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P11078 (MU1_REOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer capsid protein mu-1

Short name=Mu1

Cleaved into the following 2 chains:

  1. Outer capsid protein mu-1N
  2. Outer capsid protein mu-1C
Gene names
Name:M2
OrganismReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [Complete proteome]
Taxonomic identifier10886 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.6

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. Ref.6

Subunit structure

Heterohexamer of three sigma-3 and three Mu-1 proteins By similarity.

Subcellular location

Outer capsid protein mu-1: Virion By similarity. Host cell membrane; Lipid-anchor. 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.

Domain

The C-terminal region, phi, determines both targeting to intracellular membranes and induction of apoptosis By similarity.

Post-translational modification

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.4 Ref.5

Mu-1 and mu-1N are N-terminally myristoylated. This acylation is essential for the membrane fusion activity.

Sequence similarities

Belongs to the orthoreovirus mu-1 protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – 708707Outer capsid protein mu-1
PRO_0000040656
Chain2 – 4241Outer capsid protein mu-1N
PRO_0000344978
Chain43 – 708666Outer capsid protein mu-1C
PRO_0000040658

Sites

Site42 – 432Cleavage

Amino acid modifications

Lipidation21N-myristoyl glycine; by host Ref.4
Glycosylation31N-linked (GlcNAc...); by host Potential
Glycosylation121N-linked (GlcNAc...); by host Potential
Glycosylation811N-linked (GlcNAc...); by host Potential
Glycosylation1101N-linked (GlcNAc...); by host Potential
Glycosylation4581N-linked (GlcNAc...); by host Potential
Glycosylation4821N-linked (GlcNAc...); by host Potential
Glycosylation5281N-linked (GlcNAc...); by host Potential
Glycosylation6591N-linked (GlcNAc...); by host Potential

Experimental info

Mutagenesis21G → A: Complete loss of myristoylation and binding to sigma-3 protein. Ref.4
Mutagenesis421N → T: Complete loss of proteolytic cleavage. Ref.4
Sequence conflict2271S → T in AAA63507. Ref.2
Sequence conflict439 – 4402AQ → RVM in AAA47258. Ref.1
Sequence conflict5871N → K in AAA47258. Ref.1
Sequence conflict7011V → L in AAA47258. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11078 [UniParc].

Last modified July 22, 2008. Version 4.
Checksum: A73DDDC325588BC8

FASTA70876,271
        10         20         30         40         50         60 
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA VGDETSVTSP 

        70         80         90        100        110        120 
GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYIDEPL VVVTEHAITN FTKAEMALEF 

       130        140        150        160        170        180 
NREFLDKMRV LSVSPKYSDL LTYVDCYVGV SARQALNNFQ KQVPVITPTR QTMYVDSIQA 

       190        200        210        220        230        240 
ALKALEKWEI DLRVAQTLLP TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL 

       250        260        270        280        290        300 
AKRNGGIQWM DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI 

       310        320        330        340        350        360 
IASLAPVPAP VFAIPPKPAD YNVRTLRIDE ATWLRMIPKS MNTPFQIQVT DNTGTNWHLN 

       370        380        390        400        410        420 
LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG FIVFQSKIPF ELWTAASQIG 

       430        440        450        460        470        480 
QATVVNYVQL YAEDSSFTAQ SIIATTSLAY NYEPEQLNKT DPEMNYYLLA TFIDSAAITP 

       490        500        510        520        530        540 
TNMTQPDVWD ALLTMSPLSA GEVTVKGAVV SEVVPADLIG SYTPESLNAS LPNDAARCMI 

       550        560        570        580        590        600 
DRASKIAEAI KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM 

       610        620        630        640        650        660 
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK LSSSESIQNW 

       670        680        690        700 
TQGFLDKVSA HFPAPKPDCP TSGDSGESSN RRVKRDSYAG VVKRGYTR 

« Hide

References

[1]"Molecular cloning and sequencing of the gene (M2) encoding the major virion structural protein (mu 1-mu 1C) of serotypes 1 and 3 of mammalian reovirus."
Tarlow O., McCorquodale J.G., McCrae M.A.
Virology 164:141-146(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Complete nucleotide sequence of the M2 gene segment of reovirus type 3 dearing and analysis of its protein product mu 1."
Jayasuriya A.K., Nibert M.L., Fields B.N.
Virology 163:591-602(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"A plasmid-based reverse genetics system for animal double-stranded RNA viruses."
Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., Wilson G.J., Chappell J.D., Dermody T.S.
Cell Host Microbe 1:147-157(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Infectious clone.
[4]"Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells."
Tillotson L., Shatkin A.J.
J. Virol. 66:2180-2186(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2 AND ASN-42, PROTEOLYTIC PROCESSING.
[5]"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.
[6]"Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms."
Farsetta D.L., Chandran K., Nibert M.L.
J. Biol. Chem. 275:39693-39701(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19408 Genomic RNA. Translation: AAA47258.1.
M20161 Genomic RNA. Translation: AAA63507.1.
EF494439 Genomic RNA. Translation: ABP48917.1.
PIRM2XR4D. A28606.
M2XR3D. B28612.

3D structure databases

ProteinModelPortalP11078.
SMRP11078. Positions 10-675.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSN07.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.2040.10. 2 hits.
2.60.120.420. 1 hit.
3.90.1370.10. 1 hit.
InterProIPR009113. Mu1/VP4.
IPR015962. Mu1_membr_pen_a-bundle_sub2.
IPR015961. Mu1_membr_pen_a/b_sub.
IPR015960. Mu1_membr_pen_b-sand_sub.
[Graphical view]
PfamPF05993. Reovirus_M2. 1 hit.
[Graphical view]
SUPFAMSSF69908. SSF69908. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMU1_REOVD
AccessionPrimary (citable) accession number: P11078
Secondary accession number(s): A4ZY24, P17701
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families