Multidrug and toxin extrusion protein 1

(Redirected from SLC47A1)

Multidrug and toxin extrusion protein 1 (MATE1), also known as solute carrier family 47 member 1, is a protein that in humans is encoded by the SLC47A1 gene.[5][6] SLC47A1 belongs to the MATE (multidrug and toxic compound extrusion) family of transporters that are found in bacteria, archaea and eukaryotes.[7][8]

SLC47A1
Identifiers
AliasesSLC47A1, MATE1, solute carrier family 47 member 1
External IDsOMIM: 609832; MGI: 1914723; HomoloGene: 34364; GeneCards: SLC47A1; OMA:SLC47A1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_018242

NM_026183

RefSeq (protein)

NP_060712

NP_080459

Location (UCSC)Chr 17: 19.5 – 19.58 MbChr 11: 61.23 – 61.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gene

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The SLC47A1 gene is located within the Smith–Magenis syndrome region on chromosome 17.[5]

Function

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SLC47A1 is a member of the MATE family of transporters that excrete endogenous and exogenous toxic electrolytes through urine and bile.[6]

Discovery

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The multidrug efflux transporter NorM from V. parahaemolyticus which mediates resistance to multiple antimicrobial agents (norfloxacin, kanamycin, ethidium bromide etc.) and its homologue from E. coli were identified in 1998, which is the first of Solute carrier family 47 member.[7] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter.[9] NorM is a prototype of a new transporter family and Brown et al. named it the multidrug and toxic compound extrusion family.[8] The X-ray structure of the transporter NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.[10]

See also

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  • MATE (Multi antimicrobial extrusion protein or multidrug and toxic compound extrusion protein)

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142494Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000010122Ensembl, 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.
  5. ^ a b "Entrez Gene: FLJ10847 hypothetical protein FLJ10847".
  6. ^ a b Otsuka M, Matsumoto T, Morimoto R, Arioka S, Omote H, Moriyama Y (December 2005). "A human transporter protein that mediates the final excretion step for toxic organic cations". Proc. Natl. Acad. Sci. U.S.A. 102 (50): 17923–8. doi:10.1073/pnas.0506483102. PMC 1312386. PMID 16330770.
  7. ^ a b Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T (July 1998). "NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli". Antimicrob. Agents Chemother. 42 (7): 1778–82. doi:10.1128/AAC.42.7.1778. PMC 105682. PMID 9661020.
  8. ^ a b Brown MH, Paulsen IT, Skurray RA (January 1999). "The multidrug efflux protein NorM is a prototype of a new family of transporters". Mol. Microbiol. 31 (1): 394–5. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140. S2CID 39261040.
  9. ^ Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (December 2000). "NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump". J. Bacteriol. 182 (23): 6694–7. doi:10.1128/JB.182.23.6694-6697.2000. PMC 111412. PMID 11073914.
  10. ^ He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G (2010). "Structure of a cation-bound multidrug and toxic compound extrusion transporter". Nature. 467 (7318): 991–4. Bibcode:2010Natur.467..991H. doi:10.1038/nature09408. PMC 3152480. PMID 20861838.

Further reading

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