XB-FEAT-988106: Difference between revisions
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This is the community wiki page for the gene ''adam33'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase | This is the community wiki page for the gene ''adam33'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase | ||
The protein ADAM13 is the orthologue of human ADAM33 but | The protein ADAM13 (alfandari et al., 1997 [http://www.ncbi.nlm.nih.gov/pubmed/9070330] is the orthologue of human ADAM33 but the sequences have diverged sufficiently that the two proteins cannot functionally replace each other. ADAM13 is a cell surface metalloprotease that binds to its substrate via its cystein rich domain ([Gaultier et al., 2002][http://www.ncbi.nlm.nih.gov/pubmed/11967265]; [Smith et al., 2002][http://www.ncbi.nlm.nih.gov/pubmed/12460986]). | ||
ADAM13 binds and cleave fibronectin (Alfandari et al., 2001[http://www.ncbi.nlm.nih.gov/pubmed/11448768]), Cadherin-11 (McCusker et al., 2009[http://www.ncbi.nlm.nih.gov/pubmed/18946084]), PAPC (Cousin et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/21316592]) and ephrinB (Wei et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/20708595]). | ADAM13 binds and cleave fibronectin (Alfandari et al., 2001[http://www.ncbi.nlm.nih.gov/pubmed/11448768]), Cadherin-11 (McCusker et al., 2009[http://www.ncbi.nlm.nih.gov/pubmed/18946084]), PAPC (Cousin et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/21316592]) and ephrinB (Wei et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/20708595]). | ||
ADAM13 also cleaves itself within its cystein rich domain (Gaultier et al., 2002[http://www.ncbi.nlm.nih.gov/pubmed/11967265]). This cleavage can be followed by a cleavage by gama-secretase that release the cytoplasmic domain. The ADAM13 cytoplasmic domain translocates into the nucleus where it regulates gene expression to promote cranial neural crest cell migration (Cousin et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/21316592]). | ADAM13 also cleaves itself within its cystein rich domain (Gaultier et al., 2002[http://www.ncbi.nlm.nih.gov/pubmed/11967265]). This cleavage can be followed by a cleavage by gama-secretase that release the cytoplasmic domain. The ADAM13 cytoplasmic domain translocates into the nucleus where it regulates gene expression to promote cranial neural crest cell migration (Cousin et al., 2011[http://www.ncbi.nlm.nih.gov/pubmed/21316592]). | ||
The cytoplasmic domain of ADAM13 interacts with multiple SH# containing proteins including PACSIN-2 which negatively regulates its proteolytic activity (Cousin et al., 2000 http://www.ncbi.nlm.nih.gov/pubmed/11076687). | The cytoplasmic domain of ADAM13 interacts with multiple SH# containing proteins including PACSIN-2 which negatively regulates its proteolytic activity (Cousin et al., 2000 [http://www.ncbi.nlm.nih.gov/pubmed/11076687]). | ||
Revision as of 05:21, 3 May 2012
adam33
This is the community wiki page for the gene adam33 please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase
The protein ADAM13 (alfandari et al., 1997 [1] is the orthologue of human ADAM33 but the sequences have diverged sufficiently that the two proteins cannot functionally replace each other. ADAM13 is a cell surface metalloprotease that binds to its substrate via its cystein rich domain ([Gaultier et al., 2002][2]; [Smith et al., 2002][3]). ADAM13 binds and cleave fibronectin (Alfandari et al., 2001[4]), Cadherin-11 (McCusker et al., 2009[5]), PAPC (Cousin et al., 2011[6]) and ephrinB (Wei et al., 2011[7]).
ADAM13 also cleaves itself within its cystein rich domain (Gaultier et al., 2002[8]). This cleavage can be followed by a cleavage by gama-secretase that release the cytoplasmic domain. The ADAM13 cytoplasmic domain translocates into the nucleus where it regulates gene expression to promote cranial neural crest cell migration (Cousin et al., 2011[9]).
The cytoplasmic domain of ADAM13 interacts with multiple SH# containing proteins including PACSIN-2 which negatively regulates its proteolytic activity (Cousin et al., 2000 [10]).