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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: 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.

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

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]
Proteomesi
  • UP000007253 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42N → A: Complete loss of mu-1N cleavage and host membrane penetration. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00000406622 – 708Outer capsid protein mu-1Add BLAST707
ChainiPRO_00003449802 – 42Outer capsid protein mu-1NAdd BLAST41
ChainiPRO_000004066443 – 708Outer capsid protein mu-1CAdd BLAST666

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Glycosylationi12N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi81N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi110N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi458N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi482N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi528N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi659N-linked (GlcNAc...); by hostSequence analysis1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei42 – 43CleavageBy similarity2

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 interactor.

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 17Combined sources3
Helixi24 – 26Combined sources3
Helixi38 – 41Combined sources4
Beta strandi45 – 55Combined sources11
Helixi60 – 62Combined sources3
Beta strandi63 – 65Combined sources3
Helixi68 – 70Combined sources3
Helixi105 – 119Combined sources15
Helixi122 – 127Combined sources6
Helixi137 – 140Combined sources4
Beta strandi142 – 151Combined sources10
Helixi152 – 156Combined sources5
Beta strandi159 – 166Combined sources8
Helixi168 – 198Combined sources31
Beta strandi204 – 207Combined sources4
Helixi212 – 222Combined sources11
Helixi228 – 230Combined sources3
Helixi233 – 243Combined sources11
Turni252 – 254Combined sources3
Helixi264 – 270Combined sources7
Helixi279 – 296Combined sources18
Helixi298 – 301Combined sources4
Helixi309 – 312Combined sources4
Beta strandi319 – 321Combined sources3
Turni323 – 325Combined sources3
Turni328 – 330Combined sources3
Beta strandi334 – 336Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi344 – 351Combined sources8
Beta strandi356 – 362Combined sources7
Beta strandi366 – 369Combined sources4
Beta strandi375 – 381Combined sources7
Beta strandi398 – 408Combined sources11
Helixi410 – 412Combined sources3
Helixi416 – 418Combined sources3
Beta strandi420 – 429Combined sources10
Beta strandi432 – 434Combined sources3
Beta strandi441 – 443Combined sources3
Beta strandi448 – 452Combined sources5
Helixi454 – 457Combined sources4
Beta strandi465 – 476Combined sources12
Turni480 – 482Combined sources3
Beta strandi490 – 498Combined sources9
Beta strandi503 – 505Combined sources3
Beta strandi508 – 513Combined sources6
Helixi515 – 518Combined sources4
Helixi524 – 529Combined sources6
Helixi535 – 553Combined sources19
Turni563 – 565Combined sources3
Helixi566 – 575Combined sources10
Beta strandi581 – 583Combined sources3
Helixi589 – 605Combined sources17
Helixi607 – 611Combined sources5
Turni616 – 619Combined sources4
Helixi621 – 636Combined sources16
Helixi644 – 671Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti3N → T in AAA47237 (PubMed:3363862).Curated1
Sequence conflicti237 – 238AV → LL in AAA47237 (PubMed:3363862).Curated2
Sequence conflicti272P → L in AAA47236 (PubMed:3354208).Curated1
Sequence conflicti284K → R in AAA47236 (PubMed:3354208).Curated1
Sequence conflicti644V → M in AAA47237 (PubMed:3363862).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M19407 Genomic RNA. Translation: AAA47237.1.
M19345 mRNA. Translation: AAA47236.1.
AF490617 mRNA. Translation: AAM10735.1.
PIRiA28607. M2XR2L.
A28612. M2XR1L.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11077. 1 interactor.

Protein family/group databases

MEROPSiN07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11077.

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...

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: November 30, 2016
This is version 112 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

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 one 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.