FCN3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | FCN3 , FCNH, HAKA1, ficolin 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 604973 HomoloGene: 130523 GeneCards: FCN3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Ficolin-3 is a protein that in humans is encoded by the FCN3 gene. Ficolin-3 was initially identified as H-ficolin, in which H is after the Hakata antigen that was previously found as an autoantigen in patients who lived in the city of Hakata. [3] [4] [5]
Ficolins are a group of proteins which consist of a collagen-like domain and a fibrinogen-like domain. In human serum, there are two types of ficolins, both of which have lectin activity. The protein encoded by this gene is a thermolabile beta-2-macroglycoprotein found in all human serum and is a member of the ficolin/opsonin p35 lectin family. The protein, which was initially identified based on its reactivity with sera from patients with systemic lupus erythematosus, has been shown to have a calcium-independent lectin activity. The protein can activate the complement pathway in association with MASPs and sMAP, thereby aiding in host defense through the activation of the lectin pathway. Alternative splicing occurs at this locus and two variants, each encoding a distinct isoform, have been identified. [5]
Humoral immunity is the aspect of immunity that is mediated by macromolecules – including secreted antibodies, complement proteins, and certain antimicrobial peptides – located in extracellular fluids. Humoral immunity is named so because it involves substances found in the humors, or body fluids. It contrasts with cell-mediated immunity. Humoral immunity is also referred to as antibody-mediated immunity.
Mannan-binding lectin serine protease 1 also known as mannose-associated serine protease 1 (MASP-1) is an enzyme that in humans is encoded by the MASP1 gene.
Mannose-binding lectin (MBL), also called mannan-binding lectin or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity as an opsonin and via the lectin pathway.
C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene. CLEC4M has also been designated as CD299.
4F2 cell-surface antigen heavy chain is a protein that in humans is encoded by the SLC3A2 gene.
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.
Ficolin-2, which was initially identified as L-ficolin, is a protein that in humans is encoded by the FCN2 gene.
Sialic acid-binding Ig-like lectin 12, or Siglec-XII, is a protein that in humans, is encoded by the SIGLEC12 gene.
Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene.
Attractin is a protein that in humans is encoded by the ATRN gene.
C-type lectin domain family 11 member A is a protein that in humans is encoded by the CLEC11A gene.
Mesoderm development LRP chaperone, or MESD, is a protein that in humans is encoded by the MESD gene.
CD205 also called Lymphocyte antigen 75 is a protein that in humans is encoded by the LY75 gene.
C-type lectin domain family 1 member A is a protein that in humans is encoded by the CLEC1A gene.
Sialic acid-binding Ig-like lectin 10 is a protein that in humans is encoded by the SIGLEC10 gene. Siglec-G is often referred to as the murine paralog of human Siglec-10
C-type lectin domain family 2 member B is a protein that in humans is encoded by the CLEC2B gene.
C-type lectin domain family 12 member A is a protein that in humans is encoded by the CLEC12A gene.
The CD302 antigen also known as C-type lectin domain family 13 member A is a protein that in humans is encoded by the CD302 gene.
Ficolins are pattern recognition receptors that bind to acetyl groups present in the carbohydrates of bacterial surfaces and mediate activation of the lectin pathway of the complement cascade.
Intelectins are lectins expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins. Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence. Thus, intelectins may not function through the same lectin-complement pathway. Most intelectins are still poorly characterized and they may have diverse biological roles. Human intelectin-1 (hIntL-1) has also been shown to bind lactoferrin, but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major component of asthmatic mucus and may be involved in insulin physiology as well.