Molecular Cloning of the cDNA of LPL on Goose and the Phylogenetic Relationship in the Lipase Superfamily

Lipoprotein lipase (LPL) of Tianfu meat goose was cloned and sequenced using a RT-PCR approach. The nucleotide sequence covered 468 bp with an open reading frame of 155 amino acids. Alignment analysis indicated that the nucleotide sequences are highly conserved to other species studied including chicken, domestic guinea pig, house mouse, Norway rat, cattle, cow and goat, and the homologies are 92.38%, 73.32%, 73.90%, 75.20%, 72.95%, 71.61% and 73.06%, respectively. Topology prediction showed goose LPL including two N-linked glycosylation site Asn¹⁸⁷ and Asn²¹⁵; one catalytic triad (Asp¹⁸³ and His²⁶⁸); one conserved heparin binding site (Arg¹³⁴ to Arg¹³⁷, (RKNR)); eight cysteine residues (Cys⁶⁸ and Cys⁹⁴; Cys¹¹⁹ and Cys138; Cys130 and Cys¹³³; Cys²⁸⁵ and Cys³⁰⁶) that are involved in four disulfide bridges; and one lipid-binding site (Trp²⁵⁶ and Trp²⁵⁷ (WW)). Furthermore, molecular phylogeny analyses have shown that LPL protein families were divided into two main evolution branches, one was the LPL-EL-HL branch, and the other was the PL-PLA1 branch.