Reactome | The leading 65 amino acids of nascent membrane-bound G prote...

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created	[InstanceEdit:9830853] Stephan, Ralf, 2023-03-16
dbId	9830856
displayName	The leading 65 amino acids of nascent membrane-bound G prote...
literatureReference	[LiteratureReference:9829036] Kinetics of synthesis of respiratory syncytial virus glycoproteins [LiteratureReference:9830880] Expression and glycosylation of the respiratory syncytial virus G protein in Saccharomyces cerevisiae [LiteratureReference:9833168] Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage
modified	[InstanceEdit:9833180] Orlic-Milacic, Marija, 2023-04-13
schemaClass	Summation
text	The leading 65 amino acids of nascent membrane-bound G protein variant of RSV, assumed to be the signal sequence directing it to the endoplasmic reticulum (ER) membrane, are cleaved off by an unknown enzyme (Fernie et al, 1985; Ding et al, 1987). While the responsible peptidase has not been experimentally investigated, signal peptides of human proteins are cleaved by the signal peptidase complex (SPC) located at the endoplasmic reticulum membrane. This complex, which can exist in two versions, SPC-A and SPC-C, that differ in their catalytic subunits (SEC11A in SPC-A, and SEC11C in SPC-C), is known to be involved in cleavage of signal peptides in other viruses (Liaci et al. 2021), and is a plausible candidate for the membrane-bound G protein signal peptidase.

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