| 释义 |
- Gene
- Function
- Discovery
- See also
- References
- Further reading
{{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.[1][2] SLC47A1 belongs to the MATE (multidrug and toxic compound extrusion) family of transporters that are found in bacteria, archaea and eukaryotes.[3][4] Gene The SLC47A1 gene is located within the Smith-Magenis syndrome region on chromosome 17.[1] Function SLC47A1 is a member of the MATE family of transporters that excrete endogenous and exogenous toxic electrolytes through urine and bile.[2] 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, which is the first of Solute carrier family 47 member.[3] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter.[5] NorM is a prototype of a new transporter family and Brown et al. named it the multidrug and toxic compound extrusion family.[4] 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.[6] See also - MATE (Multi antimicrobial extrusion protein or multidrug and toxic compound extrusion protein)
References1. ^1 {{cite web | title = Entrez Gene: FLJ10847 hypothetical protein FLJ10847| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55244| accessdate = }}
2. ^1 {{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 | url = | issn = }}
3. ^1 {{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| url = | issn = }}
4. ^1 {{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| url = | issn = }}
5. ^{{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| url = | issn = }}
6. ^{{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}}
Further reading{{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 }}
- {{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 }}
- {{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 |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 }}
- {{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 }}
- {{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 }}
- {{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 }}
- {{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 |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 }}
- {{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 }}
- {{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 }}
- {{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 }}
{{refend}}{{Membrane transport proteins}}{{gene-17-stub}} 1 : Solute carrier family |