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Aquaporin-5 (AQP-5)

 AQP5_HUMAN              Reviewed;         265 AA.
P55064; Q6FGW8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 148.
RecName: Full=Aquaporin-5;
Short=AQP-5;
Name=AQP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8621489; DOI=10.1074/jbc.271.15.8599;
Lee M.D., Bhakta K.Y., Raina S., Yonescu R., Griffin C.A.,
Copeland N.G., Gilbert D.J., Jenkins N.A., Preston G.M., Agre P.;
"The human aquaporin-5 gene. Molecular characterization and
chromosomal localization.";
J. Biol. Chem. 271:8599-8604(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND INTERACTION WITH TRPV4.
PubMed=16571723; DOI=10.1074/jbc.M600549200;
Liu X., Bandyopadhyay B.C., Bandyopadhyay B., Nakamoto T., Singh B.,
Liedtke W., Melvin J.E., Ambudkar I.;
"A role for AQP5 in activation of TRPV4 by hypotonicity: concerted
involvement of AQP5 and TRPV4 in regulation of cell volume recovery.";
J. Biol. Chem. 281:15485-15495(2006).
[5]
VARIANTS PPKB GLU-38; SER-45; ASP-123; PHE-177 AND CYS-188, AND
CHARACTERIZATION OF VARIANTS GLU-38; SER-45; ASP-123; PHE-177 AND
CYS-188.
PubMed=23830519; DOI=10.1016/j.ajhg.2013.06.008;
Blaydon D.C., Lind L.K., Plagnol V., Linton K.J., Smith F.J.,
Wilson N.J., McLean W.H., Munro C.S., South A.P., Leigh I.M.,
O'Toole E.A., Lundstroem A., Kelsell D.P.;
"Mutations in AQP5, encoding a water-channel protein, cause autosomal-
dominant diffuse nonepidermolytic palmoplantar keratoderma.";
Am. J. Hum. Genet. 93:330-335(2013).
-!- FUNCTION: Forms a water-specific channel. Implicated in the
generation of saliva, tears, and pulmonary secretions. Required
for TRPV4 activation by hypotonicity (PubMed:16571723). Together
with TRPV4, controls regulatory volume decrease in salivary
epithelial cells (PubMed:16571723). {ECO:0000269|PubMed:16571723}.
-!- SUBUNIT: Interacts with TRPV4; the interaction is probably
indirect and regulates TRPV4 activation by hypotonicity.
{ECO:0000269|PubMed:16571723}.
-!- INTERACTION:
P61978:HNRNPK; NbExp=3; IntAct=EBI-746103, EBI-304185;
Q15323:KRT31; NbExp=3; IntAct=EBI-746103, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-746103, EBI-10171697;
Q99750:MDFI; NbExp=3; IntAct=EBI-746103, EBI-724076;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-746103, EBI-945833;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:Q9WTY4}; Multi-pass membrane protein
{ECO:0000255}.
-!- 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).
-!- DISEASE: Keratoderma, palmoplantar, Bothnian type (PPKB)
[MIM:600231]: A dermatological disorder characterized by diffuse
non-epidermolytic hyperkeratosis of the skin of palms and soles.
PPKB is frequently complicated by fungal infections.
{ECO:0000269|PubMed:23830519}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U46569; AAC50474.1; -; Genomic_DNA.
EMBL; U46566; AAC50474.1; JOINED; Genomic_DNA.
EMBL; U46567; AAC50474.1; JOINED; Genomic_DNA.
EMBL; U46568; AAC50474.1; JOINED; Genomic_DNA.
EMBL; CR541989; CAG46786.1; -; mRNA.
EMBL; CR542022; CAG46819.1; -; mRNA.
EMBL; BC032946; AAH32946.1; -; mRNA.
CCDS; CCDS8793.1; -.
RefSeq; NP_001642.1; NM_001651.3.
UniGene; Hs.298023; -.
PDB; 3D9S; X-ray; 2.00 A; A/B/C/D=2-265.
PDB; 5C5X; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-245.
PDB; 5DYE; X-ray; 3.50 A; A/B/C/D=1-265.
PDBsum; 3D9S; -.
PDBsum; 5C5X; -.
PDBsum; 5DYE; -.
ProteinModelPortal; P55064; -.
SMR; P55064; -.
BioGrid; 106858; 8.
DIP; DIP-46292N; -.
IntAct; P55064; 8.
MINT; MINT-1442891; -.
STRING; 9606.ENSP00000293599; -.
TCDB; 1.A.8.8.9; the major intrinsic protein (mip) family.
iPTMnet; P55064; -.
PhosphoSitePlus; P55064; -.
DMDM; 1703358; -.
PaxDb; P55064; -.
PeptideAtlas; P55064; -.
PRIDE; P55064; -.
DNASU; 362; -.
Ensembl; ENST00000293599; ENSP00000293599; ENSG00000161798.
GeneID; 362; -.
KEGG; hsa:362; -.
UCSC; uc001rvo.4; human.
CTD; 362; -.
DisGeNET; 362; -.
EuPathDB; HostDB:ENSG00000161798.6; -.
GeneCards; AQP5; -.
HGNC; HGNC:638; AQP5.
HPA; HPA065008; -.
MalaCards; AQP5; -.
MIM; 600231; phenotype.
MIM; 600442; gene.
neXtProt; NX_P55064; -.
OpenTargets; ENSG00000161798; -.
Orphanet; 2337; Non-epidermolytic palmoplantar keratoderma.
PharmGKB; PA24923; -.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P55064; -.
KO; K09867; -.
OMA; WEDHREE; -.
OrthoDB; EOG091G166T; -.
PhylomeDB; P55064; -.
TreeFam; TF312940; -.
Reactome; R-HSA-432047; Passive transport by Aquaporins.
EvolutionaryTrace; P55064; -.
GeneWiki; AQP5; -.
GenomeRNAi; 362; -.
PRO; PR:P55064; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000161798; -.
CleanEx; HS_AQP5; -.
Genevisible; P55064; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
GO; GO:0030157; P:pancreatic juice secretion; IEP:UniProtKB.
GO; GO:0046541; P:saliva secretion; IEA:Ensembl.
GO; GO:0006833; P:water transport; TAS:Reactome.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR023276; Aquaporin_5.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
PANTHER; PTHR19139:SF228; PTHR19139:SF228; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR02017; AQUAPORIN5.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disease mutation;
Glycoprotein; Membrane; Palmoplantar keratoderma; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 265 Aquaporin-5.
/FTId=PRO_0000063951.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TOPO_DOM 34 36 Extracellular. {ECO:0000255}.
TRANSMEM 37 57 Helical. {ECO:0000255}.
TOPO_DOM 58 87 Cytoplasmic. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TOPO_DOM 148 161 Cytoplasmic. {ECO:0000255}.
TRANSMEM 162 182 Helical. {ECO:0000255}.
TOPO_DOM 183 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TOPO_DOM 227 265 Cytoplasmic. {ECO:0000255}.
MOTIF 69 71 NPA 1.
MOTIF 185 187 NPA 2.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 38 38 A -> E (in PPKB; retains the ability to
traffic to the cell membrane;
dbSNP:rs398123054).
{ECO:0000269|PubMed:23830519}.
/FTId=VAR_070442.
VARIANT 45 45 I -> S (in PPKB; retains the ability to
traffic to the cell membrane;
dbSNP:rs398123055).
{ECO:0000269|PubMed:23830519}.
/FTId=VAR_070443.
VARIANT 123 123 N -> D (in PPKB; retains the ability to
traffic to the cell membrane;
dbSNP:rs398123057).
{ECO:0000269|PubMed:23830519}.
/FTId=VAR_070444.
VARIANT 177 177 I -> F (in PPKB; retains the ability to
traffic to the cell membrane;
dbSNP:rs398123056).
{ECO:0000269|PubMed:23830519}.
/FTId=VAR_070445.
VARIANT 188 188 R -> C (in PPKB; retains the ability to
traffic to the cell membrane;
dbSNP:rs368292687).
{ECO:0000269|PubMed:23830519}.
/FTId=VAR_070446.
HELIX 2 5 {ECO:0000244|PDB:3D9S}.
HELIX 8 32 {ECO:0000244|PDB:3D9S}.
STRAND 36 38 {ECO:0000244|PDB:3D9S}.
HELIX 42 64 {ECO:0000244|PDB:3D9S}.
HELIX 70 78 {ECO:0000244|PDB:3D9S}.
STRAND 80 82 {ECO:0000244|PDB:3D9S}.
HELIX 84 108 {ECO:0000244|PDB:3D9S}.
HELIX 111 114 {ECO:0000244|PDB:3D9S}.
TURN 115 118 {ECO:0000244|PDB:3D9S}.
STRAND 124 126 {ECO:0000244|PDB:5DYE}.
HELIX 128 150 {ECO:0000244|PDB:3D9S}.
HELIX 161 180 {ECO:0000244|PDB:3D9S}.
HELIX 186 196 {ECO:0000244|PDB:3D9S}.
HELIX 203 223 {ECO:0000244|PDB:3D9S}.
TURN 233 235 {ECO:0000244|PDB:3D9S}.
HELIX 236 239 {ECO:0000244|PDB:3D9S}.
SEQUENCE 265 AA; 28292 MW; 053C10E6A17EAFDA CRC64;
MKKEVCSVAF LKAVFAEFLA TLIFVFFGLG SALKWPSALP TILQIALAFG LAIGTLAQAL
GPVSGGHINP AITLALLVGN QISLLRAFFY VAAQLVGAIA GAGILYGVAP LNARGNLAVN
ALNNNTTQGQ AMVVELILTF QLALCIFAST DSRRTSPVGS PALSIGLSVT LGHLVGIYFT
GCSMNPARSF GPAVVMNRFS PAHWVFWVGP IVGAVLAAIL YFYLLFPNSL SLSERVAIIK
GTYEPDEDWE EQREERKKTM ELTTR


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