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Evolution of Mammalian KELL Blood Group Glycoproteins and Genes (KEL): Evidence for a Marsupial Origin from an Ancestral M13 Type II Endopeptidase Gene | Abstract
ISSN: 2329-9002

Journal of Phylogenetics & Evolutionary Biology
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Research Article

Evolution of Mammalian KELL Blood Group Glycoproteins and Genes (KEL): Evidence for a Marsupial Origin from an Ancestral M13 Type II Endopeptidase Gene

Roger S Holmes*
Eskitis Institute for Drug Discovery and School of Biomolecular and Physical Sciences, Griffith University, Nathan, QLD, Australia
Corresponding Author : Roger S Holmes
Eskitis Institute for Drug Discovery
School of Biomolecular and Physical Sciences
Griffith University, Nathan, QLD 4111, Australia
Tel: +61737356008
E-mail: [email protected]
Received April 14, 2013; Accepted July 17, 2013; Published July 22, 2013
Citation: Holmes RS (2013) Evolution of Mammalian KELL Blood Group Glycoproteins and Genes (KEL): Evidence for a Marsupial Origin from an Ancestral M13 Type II Endopeptidase Gene. J Phylogen Evolution Biol 1:112. doi:10.4172/2329-9002.1000112
Copyright: © 2013 Holmes RS. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

KELL is a member of the M13 family of type II neutral endopeptidases, which functions as a blood group antigen in human and animal populations. KELL amino acid sequences and structures and KEL gene locations were examined using bioinformatic data from several mammalian genome projects. Mammalian KELL sequences shared 55-99% identity, as compared with 21-31% sequence identities with other M13-like family members. Four predicted N-glycosylation sites were conserved among the mammalian KELL proteins examined. Sequence alignments, key amino acid residues and conserved predicted secondary and tertiary structures were also studied, including active site residues, predicted disulfide forming Cys residues, cytoplasmic, transmembrane and extracellular sequences and KELL C-terminus amino acid sequences. Mammalian KEL genes usually contained 18 or 19 coding exons on the direct strand. abhi binding sites within the human KEL promoter may regulate transcription within erythroid cells. Phylogenetic analyses examined the relationships and potential evolutionary origins of the mammalian KEL gene with six other vertebrate neutral endopeptidase M13 family genes. These suggested that KEL originated in an ancestral marsupial genome from a gene duplication event of a neutral endopeptidase M13-like gene.

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