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P11078

- MU1_REOVD

UniProt

P11078 - MU1_REOVD

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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

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
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

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-KW
  2. host cell mitochondrion Source: UniProtKB-KW
  3. host cell plasma membrane Source: UniProtKB-KW
  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

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA
60 70 80 90 100
VGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYIDEPL
110 120 130 140 150
VVVTEHAITN FTKAEMALEF NREFLDKMRV 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
IASLAPVPAP VFAIPPKPAD YNVRTLRIDE ATWLRMIPKS MNTPFQIQVT
360 370 380 390 400
DNTGTNWHLN LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG
410 420 430 440 450
FIVFQSKIPF ELWTAASQIG QATVVNYVQL YAEDSSFTAQ SIIATTSLAY
460 470 480 490 500
NYEPEQLNKT DPEMNYYLLA TFIDSAAITP TNMTQPDVWD ALLTMSPLSA
510 520 530 540 550
GEVTVKGAVV SEVVPADLIG 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
LSSSESIQNW TQGFLDKVSA HFPAPKPDCP TSGDSGESSN RRVKRDSYAG

VVKRGYTR
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 29, 2014
This is version 97 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