LVELIITFQL VFTIFASCDS
KRTDVTGSVA LAIGFSVAIG HLFAINYTGA SMNPARSFGP AVIMGNWENH WIYWVGPIIG
AVLAGALYEY VFCPDVELKR RLKEAFSKAA QQTKGSYMEV EDNRSQVETE DLILKPGVVH
VIDIDRGDEK KGKDSSGEVL SSV


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