Fcnb ficolin B [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Fcnbprovided by MGI
Official Full Name: ficolin Bprovided by MGI
Primary source: MGI:MGI:1341158
See related: Ensembl:ENSMUSG00000026835 AllianceGenome:MGI:1341158
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Fcn2
Summary: Enables sialic acid binding activity. Predicted to be involved in complement activation, lectin pathway. Predicted to be located in plasma membrane. Predicted to be part of serine-type endopeptidase complex. Predicted to be active in collagen-containing extracellular matrix and extracellular space. Is expressed in bone marrow; embryo; liver; spleen; and thymus. Orthologous to several human genes including FCN1 (ficolin 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in liver E18 (RPKM 15.1), liver E14 (RPKM 5.5) and 2 other tissues See more
Orthologs: human all
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Genomic context

Location:: 2 A3; 2 19.38 cM

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	2	NC_000068.8 (27966491..27974921, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	2	NC_000068.7 (28076479..28084910, complement)

Chromosome 2 - NC_000068.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Lipopolysaccharide-induced inflammation can induce a significant ficolin response.
Title: The ficolin response to LPS challenge in mice.
this study demonstrates that ficolins are important in initial innate host defense against Aspergillus fumigatus infections in vivo
Title: Ficolins Promote Fungal Clearance in vivo and Modulate the Inflammatory Cytokine Response in Host Defense against Aspergillus fumigatus.
this study shows that FCN B plays an important role in the development of collagen Ab-induced arthritis
Title: Deconstructing the Lectin Pathway in the Pathogenesis of Experimental Inflammatory Arthritis: Essential Role of the Lectin Ficolin B and Mannose-Binding Protein-Associated Serine Protease 2.
Ficolin-2 defends against virulent Mycobacteria tuberculosis infection in vivo, and its insufficiency is associated with infection in humans.
Title: Ficolin-2 defends against virulent Mycobacteria tuberculosis infection in vivo, and its insufficiency is associated with infection in humans.
Data show that ficolin-B is stored in and set free from immature granulocytic myeloid cells indicating a role in the early infection-induced cellular response of these inflammatory cells.
Title: Immature mouse granulocytic myeloid cells are characterized by production of ficolin-B.
FcnA-deficient and FcnA/ficolin B double-deficient mice lack FcnA-mediated complement activation in the sera, because of absence of complexes comprising FcnA and MBL-associated serine proteases.
Title: Mice deficient in ficolin, a lectin complement pathway recognition molecule, are susceptible to Streptococcus pneumoniae infection.
These results identify mouse ficolin-B as a functional member of the ficolin family activating complement via the lectin pathway.
Title: Functional analysis of mouse ficolin-B and detection in neutrophils.
Results show that ficolin B in mouse bone marrow is an oligomeric protein. Ficolin B contained very low, but detectable, amounts of MASP-2 and sMAP and showed detectable C4-deposition activity on immobilized N-acetylglucosamine.
Title: Mouse ficolin B has an ability to form complexes with mannose-binding lectin-associated serine proteases and activate complement through the lectin pathway.
Ficolin B showed multimeric structures and revealed binding to both N-acetylglucosamine and N-acetylgalactosamine. Ficolin B specifically recognized sialic acid residues. Ficolin B plays a distinct role through its unique carbohydrate-binding specificity.
Title: Carbohydrate-binding specificities of mouse ficolin A, a splicing variant of ficolin A and ficolin B and their complex formation with MASP-2 and sMAP.
Ficolin B exhibited a distinct ontogeny pattern that switched from embryonic liver to postnatal bone marrow and spleen. The cells that express ficolin B mRNA were identified as belonging to the myeloid cell lineage.
Title: Ficolin A and ficolin B are expressed in distinct ontogenic patterns and cell types in the mouse.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (1) 1 citation

General gene information

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Markers

Fcnb (e-PCR), detects polymorphism
- UniSTS:471078

NoName (e-PCR)
- UniSTS:487636

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables G protein-coupled receptor binding	IEA Inferred from Electronic Annotation more info
enables G protein-coupled receptor binding	ISO Inferred from Sequence Orthology more info
enables antigen binding	IBA Inferred from Biological aspect of Ancestor more info
enables antigen binding	ISO Inferred from Sequence Orthology more info
enables calcium-dependent protein binding	ISO Inferred from Sequence Orthology more info
enables carbohydrate binding	IEA Inferred from Electronic Annotation more info
enables carbohydrate derivative binding	IBA Inferred from Biological aspect of Ancestor more info
enables carbohydrate derivative binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables mannan binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables pattern recognition receptor activity	IEA Inferred from Electronic Annotation more info
enables pattern recognition receptor activity	ISO Inferred from Sequence Orthology more info
enables proteoglycan binding	ISO Inferred from Sequence Orthology more info
enables sialic acid binding	IDA Inferred from Direct Assay more info	PubMed
enables sialic acid binding	ISO Inferred from Sequence Orthology more info
enables signaling receptor binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in G protein-coupled receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in cell surface pattern recognition receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in complement activation, lectin pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in complement activation, lectin pathway	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of viral entry into host cell	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of interleukin-8 production	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of opsonization	IEA Inferred from Electronic Annotation more info
involved_in protein localization to cell surface	IEA Inferred from Electronic Annotation more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in recognition of apoptotic cell	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of collagen trimer	IEA Inferred from Electronic Annotation more info
is_active_in collagen-containing extracellular matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
part_of serine-type endopeptidase complex	IEA Inferred from Electronic Annotation more info
part_of serine-type endopeptidase complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: ficolin-2

Names: L-ficolin; collagen/fibrinogen domain-containing protein 2; ficolin-beta

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_010190.1 → NP_034320.1 ficolin-2 precursor

See identical proteins and their annotated locations for NP_034320.1

Status: PROVISIONAL

Source sequence(s)

BC107220

Consensus CDS

CCDS15832.1

UniProtKB/Swiss-Prot

O70497, Q3KNL6

Related

ENSMUSP00000028179.9, ENSMUST00000028179.15

Conserved Domains (2) summary

pfam01391
Location:40 → 95

Collagen; Collagen triple helix repeat (20 copies)

cd00087
Location:103 → 312

FReD; Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000068.8 Reference GRCm39 C57BL/6J

Range

27966491..27974921 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006497676.5 → XP_006497739.1 ficolin-2 isoform X1

Conserved Domains (2) summary

pfam01391
Location:40 → 95

Collagen; Collagen triple helix repeat (20 copies)

cd00087
Location:103 → 238

FReD; Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular ...