Literature summary for 3.4.24.81 extracted from

Marcello, E.; Gardoni, F.; Di Luca, M.; Perez-Otano, I.
An arginine stretch limits ADAM10 exit from the endoplasmic reticulum (2010), J. Biol. Chem., 285, 10376-10384.

Search for more literature for 3.4.24.81

Cloned(Commentary)

Cloned (Comment)	Organism
generation of ADAM10chimeras of the extracellular domain of the human interleukin-2 receptor with the intracellular C-terminal domain of mouse ADAM10. Transfection into COS7 cells	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	identification of an endoplasmic reticulum retention motif within the ADAM10 intracellular C-terminal tail. Sequential deletion/mutagenesis analyses shows that an arginine-rich (723RRR) sequence is responsible for the retention of ADAM10 in the endoplasmic reticulum and its inefficient surface trafficking. Mutating the second arginine to alanine is sufficient to allow endoplasmic reticulum exit and surface expression in both heterologous cells and hippocampal neurons	Mus musculus	5783	-
membrane	transmembrane glycoprotein	Mus musculus	16020	-

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	transmembrane glycoprotein	Mus musculus
proteolytic modification	synthesized in an inactive form, which is proteolytically activated during its forward transport along the secretory pathway and at the plasma membrane	Mus musculus

Synonyms

Synonyms	Comment	Organism
ADAM10	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	the enzyme is responsible for the ectodomain shedding of a number of proteins implicated in the pathogenesis of diseases ranging from cancer to Alzheimer's disease	Mus musculus

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Release 2023.1 (January 2023)