MU1_REOVL
ID MU1_REOVL Reviewed; 708 AA.
AC P11077; Q85657; Q8QR20;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 25-MAY-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 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10884;
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 [MRNA].
RX PubMed=3354208; DOI=10.1016/0042-6822(88)90301-7;
RA Wiener J.R., Joklik W.K.;
RT "Evolution of reovirus genes: a comparison of serotype 1, 2, and 3 M2
RT genome segments, which encode the major structural capsid protein mu 1C.";
RL Virology 163:603-613(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate T1/Human/Ohio/1953;
RX PubMed=10196289; DOI=10.1128/jvi.73.5.3941-3950.1999;
RA Chandran K., Walker S.B., Chen Y., Contreras C.M., Schiff L.A., Baker T.S.,
RA Nibert M.L.;
RT "In vitro recoating of reovirus cores with baculovirus-expressed outer-
RT capsid proteins mu1 and sigma3.";
RL J. Virol. 73:3941-3950(1999).
RN [4]
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 [5]
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).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASN-42.
RX PubMed=15280481; DOI=10.1128/jvi.78.16.8732-8745.2004;
RA Odegard A.L., Chandran K., Zhang X., Parker J.S.L., Baker T.S.,
RA Nibert M.L.;
RT "Putative autocleavage of outer capsid protein micro1, allowing release of
RT myristoylated peptide micro1N during particle uncoating, is critical for
RT cell entry by reovirus.";
RL J. Virol. 78:8732-8745(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16912293; DOI=10.1128/jvi.02601-05;
RA Coffey C.M., Sheh A., Kim I.S., Chandran K., Nibert M.L., Parker J.S.L.;
RT "Reovirus outer capsid protein micro1 induces apoptosis and associates with
RT lipid droplets, endoplasmic reticulum, and mitochondria.";
RL J. Virol. 80:8422-8438(2006).
RN [8]
RP FUNCTION.
RX PubMed=17005655; DOI=10.1128/jvi.01343-06;
RA Zhang L., Chandran K., Nibert M.L., Harrison S.C.;
RT "Reovirus mu1 structural rearrangements that mediate membrane
RT penetration.";
RL J. Virol. 80:12367-12376(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASN-42.
RX PubMed=18369316; DOI=10.1038/emboj.2008.60;
RA Ivanovic T., Agosto M.A., Zhang L., Chandran K., Harrison S.C.,
RA Nibert M.L.;
RT "Peptides released from reovirus outer capsid form membrane pores that
RT recruit virus particles.";
RL EMBO J. 27:1289-1298(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SIGMA-3.
RX PubMed=11832217; DOI=10.1016/s0092-8674(02)00612-8;
RA Liemann S., Chandran K., Baker T.S., Nibert M.L., Harrison S.C.;
RT "Structure of the reovirus membrane-penetration protein, Mu1, in a complex
RT with is protector protein, Sigma3.";
RL Cell 108:283-295(2002).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
RX PubMed=16216585; DOI=10.1016/j.str.2005.07.012;
RA Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L.,
RA Baker T.S.;
RT "Features of reovirus outer capsid protein mu1 revealed by electron
RT cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom
RT resolution.";
RL Structure 13:1545-1557(2005).
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.
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 -!- SUBUNIT: Heterohexamer of three sigma-3 and three Mu-1 proteins.
CC {ECO:0000269|PubMed:11832217}.
CC -!- SUBCELLULAR LOCATION: [Outer capsid protein mu-1]: Virion. Host cell
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Host endoplasmic
CC reticulum. Host mitochondrion. Note=Found in the outer capsid. Seems to
CC associate with cell membranes. This association is enhanced by
CC myristoylation (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C-terminal region, phi, determines both targeting to
CC intracellular membranes and induction of apoptosis. {ECO:0000305}.
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 -!- PTM: Mu-1 and mu-1N are N-terminally myristoylated. This acylation is
CC essential for the membrane fusion activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the orthoreovirus mu-1 protein family.
CC {ECO:0000305}.
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DR EMBL; M19407; AAA47237.1; -; Genomic_RNA.
DR EMBL; M19345; AAA47236.1; -; mRNA.
DR EMBL; AF490617; AAM10735.1; -; mRNA.
DR PIR; A28607; M2XR2L.
DR PIR; A28612; M2XR1L.
DR PDB; 1JMU; X-ray; 2.80 A; A/C/E=2-42, B/D/F=43-708.
DR PDB; 2CSE; EM; 7.00 A; A/B/C/J/K/L/P/Q/R/T=1-708.
DR PDB; 6XF8; EM; 6.50 A; F/K=43-675.
DR PDB; 6ZTY; EM; -; H/I/J=10-675.
DR PDB; 6ZTZ; EM; -; K/L/M=10-675.
DR PDBsum; 1JMU; -.
DR PDBsum; 2CSE; -.
DR PDBsum; 6XF8; -.
DR PDBsum; 6ZTY; -.
DR PDBsum; 6ZTZ; -.
DR SMR; P11077; -.
DR IntAct; P11077; 1.
DR MEROPS; N07.001; -.
DR EvolutionaryTrace; P11077; -.
DR Proteomes; UP000007253; 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:0019028; C:viral capsid; IDA:CACAO.
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 3D-structure; 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 /evidence="ECO:0000250"
FT CHAIN 2..708
FT /note="Outer capsid protein mu-1"
FT /id="PRO_0000040662"
FT CHAIN 2..42
FT /note="Outer capsid protein mu-1N"
FT /id="PRO_0000344980"
FT CHAIN 43..708
FT /note="Outer capsid protein mu-1C"
FT /id="PRO_0000040664"
FT REGION 674..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 42..43
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
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 42
FT /note="N->A: Complete loss of mu-1N cleavage and host
FT membrane penetration."
FT /evidence="ECO:0000269|PubMed:15280481,
FT ECO:0000269|PubMed:18369316"
FT CONFLICT 3
FT /note="N -> T (in Ref. 1; AAA47237)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="AV -> LL (in Ref. 1; AAA47237)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> L (in Ref. 2; AAA47236)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="K -> R (in Ref. 2; AAA47236)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="V -> M (in Ref. 1; AAA47237)"
FT /evidence="ECO:0000305"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 168..198
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6ZTY"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6ZTY"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 398..408
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 465..476
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 535..553
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 566..575
FT /evidence="ECO:0007829|PDB:1JMU"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 589..605
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 607..611
FT /evidence="ECO:0007829|PDB:1JMU"
FT TURN 616..619
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 621..636
FT /evidence="ECO:0007829|PDB:1JMU"
FT HELIX 644..671
FT /evidence="ECO:0007829|PDB:1JMU"
SQ SEQUENCE 708 AA; 76233 MW; 12F3839798DF355F CRC64;
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA IGDETSVTSP
GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYNDEPL VVVTEHAIAN FTKAEMALEF
NREFLDKLRV LSVSPKYSDL LTYVDCYVGV SARQALNNFQ KQVPVITPTR QTMYVDSIQA
ALKALEKWEI DLRVAQTLLP TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL
AKRNGGIQWM DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI
IASLVPVPAP VFAIPPKPAD YNVRTLKIDE ATWLRMIPKT MGTPFQIQVT DNTGTNWHLN
LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG FIVFQSKIPF ELWTAASQIG
QATVVNYVQL YAEDSSFTAQ SIIATTSLAY NYEPEQLNKT DPEMNYYLLA TFIDSAAITP
TNMTQPDVWD ALLTMSPLSA GEVTVKGAVV SEVVPAELIG SYTPESLNAS LPNDAARCMI
DRASKIAEAI KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK LSSSESIQNW
TQGFLDKVST HFPAPKPDCP TNGDGSEPSA RRVKRDSYAG VVKRGYTR
