MU1_REOVD
ID MU1_REOVD Reviewed; 708 AA.
AC P11078; A4ZY24; P17701;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 23-FEB-2022, entry version 130.
DE RecName: Full=Outer capsid protein mu-1;
DE Short=Mu1;
DE Contains:
DE RecName: Full=Outer capsid protein mu-1N;
DE Contains:
DE RecName: Full=Outer capsid protein mu-1C;
GN Name=M2;
OS Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10886;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3363862; DOI=10.1016/0042-6822(88)90629-0;
RA Tarlow O., McCorquodale J.G., McCrae M.A.;
RT "Molecular cloning and sequencing of the gene (M2) encoding the major
RT virion structural protein (mu 1-mu 1C) of serotypes 1 and 3 of mammalian
RT reovirus.";
RL Virology 164:141-146(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3354207; DOI=10.1016/0042-6822(88)90300-5;
RA Jayasuriya A.K., Nibert M.L., Fields B.N.;
RT "Complete nucleotide sequence of the M2 gene segment of reovirus type 3
RT dearing and analysis of its protein product mu 1.";
RL Virology 163:591-602(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone;
RX PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA Wilson G.J., Chappell J.D., Dermody T.S.;
RT "A plasmid-based reverse genetics system for animal double-stranded RNA
RT viruses.";
RL Cell Host Microbe 1:147-157(2007).
RN [4]
RP MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2 AND ASN-42, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=1548757; DOI=10.1128/jvi.66.4.2180-2186.1992;
RA Tillotson L., Shatkin A.J.;
RT "Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide
RT mu 1 are required for site-specific cleavage to mu 1C in transfected
RT cells.";
RL J. Virol. 66:2180-2186(1992).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1328674; DOI=10.1128/jvi.66.11.6408-6418.1992;
RA Nibert M.L., Fields B.N.;
RT "A carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious
RT subvirion particles of mammalian reoviruses and is proposed to have a role
RT in penetration.";
RL J. Virol. 66:6408-6418(1992).
RN [6]
RP FUNCTION.
RX PubMed=11007773; DOI=10.1074/jbc.m004562200;
RA Farsetta D.L., Chandran K., Nibert M.L.;
RT "Transcriptional activities of reovirus RNA polymerase in recoated cores.
RT Initiation and elongation are regulated by separate mechanisms.";
RL J. Biol. Chem. 275:39693-39701(2000).
CC -!- FUNCTION: Major outer capsid protein involved in host cell membrane
CC penetration. In the endocytic compartment, outer-capsid protein sigma-3
CC is removed by cathepsin proteases, which exposes the viral membrane-
CC penetration protein mu-1. Both myristoylated peptides mu-1N and phi are
CC released during infectious subvirion particles (ISVP) formation in the
CC endosome. They associate with host membranes and mu-1N induces
CC permeabilization and delivery of transcriptionally active viral
CC particles into the host cell cytoplasm. Seems to induce apoptosis in
CC the host cell (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The viral outer shell polypeptides, of which mu-1 is one,
CC impose structural constraints that prevent elongation of nascent
CC transcripts by the RNA-dependent RNA polymerase lambda-3.
CC {ECO:0000269|PubMed:11007773}.
CC -!- SUBUNIT: Heterohexamer of three sigma-3 and three Mu-1 proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Outer capsid protein mu-1]: Virion
CC {ECO:0000250}. Host cell membrane; Lipid-anchor. Host endoplasmic
CC reticulum {ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Found
CC in the outer capsid. Seems to associate with cell membranes. This
CC association is enhanced by myristoylation.
CC -!- DOMAIN: The C-terminal region, phi, determines both targeting to
CC intracellular membranes and induction of apoptosis. {ECO:0000250}.
CC -!- PTM: Cleaved during the endosomal proteolytic disassembly of the outer
CC capsid. Mu-1 is proteolytically cleaved into mu-1N and mu-1C during the
CC maturation step to generate the ISVP. Cleavage of mu-1 to mu-1C is
CC dependent on myristoylation and binding to sigma-3 protein. Mu-1C is
CC further cleaved into delta (59 kDa), and phi (13 kDa) segments during
CC entry into the host cell cytoplasm. {ECO:0000269|PubMed:1328674,
CC ECO:0000269|PubMed:1548757}.
CC -!- PTM: Mu-1 and mu-1N are N-terminally myristoylated. This acylation is
CC essential for the membrane fusion activity.
CC {ECO:0000269|PubMed:1548757}.
CC -!- SIMILARITY: Belongs to the orthoreovirus mu-1 protein family.
CC {ECO:0000305}.
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DR EMBL; M19408; AAA47258.1; -; Genomic_RNA.
DR EMBL; M20161; AAA63507.1; -; Genomic_RNA.
DR EMBL; EF494439; ABP48917.1; -; Genomic_RNA.
DR PIR; A28606; M2XR4D.
DR PIR; B28612; M2XR3D.
DR SMR; P11078; -.
DR ELM; P11078; -.
DR MEROPS; N07.001; -.
DR iPTMnet; P11078; -.
DR PRIDE; P11078; -.
DR Proteomes; UP000006373; Genome.
DR Proteomes; UP000165799; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR GO; GO:0046812; F:host cell surface binding; IEA:InterPro.
DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.10.2040.10; -; 1.
DR Gene3D; 1.10.2050.10; -; 1.
DR Gene3D; 2.60.120.420; -; 1.
DR Gene3D; 3.90.1370.10; -; 1.
DR InterPro; IPR009113; Mu1/VP4.
DR InterPro; IPR036256; Mu1/VP4_sf.
DR InterPro; IPR015961; Mu1_membr_pen_domI.
DR InterPro; IPR015962; Mu1_membr_pen_domII.
DR InterPro; IPR044937; Mu1_membr_pen_domIII.
DR InterPro; IPR015960; Mu1_membr_pen_domIV.
DR Pfam; PF05993; Reovirus_M2; 1.
DR SUPFAM; SSF69908; SSF69908; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Capsid protein; Glycoprotein; Host cell membrane;
KW Host endoplasmic reticulum; Host membrane; Host mitochondrion; Lipoprotein;
KW Membrane; Myristate; Outer capsid protein; Reference proteome;
KW Viral penetration into host cytoplasm;
KW Viral penetration via permeabilization of host membrane; Virion;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..708
FT /note="Outer capsid protein mu-1"
FT /id="PRO_0000040656"
FT CHAIN 2..42
FT /note="Outer capsid protein mu-1N"
FT /id="PRO_0000344978"
FT CHAIN 43..708
FT /note="Outer capsid protein mu-1C"
FT /id="PRO_0000040658"
FT REGION 675..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 42..43
FT /note="Cleavage"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:1548757"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 2
FT /note="G->A: Complete loss of myristoylation and binding to
FT sigma-3 protein."
FT /evidence="ECO:0000269|PubMed:1548757"
FT MUTAGEN 42
FT /note="N->T: Complete loss of proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:1548757"
FT CONFLICT 227
FT /note="S -> T (in Ref. 2; AAA63507)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="AQ -> RVM (in Ref. 1; AAA47258)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="N -> K (in Ref. 1; AAA47258)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="V -> L (in Ref. 1; AAA47258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 76271 MW; A73DDDC325588BC8 CRC64;
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA VGDETSVTSP
GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYIDEPL VVVTEHAITN FTKAEMALEF
NREFLDKMRV LSVSPKYSDL LTYVDCYVGV SARQALNNFQ KQVPVITPTR QTMYVDSIQA
ALKALEKWEI DLRVAQTLLP TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL
AKRNGGIQWM DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI
IASLAPVPAP VFAIPPKPAD YNVRTLRIDE ATWLRMIPKS MNTPFQIQVT DNTGTNWHLN
LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG FIVFQSKIPF ELWTAASQIG
QATVVNYVQL YAEDSSFTAQ SIIATTSLAY NYEPEQLNKT DPEMNYYLLA TFIDSAAITP
TNMTQPDVWD ALLTMSPLSA GEVTVKGAVV SEVVPADLIG SYTPESLNAS LPNDAARCMI
DRASKIAEAI KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK LSSSESIQNW
TQGFLDKVSA HFPAPKPDCP TSGDSGESSN RRVKRDSYAG VVKRGYTR
