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P12397

- MU1_REOVJ

UniProt

P12397 - MU1_REOVJ

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Protein
Outer capsid protein mu-1
Gene
M2
Organism
Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.
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.

Sites

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

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
Complete GO annotation...

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

TCDBi1.A.60.1.1. the mammalian reovirus pre-forming peptide, mu-1 (mu-1) family.

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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
Taxonomic identifieri10885 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000006370: Genome

Subcellular locationi

Chain 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.

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
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 708707Outer capsid protein mu-1
PRO_0000040659Add
BLAST
Chaini2 – 4241Outer capsid protein mu-1N
PRO_0000344979Add
BLAST
Chaini43 – 708666Outer capsid protein mu-1C
PRO_0000040661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Glycosylationi3 – 31N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi12 – 121N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi81 – 811N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi110 – 1101N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi458 – 4581N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi482 – 4821N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi528 – 5281N-linked (GlcNAc...); by host Reviewed prediction

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

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP12397.
SMRiP12397. Positions 10-675.

Family & Domainsi

Domaini

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

Sequence similaritiesi

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.

P12397-1 [UniParc]FASTAAdd to Basket

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MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA    50
IGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYNDEPL 100
VVVTEHAIAN FTKAEMALEF NREFLDKLRV LSVSPKYSDL LTYVDCYVGV 150
SARQALNNFQ KQVPVITPTR QTMYVDSIQA ALKALEKWEI DLRVAQTLLP 200
TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL AKRNGGIQWM 250
DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI 300
IASLVPVPAP VFAIPPKPAD YNVRTLKIDE ATWLRMIPKT MNTPFQIQVT 350
DNTGTSWHMN LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG 400
FIVFQSKIPF ELWTAASQIG QATVVNYVQL YAEDSSFTAQ SIIATTSLAY 450
NYEPEQLNKT DPEMNYYLLA AFIDSAAIST SNMTQPDVWD ALLTMSPLSA 500
GEVTVKGAVV SEVIPADLVG SYTPESLNAS LPNDAARCMI DRASKIAEAI 550
KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM 600
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK 650
LSSSESIQSW TQGFLDKVST HFPAPKPDCP QSGDSGDGSA RRLKRDSYAG 700
VVKRGYTR 708
Length:708
Mass (Da):76,146
Last modified:January 23, 2007 - v3
Checksum:i503DEE3053DEF422
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19355 mRNA. Translation: AAA47246.1.
PIRiB28607. M2XR2J.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19355 mRNA. Translation: AAA47246.1 .
PIRi B28607. M2XR2J.

3D structure databases

ProteinModelPortali P12397.
SMRi P12397. Positions 10-675.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 1.A.60.1.1. the mammalian reovirus pre-forming peptide, mu-1 (mu-1) family.

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. "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].
  2. "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.

Entry informationi

Entry nameiMU1_REOVJ
AccessioniPrimary (citable) accession number: P12397
Secondary accession number(s): Q85659, Q89834
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 87 of the entry and version 3 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

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