VME1_CVM2
ID VME1_CVM2 Reviewed; 228 AA.
AC Q9JEB4; Q9PY97;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE Short=M protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=E1 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Matrix glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Membrane glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
GN Name=M {ECO:0000255|HAMAP-Rule:MF_04202}; ORFNames=6;
OS Murine coronavirus (strain 2) (MHV-2) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=76344;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION AT ASN-2.
RX PubMed=10725548; DOI=10.1016/s0168-1702(99)00134-3;
RA Yamada Y.K., Yabe M., Ohtsuki T., Taguchi F.;
RT "Unique N-linked glycosylation of murine coronavirus MHV-2 membrane protein
RT at the conserved O-linked glycosylation site.";
RL Virus Res. 66:149-154(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11502093; DOI=10.1006/exmp.2001.2378;
RA Das Sarma J., Fu L., Hingley S.T., Lavi E.;
RT "Mouse hepatitis virus type-2 infection in mice: an experimental model
RT system of acute meningitis and hepatitis.";
RL Exp. Mol. Pathol. 71:1-12(2001).
CC -!- FUNCTION: Component of the viral envelope that plays a central role in
CC virus morphogenesis and assembly via its interactions with other viral
CC proteins. {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBUNIT: Homomultimer. Interacts with envelope E protein in the budding
CC compartment of the host cell, which is located between endoplasmic
CC reticulum and the Golgi complex. Forms a complex with HE and S
CC proteins. Interacts with nucleocapsid N protein. This interaction
CC probably participates in RNA packaging into the virus.
CC {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Note=Largely embedded in the lipid bilayer.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
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DR EMBL; AF126508; AAF36439.1; -; mRNA.
DR EMBL; AF201929; AAF19388.1; -; mRNA.
DR iPTMnet; Q9JEB4; -.
DR Proteomes; UP000139707; 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:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule.
DR CDD; cd21568; HCoV-like_M; 1.
DR HAMAP; MF_04202; BETA_CORONA_M; 1.
DR InterPro; IPR002574; M_CoV.
DR InterPro; IPR044362; M_HCoV-like.
DR Pfam; PF01635; CoV_M; 1.
DR PROSITE; PS51927; COV_M; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral immunoevasion; Viral matrix protein; Virion.
FT CHAIN 1..228
FT /note="Membrane protein"
FT /id="PRO_0000106036"
FT TOPO_DOM 2..25
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 47..56
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 78..85
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 107..228
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:10725548"
FT CONFLICT 2
FT /note="N -> T (in Ref. 2; AAF19388)"
FT CONFLICT 128
FT /note="T -> I (in Ref. 2; AAF19388)"
SQ SEQUENCE 228 AA; 26147 MW; 325AC1BE19B06823 CRC64;
MNSTTQAPQP VYQWTADEAI RFLKEWNFSL GIILLFVTII LQFGYTSRSM FVYVVKMILL
WLMWPLTIVL CIFNCVYALN NVYLGFSIVF TIVSIIMWIM YFVNSIRLFI RTGSWWSFNP
ETNNLMCTDM KGTVYVRPII EDYHTLTATI IRGHLYMQGV KLGTGFSLSD LPAYVTVAKV
SHLCTYKRAF LDKVDGVSGF AVYVKSKVGN YRLPSNKPSG MDTALLRI
