4q95: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q95 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q95 RCSB], [http://www.ebi.ac.uk/pdbsum/4q95 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q95 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q95 RCSB], [http://www.ebi.ac.uk/pdbsum/4q95 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/HRSL3_HUMAN HRSL3_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:17374643</ref> <ref>PMID:19615464</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Phosphatidylcholine--retinol O-acyltransferase]] | [[Category: Phosphatidylcholine--retinol O-acyltransferase]] | ||
[[Category: Golczak, M | [[Category: Golczak, M]] | ||
[[Category: Kiser, P D | [[Category: Kiser, P D]] | ||
[[Category: Palczewski, K | [[Category: Palczewski, K]] | ||
[[Category: Sears, A E | [[Category: Sears, A E]] | ||
[[Category: Acylation]] | [[Category: Acylation]] | ||
[[Category: Alpha/beta fold]] | [[Category: Alpha/beta fold]] | ||
