M_EAVBU
ID M_EAVBU Reviewed; 162 AA.
AC P28991;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 23-FEB-2022, entry version 71.
DE RecName: Full=Membrane protein;
DE Short=Protein M;
GN Name=M; ORFNames=6;
OS Equine arteritis virus (strain Bucyrus) (EAV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Equarterivirinae;
OC Alphaarterivirus; Alphaarterivirus equid.
OX NCBI_TaxID=299386;
OH NCBI_TaxID=9788; Equidae (horses).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1851863; DOI=10.1128/jvi.65.6.2910-2920.1991;
RA den Boon J.A., Snijder E.J., Chirnside E.D., de Vries A.A.F.,
RA Horzinek M.C., Spaan W.J.M.;
RT "Equine arteritis virus is not a togavirus but belongs to the
RT coronaviruslike superfamily.";
RL J. Virol. 65:2910-2920(1991).
RN [2]
RP SUBUNIT, AND MUTAGENESIS OF CYS-8.
RX PubMed=12477814; DOI=10.1128/jvi.77.1.97-104.2003;
RA Snijder E.J., Dobbe J.C., Spaan W.J.;
RT "Heterodimerization of the two major envelope proteins is essential for
RT arterivirus infectivity.";
RL J. Virol. 77:97-104(2003).
CC -!- FUNCTION: Major envelope protein.
CC -!- SUBUNIT: Heterodimer with glycoprotein 5; disulfide-linked. This
CC heterodimerization is required for transport to the Golgi complex.
CC {ECO:0000269|PubMed:12477814}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Host membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arteriviridae membrane protein family.
CC {ECO:0000305}.
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DR EMBL; X53459; CAA37545.1; -; Genomic_RNA.
DR PIR; G39925; MMWVEV.
DR RefSeq; NP_065660.1; NC_002532.2.
DR GeneID; 921340; -.
DR KEGG; vg:921340; -.
DR Proteomes; UP000000353; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR001332; Arteri_GP5.
DR Pfam; PF00951; Arteri_Gl; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Host membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..162
FT /note="Membrane protein"
FT /id="PRO_0000080874"
FT TOPO_DOM 1..10
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..40
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..67
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..162
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DISULFID 8
FT /note="Interchain (with C-34 in GP5)"
FT MUTAGEN 8
FT /note="C->S: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:12477814"
SQ SEQUENCE 162 AA; 17744 MW; F966782FA7AB35A1 CRC64;
MGAIDSFCGD GILGEYLDYF ILSVPLLLLL TRYVASGLVY VLTALFYSFV LAAYIWFVIV
GRAFSTAYAF VLLAAFLLLV MRMIVGMMPR LRSIFNHRQL VVADFVDTPS GPVPIPRSTT
QVVVRGNGYT AVGNKLVDGV KTITSAGRLF SKRTAATAYK LQ
