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	<entry>
		<id>https://www.wikidoc.org/index.php?title=Fibrinogen_c_domain_containing_1&amp;diff=1422888</id>
		<title>Fibrinogen c domain containing 1</title>
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		<updated>2017-10-29T20:35:50Z</updated>

		<summary type="html">&lt;p&gt;160.5.183.197: Expanded on the structure and function of the FIBCD1 protein.&lt;/p&gt;
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&lt;div&gt;{{Underlinked|date=April 2016}}&lt;br /&gt;
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{{Infobox_gene}}&lt;br /&gt;
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&#039;&#039;&#039;Fibrinogen C domain containing 1&#039;&#039;&#039; &#039;&#039;&#039;(FIBCD1)&#039;&#039;&#039; is a [[protein]] that in humans is encoded by the &#039;&#039;FIBCD1&#039;&#039; [[gene]] localized on [[Chromosome 9 (human)|chromosome]] 9q34.1 in close proximity to the genes encoding L- and M-ficolin.&lt;br /&gt;
&amp;lt;ref name=&amp;quot;entrez&amp;quot;&amp;gt;&lt;br /&gt;
{{cite web&lt;br /&gt;
| title = Entrez Gene: Fibrinogen C domain containing 1&lt;br /&gt;
| url = https://www.ncbi.nlm.nih.gov/gene/84929&lt;br /&gt;
| accessdate = 2016-03-08&lt;br /&gt;
}}&amp;lt;/ref&amp;gt; FIBCD1 is thought to have a role in both host defence and gut homeostasis. &lt;br /&gt;
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==Function==&lt;br /&gt;
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FIBCD1 is a type II trans-membrane endocytic receptor that is expressed apically on enterocytes and on airway epithelial cells (Schlosser &#039;&#039;et al.&#039;&#039;, 2009). It is thought to mediate the endocytosis of bound ligands which are released to the surroundings after degradation, with FIBCD1 being recycled to the plasma membrane. &lt;br /&gt;
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The homology between FIBCD1 and members of the ficolins, which are extensively characterised pattern-recognition molecules that have roles in the immune response, indicate FIBCD1 may have a role in host defence. Two potential phosphorylation sites in the cytoplasmic part of FIBCD1 suggest that FIBCD1 also may be a signaling protein (Schlosser &#039;&#039;et al.&#039;&#039;, 2009).&lt;br /&gt;
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== Structure ==&lt;br /&gt;
FIBCD1 forms homo-tetramers in the plasma membrane, with each protein chain consisting of: a short cytoplasmic tail, a trans-membrane helix, and an ectodomain containing a coiled-coil region, a polycationic region, and a C-terminal fibrinogen-like recognition domain, otherwise known as the FReD (Shrive, &#039;&#039;et al.&#039;&#039;, 2014)&amp;lt;ref&amp;gt;{{Cite journal|last=Shrive|first=Annette K.|last2=Moeller|first2=Jesper B.|last3=Burns|first3=Ian|last4=Paterson|first4=Jenny M.|last5=Shaw|first5=Amy J.|last6=Schlosser|first6=Anders|last7=Sorensen|first7=Grith L.|last8=Greenhough|first8=Trevor J.|last9=Holmskov|first9=Uffe|date=2014-01-31|title=Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein|url=http://www.jbc.org/content/289/5/2880|journal=Journal of Biological Chemistry|language=en|volume=289|issue=5|pages=2880–2887|doi=10.1074/jbc.m113.520577|issn=0021-9258|pmid=24293368}}&amp;lt;/ref&amp;gt;.&lt;br /&gt;
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== References ==&lt;br /&gt;
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{{reflist}}&lt;br /&gt;
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== Further reading ==&lt;br /&gt;
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{{refbegin | 2}}&lt;br /&gt;
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*{{cite journal |vauthors=Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Moestrup SK, Holmskov U |title=Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin |journal=J. Immunol. |volume=183 |issue=6 |pages=3800–9 |year=2009 |pmid=19710473 |doi=10.4049/jimmunol.0901526 |url=}}&lt;br /&gt;
{{refend}}&lt;br /&gt;
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{{NLM content}}&lt;br /&gt;
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[[Category:Human proteins]]&lt;br /&gt;
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{{gene-9-stub}}&lt;br /&gt;
{{protein-stub}}&lt;/div&gt;</summary>
		<author><name>160.5.183.197</name></author>
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