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High affinity copper uptake protein 1

{{Short description|Protein-coding gene in the species Homo sapiens}}

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High affinity copper uptake protein 1 (CTR1) is a protein that in humans is encoded by the SLC31A1 gene.{{cite journal | vauthors = Zhou B, Gitschier J | title = hCTR1: a human gene for copper uptake identified by complementation in yeast | journal = Proc Natl Acad Sci U S A | volume = 94 | issue = 14 | pages = 7481–6 |date=Aug 1997 | pmid = 9207117 | pmc = 23847 | doi =10.1073/pnas.94.14.7481 | bibcode = 1997PNAS...94.7481Z | doi-access = free }}{{cite web | title = Entrez Gene: SLC31A1 solute carrier family 31 (copper transporters), member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1317}}

Copper is an element essential for life, but excessive copper can be toxic or even lethal to the cell. Therefore, cells have developed sophisticated ways to maintain a critical copper balance, with the intake, export, and intracellular compartmentalization or buffering of copper strictly regulated. The 2 related genes ATP7A and ATP7B, responsible for the human diseases Menkes syndrome and Wilson disease, respectively, are involved in copper export. In S. cerevisiae, the copper uptake genes CTR1, CTR2, and CTR3 have been identified, and in human the CTR1 and CTR2 (MIM 603088) genes have been identified.

Clinical significance

In 2022, a new autosomal-recessive disease was discovered that is caused by mutations of the CTR1 gene.{{cite journal | vauthors = Batzios S, Tal G, DiStasio AT, Peng Y, Charalambous C, Nicolaides P, Kamsteeg EJ, Korman SH, Mandel H, Steinbach PJ, Yi L, Fair SR, Hester ME, Drousiotou A, Kaler SG | title = Newly identified disorder of copper metabolism caused by variants in CTR1, a high-affinity copper transporter | journal = Human Molecular Genetics | volume = 31| issue = 24| pages = 4121–4130| date = August 2022 | pmid = 35913762 | doi = 10.1093/hmg/ddac156 | url = | pmc = 9759326 }} The disease is characterized by profound deficiency of copper in the central nervous system and presents with infantile seizures and neurodegeneration.

See also

References

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Further reading

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  • {{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=Møller LB, Petersen C, Lund C, Horn N |title=Characterization of the hCTR1 gene: genomic organization, functional expression, and identification of a highly homologous processed gene |journal=Gene |volume=257 |issue= 1 |pages= 13–22 |year= 2001 |pmid= 11054564 |doi=10.1016/S0378-1119(00)00394-2 }}
  • {{cite journal | vauthors=Lee J, Peña MM, Nose Y, Thiele DJ |title=Biochemical characterization of the human copper transporter Ctr1 |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4380–7 |year= 2002 |pmid= 11734551 |doi= 10.1074/jbc.M104728200 |doi-access= free }}
  • {{cite journal | vauthors=Puig S, Lee J, Lau M, Thiele DJ |title=Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26021–30 |year= 2002 |pmid= 11983704 |doi= 10.1074/jbc.M202547200 |doi-access= free }}
  • {{cite journal |vauthors=Klomp AE, Tops BB, Van Denberg IE, etal |title=Biochemical characterization and subcellular localization of human copper transporter 1 (hCTR1) |journal=Biochem. J. |volume=364 |issue= Pt 2 |pages= 497–505 |year= 2002 |pmid= 12023893 |doi= 10.1042/BJ20011803 | pmc=1222595 }}
  • {{cite journal | vauthors=Eisses JF, Kaplan JH |title=Molecular characterization of hCTR1, the human copper uptake protein |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29162–71 |year= 2002 |pmid= 12034741 |doi= 10.1074/jbc.M203652200 |doi-access= free}}
  • {{cite journal | vauthors=Lee J, Petris MJ, Thiele DJ |title=Characterization of mouse embryonic cells deficient in the ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40253–9 |year= 2002 |pmid= 12177073 |doi= 10.1074/jbc.M208002200 |doi-access= free }}
  • {{cite journal |vauthors=Klomp AE, Juijn JA, van der Gun LT, etal |title=The N-terminus of the human copper transporter 1 (hCTR1) is localized extracellularly, and interacts with itself |journal=Biochem. J. |volume=370 |issue= Pt 3 |pages= 881–9 |year= 2003 |pmid= 12466020 |doi= 10.1042/BJ20021128 | pmc=1223224 }}
  • {{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 | vauthors=Petris MJ, Smith K, Lee J, Thiele DJ |title=Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1 |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9639–46 |year= 2003 |pmid= 12501239 |doi= 10.1074/jbc.M209455200 |doi-access= free }}
  • {{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 |vauthors=Guo Y, Smith K, Lee J, etal |title=Identification of methionine-rich clusters that regulate copper-stimulated endocytosis of the human Ctr1 copper transporter |journal=J. Biol. Chem. |volume=279 |issue= 17 |pages= 17428–33 |year= 2004 |pmid= 14976198 |doi= 10.1074/jbc.M401493200 |doi-access= free }}
  • {{cite journal | vauthors=Guo Y, Smith K, Petris MJ |title=Cisplatin stabilizes a multimeric complex of the human Ctr1 copper transporter: requirement for the extracellular methionine-rich clusters |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46393–9 |year= 2004 |pmid= 15326162 |doi= 10.1074/jbc.M407777200 |doi-access= free }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal | vauthors=Eisses JF, Chi Y, Kaplan JH |title=Stable plasma membrane levels of hCTR1 mediate cellular copper uptake |journal=J. Biol. Chem. |volume=280 |issue= 10 |pages= 9635–9 |year= 2005 |pmid= 15634665 |doi= 10.1074/jbc.M500116200 |doi-access= free }}
  • {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
  • {{cite journal |vauthors=Hardman B, Manuelpillai U, Wallace EM, etal |title=Expression, localisation and hormone regulation of the human copper transporter hCTR1 in placenta and choriocarcinoma Jeg-3 cells |journal=Placenta |volume=27 |issue= 9–10 |pages= 968–77 |year= 2006 |pmid= 16356544 |doi= 10.1016/j.placenta.2005.10.011 }}
  • {{cite journal | vauthors=Aller SG, Unger VM |title=Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 10 |pages= 3627–32 |year= 2006 |pmid= 16501047 |doi= 10.1073/pnas.0509929103 | pmc=1450133 |bibcode=2006PNAS..103.3627A |doi-access=free }}

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{{Membrane transport proteins}}

{{Metal metabolism}}

Category:Solute carrier family

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