CDH8
From Wikipedia, the free encyclopedia
Cadherin 8, type 2
|
||||||||||||||
PDB rendering based on 1zxk. | ||||||||||||||
Available structures: 1zxk, 2a62 | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | CDH8; Nbla04261 | |||||||||||||
External IDs | OMIM: 603008 MGI: 107434 HomoloGene: 55604 | |||||||||||||
|
||||||||||||||
RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 1006 | 12564 | ||||||||||||
Ensembl | ENSG00000150394 | ENSMUSG00000036510 | ||||||||||||
Uniprot | P55286 | Q3UTL9 | ||||||||||||
Refseq | NM_001796 (mRNA) NP_001787 (protein) |
NM_001039154 (mRNA) NP_001034243 (protein) |
||||||||||||
Location | Chr 16: 60.24 - 60.63 Mb | Chr 8: 101.92 - 102.31 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Cadherin 8, type 2, also known as CDH8, is a human gene.[1]
This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the protein's homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. This particular cadherin is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.[1]
[edit] References
[edit] Further reading
- Suzuki S, Sano K, Tanihara H (1991). "Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.". Cell Regul. 2 (4): 261–70. PMID 2059658.
- Tanihara H, Sano K, Heimark RL, et al. (1995). "Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin.". Cell Adhes. Commun. 2 (1): 15–26. PMID 7982033.
- Kido M, Obata S, Tanihara H, et al. (1998). "Molecular properties and chromosomal location of cadherin-8.". Genomics 48 (2): 186–94. doi: . PMID 9521872.
- Kremmidiotis G, Baker E, Crawford J, et al. (1998). "Localization of human cadherin genes to chromosome regions exhibiting cancer-related loss of heterozygosity.". Genomics 49 (3): 467–71. doi: . PMID 9615235.
- Shimoyama Y, Tsujimoto G, Kitajima M, Natori M (2001). "Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins.". Biochem. J. 349 (Pt 1): 159–67. PMID 10861224.
- Blaschke S, Mueller CA, Markovic-Lipkovski J, et al. (2002). "Expression of cadherin-8 in renal cell carcinoma and fetal kidney.". Int. J. Cancer 101 (4): 327–34. doi: . PMID 12209956.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi: . PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.