UniProt functional annotation for P11077



	UniProt functional annotation for P11077

UniProt code: P11077.

Organism: Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).

Taxonomy: Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.

Function: Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane- penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.

Function: The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.

Subunit: Heterohexamer of three sigma-3 and three Mu-1 proteins. {ECO:0000269|PubMed:11832217}.

Subcellular location: [Outer capsid protein mu-1]: Virion. Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Host endoplasmic reticulum. Host mitochondrion. Note=Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation (By similarity). {ECO:0000250}.

Domain: The C-terminal region, phi, determines both targeting to intracellular membranes and induction of apoptosis. {ECO:0000305}.

Ptm: Cleaved during the endosomal proteolytic disassembly of the outer capsid. Mu-1 is proteolytically cleaved into mu-1N and mu-1C during the maturation step to generate the ISVP. Cleavage of mu-1 to mu-1C is dependent on myristoylation and binding to sigma-3 protein. Mu-1C is further cleaved into delta (59 kDa), and phi (13 kDa) segments during entry into the host cell cytoplasm. {ECO:0000269|PubMed:1328674}.

Ptm: Mu-1 and mu-1N are N-terminally myristoylated. This acylation is essential for the membrane fusion activity (By similarity). {ECO:0000250}.

Similarity: Belongs to the orthoreovirus mu-1 protein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.



Function:		Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane- penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.



Function:		The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.


Subunit:		Heterohexamer of three sigma-3 and three Mu-1 proteins. {ECO:0000269\|PubMed:11832217}.
Subcellular location:		[Outer capsid protein mu-1]: Virion. Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Host endoplasmic reticulum. Host mitochondrion. Note=Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation (By similarity). {ECO:0000250}.
Domain:		The C-terminal region, phi, determines both targeting to intracellular membranes and induction of apoptosis. {ECO:0000305}.
Ptm:		Cleaved during the endosomal proteolytic disassembly of the outer capsid. Mu-1 is proteolytically cleaved into mu-1N and mu-1C during the maturation step to generate the ISVP. Cleavage of mu-1 to mu-1C is dependent on myristoylation and binding to sigma-3 protein. Mu-1C is further cleaved into delta (59 kDa), and phi (13 kDa) segments during entry into the host cell cytoplasm. {ECO:0000269\|PubMed:1328674}.
Ptm:		Mu-1 and mu-1N are N-terminally myristoylated. This acylation is essential for the membrane fusion activity (By similarity). {ECO:0000250}.
Similarity:		Belongs to the orthoreovirus mu-1 protein family. {ECO:0000305}.