A cDNA (1.1 kb) containing the complete coding sequence for the mouse G(M2) activator protein was isolated from a mouse macrophage library using a cDNA for the human protein as a probe. There was a single ATG located 12 bp from the 5' end of the cDNA clone followed by an open reading frame of 579 bp. Northern blot analysis of mouse macrophage RNA showed that there was a single band with a mobility corresponding to a size of 2.3 kb. We deduce from this that the mouse mRNA, in common with the mRNA for the human G(M2) activator protein, has a long 3' untranslated sequence of approx. 1.7 kb. Alignment of the mouse and human deduced amino acid sequences showed 68% identity overall and 75% identity for the sequence on the C-terminal side of the first 31 residues, which in the human G(M2) activator protein contains the signal peptide. Hydropathicity plots showed great similarity between the mouse and human sequences even in regions of low sequence similarity. There is a single N-glycosylation site in the mouse G(M2) activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single site reported in the human G(M2) activator protein sequence (Asn63-Val-Thr).

Cloning and sequence analysis of a cDNA clone coding for the mouse GM2 activator protein.

ORLACCHIO, Aldo;BECCARI, Tommaso
1993

Abstract

A cDNA (1.1 kb) containing the complete coding sequence for the mouse G(M2) activator protein was isolated from a mouse macrophage library using a cDNA for the human protein as a probe. There was a single ATG located 12 bp from the 5' end of the cDNA clone followed by an open reading frame of 579 bp. Northern blot analysis of mouse macrophage RNA showed that there was a single band with a mobility corresponding to a size of 2.3 kb. We deduce from this that the mouse mRNA, in common with the mRNA for the human G(M2) activator protein, has a long 3' untranslated sequence of approx. 1.7 kb. Alignment of the mouse and human deduced amino acid sequences showed 68% identity overall and 75% identity for the sequence on the C-terminal side of the first 31 residues, which in the human G(M2) activator protein contains the signal peptide. Hydropathicity plots showed great similarity between the mouse and human sequences even in regions of low sequence similarity. There is a single N-glycosylation site in the mouse G(M2) activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single site reported in the human G(M2) activator protein sequence (Asn63-Val-Thr).
1993
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11391/908530
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