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P11077

- MU1_REOVL

UniProt

P11077 - MU1_REOVL

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Protein

Outer capsid protein mu-1

Gene

M2

Organism
Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
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.
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.

Sites

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

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 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Taxonomic identifieri10884 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000007253: Genome

Subcellular locationi

Chain Outer capsid protein mu-1 : Virion. Host cell membrane By similarity; Lipid-anchor By similarity. Host endoplasmic reticulum. Host mitochondrion
Note: Found in the outer capsid. Seems to associate with cell membranes. This association is enhanced by myristoylation (By similarity).By similarity

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 capsid Source: CACAO
  6. 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
Mutagenesisi42 – 421N → A: Complete loss of mu-1N cleavage and host membrane penetration. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 708707Outer capsid protein mu-1PRO_0000040662Add
BLAST
Chaini2 – 4241Outer capsid protein mu-1NPRO_0000344980Add
BLAST
Chaini43 – 708666Outer capsid protein mu-1CPRO_0000040664Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

IntActiP11077. 1 interaction.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 173
Helixi24 – 263
Helixi38 – 414
Beta strandi45 – 5511
Helixi60 – 623
Beta strandi63 – 653
Helixi68 – 703
Helixi105 – 11915
Helixi122 – 1276
Helixi137 – 1404
Beta strandi142 – 15110
Helixi152 – 1565
Beta strandi159 – 1668
Helixi168 – 19831
Beta strandi204 – 2074
Helixi212 – 22211
Helixi228 – 2303
Helixi233 – 24311
Turni252 – 2543
Helixi264 – 2707
Helixi279 – 29618
Helixi298 – 3014
Helixi309 – 3124
Beta strandi319 – 3213
Turni323 – 3253
Turni328 – 3303
Beta strandi334 – 3363
Beta strandi339 – 3413
Beta strandi344 – 3518
Beta strandi356 – 3627
Beta strandi366 – 3694
Beta strandi375 – 3817
Beta strandi398 – 40811
Helixi410 – 4123
Helixi416 – 4183
Beta strandi420 – 42910
Beta strandi432 – 4343
Beta strandi441 – 4433
Beta strandi448 – 4525
Helixi454 – 4574
Beta strandi465 – 47612
Turni480 – 4823
Beta strandi490 – 4989
Beta strandi503 – 5053
Beta strandi508 – 5136
Helixi515 – 5184
Helixi524 – 5296
Helixi535 – 55319
Turni563 – 5653
Helixi566 – 57510
Beta strandi581 – 5833
Helixi589 – 60517
Helixi607 – 6115
Turni616 – 6194
Helixi621 – 63616
Helixi644 – 67128

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMUX-ray2.80A/C/E2-42[»]
B/D/F43-708[»]
2CSEelectron microscopy7.00A/B/C/J/K/L/P/Q/R/T1-708[»]
ProteinModelPortaliP11077.
SMRiP11077. Positions 10-675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11077.

Family & Domainsi

Domaini

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

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.

P11077-1 [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 MGTPFQIQVT
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 SEVVPAELIG 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 TQGFLDKVST HFPAPKPDCP TNGDGSEPSA RRVKRDSYAG

VVKRGYTR
Length:708
Mass (Da):76,233
Last modified:July 22, 2008 - v4
Checksum:i12F3839798DF355F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31N → T in AAA47237. (PubMed:3363862)Curated
Sequence conflicti237 – 2382AV → LL in AAA47237. (PubMed:3363862)Curated
Sequence conflicti272 – 2721P → L in AAA47236. (PubMed:3354208)Curated
Sequence conflicti284 – 2841K → R in AAA47236. (PubMed:3354208)Curated
Sequence conflicti644 – 6441V → M in AAA47237. (PubMed:3363862)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19407 Genomic RNA. Translation: AAA47237.1.
M19345 mRNA. Translation: AAA47236.1.
AF490617 mRNA. Translation: AAM10735.1.
PIRiA28607. M2XR2L.
A28612. M2XR1L.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19407 Genomic RNA. Translation: AAA47237.1 .
M19345 mRNA. Translation: AAA47236.1 .
AF490617 mRNA. Translation: AAM10735.1 .
PIRi A28607. M2XR2L.
A28612. M2XR1L.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JMU X-ray 2.80 A/C/E 2-42 [» ]
B/D/F 43-708 [» ]
2CSE electron microscopy 7.00 A/B/C/J/K/L/P/Q/R/T 1-708 [» ]
ProteinModelPortali P11077.
SMRi P11077. Positions 10-675.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11077. 1 interaction.

Protein family/group databases

MEROPSi N07.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11077.

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. "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].
  3. "In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins mu1 and sigma3."
    Chandran K., Walker S.B., Chen Y., Contreras C.M., Schiff L.A., Baker T.S., Nibert M.L.
    J. Virol. 73:3941-3950(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Isolate T1/Human/Ohio/1953.
  4. "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.
  5. "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.
  6. "Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus."
    Odegard A.L., Chandran K., Zhang X., Parker J.S.L., Baker T.S., Nibert M.L.
    J. Virol. 78:8732-8745(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-42.
  7. "Reovirus outer capsid protein micro1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria."
    Coffey C.M., Sheh A., Kim I.S., Chandran K., Nibert M.L., Parker J.S.L.
    J. Virol. 80:8422-8438(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Reovirus mu1 structural rearrangements that mediate membrane penetration."
    Zhang L., Chandran K., Nibert M.L., Harrison S.C.
    J. Virol. 80:12367-12376(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Peptides released from reovirus outer capsid form membrane pores that recruit virus particles."
    Ivanovic T., Agosto M.A., Zhang L., Chandran K., Harrison S.C., Nibert M.L.
    EMBO J. 27:1289-1298(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-42.
  10. "Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3."
    Liemann S., Chandran K., Baker T.S., Nibert M.L., Harrison S.C.
    Cell 108:283-295(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SIGMA-3.
  11. "Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution."
    Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S.
    Structure 13:1545-1557(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).

Entry informationi

Entry nameiMU1_REOVL
AccessioniPrimary (citable) accession number: P11077
Secondary accession number(s): Q85657, Q8QR20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 22, 2008
Last modified: October 29, 2014
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3