VEMP_CVMA5
ID VEMP_CVMA5 Reviewed; 83 AA.
AC P0C2R0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 07-APR-2021, entry version 63.
DE RecName: Full=Envelope small membrane protein {ECO:0000255|HAMAP-Rule:MF_04204};
DE Short=E protein {ECO:0000255|HAMAP-Rule:MF_04204};
DE Short=sM protein {ECO:0000255|HAMAP-Rule:MF_04204};
GN Name=E {ECO:0000255|HAMAP-Rule:MF_04204}; Synonyms=sM; ORFNames=5b;
OS Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11142;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate C12 mutant;
RX PubMed=9426441; DOI=10.1006/viro.1997.8877;
RA Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.;
RT "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
RT associated with a Q159L amino acid substitution in the spike protein.";
RL Virology 239:1-10(1997).
RN [2]
RP INTERACTION WITH E PROTEIN.
RX PubMed=10544100; DOI=10.1006/viro.1999.9955;
RA Maeda J., Maeda A., Makino S.;
RT "Release of coronavirus E protein in membrane vesicles from virus-infected
RT cells and E protein-expressing cells.";
RL Virology 263:265-272(1999).
RN [3]
RP FUNCTION.
RX PubMed=10438879; DOI=10.1128/jvi.73.9.7853-7859.1999;
RA An S., Chen C.-J., Yu X., Leibowitz J.L., Makino S.;
RT "Induction of apoptosis in murine coronavirus-infected cultured cells and
RT demonstration of E protein as an apoptosis inducer.";
RL J. Virol. 73:7853-7859(1999).
RN [4]
RP CHARACTERIZATION, AND TOPOLOGY.
RX PubMed=10666264; DOI=10.1128/jvi.74.5.2333-2342.2000;
RA Raamsman M.J., Locker J.K., de Hooge A., de Vries A.A.F., Griffiths G.,
RA Vennema H., Rottier P.J.M.;
RT "Characterization of the coronavirus mouse hepatitis virus strain A59 small
RT membrane protein E.";
RL J. Virol. 74:2333-2342(2000).
RN [5]
RP TOPOLOGY.
RX PubMed=11277690; DOI=10.1006/viro.2001.0818;
RA Maeda J., Repass J.F., Maeda A., Makino S.;
RT "Membrane topology of coronavirus E protein.";
RL Virology 281:163-169(2001).
RN [6]
RP FUNCTION.
RX PubMed=15963987; DOI=10.1016/j.febslet.2005.05.046;
RA Madan V., Garcia Mde J., Sanz M.A., Carrasco L.;
RT "Viroporin activity of murine hepatitis virus E protein.";
RL FEBS Lett. 579:3607-3612(2005).
CC -!- FUNCTION: Component of the viral envelope that plays a central role in
CC virus morphogenesis and assembly. It is sufficient to form virus-like
CC particles. Seems to be important for creating the membrane curvature
CC needed to acquire the rounded, stable and infectious particle
CC phenotype. Acts as a viroporin, inducing the formation of hydrophilic
CC pores in cellular membranes. Also induces apoptosis.
CC {ECO:0000269|PubMed:10438879, ECO:0000269|PubMed:15963987}.
CC -!- FUNCTION: Plays a central role in virus morphogenesis and assembly.
CC Acts as a viroporin and self-assembles in host membranes forming
CC pentameric protein-lipid pores that allow ion transport. Also plays a
CC role in the induction of apoptosis. {ECO:0000255|HAMAP-Rule:MF_04204}.
CC -!- SUBUNIT: Homopentamer. Interacts with membrane protein M in the budding
CC compartment of the host cell, which is located between endoplasmic
CC reticulum and the Golgi complex. Interacts with Nucleoprotein.
CC {ECO:0000255|HAMAP-Rule:MF_04204}.
CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04204}; Single-pass type III membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04204}. Note=The cytoplasmic tail functions
CC as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04204}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses E protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04204}.
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DR EMBL; AF029248; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR TCDB; 1.A.65.1.1; the coronavirus viroporin e protein (viroporin e) family.
DR Proteomes; UP000007192; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0044662; P:disruption by virus of host cell membrane; IDA:CACAO.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:InterPro.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR CDD; cd21532; HKU1-CoV-like_E; 1.
DR HAMAP; MF_04204; BETA_CORONA_E; 1.
DR InterPro; IPR043506; E_protein_bCoV.
DR InterPro; IPR003873; E_protein_CoV.
DR Pfam; PF02723; CoV_E; 1.
DR PROSITE; PS51926; COV_E; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Host Golgi apparatus; Host membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..83
FT /note="Envelope small membrane protein"
FT /id="PRO_0000284092"
FT TOPO_DOM 1..16
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
FT TOPO_DOM 38..79
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04204"
SQ SEQUENCE 83 AA; 9667 MW; DB23452E548E105B CRC64;
MFNLFLTDTV WYVGQIIFIF AVCLMVTIIV VAFLASIKLC IQLCGLCNTL VLSPSIYLYD
RSKQLYKYYN EEMRLPLLEV DDI
