Multidrug and toxin extrusion protein 2

SLC47A2
Identifiers
Aliases	SLC47A2 , MATE2, MATE2-B, MATE2-K, MATE2K, solute carrier family 47 member 2
External IDs	OMIM: 609833; HomoloGene: 135027; GeneCards: SLC47A2; OMA:SLC47A2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17p11.2 Start 19,678,288 bp [1] End 19,718,979 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube gums caput epididymis human kidney gingival epithelium skin of limb skin of leg skin of abdomen hypothalamus C1 segment n/a More reference expression data BioGPS n/a
Gene ontology Molecular function antiporter activity xenobiotic transmembrane transporter activity Cellular component integral component of membrane plasma membrane membrane Biological process transmembrane transport xenobiotic export xenobiotic transmembrane transport xenobiotic transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 146802 n/a Ensembl ENSG00000180638 n/a UniProt Q86VL8 n/a 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 Mb n/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

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

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

1. GRCh38: Ensembl release 89: ENSG00000180638 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: MATE2 H+/organic cation antiporter".
4. 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

• Tanihara Y, Masuda S, Sato T, Katsura T, Ogawa O, Inui K (July 2007). "Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters". Biochemical Pharmacology. 74 (2): 359–71. doi:10.1016/j.bcp.2007.04.010. hdl: 2433/124277 . PMID   17509534.
• Omote H, Hiasa M, Matsumoto T, Otsuka M, Moriyama Y (November 2006). "The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations". Trends in Pharmacological Sciences. 27 (11): 587–93. doi:10.1016/j.tips.2006.09.001. PMID   16996621.
• Masuda S, Terada T, Yonezawa A, Tanihara Y, Kishimoto K, Katsura T, Ogawa O, Inui K (August 2006). "Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2". Journal of the American Society of Nephrology. 17 (8): 2127–35. doi: 10.1681/ASN.2006030205 . PMID   16807400.
• 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". Proceedings of the National Academy of Sciences of the United States of America. 102 (50): 17923–8. doi: 10.1073/pnas.0506483102 . PMC   1312386 . PMID   16330770.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.