GP4_PRRSL
ID GP4_PRRSL Reviewed; 183 AA.
AC Q04568;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 07-OCT-2020, entry version 74.
DE RecName: Full=Glycoprotein 4;
DE Short=Protein GP4;
DE Flags: Precursor;
GN Name=GP4; ORFNames=4;
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).
CC -!- FUNCTION: Minor envelope protein. Along with GP2a, serves as the viral
CC attachment protein responsible for mediating interactions with CD163
CC thereby playing a role in virus entry into susceptible host cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of GP2a, GP3, and GP4 (By similarity). The GP2a-
CC GP3-GP4 complex associates with the E protein (Probable). Interacts
CC with glycoprotein 5 (By similarity). Interacts with host CD163; this
CC interaction plays a role in virus entry into host cell (By similarity).
CC {ECO:0000250, ECO:0000305}.
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}. Note=Only a small fraction of GP4
CC synthesized in infected cells ends up in virions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arteriviridae GP4 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; AAA46277.1; -; Genomic_RNA.
DR EMBL; L04493; AAA47104.1; -; Genomic_RNA.
DR PIR; D45392; D45392.
DR PIR; E36861; E36861.
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:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR003412; Arteri_GP4.
DR Pfam; PF02497; Arteri_GP4; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..183
FT /note="Glycoprotein 4"
FT /id="PRO_0000080881"
FT TOPO_DOM 23..157
FT /note="Virion surface"
FT /evidence="ECO:0000250"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..183
FT /note="Intravirion"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="F -> L (in Ref. 2; AAA47104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 19990 MW; 54235DA84DA6AB5C CRC64;
MAAATLFFLA GAQHIMVSEA FACKPCFSTH LSDIETNTTA AAGFMVLQDI NCFRPHGVSA
AQEKISFGKS SQCREAVGTP QYITITANVT DESYLYNADL LMLSACLFYA SEMSEKGFKV
IFGNVSGVVS ACVNFTDYVA HVTQHTQQHH LVIDHIRLLH FLTPSAMRWA TTIACLFAIL
LAI
