Aquaporin-3

AQP3
Identifiers
Aliases	AQP3, AQP-3, GIL, aquaporin 3 (Gill blood group)
External IDs	OMIM: 600170; MGI: 1333777; HomoloGene: 21025; GeneCards: AQP3; OMA:AQP3 - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	33,447,596 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	41,098,183 bp
RNA expression pattern
	Top expressed in
	nasal epithelium; ; gingival epithelium; ; mucosa of pharynx; ; epithelium of nasopharynx; ; parotid gland; ; human penis; ; palpebral conjunctiva; ; vulva; ; oral cavity; ; nipple;
	Top expressed in
	lip; ; olfactory epithelium; ; transitional epithelium of urinary bladder; ; yolk sac; ; esophagus; ; right kidney; ; mucous cell of stomach; ; skin of external ear; ; conjunctival fornix; ; cornea;
	More reference expression data
	n/a
Gene ontology
Molecular function	water channel activity; glycerol channel activity; transporter activity; channel activity; urea transmembrane transporter activity;
Cellular component	cytoplasm; integral component of membrane; membrane; cell-cell junction; plasma membrane; basolateral plasma membrane; nucleus;
Biological process	positive regulation of immune system process; excretion; response to vitamin D; response to retinoic acid; water transport; urea transport; odontogenesis; response to calcium ion; renal water homeostasis; regulation of keratinocyte differentiation; renal water absorption; glycerol transport; cellular response to oxygen-glucose deprivation; cellular response to hypoxia; transmembrane transport; urea transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	360
	11828
	ENSG00000165272
	ENSMUSG00000028435
	Q92482
	Q8R2N1
	NM_004925; NM_001318144
	NM_016689
	NP_001305073; NP_004916
	NP_057898
	Wikidata
View/Edit Human	View/Edit Mouse

Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene.^[5] It is found in the basolateral cell membrane of principal collecting duct cells and provides a pathway for water to exit these cells.^[6] Aquaporin-3 is also permeable to glycerol, ammonia, urea, and hydrogen peroxide. It is expressed in various tissues including the skin, respiratory tract, and kidneys as well as various types of cancers.^[7] In the kidney, aquaproin-3 is unresponsive to the antidiuretic hormone vasopressin, unlike aquaporin-2.^[8] This protein is also a determinant for the GIL blood group system.^[9]

Suberoylanilide hydroxamic acid (SAHA) (a HDAC inhibitor) increases expression of aquaporin-3 in normal skin cells (keratinocytes).^[10]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000165272 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028435 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. 18 (10): 2106. doi:10.3390/ijms18102106. PMC 5666788. PMID 28991174.
^ Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct". Annu. Rev. Physiol. 60: 199–220. doi:10.1146/annurev.physiol.60.1.199. PMID 9558461.
^ Oliveira Pinho J, Matias M, Gaspar MM (October 2019). "Emergent Nanotechnological Strategies for Systemic Chemotherapy against Melanoma". Nanomaterials. 9 (10): 1455. doi:10.3390/nano9101455. PMC 6836019. PMID 31614947.
^ Dibas AI, Mia AJ, Yorio, T (1998). "Aquaporins (Water Channels): Role in Vasopressin-Activated Water Transport". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. doi:10.3181/00379727-219-44332. PMID 9824541. S2CID 28952956.
^ Roudier N, Ripoche P, Gane P, Le Pennec PY, Daniels G, Cartron JP, Bailly P (2002). "AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL". J. Biol. Chem. 277 (48): 45854–9. doi:10.1074/jbc.M208999200. PMID 12239222.
^ University, Medical College of Georgia at Augusta. "Cancer therapy shows promise for psoriasis treatment". medicalxpress.com.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000165272 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028435 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid28991174-5] Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. 18 (10): 2106. doi:10.3390/ijms18102106. PMC 5666788. PMID 28991174.

[pmid9558461-6] Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct". Annu. Rev. Physiol. 60: 199–220. doi:10.1146/annurev.physiol.60.1.199. PMID 9558461.

[pmid31614947-7] Oliveira Pinho J, Matias M, Gaspar MM (October 2019). "Emergent Nanotechnological Strategies for Systemic Chemotherapy against Melanoma". Nanomaterials. 9 (10): 1455. doi:10.3390/nano9101455. PMC 6836019. PMID 31614947.

[pmid9824541-8] Dibas AI, Mia AJ, Yorio, T (1998). "Aquaporins (Water Channels): Role in Vasopressin-Activated Water Transport". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. doi:10.3181/00379727-219-44332. PMID 9824541. S2CID 28952956.

[pmid12239222-9] Roudier N, Ripoche P, Gane P, Le Pennec PY, Daniels G, Cartron JP, Bailly P (2002). "AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL". J. Biol. Chem. 277 (48): 45854–9. doi:10.1074/jbc.M208999200. PMID 12239222.

[MCG2017-10] University, Medical College of Georgia at Augusta. "Cancer therapy shows promise for psoriasis treatment". medicalxpress.com.

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