Biochem. Biophys. Res. Commun.

An ATX1 homologue of 503 bp length was cloned from a rat cDNA library, and the deduced protein from the cDNA was found to contain 68 amino acids with a predicted molecular mass of 7.2 kDa. The rat ATX1 homologue protein (Rah1p), which shows 35%, 38%, and 89% identities with Atx1p, CUC-1, and HAH1, respectively, conserves both the MTCXXC copper-binding site in the N terminus and the KTGK lysine-rich region in the C terminus. In Northern blot analysis, rah1 mRNA was found to be expressed at high levels in the liver, small intestine, and testis. Expression of rah1 cDNA complemented a null atx1 mutant strain in yeast. Thus, Rah1p was concluded to be a functional copper chaperone.

Source:http://purl.uniprot.org/citations/10558899

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http://purl.uniprot.org/cit...rdfs:commentAn ATX1 homologue of 503 bp length was cloned from a rat cDNA library, and the deduced protein from the cDNA was found to contain 68 amino acids with a predicted molecular mass of 7.2 kDa. The rat ATX1 homologue protein (Rah1p), which shows 35%, 38%, and 89% identities with Atx1p, CUC-1, and HAH1, respectively, conserves both the MTCXXC copper-binding site in the N terminus and the KTGK lysine-rich region in the C terminus. In Northern blot analysis, rah1 mRNA was found to be expressed at high levels in the liver, small intestine, and testis. Expression of rah1 cDNA complemented a null atx1 mutant strain in yeast. Thus, Rah1p was concluded to be a functional copper chaperone.lld:uniprot
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http://purl.uniprot.org/cit...uniprot:nameBiochem. Biophys. Res. Commun.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorSakurai H.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorHiromura M.lld:uniprot
http://purl.uniprot.org/cit...uniprot:date1999lld:uniprot
http://purl.uniprot.org/cit...uniprot:pages509-512lld:uniprot
http://purl.uniprot.org/cit...uniprot:titleMolecular cloning of rat ATX1 homologue protein.lld:uniprot
http://purl.uniprot.org/cit...uniprot:volume265lld:uniprot
http://purl.uniprot.org/cit...dc-term:identifierdoi:10.1006/bbrc.1999.1678lld:uniprot
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