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VEMP_PEDV7
ID   VEMP_PEDV7              Reviewed;          76 AA.
AC   Q84706;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 95.
DE   RecName: Full=Envelope small membrane protein {ECO:0000255|HAMAP-Rule:MF_04205};
DE            Short=E protein {ECO:0000255|HAMAP-Rule:MF_04205};
DE            Short=sM protein {ECO:0000255|HAMAP-Rule:MF_04205};
GN   Name=E {ECO:0000255|HAMAP-Rule:MF_04205}; Synonyms=sM; ORFNames=4;
OS   Porcine epidemic diarrhea virus (strain CV777) (PEDV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Pedacovirus.
OX   NCBI_TaxID=229032;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8291230; DOI=10.1006/viro.1994.1058;
RA   Duarte M., Tobler K., Bridgen A., Rasschaert D., Ackermann M., Laude H.;
RT   "Sequence analysis of the porcine epidemic diarrhea virus genome between
RT   the nucleocapsid and spike protein genes reveals a polymorphic ORF.";
RL   Virology 198:466-476(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9782358; DOI=10.1007/978-1-4615-5331-1_101;
RA   Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
RT   "Further analysis of the genome of porcine epidemic diarrhea virus.";
RL   Adv. Exp. Med. Biol. 440:781-786(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11724265; DOI=10.1023/a:1011831902219;
RA   Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
RT   "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome
RT   sequence.";
RL   Virus Genes 23:137-144(2001).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST IRF3.
RX   PubMed=33486326; DOI=10.1016/j.vetmic.2021.108994;
RA   Zheng L., Wang X., Guo D., Cao J., Cheng L., Li X., Zou D., Zhang Y.,
RA   Xu J., Wu X., Shen Y., Wang H., Yu W., Li L., Xiao L., Song B., Ma J.,
RA   Liu X., Li P., Xu S., Xu X., Zhang H., Wu Z., Cao H.;
RT   "Porcine epidemic diarrhea virus E protein suppresses RIG-I signaling-
RT   mediated interferon-beta production.";
RL   Vet. Microbiol. 254:108994-108994(2021).
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 (By similarity). Counteracts the
CC       production of type I interferon by interacting with host IRF3 component
CC       and preventing its translocation to the host nucleus.
CC       {ECO:0000255|HAMAP-Rule:MF_04205}.
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 (By
CC       similarity). Interacts with host IRF3; this interaction inhibits type I
CC       IFN production (PubMed:33486326). {ECO:0000255|HAMAP-Rule:MF_04205,
CC       ECO:0000269|PubMed:33486326}.
CC   -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04205}; Single-pass type III membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04205}. Host endoplasmic reticulum
CC       {ECO:0000269|PubMed:33486326}. Note=The cytoplasmic tail functions as a
CC       Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04205}.
CC   -!- SIMILARITY: Belongs to the alphacoronaviruses E protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04205}.
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DR   EMBL; Z24733; CAA80856.1; -; Genomic_RNA.
DR   EMBL; AF353511; AAK38658.1; -; Genomic_RNA.
DR   PIR; C49591; C49591.
DR   RefSeq; NP_598312.1; NC_003436.1.
DR   GeneID; 935180; -.
DR   KEGG; vg:935180; -.
DR   Proteomes; UP000008159; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:CACAO.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IDA:CACAO.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0044662; P:disruption by virus of host cell membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:InterPro.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04205; ALPHA_CORONA_E; 1.
DR   InterPro; IPR043507; E_protein_aCoV.
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 endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Membrane; Transmembrane; Transmembrane helix; Viral immunoevasion.
FT   CHAIN           1..76
FT                   /note="Envelope small membrane protein"
FT                   /id="PRO_0000283980"
FT   TOPO_DOM        1..14
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04205"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04205"
FT   TOPO_DOM        36..76
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04205"
SQ   SEQUENCE   76 AA;  8810 MW;  41760B6B86A1E383 CRC64;
     MLQLVNDNGL VVNVILWLFV LFFLLIISIT FVQLVNLCFT CHRLCNSAVY TPIGRLYRVY
     KSYMRIDPLP STVIDV
 
 
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