Multidrug and toxin extrusion protein 1: Difference between revisions

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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{PBB|geneid=55244}}
{{Infobox_gene}}
'''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]].<ref name="entrez">{{cite web | title = Entrez Gene: FLJ10847 hypothetical protein FLJ10847| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55244| accessdate = }}</ref><ref name="pmid16330770">{{cite journal | author = Otsuka M, Matsumoto T, Morimoto R, Arioka S, Omote H, Moriyama Y | title = A human transporter protein that mediates the final excretion step for toxic organic cations | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 50 | pages = 17923–8 | year = 2005 | month = December | pmid = 16330770 | pmc = 1312386 | doi = 10.1073/pnas.0506483102 | url = | issn = }}</ref> SLC47A1 belongs to the MATE (multidrug and toxic compound extrusion) family of transporters that are found in bacteria, archaea and eukaryotes.<ref name="pmid9661020">{{cite journal | author = 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 = Antimicrob. Agents Chemother. | volume = 42 | issue = 7 | pages = 1778–82 | year = 1998 | month = July | pmid = 9661020 | pmc = 105682 | doi = | url = | issn = }}</ref><ref name="pmid9987140">{{cite journal | author = Brown MH, Paulsen IT, Skurray RA | title = The multidrug efflux protein NorM is a prototype of a new family of transporters | journal = Mol. Microbiol. | volume = 31 | issue = 1 | pages = 394–5 | year = 1999 | month = January | pmid = 9987140 | doi = 10.1046/j.1365-2958.1999.01162.x| url = | issn = }}</ref>
'''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]].<ref name="entrez">{{cite web | title = Entrez Gene: FLJ10847 hypothetical protein FLJ10847| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55244}}</ref><ref name="pmid16330770">{{cite journal | vauthors = Otsuka M, Matsumoto T, Morimoto R, Arioka S, Omote H, Moriyama Y | title = A human transporter protein that mediates the final excretion step for toxic organic cations | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 50 | pages = 17923–8 |date=December 2005 | pmid = 16330770 | pmc = 1312386 | doi = 10.1073/pnas.0506483102 | doi-access = free }}</ref> SLC47A1 belongs to the MATE (multidrug and toxic compound extrusion) family of transporters that are found in bacteria, archaea and eukaryotes.<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 = Antimicrob. Agents Chemother. | volume = 42 | issue = 7 | pages = 1778–82 |date=July 1998 | pmid = 9661020 | pmc = 105682 | doi = 10.1128/AAC.42.7.1778}}</ref><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 = Mol. Microbiol. | 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>


== Gene ==
== Gene ==


The ''SLC47A1'' gene is located within the [[Smith-Magenis syndrome]] region on chromosome 17.<ref name="entrez"/>
The ''SLC47A1'' gene is located within the [[Smith–Magenis syndrome]] region on chromosome 17.<ref name="entrez"/>


== Function ==
== Function ==
Line 12: Line 13:
== Discovery ==
== Discovery ==


The multidrug [[efflux]] [[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, which is the first of Solute carrier family 47 member.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux]] transporter. <ref name="pmid11073914">{{cite journal | author = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump | journal = J. Bacteriol. | volume = 182 | issue = 23 | pages = 6694–7 | year = 2000 | month = December | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000| url = | issn = }}</ref> NorM is a prototype of a new [[transporter]] family and Brown ''et al.''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140"/> 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.<ref name="pmid20861838">{{cite journal | author = He X, Szewczyk P, Karykin A, 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| year = 2010 | month = | pmid = 20861838 | doi = 10.1038/nature09408}}</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, which is the first of Solute carrier family 47 member.<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.<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 = J. Bacteriol. | 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"/> 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.<ref name="pmid20861838">{{cite journal | vauthors = He X, Szewczyk P, Karykin A, 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| year = 2010 | pmid = 20861838 | doi = 10.1038/nature09408 | pmc=3152480| bibcode = 2010Natur.467..991H }}</ref>


== See also ==
== See also ==
Line 22: Line 23:
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
{{PBB_Further_reading
*{{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
| citations =
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal |vauthors=Bi W, Yan J, Stankiewicz P, etal |title=Genes in a refined Smith-Magenis syndrome critical deletion interval on chromosome 17p11.2 and the syntenic region of the mouse. |journal=Genome Res. |volume=12 |issue= 5 |pages= 713–28 |year= 2002 |pmid= 11997338 |doi= 10.1101/gr.73702 | pmc=186594 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal | author=Bi W, Yan J, Stankiewicz P, ''et al.'' |title=Genes in a refined Smith-Magenis syndrome critical deletion interval on chromosome 17p11.2 and the syntenic region of the mouse. |journal=Genome Res. |volume=12 |issue= 5 |pages= 713–28 |year= 2002 |pmid= 11997338 |doi= 10.1101/gr.73702 | pmc=186594 }}
*{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal |vauthors=Otsuka M, Matsumoto T, Morimoto R, etal |title=A human transporter protein that mediates the final excretion step for toxic organic cations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 50 |pages= 17923–8 |year= 2006 |pmid= 16330770 |doi= 10.1073/pnas.0506483102 | pmc=1312386 |doi-access=free }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | vauthors=Ohta KY, Inoue K, Hayashi Y, Yuasa H |title=Molecular identification and functional characterization of rat multidrug and toxin extrusion type transporter 1 as an organic cation/H+ antiporter in the kidney. |journal=Drug Metab. Dispos. |volume=34 |issue= 11 |pages= 1868–74 |year= 2006 |pmid= 16928787 |doi= 10.1124/dmd.106.010876 |s2cid=7746302 }}
*{{cite journal | author=Otsuka M, Matsumoto T, Morimoto R, ''et al.'' |title=A human transporter protein that mediates the final excretion step for toxic organic cations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 50 |pages= 17923–8 |year= 2006 |pmid= 16330770 |doi= 10.1073/pnas.0506483102 | pmc=1312386 }}
*{{cite journal |vauthors=Omote H, Hiasa M, Matsumoto T, etal |title=The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations. |journal=Trends Pharmacol. Sci. |volume=27 |issue= 11 |pages= 587–93 |year= 2007 |pmid= 16996621 |doi= 10.1016/j.tips.2006.09.001 }}
*{{cite journal | author=Ohta KY, Inoue K, Hayashi Y, Yuasa H |title=Molecular identification and functional characterization of rat multidrug and toxin extrusion type transporter 1 as an organic cation/H+ antiporter in the kidney. |journal=Drug Metab. Dispos. |volume=34 |issue= 11 |pages= 1868–74 |year= 2006 |pmid= 16928787 |doi= 10.1124/dmd.106.010876 }}
*{{cite journal |vauthors=Tsuda M, Terada T, Asaka J, etal |title=Oppositely directed H+ gradient functions as a driving force of rat H+/organic cation antiporter MATE1. |journal=Am. J. Physiol. Renal Physiol. |volume=292 |issue= 2 |pages= F593–8 |year= 2007 |pmid= 17047166 |doi= 10.1152/ajprenal.00312.2006 |s2cid=15246627 }}
*{{cite journal | author=Omote H, Hiasa M, Matsumoto T, ''et al.'' |title=The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations. |journal=Trends Pharmacol. Sci. |volume=27 |issue= 11 |pages= 587–93 |year= 2007 |pmid= 16996621 |doi= 10.1016/j.tips.2006.09.001 }}
*{{cite journal | vauthors=Chen Y, Zhang S, Sorani M, Giacomini KM |title=Transport of paraquat by human organic cation transporters and multidrug and toxic compound extrusion family. |journal=J. Pharmacol. Exp. Ther. |volume=322 |issue= 2 |pages= 695–700 |year= 2007 |pmid= 17495125 |doi= 10.1124/jpet.107.123554 |s2cid=17580413 }}
*{{cite journal | author=Tsuda M, Terada T, Asaka J, ''et al.'' |title=Oppositely directed H+ gradient functions as a driving force of rat H+/organic cation antiporter MATE1. |journal=Am. J. Physiol. Renal Physiol. |volume=292 |issue= 2 |pages= F593–8 |year= 2007 |pmid= 17047166 |doi= 10.1152/ajprenal.00312.2006 }}
*{{cite journal |vauthors=Tanihara Y, Masuda S, Sato T, etal |title=Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters. |journal=Biochem. Pharmacol. |volume=74 |issue= 2 |pages= 359–71 |year= 2007 |pmid= 17509534 |doi= 10.1016/j.bcp.2007.04.010 |hdl=2433/124277 |hdl-access=free }}
*{{cite journal | author=Chen Y, Zhang S, Sorani M, Giacomini KM |title=Transport of paraquat by human organic cation transporters and multidrug and toxic compound extrusion family. |journal=J. Pharmacol. Exp. Ther. |volume=322 |issue= 2 |pages= 695–700 |year= 2007 |pmid= 17495125 |doi= 10.1124/jpet.107.123554 }}
*{{cite journal |vauthors=Kajiwara M, Terada T, Asaka J, etal |title=Critical roles of Sp1 in gene expression of human and rat H+/organic cation antiporter MATE1. |journal=Am. J. Physiol. Renal Physiol. |volume=293 |issue= 5 |pages= F1564–70 |year= 2007 |pmid= 17855482 |doi= 10.1152/ajprenal.00322.2007 |s2cid=46209703 }}
*{{cite journal | author=Tanihara Y, Masuda S, Sato T, ''et al.'' |title=Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters. |journal=Biochem. Pharmacol. |volume=74 |issue= 2 |pages= 359–71 |year= 2007 |pmid= 17509534 |doi= 10.1016/j.bcp.2007.04.010 }}
*{{cite journal | author=Kajiwara M, Terada T, Asaka J, ''et al.'' |title=Critical roles of Sp1 in gene expression of human and rat H+/organic cation antiporter MATE1. |journal=Am. J. Physiol. Renal Physiol. |volume=293 |issue= 5 |pages= F1564–70 |year= 2007 |pmid= 17855482 |doi= 10.1152/ajprenal.00322.2007 }}
}}
{{refend}}
{{refend}}


{{Membrane transport proteins}}
{{Membrane transport proteins}}

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[[Category:Solute carrier family]]
[[Category:Solute carrier family]]

Latest revision as of 20:57, 13 October 2022

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

55244

67473

Ensembl

ENSG00000142494

ENSMUSG00000010122

UniProt

Q96FL8

Q8K0H1

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

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]

Gene[edit]

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

Function[edit]

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

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, 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[edit]

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

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142494 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000010122 – Ensembl, 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[edit]


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