Multidrug and toxin extrusion protein 2: Difference between revisions
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Importing Wikidata short description: "Protein-coding gene in the species Homo sapiens" |
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== Function == |
== Function == |
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This gene encodes a protein belonging to a family of transporters involved in 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.<ref name="pmid9661020">{{cite journal | vauthors = Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T | title = NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli | journal = Antimicrobial Agents and Chemotherapy | volume = 42 | issue = 7 | pages = 1778–82 | date = July 1998 | pmid = 9661020 | pmc = 105682 | doi = 10.1128/AAC.42.7.1778}}</ref> 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.<ref name="entrez"/> |
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.<ref name="pmid9661020">{{cite journal | vauthors = Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T | title = NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli | journal = Antimicrobial Agents and Chemotherapy | volume = 42 | issue = 7 | pages = 1778–82 | date = July 1998 | pmid = 9661020 | pmc = 105682 | doi = 10.1128/AAC.42.7.1778}}</ref> 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.<ref name="entrez"/> |
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== Discovery == |
== Discovery == |
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The multidrug [[efflux (microbiology)|efflux]] [[Membrane transport protein|transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]]'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.) and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux (microbiology)|efflux]] transporter discovered.<ref name="pmid11073914">{{cite journal | vauthors = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump | journal = Journal of Bacteriology | volume = 182 | issue = 23 | pages = 6694–7 | date = December 2000 | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000 }}</ref> NorM is a prototype of a new [[Membrane transport protein|transporter]] family and Brown ''et al''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140">{{cite journal | vauthors = Brown MH, Paulsen IT, Skurray RA | title = The multidrug efflux protein NorM is a prototype of a new family of transporters | journal = Molecular Microbiology | volume = 31 | issue = 1 | pages = 394–5 | date = January 1999 | pmid = 9987140 | doi = 10.1046/j.1365-2958.1999.01162.x | s2cid = 39261040 | doi-access = free }}</ref> The X-ray structure of the 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.<ref name="pmid20861838">{{cite journal | vauthors = He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, Chang G | title = Structure of a cation-bound multidrug and toxic compound extrusion transporter | journal = Nature | volume = 467 | issue = 7318 | pages = 991–4 | date = October 2010 | pmid = 20861838 | pmc = 3152480 | doi = 10.1038/nature09408 | bibcode = 2010Natur.467..991H }}</ref> |
The multidrug [[efflux (microbiology)|efflux]] [[Membrane transport protein|transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]],'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.), and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998.<ref name="pmid9661020"/> NorM seems to function as a drug/sodium [[antiporter]], which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux (microbiology)|efflux]] transporter discovered.<ref name="pmid11073914">{{cite journal | vauthors = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump | journal = Journal of Bacteriology | volume = 182 | issue = 23 | pages = 6694–7 | date = December 2000 | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000 }}</ref> NorM is a prototype of a new [[Membrane transport protein|transporter]] family, and Brown ''et al''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140">{{cite journal | vauthors = Brown MH, Paulsen IT, Skurray RA | title = The multidrug efflux protein NorM is a prototype of a new family of transporters | journal = Molecular Microbiology | volume = 31 | issue = 1 | pages = 394–5 | date = January 1999 | pmid = 9987140 | doi = 10.1046/j.1365-2958.1999.01162.x | s2cid = 39261040 | doi-access = free }}</ref> 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.<ref name="pmid20861838">{{cite journal | vauthors = He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, Chang G | title = Structure of a cation-bound multidrug and toxic compound extrusion transporter | journal = Nature | volume = 467 | issue = 7318 | pages = 991–4 | date = October 2010 | pmid = 20861838 | pmc = 3152480 | doi = 10.1038/nature09408 | bibcode = 2010Natur.467..991H }}</ref> |
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== References == |
== References == |
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Latest revision as of 06:59, 23 April 2024
| SLC47A2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Multidrug and toxin extrusion protein 2 is a protein which in humans is encoded by the SLC47A2 gene.[3]
Function[edit]
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[edit]
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[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000180638 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: MATE2 H+/organic cation antiporter".
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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[edit]
- 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.
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