P12397 (MU1_REOVJ) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 85. History...
Names and origin
|Protein names||Recommended name:|
Outer capsid protein mu-1
|Organism||Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2) [Complete proteome]|
|Taxonomic identifier||10885 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Spinareovirinae › Orthoreovirus ›|
|Virus host||Mammalia [TaxID: 40674]|
|Sequence length||708 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 By similarity.
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 By similarity.
Heterohexamer of three sigma-3 and three Mu-1 proteins By similarity.
Outer capsid protein mu-1: Virion By similarity. Host cell membrane; Lipid-anchor By similarity. Host endoplasmic reticulum By similarity. Host mitochondrion By similarity. Note: Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation By similarity.
The C-terminal region, phi, determines both targeting to intracellular membranes and induction of apoptosis By similarity.
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. Ref.2
Mu-1 and mu-1N are N-terminally myristoylated. This acylation is essential for the membrane fusion activity By similarity.
Belongs to the orthoreovirus mu-1 protein family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed; by host By similarity|
|Chain||2 – 708||707||Outer capsid protein mu-1||PRO_0000040659|
|Chain||2 – 42||41||Outer capsid protein mu-1N||PRO_0000344979|
|Chain||43 – 708||666||Outer capsid protein mu-1C||PRO_0000040661|
|Site||42 – 43||2||Cleavage By similarity|
Amino acid modifications
|Lipidation||2||1||N-myristoyl glycine; by host By similarity|
|Glycosylation||3||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||12||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||81||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||110||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||458||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||482||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||528||1||N-linked (GlcNAc...); by host Potential|
|||"Evolution of reovirus genes: a comparison of serotype 1, 2, and 3 M2 genome segments, which encode the major structural capsid protein mu 1C."|
Wiener J.R., Joklik W.K.
Virology 163:603-613(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
|||"A carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration."|
Nibert M.L., Fields B.N.
J. Virol. 66:6408-6418(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
|M19355 mRNA. Translation: AAA47246.1.|
|PIR||M2XR2J. B28607. |
3D structure databases
|SMR||P12397. Positions 10-675. |
Protein family/group databases
|TCDB||1.A.60.1.1. the mammalian reovirus pre-forming peptide, mu-1 (mu-1) family. |
Protocols and materials databases
Family and domain databases
|Gene3D||1.10.2040.10. 2 hits. |
22.214.171.1240. 1 hit.
3.90.1370.10. 1 hit.
|InterPro||IPR009113. Mu1/VP4. |
|Pfam||PF05993. Reovirus_M2. 1 hit. |
|SUPFAM||SSF69908. SSF69908. 1 hit. |
|Accession||Primary (citable) accession number: P12397|
Secondary accession number(s): Q85659, Q89834
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families