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

Author:

Bellachioma G1,Stirling J L2,Orlacchio A1,Beccari T1

Affiliation:

1. Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Universita di Perugia, via del Giochetto, cp 37 succ. 3, 06126 Perugia, Italy.

2. Division of Life Sciences, King's College London, Kensington Campus, Campden Hill, London W8 7AH, U.K.

Abstract

A cDNA (1.1 kb) containing the complete coding sequence for the mouse GM2 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 GM2 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 GM2 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 GM2 activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single site reported in the human GM2 activator protein sequence (Asn63-Val-Thr).

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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