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		<title>PTPLA - Revision history</title>
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		<updated>2026-04-10T20:29:06Z</updated>
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		<id>http://www.phosphatome.net/wiki/index.php?title=PTPLA&amp;diff=599&amp;oldid=prev</id>
		<title>Gerard: Created page with &quot;__noTOC__  ==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), ba...&quot;</title>
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				<updated>2014-12-01T19:13:59Z</updated>
		
		<summary type="html">&lt;p&gt;Created page with &amp;quot;__noTOC__  ==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), ba...&amp;quot;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;__noTOC__&lt;br /&gt;
&lt;br /&gt;
==PTPLA/PTP-like==&lt;br /&gt;
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 &amp;lt;cite&amp;gt;Uwanogho&amp;lt;/cite&amp;gt;. 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 &amp;lt;cite&amp;gt;Kihara&amp;lt;/cite&amp;gt;. Human PTPLA proteins were later also found to be 3-hydroxyacyl-CoA dehydratases &amp;lt;cite&amp;gt;Ikeda&amp;lt;/cite&amp;gt;.&lt;br /&gt;
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==== References ====&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Uwanogho pmid=10644438&lt;br /&gt;
#Kihara pmid=18272525&lt;br /&gt;
#Ikeda pmid=18554506&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;/div&gt;</summary>
		<author><name>Gerard</name></author>	</entry>

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