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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
 
 
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