M_PRRSL
ID M_PRRSL Reviewed; 173 AA.
AC Q04565;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Membrane protein;
DE Short=Protein M;
GN Name=M; ORFNames=6;
OS Porcine reproductive and respiratory syndrome virus (strain Lelystad)
OS (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Betaarterivirus; Eurpobartevirus; Betaarterivirus suid 1.
OX NCBI_TaxID=11049;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8517032; DOI=10.1006/viro.1993.1008;
RA Meulenberg J.J.M., Hulst M.M., de Meijer E.J., Moonen P.L.J.M.,
RA den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.M.;
RT "Lelystad virus, the causative agent of porcine epidemic abortion and
RT respiratory syndrome (PEARS), is related to LDV and EAV.";
RL Virology 192:62-72(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Boxmeer 10;
RX PubMed=8438574; DOI=10.1006/viro.1993.1129;
RA Conzelmann K.K., Visser N., van Woensel P., Thiel H.J.;
RT "Molecular characterization of porcine reproductive and respiratory
RT syndrome virus, a member of the arterivirus group.";
RL Virology 193:329-339(1993).
CC -!- FUNCTION: Major envelope protein.
CC -!- SUBUNIT: Heterodimer with the membrane protein; disulfide-linked. This
CC heterodimerization is required for transport to the Golgi complex (By
CC similarity). {ECO:0000250}.
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; M96262; AAA46279.1; -; Genomic_RNA.
DR EMBL; L04493; AAA47106.1; -; Genomic_RNA.
DR PIR; A44281; A44281.
DR PIR; F45392; F45392.
DR Proteomes; UP000006687; 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 3: Inferred from homology;
KW Disulfide bond; Host membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..173
FT /note="Membrane protein"
FT /id="PRO_0000080875"
FT TOPO_DOM 1..11
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..39
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..69
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..173
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DISULFID 8
FT /note="Interchain (with C-24 in GP5)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 18925 MW; C132BB01B171441A CRC64;
MGGLDDFCND PIAAQKLVLA FSITYTPIMI YALKVSRGRL LGLLHILIFL NCSFTFGYMT
YVHFQSTNRV ALTLGAVVAL LWGVYSFTES WKFITSRCRL CCLGRRYILA PAHHVESAAG
LHSISASGNR AYAVRKPGLT SVNGTLVPGL RSLVLGGKRA VKRGVVNLVK YGR