CELSR2: Difference between revisions

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{{Infobox_gene}}
 
'''Cadherin EGF LAG seven-pass G-type receptor 2''' is a [[protein]] that in humans is encoded by the ''CELSR2'' [[gene]].<ref name="pmid9693030">{{cite journal | vauthors = Nakayama M, Nakajima D, Nagase T, Nomura N, Seki N, Ohara O | title = Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening | journal = Genomics | volume = 51 | issue = 1 | pages = 27–34 |date=Sep 1998 | pmid = 9693030 | pmc = | doi = 10.1006/geno.1998.5341 }}</ref><ref name="entrez"/>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)
| HGNCid = 3231
| Symbol = CELSR2
| AltSymbols =; CDHF10; EGFL2; FLJ34118; FLJ42737; FLJ45143; FLJ45845; Flamingo1; KIAA0279; MEGF3
| OMIM = 604265
| ECnumber = 
| Homologene = 1078
| MGIid = 1858235
| GeneAtlas_image1 = PBB_GE_CELSR2_204029_at_tn.png
| GeneAtlas_image2 = PBB_GE_CELSR2_36499_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004930 |text = G-protein coupled receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1952
    | Hs_Ensembl = ENSG00000143126
    | Hs_RefseqProtein = NP_001399
    | Hs_RefseqmRNA = NM_001408
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 109594164
    | Hs_GenLoc_end = 109619895
    | Hs_Uniprot = Q9HCU4
    | Mm_EntrezGene = 53883
    | Mm_Ensembl = ENSMUSG00000068740
    | Mm_RefseqmRNA = NM_001004177
    | Mm_RefseqProtein = NP_001004177
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 108519950
    | Mm_GenLoc_end = 108543550
    | Mm_Uniprot = Q9R0M0
  }}
}}
'''Cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)''', also known as '''CELSR2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1952| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1952| accessdate = }}</ref>
| summary_text = 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 [[cadherin]]s; a subpopulation that does not interact with [[catenin]]s. 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.<ref name="entrez">{{cite web | title = Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1952| accessdate = }}</ref>
}}
}}


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CELSR2}}


==Further reading==
==Further reading==
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{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Nagase T, Seki N, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321-9, 341-54 |year= 1997 |pmid= 9039502 |doi= }}
*{{cite journal  | vauthors=Nagase T, Seki N, Ishikawa K |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321–9, 341–54 |year= 1997 |pmid= 9039502 |doi=10.1093/dnares/3.5.321  |display-authors=etal}}
*{{cite journal  | author=Nakayama M, Nakajima D, Nagase T, ''et al.'' |title=Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening. |journal=Genomics |volume=51 |issue= 1 |pages= 27-34 |year= 1998 |pmid= 9693030 |doi= 10.1006/geno.1998.5341 }}
*{{cite journal  | vauthors=Wu Q, Maniatis T |title=A striking organization of a large family of human neural cadherin-like cell adhesion genes. |journal=Cell |volume=97 |issue= 6 |pages= 779–90 |year= 1999 |pmid= 10380929 |doi=10.1016/S0092-8674(00)80789-8 }}
*{{cite journal  | author=Wu Q, Maniatis T |title=A striking organization of a large family of human neural cadherin-like cell adhesion genes. |journal=Cell |volume=97 |issue= 6 |pages= 779-90 |year= 1999 |pmid= 10380929 |doi=  }}
*{{cite journal  | vauthors=Wu Q, Maniatis T |title=Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3124–9 |year= 2000 |pmid= 10716726 |doi= 10.1073/pnas.060027397 | pmc=16203 }}
*{{cite journal  | author=Wu Q, Maniatis T |title=Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3124-9 |year= 2000 |pmid= 10716726 |doi= 10.1073/pnas.060027397 }}
*{{cite journal  | vauthors=Vincent JB, Skaug J, Scherer SW |title=The human homologue of flamingo, EGFL2, encodes a brain-expressed large cadherin-like protein with epidermal growth factor-like domains, and maps to chromosome 1p13.3-p21.1 |journal=DNA Res. |volume=7 |issue= 3 |pages= 233–5 |year= 2001 |pmid= 10907856 |doi=10.1093/dnares/7.3.233 }}
*{{cite journal  | author=Vincent JB, Skaug J, Scherer SW |title=The human homologue of flamingo, EGFL2, encodes a brain-expressed large cadherin-like protein with epidermal growth factor-like domains, and maps to chromosome 1p13.3-p21.1. |journal=DNA Res. |volume=7 |issue= 3 |pages= 233-5 |year= 2001 |pmid= 10907856 |doi=  }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
}}
{{refend}}
{{refend}}
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{{NLM content}}
{{NLM content}}
{{G protein-coupled receptors}}
{{G protein-coupled receptors}}
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[[Category:Adhesion GPCRs]]
[[Category:Adhesion GPCRs]]
[[Category:G protein coupled receptors]]
[[Category:G protein-coupled receptors]]
 
{{transmembranereceptor-stub}}
{{WH}}
{{WS}}

Latest revision as of 18:00, 24 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Cadherin EGF LAG seven-pass G-type receptor 2 is a protein that in humans is encoded by the CELSR2 gene.[1][2]

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.[2]

See also

References

  1. ↑ Nakayama M, Nakajima D, Nagase T, Nomura N, Seki N, Ohara O (Sep 1998). "Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening". Genomics. 51 (1): 27–34. doi:10.1006/geno.1998.5341. PMID 9693030.
  2. ↑ 2.0 2.1 "Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)".

External links

Further reading

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

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