CELSR3

Also known as CDHF11, EGFL1, FMI1, HFMI1, MEGF2, RESDA1, ADGRC3, cadherin EGF LAG seven-pass G-type receptor 3

Cadherin EGF LAG seven-pass G-type receptor 3 is a protein that in humans is encoded by the CELSR3 gene.

Gene data

CELSR3

Name: cadherin EGF LAG seven-pass G-type receptor 3
Type: protein-coding
Aliases: ADGRC3, CDHF11, EGFL1, FMI1, HFMI1, MEGF2, RESDA1

This gene belongs to the flamingo subfamily, which is included in the cadherin superfamily. The flamingo cadherins consist of nonclassic-type cadherins that do not interact with catenins. They are plasma membrane proteins containing seven epidermal growth factor-like repeats, nine cadherin domains and two laminin A G-type repeats in their ectodomain. They also have seven transmembrane domains, a characteristic feature of their subfamily. The encoded protein may be involved in the regulation of contact-dependent neurite growth and may play a role in tumor formation. [provided by RefSeq, Jun 2013].

via MyGene.info

Gene · Ensembl

cadherin EGF LAG seven-pass G-type receptor 3

Symbol: CELSR3
Biotype: Protein coding
Organism: Homo sapiens
Location: 3:48,636,463-48,662,886
Strand: Reverse (−)
Assembly: GRCh38

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via Ensembl · EMBL-EBI

Wikidata facts

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HomoloGene ID: 1077
exact match: identifiers.org/ncbigene/1951
genomic end: 48662886
genomic start: 48636463
cytogenetic location: 3p21.31

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Cadherin EGF LAG seven-pass G-type receptor 3 is a protein that in humans is encoded by the CELSR3 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.