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Multidrug and toxin extrusion protein 2

From Wikipedia, the free encyclopedia
SLC47A2
Identifiers
AliasesSLC47A2, MATE2, MATE2-B, MATE2-K, MATE2K, solute carrier family 47 member 2
External IDsOMIM: 609833; HomoloGene: 135027; GeneCards: SLC47A2; OMA:SLC47A2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001099646
NM_001256663
NM_152908

n/a

RefSeq (protein)

NP_001093116
NP_001243592
NP_690872

n/a

Location (UCSC)Chr 17: 19.68 – 19.72 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Multidrug and toxin extrusion protein 2 is a protein which in humans is encoded by the SLC47A2 gene.[3]

Function

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This gene encodes a protein belonging to a family of transporters involved in the excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE (multi antimicrobial extrusion protein or multidrug and toxic compound extrusion) protein family responsible for drug resistance.[4] This gene is one of two members of the MATE transporter family located near each other on chromosome 17. Alternatively, spliced transcript variants encoding different isoforms have been identified for this gene.[3]

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.[4] NorM seems to function as a drug/sodium antiporter, which is the first example of Na+-coupled multidrug efflux transporter discovered.[5] NorM is a prototype of a new transporter family, and Brown et al. named it the multidrug and toxic compound extrusion family.[6] The X-ray structure of the NorM was determined to be 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.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000180638Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ a b "Entrez Gene: MATE2 H+/organic cation antiporter".
  4. ^ 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". Antimicrobial Agents and Chemotherapy. 42 (7): 1778–82. doi:10.1128/AAC.42.7.1778. PMC 105682. PMID 9661020.
  5. ^ Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (December 2000). "NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump". Journal of Bacteriology. 182 (23): 6694–7. doi:10.1128/JB.182.23.6694-6697.2000. PMC 111412. PMID 11073914.
  6. ^ Brown MH, Paulsen IT, Skurray RA (January 1999). "The multidrug efflux protein NorM is a prototype of a new family of transporters". Molecular Microbiology. 31 (1): 394–5. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140. S2CID 39261040.
  7. ^ He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, Chang G (October 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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