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P11078

- MU1_REOVD

UniProt

P11078 - MU1_REOVD

Protein

Outer capsid protein mu-1

Gene

M2

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 4 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    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.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-3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei42 – 432Cleavage

    GO - Molecular functioni

    1. host cell surface binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. pathogenesis Source: InterPro
    3. permeabilization of host organelle membrane involved in viral entry into host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membrane, Virus entry into host cell

    Protein family/group databases

    MEROPSiN07.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Outer capsid protein mu-1
    Short name:
    Mu1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:M2
    OrganismiReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
    Taxonomic identifieri10886 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
    Virus hostiMammalia [TaxID: 40674]
    ProteomesiUP000006373: Genome

    Subcellular locationi

    Chain 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.

    GO - Cellular componenti

    1. host cell endoplasmic reticulum Source: UniProtKB-SubCell
    2. host cell mitochondrion Source: UniProtKB-SubCell
    3. host cell plasma membrane Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB-KW
    5. viral outer capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host endoplasmic reticulum, Host membrane, Host mitochondrion, Membrane, Outer capsid protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Complete loss of myristoylation and binding to sigma-3 protein. 1 Publication
    Mutagenesisi42 – 421N → T: Complete loss of proteolytic cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host
    Chaini2 – 708707Outer capsid protein mu-1PRO_0000040656Add
    BLAST
    Chaini2 – 4241Outer capsid protein mu-1NPRO_0000344978Add
    BLAST
    Chaini43 – 708666Outer capsid protein mu-1CPRO_0000040658Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
    Glycosylationi3 – 31N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi12 – 121N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi81 – 811N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi110 – 1101N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi528 – 5281N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi659 – 6591N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Myristate

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP11078.
    SMRiP11078. Positions 10-675.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Belongs to the orthoreovirus mu-1 protein family.Curated

    Family and domain databases

    Gene3Di1.10.2040.10. 2 hits.
    2.60.120.420. 1 hit.
    3.90.1370.10. 1 hit.
    InterProiIPR009113. 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]
    PfamiPF05993. Reovirus_M2. 1 hit.
    [Graphical view]
    SUPFAMiSSF69908. SSF69908. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11078-1 [UniParc]FASTAAdd to Basket

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    MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA    50
    VGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYIDEPL 100
    VVVTEHAITN FTKAEMALEF NREFLDKMRV LSVSPKYSDL LTYVDCYVGV 150
    SARQALNNFQ KQVPVITPTR QTMYVDSIQA ALKALEKWEI DLRVAQTLLP 200
    TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL AKRNGGIQWM 250
    DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI 300
    IASLAPVPAP VFAIPPKPAD YNVRTLRIDE ATWLRMIPKS MNTPFQIQVT 350
    DNTGTNWHLN LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG 400
    FIVFQSKIPF ELWTAASQIG QATVVNYVQL YAEDSSFTAQ SIIATTSLAY 450
    NYEPEQLNKT DPEMNYYLLA TFIDSAAITP TNMTQPDVWD ALLTMSPLSA 500
    GEVTVKGAVV SEVVPADLIG SYTPESLNAS LPNDAARCMI DRASKIAEAI 550
    KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM 600
    QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK 650
    LSSSESIQNW TQGFLDKVSA HFPAPKPDCP TSGDSGESSN RRVKRDSYAG 700
    VVKRGYTR 708
    Length:708
    Mass (Da):76,271
    Last modified:July 22, 2008 - v4
    Checksum:iA73DDDC325588BC8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti227 – 2271S → T in AAA63507. (PubMed:3354207)Curated
    Sequence conflicti439 – 4402AQ → RVM in AAA47258. (PubMed:3363862)Curated
    Sequence conflicti587 – 5871N → K in AAA47258. (PubMed:3363862)Curated
    Sequence conflicti701 – 7011V → L in AAA47258. (PubMed:3363862)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19408 Genomic RNA. Translation: AAA47258.1.
    M20161 Genomic RNA. Translation: AAA63507.1.
    EF494439 Genomic RNA. Translation: ABP48917.1.
    PIRiA28606. M2XR4D.
    B28612. M2XR3D.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19408 Genomic RNA. Translation: AAA47258.1 .
    M20161 Genomic RNA. Translation: AAA63507.1 .
    EF494439 Genomic RNA. Translation: ABP48917.1 .
    PIRi A28606. M2XR4D.
    B28612. M2XR3D.

    3D structure databases

    ProteinModelPortali P11078.
    SMRi P11078. Positions 10-675.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi N07.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.2040.10. 2 hits.
    2.60.120.420. 1 hit.
    3.90.1370.10. 1 hit.
    InterProi IPR009113. 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 ]
    Pfami PF05993. Reovirus_M2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69908. SSF69908. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiMU1_REOVD
    AccessioniPrimary (citable) accession number: P11078
    Secondary accession number(s): A4ZY24, P17701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 96 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3