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Aquaporin-3 (AQP-3) (Aquaglyceroporin-3)

 AQP3_HUMAN              Reviewed;         292 AA.
Q92482; A8K843; B2RE16; D3DRL3; O00108; Q6FGT2; Q6FGW6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
27-SEP-2017, entry version 157.
RecName: Full=Aquaporin-3;
Short=AQP-3;
AltName: Full=Aquaglyceroporin-3;
Name=AQP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=7558005; DOI=10.1006/geno.1995.1055;
Ishibashi K., Sasaki S., Saito F., Ikeuchi T., Marumo F.;
"Structure and chromosomal localization of a human water channel
(AQP3) gene.";
Genomics 27:352-354(1995).
[2]
SEQUENCE REVISION TO 91; 96 AND 186.
Ishibashi K.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND GIL BLOOD GROUP SYSTEM.
TISSUE=Blood;
PubMed=12239222; DOI=10.1074/jbc.M208999200;
Roudier N., Ripoche P., Gane P., Le Pennec P.Y., Daniels G.,
Cartron J.-P., Bailly P.;
"AQP3 deficiency in humans and the molecular basis of a novel blood
group system, GIL.";
J. Biol. Chem. 277:45854-45859(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Esophagus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-43.
SeattleSNPs variation discovery resource;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[11]
INDUCTION.
PubMed=18495115; DOI=10.1016/j.ejphar.2008.03.063;
Okahira M., Kubota M., Iguchi K., Usui S., Hirano K.;
"Regulation of aquaporin 3 expression by magnesium ion.";
Eur. J. Pharmacol. 588:26-32(2008).
-!- FUNCTION: Water channel required to promote glycerol permeability
and water transport across cell membranes. Acts as a glycerol
transporter in skin and plays an important role in regulating SC
(stratum corneum) and epidermal glycerol content. Involved in skin
hydration, wound healing, and tumorigenesis. Provides kidney
medullary collecting duct with high permeability to water, thereby
permitting water to move in the direction of an osmotic gradient.
Slightly permeable to urea and may function as a water and urea
exit mechanism in antidiuresis in collecting duct cells. It may
play an important role in gastrointestinal tract water transport
and in glycerol metabolism (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
membrane protein. Note=In collecting ducts of kidney.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92482-1; Sequence=Displayed;
Name=2; Synonyms=delta5;
IsoId=Q92482-2; Sequence=VSP_003229, VSP_003230;
Note=Due to a polymorphism at the 5'-splice donor site of intron
5, leading to exon 5 skipping and premature termination of
translation. This is the molecular basis of the GIL blood
group.;
-!- TISSUE SPECIFICITY: Widely expressed in epithelial cells of kidney
(collecting ducts) and airways, in keratinocytes, immature
dendritic cells and erythrocytes. Isoform 2 is not detectable in
erythrocytes at the protein level.
-!- INDUCTION: Up-regulated by magnesium.
{ECO:0000269|PubMed:18495115}.
-!- 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).
-!- POLYMORPHISM: AQP3 is responsible for the GIL blood group system.
Isoform 2 is detected in GIL-negative individuals that lack
functional AQP3.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=gil";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/aqp3/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB001325; BAA19237.1; -; mRNA.
EMBL; AJ493597; CAD38526.1; -; mRNA.
EMBL; CR541991; CAG46788.1; -; mRNA.
EMBL; CR542025; CAG46822.1; -; mRNA.
EMBL; BT007199; AAP35863.1; -; mRNA.
EMBL; AK292208; BAF84897.1; -; mRNA.
EMBL; AK315760; BAG38113.1; -; mRNA.
EMBL; DQ083949; AAY68214.1; -; Genomic_DNA.
EMBL; AL356218; CAI13311.1; -; Genomic_DNA.
EMBL; CH471071; EAW58500.1; -; Genomic_DNA.
EMBL; CH471071; EAW58504.1; -; Genomic_DNA.
EMBL; BC013566; AAH13566.1; -; mRNA.
CCDS; CCDS6542.1; -. [Q92482-1]
PIR; A57119; A57119.
RefSeq; NP_001305073.1; NM_001318144.1.
RefSeq; NP_004916.1; NM_004925.4. [Q92482-1]
UniGene; Hs.234642; -.
ProteinModelPortal; Q92482; -.
BioGrid; 106856; 3.
IntAct; Q92482; 4.
STRING; 9606.ENSP00000297991; -.
BioMuta; AQP3; -.
DMDM; 2497938; -.
PaxDb; Q92482; -.
PeptideAtlas; Q92482; -.
PRIDE; Q92482; -.
DNASU; 360; -.
Ensembl; ENST00000297991; ENSP00000297991; ENSG00000165272. [Q92482-1]
GeneID; 360; -.
KEGG; hsa:360; -.
UCSC; uc003zsx.4; human. [Q92482-1]
CTD; 360; -.
DisGeNET; 360; -.
EuPathDB; HostDB:ENSG00000165272.14; -.
GeneCards; AQP3; -.
HGNC; HGNC:636; AQP3.
HPA; HPA014924; -.
MIM; 600170; gene.
MIM; 607457; phenotype.
neXtProt; NX_Q92482; -.
OpenTargets; ENSG00000165272; -.
PharmGKB; PA24921; -.
eggNOG; KOG0224; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00510000046311; -.
HOGENOM; HOG000288287; -.
HOVERGEN; HBG106057; -.
InParanoid; Q92482; -.
KO; K09876; -.
OMA; ITSMLMG; -.
OrthoDB; EOG091G0FMS; -.
PhylomeDB; Q92482; -.
TreeFam; TF313173; -.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-432047; Passive transport by Aquaporins.
ChiTaRS; AQP3; human.
GeneWiki; Aquaporin_3; -.
GenomeRNAi; 360; -.
PRO; PR:Q92482; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165272; -.
CleanEx; HS_AQP3; -.
Genevisible; Q92482; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IC:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015254; F:glycerol channel activity; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; NAS:ProtInc.
GO; GO:0015250; F:water channel activity; EXP:Reactome.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
GO; GO:0002684; P:positive regulation of immune system process; IDA:BHF-UCL.
GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:BHF-UCL.
GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0051592; P:response to calcium ion; TAS:BHF-UCL.
GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
GO; GO:0033280; P:response to vitamin D; TAS:BHF-UCL.
GO; GO:0006810; P:transport; NAS:ProtInc.
GO; GO:0015840; P:urea transport; IEA:Ensembl.
GO; GO:0006833; P:water transport; TAS:BHF-UCL.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR023275; Aquaporin_3.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
Pfam; PF00230; MIP; 1.
PRINTS; PR02015; AQUAPORIN3.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
2: Evidence at transcript level;
Alternative splicing; Blood group antigen; Cell membrane;
Complete proteome; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 292 Aquaporin-3.
/FTId=PRO_0000063943.
TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 53 Extracellular. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255}.
TOPO_DOM 75 109 Cytoplasmic. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TOPO_DOM 131 157 Extracellular. {ECO:0000255}.
TRANSMEM 158 178 Helical. {ECO:0000255}.
TOPO_DOM 179 188 Cytoplasmic. {ECO:0000255}.
TRANSMEM 189 209 Helical. {ECO:0000255}.
TOPO_DOM 210 244 Extracellular. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TOPO_DOM 266 292 Cytoplasmic. {ECO:0000255}.
MOTIF 83 85 NPA 1.
MOTIF 215 217 NPA 2.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 165 281 FIGTASLIVCVLAIVDPYNNPVPRGLEAFTVGLVVLVIGTS
MGFNSGYAVNPARDFGPRLFTALAGWGSAVFTTGQHWWWVP
IVSPLLGSIAGVFVYQLMIGCHLEQPPPSNEEENV -> DR
PALVVGAHRVPTPGLHCGCLRVPADDRLPPGAAPTLQRGRE
CEAGPCEAQGADLSGKGHLPLRCPGLEHPLTVQGHSQEAPL
HDPPFQAKELPIYPHPTKTAPSGFPLDLAQIAP (in
isoform 2).
{ECO:0000303|PubMed:12239222}.
/FTId=VSP_003229.
VAR_SEQ 282 292 Missing (in isoform 2).
{ECO:0000303|PubMed:12239222}.
/FTId=VSP_003230.
VARIANT 43 43 V -> M (in dbSNP:rs34942735).
{ECO:0000269|Ref.7}.
/FTId=VAR_025089.
CONFLICT 23 23 R -> G (in Ref. 6; BAF84897).
{ECO:0000305}.
CONFLICT 137 137 V -> A (in Ref. 4; CAG46822).
{ECO:0000305}.
SEQUENCE 292 AA; 31544 MW; A9555E9576EABA9C CRC64;
MGRQKELVSR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN
LAFGFAVTLG ILIAGQVSGA HLNPAVTFAM CFLAREPWIK LPIYTLAQTL GAFLGAGIVF
GLYYDAIWHF ADNQLFVSGP NGTAGIFATY PSGHLDMING FFDQFIGTAS LIVCVLAIVD
PYNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTALAG WGSAVFTTGQ
HWWWVPIVSP LLGSIAGVFV YQLMIGCHLE QPPPSNEEEN VKLAHVKHKE QI


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