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Literature summary extracted from

  • Schwartz, M.S.; Benci, J.L.; Selote, D.S.; Sharma, A.K.; Chen, A.G.; Dang, H.; Fares, H.; Vatamaniuk, O.K.
    Detoxification of multiple heavy metals by a half-molecule ABC transporter, HMT-1, and coelomocytes of Caenorhabditis elegans (2010), PLoS ONE, 5, e9564.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.2 Caenorhabditis elegans
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-
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7.2.2.2 Caenorhabditis elegans G5EFD4
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.2 coelomocyte
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 Caenorhabditis elegans
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7.2.2.2 coelomocyte phytochelatin synthase pcs-1 and hmt-1 are co-expressed in coelomocytes. Coelomocytes are essential mainly for detoxification of heavy metals, but not of oxidative stress, a by-product of heavy metal toxicity Caenorhabditis elegans
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7.2.2.2 intestine
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 Caenorhabditis elegans
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7.2.2.2 neuron head neurons Caenorhabditis elegans
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Synonyms

EC Number Synonyms Comment Organism
7.2.2.2 half-molecule ATP-binding cassette (ABC) transporter
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 Caenorhabditis elegans
7.2.2.2 HMT-1
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 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
7.2.2.2 malfunction hmt-1 deletion alleles of Caenorhabditis elegans are hypersensitive to Cd Caenorhabditis elegans
7.2.2.2 physiological function functional in vivo assays show that HMT-1 from Caenorhabditis elegans, functions distinctly from its Schizosaccharomyces pombe counterpart in that in addition to Cd it confers tolerance to arsenic and copper while acting independently of phytochelatin synthase Caenorhabditis elegans
7.2.2.2 physiological function in addition to Cd, HMT-1 confers tolerance to arsenic and copper while acting independently of phytochelatin synthase pcs-1 Caenorhabditis elegans