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2cxj
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cxj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CXJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2cxj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CXJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CXJ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cxj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cxj RCSB], [http://www.ebi.ac.uk/pdbsum/2cxj PDBsum]</span></td></tr> | + | </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=2cxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cxj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cxj RCSB], [http://www.ebi.ac.uk/pdbsum/2cxj PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/S10AD_MOUSE S10AD_MOUSE]] Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine.<ref>PMID:12746488</ref> <ref>PMID:17991455</ref> <ref>PMID:11432880</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[S100 protein|S100 protein]] | *[[S100 protein|S100 protein]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Kumar, T K.S | + | [[Category: Kumar, T K.S]] |
| - | [[Category: Vaithiyalingam, S | + | [[Category: Vaithiyalingam, S]] |
| - | [[Category: Yu, C | + | [[Category: Yu, C]] |
[[Category: Fgf]] | [[Category: Fgf]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
Revision as of 08:42, 25 December 2014
3D Solution Structure of S100A13
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