F
IPR002657

Bile acid:sodium symporter/arsenical resistance protein Acr3

InterPro entry
Short nameBilAc:Na_symport/Acr3
Overlapping
homologous
superfamilies
 
family relationships

Description

This family of proteins are found both in prokaryotes and eukaryotes. They are related to the human bile acid:sodium symporters (TC 2.A.28), which are transmembrane proteins functioning in the liver in the uptake of bile acids from portal blood plasma, a process mediated by the co-transport of Na+
[1]
.

This entry also includes members of the ACR3 family of arsenite (As(III)) permeases, which confer resistance to arsenic by extrusion from cells
[9]
. They exist in prokaryotes and eukaryotes (lower plants and fungi)
[8, 5]
. The ACR3 permeases have ten-transmembrane span topology
[6]
. Corynebacterium glutamicum has three Acr3 proteins, CgAcr3-1, CgAcr3-2, and CgAcr3-3. CgAcr3-1 is thought to be an antiporter that catalyses arsenite-proton exchange
[10]
.

The Shewanella oneidensis Acr3 is not able to transport As(III) and confers resistance only to arsenate (As(V))
[3]
, whereas the Acr3 orthologue from Synechocystis mediates tolerance to As(III), As(V) and antimonite (Sb(III))
[4]
.

In budding yeast, overexpression of the Acr3 gene confers an arsenite- but not an arsenate-resistance phenotype
[2]
. Saccharomyces cerevisiae Acr3 is a plasma membrane metalloid/H+ antiporter that transports arsenite and antimonite
[7]
.

References

1.Functional expression cloning and characterization of the hepatocyte Na+/bile acid cotransport system. Hagenbuch B, Stieger B, Foguet M, Lubbert H, Meier PJ. Proc. Natl. Acad. Sci. U.S.A. 88, 10629-33, (1991). View articlePMID: 1961729

2.Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Bobrowicz P, Wysocki R, Owsianik G, Goffeau A, Ulaszewski S. Yeast 13, 819-28, (1997). View articlePMID: 9234670

3.Investigation of the structure and function of a Shewanella oneidensis arsenical-resistance family transporter. Xia X, Postis VL, Rahman M, Wright GS, Roach PC, Deacon SE, Ingram JC, Henderson PJ, Findlay JB, Phillips SE, McPherson MJ, Baldwin SA. Mol. Membr. Biol. 25, 691-705, (2008). View articlePMID: 19039703

4.Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. strain PCC 6803. Lopez-Maury L, Florencio FJ, Reyes JC. J. Bacteriol. 185, 5363-71, (2003). View articlePMID: 12949088

5.Multiple cysteine residues are necessary for sorting and transport activity of the arsenite permease Acr3p from Saccharomyces cerevisiae. Maciaszczyk-Dziubinska E, Migocka M, Wawrzycka D, Markowska K, Wysocki R. Biochim. Biophys. Acta 1838, 747-55, (2014). View articlePMID: 24291645

6.Transmembrane topology of the Acr3 family arsenite transporter from Bacillus subtilis. Aaltonen EK, Silow M. Biochim. Biophys. Acta 1778, 963-73, (2008). View articlePMID: 18088595

7.Acr3p is a plasma membrane antiporter that catalyzes As(III)/H(+) and Sb(III)/H(+) exchange in Saccharomyces cerevisiae. Maciaszczyk-Dziubinska E, Migocka M, Wysocki R. Biochim. Biophys. Acta 1808, 1855-9, (2011). View articlePMID: 21447319

8.A vacuolar arsenite transporter necessary for arsenic tolerance in the arsenic hyperaccumulating fern Pteris vittata is missing in flowering plants. Indriolo E, Na G, Ellis D, Salt DE, Banks JA. Plant Cell 22, 2045-57, (2010). View articlePMID: 20530755

9.Properties of arsenite efflux permeases (Acr3) from Alkaliphilus metalliredigens and Corynebacterium glutamicum. Fu HL, Meng Y, Ordonez E, Villadangos AF, Bhattacharjee H, Gil JA, Mateos LM, Rosen BP. J. Biol. Chem. 284, 19887-95, (2009). View articlePMID: 19494117

10.Efflux permease CgAcr3-1 of Corynebacterium glutamicum is an arsenite-specific antiporter. Villadangos AF, Fu HL, Gil JA, Messens J, Rosen BP, Mateos LM. J. Biol. Chem. 287, 723-35, (2012). View articlePMID: 22102279

GO terms

biological process

  • None

molecular function

  • None

cellular component

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