PTPLA

PTPLA/PTP-like

The PTPLA or PTP-like family was first cloned from humans, and reported as having a catalytic motif like that of PTPs (Cx5P in place of Cx5R), based on a Prosite analysis [1]. This family has homologs as diverse as in plants and in yeast, but no homology to the PTP fold, and even the Cx5P motif is not well conserved. The yeast homolog, Phs1, is reported as a 3-hydroxyacyl-CoA dehydratase that catalyzes the elongation of very long-chain fatty acids and is predicted to be a multi-transmembrane protein [2]. Human PTPLA proteins were later also found to be 3-hydroxyacyl-CoA dehydratases [3].

References

1. Uwanogho DA, Hardcastle Z, Balogh P, Mirza G, Thornburg KL, Ragoussis J, and Sharpe PT. Molecular cloning, chromosomal mapping, and developmental expression of a novel protein tyrosine phosphatase-like gene. Genomics. 1999 Dec 15;62(3):406-16. DOI:10.1006/geno.1999.5950 |
2. Kihara A, Sakuraba H, Ikeda M, Denpoh A, and Igarashi Y. Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation. J Biol Chem. 2008 Apr 25;283(17):11199-209. DOI:10.1074/jbc.M708993200 |
3. Ikeda M, Kanao Y, Yamanaka M, Sakuraba H, Mizutani Y, Igarashi Y, and Kihara A. Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis. FEBS Lett. 2008 Jul 9;582(16):2435-40. DOI:10.1016/j.febslet.2008.06.007 |