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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: 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).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 – 432CleavageBy similarity

GO - Molecular functioni

GO - Biological processi

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 Componenti: Genome

Subcellular locationi

Outer capsid protein mu-1 :

GO - Cellular componenti

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 hostBy similarity
Chaini2 – 708707Outer capsid protein mu-1PRO_0000040659Add
BLAST
Chaini2 – 4241Outer capsid protein mu-1NPRO_0000344979Add
BLAST
Chaini43 – 708666Outer capsid protein mu-1CPRO_0000040661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
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

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).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.
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.

P12397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA
60 70 80 90 100
IGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYNDEPL
110 120 130 140 150
VVVTEHAIAN FTKAEMALEF NREFLDKLRV LSVSPKYSDL LTYVDCYVGV
160 170 180 190 200
SARQALNNFQ KQVPVITPTR QTMYVDSIQA ALKALEKWEI DLRVAQTLLP
210 220 230 240 250
TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL AKRNGGIQWM
260 270 280 290 300
DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI
310 320 330 340 350
IASLVPVPAP VFAIPPKPAD YNVRTLKIDE ATWLRMIPKT MNTPFQIQVT
360 370 380 390 400
DNTGTSWHMN LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG
410 420 430 440 450
FIVFQSKIPF ELWTAASQIG QATVVNYVQL YAEDSSFTAQ SIIATTSLAY
460 470 480 490 500
NYEPEQLNKT DPEMNYYLLA AFIDSAAIST SNMTQPDVWD ALLTMSPLSA
510 520 530 540 550
GEVTVKGAVV SEVIPADLVG SYTPESLNAS LPNDAARCMI DRASKIAEAI
560 570 580 590 600
KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM
610 620 630 640 650
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK
660 670 680 690 700
LSSSESIQSW TQGFLDKVST HFPAPKPDCP QSGDSGDGSA RRLKRDSYAG

VVKRGYTR
Length:708
Mass (Da):76,146
Last modified:January 23, 2007 - v3
Checksum:i503DEE3053DEF422
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19355 mRNA. Translation: AAA47246.1.
PIRiB28607. M2XR2J.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19355 mRNA. Translation: AAA47246.1.
PIRiB28607. M2XR2J.

3D structure databases

ProteinModelPortaliP12397.
SMRiP12397. Positions 10-675.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 90 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.