Sodium–hydrogen antiporter 3

Solute carrier family 9 (sodium/hydrogen exchanger), member 3
Identifiers
Symbols	SLC9A3; MGC126718; MGC126720; NHE3
External IDs	OMIM: 182307 MGI: 105064 HomoloGene: 55804 GeneCards: SLC9A3 Gene
Gene Ontology Molecular function • antiporter activity • solute:hydrogen antiporter activity • sodium:hydrogen antiporter activity • sodium:hydrogen antiporter activity Cellular component • plasma membrane • brush border • cell surface • integral to membrane • apical plasma membrane • brush border membrane Biological process • regulation of sodium ion transport • ion transport • cation transport • regulation of pH • receptor-mediated endocytosis • circadian rhythm • response to glucocorticoid stimulus • transmembrane transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6550	105243
Ensembl	ENSG00000066230	ENSMUSG00000036123
UniProt	P48764	n/a
RefSeq (mRNA)	NM_004174.2	NM_001081060.1
RefSeq (protein)	NP_004165.2	NP_001074529.1
Location (UCSC)	Chr 5: 0.47 – 0.52 Mb	Chr 13: 74.26 – 74.3 Mb
PubMed search	[1]	[2]

Sodium–hydrogen antiporter 3 also known as sodium–hydrogen exchanger 3 (NHE3) or solute carrier family 9 member 3 (SLC9A3) is a protein that in humans is encoded by the SLC9A3 gene.^[1][2]

SLC9A3 is a sodium–hydrogen antiporter. It is found in the nephron of the kidney and in the apical membrane of enterocytes of the intestine. It is primarily responsible for maintaining the balance of sodium.^[3]

Regulation

Protein kinase C stimulates NHE3, while protein kinase A inhibits it. ^[4]

There is a specific protein functioning as an NHE3 regulator, Sodium-hydrogen antiporter 3 regulator 1.

Interactions

Sodium-hydrogen antiporter 3 has been shown to interact with CHP.^[5]

References

1. ^ "Entrez Gene: SLC9A3 Solute carrier family 9 (sodium/hydrogen exchanger), member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6550. 
2. ^ Brant SR, Bernstein M, Wasmuth JJ, Taylor EW, McPherson JD, Li X, Walker S, Pouyssegur J, Donowitz M, Tse CM (March 1993). "Physical and genetic mapping of a human apical epithelial Na+/H+ exchanger (NHE3) isoform to chromosome 5p15.3". Genomics 15 (3): 668–72. doi:10.1006/geno.1993.1122. PMID 8096830. 
3. ^ VI. Mechanisms of Salt & Water Reabsorption
4. ^ 852 Walter F., PhD. Boron (2005). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. ISBN 1-4160-2328-3.  Page 852
5. ^ Inoue, Hiroki; Nakamura Yutaka, Nagita Mana, Takai Tomoyo, Masuda Miho, Nakamura Norihiro, Kanazawa Hiroshi (Feb. 2003). "Calcineurin homologous protein isoform 2 (CHP2), Na+/H+ exchangers-binding protein, is expressed in intestinal epithelium". Biol. Pharm. Bull. (Japan) 26 (2): 148–55. doi:10.1248/bpb.26.148. ISSN 0918-6158. PMID 12576672. 

Further reading

• McDonough AA, Leong PK, Yang LE (2003). "Mechanisms of pressure natriuresis: how blood pressure regulates renal sodium transport.". Ann. N. Y. Acad. Sci. 986: 669–77. doi:10.1111/j.1749-6632.2003.tb07281.x. PMID 12763917. 
• Orlowski J, Kandasamy RA, Shull GE (1992). "Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins.". J. Biol. Chem. 267 (13): 9331–9. PMID 1577762. 
• Brant SR, Yun CH, Donowitz M, Tse CM (1995). "Cloning, tissue distribution, and functional analysis of the human Na+/N+ exchanger isoform, NHE3.". Am. J. Physiol. 269 (1 Pt 1): C198–206. PMID 7631746. 
• Colombani V, Silviani V, Marteau C, et al. (1996). "Presence of the NHE3 isoform of the Na+/H+ exchanger in human gallbladder.". Clin. Sci. 91 (2): 209–12. PMID 8795445. 
• Dudeja PK, Rao DD, Syed I, et al. (1996). "Intestinal distribution of human Na+/H+ exchanger isoforms NHE-1, NHE-2, and NHE-3 mRNA.". Am. J. Physiol. 271 (3 Pt 1): G483–93. PMID 8843774. 
• Lin X, Barber DL (1996). "A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange.". Proc. Natl. Acad. Sci. U.S.A. 93 (22): 12631–6. doi:10.1073/pnas.93.22.12631. PMC 38044. PMID 8901634. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38044. 
• Yun CH, Lamprecht G, Forster DV, Sidor A (1998). "NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin.". J. Biol. Chem. 273 (40): 25856–63. doi:10.1074/jbc.273.40.25856. PMID 9748260. 
• Biemesderfer D, Nagy T, DeGray B, Aronson PS (1999). "Specific association of megalin and the Na+/H+ exchanger isoform NHE3 in the proximal tubule.". J. Biol. Chem. 274 (25): 17518–24. doi:10.1074/jbc.274.25.17518. PMID 10364184. 
• Mobasheri A, Golding S, Pagakis SN, et al. (1999). "Expression of cation exchanger NHE and anion exchanger AE isoforms in primary human bone-derived osteoblasts.". Cell Biol. Int. 22 (7–8): 551–62. doi:10.1006/cbir.1998.0299. PMID 10452823. 
• Trujillo E, Alvarez de la Rosa D, Mobasheri A, et al. (1999). "Sodium transport systems in human chondrocytes. II. Expression of ENaC, Na+/K+/2Cl- cotransporter and Na+/H+ exchangers in healthy and arthritic chondrocytes.". Histol. Histopathol. 14 (4): 1023–31. PMID 10506918. 
• Repishti M, Hogan DL, Pratha V, et al. (2001). "Human duodenal mucosal brush border Na(+)/H(+) exchangers NHE2 and NHE3 alter net bicarbonate movement.". Am. J. Physiol. Gastrointest. Liver Physiol. 281 (1): G159–63. PMID 11408268. 
• Malakooti J, Memark VC, Dudeja PK, Ramaswamy K (2002). "Molecular cloning and functional analysis of the human Na(+)/H(+) exchanger NHE3 promoter.". Am. J. Physiol. Gastrointest. Liver Physiol. 282 (3): G491–500. doi:10.1152/ajpgi.00273.2001. PMID 11841999. 
• Gekle M, Serrano OK, Drumm K, et al. (2002). "NHE3 serves as a molecular tool for cAMP-mediated regulation of receptor-mediated endocytosis.". Am. J. Physiol. Renal Physiol. 283 (3): F549–58. doi:10.1152/ajprenal.00206.2001. PMID 12167607. 
• Kennedy DJ, Leibach FH, Ganapathy V, Thwaites DT (2003). "Optimal absorptive transport of the dipeptide glycylsarcosine is dependent on functional Na+/H+ exchange activity.". Pflugers Arch. 445 (1): 139–46. doi:10.1007/s00424-002-0910-1. PMID 12397398. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Lee SH, Seok YS, Jung HH, et al. (2003). "Expression of mRNA transcripts of the Na+/H+ and Cl-/HCO3- exchanger isoforms in human nasal mucosa.". Acta Otolaryngol. 122 (8): 866–71. doi:10.1080/003655402/000028045. PMID 12542207. 
• Inoue H, Nakamura Y, Nagita M, et al. (2003). "Calcineurin homologous protein isoform 2 (CHP2), Na+/H+ exchangers-binding protein, is expressed in intestinal epithelium.". Biol. Pharm. Bull. 26 (2): 148–55. doi:10.1248/bpb.26.148. PMID 12576672. 
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 

External links

• MeSH Sodium-Hydrogen+Exchanger

P-type ATPase (3.A.3)

• 3.A.3.1.1: Na⁺/K⁺ transporting: ATP1A1, ATP1A2, ATP1A3, ATP1A4, ATP1B1, ATP1B2, ATP1B3, ATP1B4, ATP1G1

• 3.A.3.1.2: H+/K+, H⁺/K⁺ exchanging: ATP4A, ATP4B

• 3.A.3.1.4: H⁺/K⁺ transporting, nongastric: ATP12A

• 3.A.3.2: Ca+ (SERCA, PMCA, SPCA) / Ca⁺⁺ transporting: ATP2A1, ATP2A2, ATP2A3, ATP2B1, ATP2B2, ATP2B3, ATP2B4, ATP2C1

• 3.A.3.5: Cu⁺⁺ transporting: ATP7A, ATP7B

• 3.A.3.8.8: flippase: ATP8A2

Other/ungrouped:

Na+/K+ - H+

• Mg⁺⁺ transporting: ATP3
• Class I, type 8: ATP8A1, ATP8B1, ATP8B2, ATP8B3, ATP8B4
• Class II, type 9: ATP9A, ATP9B
• Class V, type 10: ATP10A, ATP10B, ATP10D
• Class VI, type 11: ATP11A, ATP11B, ATP11C
• type 13: ATP13A1, ATP13A2, ATP13A3, ATP13A4, ATP13A5

see also ATPase disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr