MU1_REOVJ
ID MU1_REOVJ Reviewed; 708 AA.
AC P12397; Q85659; Q89834;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 117.
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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10885;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
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 [2]
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).
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:0000250}.
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 {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Host endoplasmic reticulum {ECO:0000250}. Host
CC mitochondrion {ECO:0000250}. 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: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 -!- 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; M19355; AAA47246.1; -; mRNA.
DR PIR; B28607; M2XR2J.
DR SMR; P12397; -.
DR TCDB; 1.A.60.1.1; the mammalian reovirus pre-forming peptide, mu-1 (mu-1) family.
DR Proteomes; UP000006370; 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;
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_0000040659"
FT CHAIN 2..42
FT /note="Outer capsid protein mu-1N"
FT /id="PRO_0000344979"
FT CHAIN 43..708
FT /note="Outer capsid protein mu-1C"
FT /id="PRO_0000040661"
FT REGION 671..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 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"
SQ SEQUENCE 708 AA; 76146 MW; 503DEE3053DEF422 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 MNTPFQIQVT DNTGTSWHMN
LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG FIVFQSKIPF ELWTAASQIG
QATVVNYVQL YAEDSSFTAQ SIIATTSLAY NYEPEQLNKT DPEMNYYLLA AFIDSAAIST
SNMTQPDVWD ALLTMSPLSA GEVTVKGAVV SEVIPADLVG SYTPESLNAS LPNDAARCMI
DRASKIAEAI KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK LSSSESIQSW
TQGFLDKVST HFPAPKPDCP QSGDSGDGSA RRLKRDSYAG VVKRGYTR
