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GeneQ17916070· pop 5· linked from 489 articles

Also known as CDHF10, EGFL2, Flamingo1, MEGF3, ADGRC2, cadherin EGF LAG seven-pass G-type receptor 2

Cadherin EGF LAG seven-pass G-type receptor 2 is a protein that in humans is encoded by the CELSR2 gene.

Gene data

CELSR2
Name
cadherin EGF LAG seven-pass G-type receptor 2
Type
protein-coding
Aliases
ADGRC2, CDHF10, EGFL2, Flamingo1, MEGF3

The protein encoded by this gene is a member of the flamingo subfamily, part of the cadherin superfamily. The flamingo subfamily consists of nonclassic-type cadherins; a subpopulation that does not interact with catenins. The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like repeats and two laminin A G-type repeats in their ectodomain. They also have seven transmembrane domains, a characteristic unique to this subfamily. It is postulated that these proteins are receptors involved in contact-mediated communication, with cadherin domains acting as homophilic binding regions and the EGF-like domains involved in cell adhesion and receptor-ligand interactions. The specific function of this particular member has not been determined. [provided by RefSeq, Jul 2008].

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Gene · Ensembl

cadherin EGF LAG seven-pass G-type receptor 2

Symbol
CELSR2
Biotype
Protein coding
Organism
Homo sapiens
Location
1:109,249,539-109,275,751
Strand
Forward (+)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Show 5 more facts
HomoloGene ID
1078
genomic end
109275751
genomic start
109249539
cytogenetic location
1p13.3
Sources (6)

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Cadherin EGF LAG seven-pass G-type receptor 2 is a protein that in humans is encoded by the CELSR2 gene.

The protein encoded by this gene is a member of the flamingo subfamily, part of the cadherin superfamily. The flamingo subfamily consists of nonclassic-type cadherins; a subpopulation that does not interact with catenins. The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like repeats and two laminin A G-type repeats in their ectodomain. They also have seven transmembrane domains, a characteristic unique to this subfamily. It is postulated that these proteins are receptors involved in contact-mediated communication, with cadherin domains acting as homophilic binding regions and the EGF-like domains involved in cell adhesion and receptor-ligand interactions. The specific function of this particular member has not been determined.

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