Fibrinogen c domain containing 1: Difference between revisions

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{{Underlinked|date=April 2016}}
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{{Infobox_gene}}


'''Fibrinogen C domain containing 1''' '''(FIBCD1)''' is a [[protein]] that in humans is encoded by the ''FIBCD1'' [[gene]] localized on [[Chromosome 9 (human)|chromosome]] 9q34.1 in close proximity to the genes encoding L- and M-ficolin.
'''Fibrinogen C domain containing 1''' '''(FIBCD1)''' is a [[protein]] that in humans is encoded by the ''FIBCD1'' [[gene]] localized on [[Chromosome 9 (human)|chromosome]] 9q34.1 in close proximity to the genes encoding L- and M-ficolin.{{R|"entrez"}} FIBCD1 is thought to have a role in both host defence and gut homeostasis.  
<ref name="entrez">
{{cite web
| title = Entrez Gene: Fibrinogen C domain containing 1
| url = https://www.ncbi.nlm.nih.gov/gene/84929
| accessdate = 2016-03-08
}}</ref> FIBCD1 is thought to have a role in both host defence and gut homeostasis.  


==Function==
==Function==


FIBCD1 is a type II trans-membrane endocytic receptor that is expressed apically on enterocytes and on airway epithelial cells (Schlosser ''et al.'', 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.  
FIBCD1 is a type II trans-membrane [[endocytic]] receptor that is expressed apically on [[enterocytes]] and on airway [[epithelial cells]] (Schlosser ''et al.'', 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]].  


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 ''et al.'', 2009).
The homology between FIBCD1 and members of the [[ficolin]]s, 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 ''et al.'', 2009).


== Structure ==
== Structure ==
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, ''et al.'', 2014)<ref>{{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}}</ref>.
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, ''et al.'', 2014){{R|"Shrive"}}


== References ==
== References ==


{{reflist}}
{{reflist|refs=
 
<ref name="Shrive">{{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|pmc=3908420}}</ref>
 
<ref name="entrez">{{cite web| title = Entrez Gene: Fibrinogen C domain containing 1| url = https://www.ncbi.nlm.nih.gov/gene/84929| accessdate = 2016-03-08}}</ref>
 
}}


== Further reading ==
== Further reading ==

Revision as of 03:36, 13 August 2018

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Wikidata
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Fibrinogen C domain containing 1 (FIBCD1) is a protein that in humans is encoded by the FIBCD1 gene localized on chromosome 9q34.1 in close proximity to the genes encoding L- and M-ficolin.[1] FIBCD1 is thought to have a role in both host defence and gut homeostasis.

Function

FIBCD1 is a type II trans-membrane endocytic receptor that is expressed apically on enterocytes and on airway epithelial cells (Schlosser et al., 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.

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 et al., 2009).

Structure

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, et al., 2014)[2]

References

  1. ↑ "Entrez Gene: Fibrinogen C domain containing 1". Retrieved 2016-03-08.
  2. ↑ Shrive, Annette K.; Moeller, Jesper B.; Burns, Ian; Paterson, Jenny M.; Shaw, Amy J.; Schlosser, Anders; Sorensen, Grith L.; Greenhough, Trevor J.; Holmskov, Uffe (2014-01-31). "Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein". Journal of Biological Chemistry. 289 (5): 2880–2887. doi:10.1074/jbc.m113.520577. ISSN 0021-9258. PMC 3908420. PMID 24293368.

Further reading

  • Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Moestrup SK, Holmskov U (2009). "Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin". J. Immunol. 183 (6): 3800–9. doi:10.4049/jimmunol.0901526. PMID 19710473.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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