E_EAVBU
ID E_EAVBU Reviewed; 67 AA.
AC Q91DM1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 61.
DE RecName: Full=Envelope small membrane protein;
DE Short=Protein E;
DE AltName: Full=Glycoprotein 2a;
DE Short=Protein GP2a;
GN Name=GP2a; ORFNames=2a;
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 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Snijder E.J.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone SD 01-08;
RX PubMed=17325365; DOI=10.1099/vir.0.82415-0;
RA Balasuriya U.B., Snijder E.J., Heidner H.W., Zhang J.,
RA Zevenhoven-Dobbe J.C., Boone J.D., McCollum W.H., Timoney P.J.,
RA MacLachlan N.J.;
RT "Development and characterization of an infectious cDNA clone of the
RT virulent Bucyrus strain of Equine arteritis virus.";
RL J. Gen. Virol. 88:918-924(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate F11, Isolate F12, Isolate F13, Isolate F14, Isolate F24,
RC Isolate F25, Isolate F26, Isolate F5, Isolate F6, Isolate F7, and
RC Isolate F8;
RX PubMed=17680321; DOI=10.1007/s00705-007-1040-z;
RA Zhang J., Miszczak F., Pronost S., Fortier C., Balasuriya U.B.,
RA Zientara S., Fortier G., Timoney P.J.;
RT "Genetic variation and phylogenetic analysis of 22 French isolates of
RT equine arteritis virus.";
RL Arch. Virol. 152:1977-1994(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=ARTAC vaccine, HK116, and HK25;
RX PubMed=18619638; DOI=10.1016/j.virol.2008.06.003;
RA Zhang J., Go Y.Y., MacLachlan N.J., Meade B.J., Timoney P.J.,
RA Balasuriya U.B.R.;
RT "Amino acid substitutions in the structural or nonstructural proteins of a
RT vaccine strain of equine arteritis virus are associated with its
RT attenuation.";
RL Virology 378:355-362(2008).
RN [6]
RP IDENTIFICATION.
RX PubMed=10400725; DOI=10.1128/jvi.73.8.6335-6345.1999;
RA Snijder E.J., van Tol H., Pedersen K.W., Raamsman M.J., de Vries A.A.;
RT "Identification of a novel structural protein of arteriviruses.";
RL J. Virol. 73:6335-6345(1999).
RN [7]
RP MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=19656967; DOI=10.1099/vir.0.011957-0;
RA Thaa B., Kabatek A., Zevenhoven-Dobbe J.C., Snijder E.J., Herrmann A.,
RA Veit M.;
RT "Myristoylation of the arterivirus E protein: the fatty acid modification
RT is not essential for membrane association but contributes significantly to
RT virus infectivity.";
RL J. Gen. Virol. 90:2704-2712(2009).
CC -!- FUNCTION: Minor envelope protein. May function as a viroporin in the
CC virion envelope that facilitates uncoating of the virus in order to
CC release the genomic RNA into the cytoplasm for subsequent replication
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer. Associates with itself into higher-order
CC structures, including dimers, trimers and tetramers. Associates with
CC the GP2b-GP3-GP4 complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
CC Golgi apparatus membrane {ECO:0000305}; Single-pass type I membrane
CC protein {ECO:0000305}. Secreted {ECO:0000250}.
CC -!- PTM: Myristoylated. {ECO:0000269|PubMed:19656967}.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the arteriviridae E protein family.
CC {ECO:0000305}.
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DR EMBL; DQ846750; ABI64072.1; -; Genomic_RNA.
DR EMBL; X53459; CAC42776.1; -; Genomic_RNA.
DR EMBL; EF492543; ABR92765.1; -; Genomic_RNA.
DR EMBL; EF492544; ABR92772.1; -; Genomic_RNA.
DR EMBL; EF492545; ABR92779.1; -; Genomic_RNA.
DR EMBL; EF492546; ABR92786.1; -; Genomic_RNA.
DR EMBL; EF492549; ABR92807.1; -; Genomic_RNA.
DR EMBL; EF492550; ABR92814.1; -; Genomic_RNA.
DR EMBL; EF492551; ABR92821.1; -; Genomic_RNA.
DR EMBL; EF492552; ABR92828.1; -; Genomic_RNA.
DR EMBL; EF492562; ABR92898.1; -; Genomic_RNA.
DR EMBL; EF492563; ABR92905.1; -; Genomic_RNA.
DR EMBL; EF492564; ABR92912.1; -; Genomic_RNA.
DR EMBL; EU586273; ACE82258.1; -; Genomic_RNA.
DR EMBL; EU586274; ACE82267.1; -; Genomic_RNA.
DR EMBL; EU586275; ACE82276.1; -; Genomic_RNA.
DR RefSeq; NP_127508.1; NC_002532.2.
DR SMR; Q91DM1; -.
DR TCDB; 1.A.116.1.6; the pore-forming porcine reproductive and respiratory syndrome virus viroporin (prrsv) family.
DR iPTMnet; Q91DM1; -.
DR GeneID; 921345; -.
DR KEGG; vg:921345; -.
DR Proteomes; UP000000353; Genome.
DR Proteomes; UP000138219; Genome.
DR Proteomes; UP000161084; Genome.
DR Proteomes; UP000169900; Genome.
DR Proteomes; UP000170187; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Ion channel; Ion transport; Lipoprotein; Membrane;
KW Myristate; Reference proteome; Secreted; Transmembrane;
KW Transmembrane helix; Transport; Viral envelope protein; Viral ion channel;
KW Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:19656967"
FT CHAIN 2..67
FT /note="Envelope small membrane protein"
FT /id="PRO_0000351499"
FT TOPO_DOM 2..27
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..67
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 2..15
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:19656967"
FT MUTAGEN 2
FT /note="G->A: Absence of myristoylation. Decreased
FT infectivity."
FT /evidence="ECO:0000269|PubMed:19656967"
SQ SEQUENCE 67 AA; 7371 MW; 3BB6732A4BAFA23F CRC64;
MGLVWSLISN SIQTIIADFA ISVIDAALFF LMLLALAVVT VFLFWLIVAI GRSLVARCSR
GARYRPV
