E_PRRSL
ID E_PRRSL Reviewed; 70 AA.
AC P0C6Y6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 07-OCT-2020, entry version 40.
DE RecName: Full=Envelope small membrane protein;
DE Short=Protein E;
DE AltName: Full=Glycoprotein 2b;
DE Short=Protein GP2b;
DE AltName: Full=Gs;
GN Name=GP2b; ORFNames=2b;
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).
RN [3]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16160177; DOI=10.1128/jvi.79.19.12495-12506.2005;
RA Wissink E.H., Kroese M.V., van Wijk H.A., Rijsewijk F.A., Meulenberg J.J.,
RA Rottier P.J.;
RT "Envelope protein requirements for the assembly of infectious virions of
RT porcine reproductive and respiratory syndrome virus.";
RL J. Virol. 79:12495-12506(2005).
RN [4]
RP CHARACTERIZATION, AND FUNCTION.
RC STRAIN=PA8;
RX PubMed=16904148; DOI=10.1016/j.virol.2006.07.013;
RA Lee C., Yoo D.;
RT "The small envelope protein of porcine reproductive and respiratory
RT syndrome virus possesses ion channel protein-like properties.";
RL Virology 355:30-43(2006).
RN [5]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=19951726; DOI=10.1016/j.virusres.2009.11.016;
RA Du Y., Zuckermann F.A., Yoo D.;
RT "Myristoylation of the small envelope protein of porcine reproductive and
RT respiratory syndrome virus is non-essential for virus infectivity but
RT promotes its growth.";
RL Virus Res. 147:294-299(2010).
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 {ECO:0000269|PubMed:16904148}.
CC -!- SUBUNIT: Homooligomer. Associates with itself into higher-order
CC structures, including dimers, trimers and tetramers. Associates with
CC the GP2a-GP3-GP4 complex (Probable). {ECO:0000305|PubMed:16160177}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:16160177};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16160177}. Host
CC endoplasmic reticulum membrane {ECO:0000269|PubMed:16160177}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16160177}. Host Golgi
CC apparatus membrane {ECO:0000269|PubMed:16160177}; Single-pass type I
CC membrane protein {ECO:0000269|PubMed:16160177}. Secreted
CC {ECO:0000269|PubMed:16160177}.
CC -!- PTM: Myristoylated. {ECO:0000269|PubMed:19951726}.
CC -!- PTM: Not glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arteriviridae E protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M96262; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR TCDB; 1.A.116.1.1; the pore-forming porcine reproductive and respiratory syndrome virus viroporin (prrsv) family.
DR iPTMnet; P0C6Y6; -.
DR Proteomes; UP000006687; 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.
DR InterPro; IPR009775; GP2b.
DR Pfam; PF07069; PRRSV_2b; 1.
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:19951726"
FT CHAIN 2..70
FT /note="Envelope small membrane protein"
FT /id="PRO_0000351500"
FT TOPO_DOM 2..25
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..70
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:19951726"
SQ SEQUENCE 70 AA; 7743 MW; 02090C6445777C53 CRC64;
MGSLWSKISQ LFVDAFTEFL VSVVDIAIFL AILFGFTVAG WLLVFLLRVV CSALLRSRSA
IHSPELSKVL
