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Glycoprotein 5 (Protein GP5) (G(L))

 GP5_PRRSL               Reviewed;         201 AA.
Q04569;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
10-MAY-2017, entry version 69.
RecName: Full=Glycoprotein 5;
Short=Protein GP5;
AltName: Full=G(L);
Flags: Precursor;
Name=GP5; ORFNames=5;
Porcine reproductive and respiratory syndrome virus (strain Lelystad)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=11049;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8517032; DOI=10.1006/viro.1993.1008;
Meulenberg J.J.M., Hulst M.M., de Meijer E.J., Moonen P.L.J.M.,
den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.M.;
"Lelystad virus, the causative agent of porcine epidemic abortion and
respiratory syndrome (PEARS), is related to LDV and EAV.";
Virology 192:62-72(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Boxmeer 10;
PubMed=8438574; DOI=10.1006/viro.1993.1129;
Conzelmann K.K., Visser N., van Woensel P., Thiel H.J.;
"Molecular characterization of porcine reproductive and respiratory
syndrome virus, a member of the arterivirus group.";
Virology 193:329-339(1993).
[3]
CHARACTERIZATION.
STRAIN=FL-12;
PubMed=16571816; DOI=10.1128/JVI.80.8.3994-4004.2006;
Ansari I.H., Kwon B., Osorio F.A., Pattnaik A.K.;
"Influence of N-linked glycosylation of porcine reproductive and
respiratory syndrome virus GP5 on virus infectivity, antigenicity, and
ability to induce neutralizing antibodies.";
J. Virol. 80:3994-4004(2006).
[4]
FUNCTION.
PubMed=10073688;
Nauwynck H.J., Duan X., Favoreel H.W., Van Oostveldt P.,
Pensaert M.B.;
"Entry of porcine reproductive and respiratory syndrome virus into
porcine alveolar macrophages via receptor-mediated endocytosis.";
J. Gen. Virol. 80:297-305(1999).
[5]
FUNCTION, AND INTERACTION WITH PIG SIGLEC1.
PubMed=17567703; DOI=10.1128/JVI.00569-07;
Delputte P.L., Van Breedam W., Delrue I., Oetke C., Crocker P.R.,
Nauwynck H.J.;
"Porcine arterivirus attachment to the macrophage-specific receptor
sialoadhesin is dependent on the sialic acid-binding activity of the
N-terminal immunoglobulin domain of sialoadhesin.";
J. Virol. 81:9546-9550(2007).
[6]
SUBCELLULAR LOCATION.
PubMed=17913250; DOI=10.1016/j.jviromet.2007.08.018;
Matanin B.M., Huang Y., Meng X.J., Zhang C.;
"Purification of the major envelop protein GP5 of porcine reproductive
and respiratory syndrome virus (PRRSV) from native virions.";
J. Virol. Methods 147:127-135(2008).
[7]
FUNCTION, AND INTERACTION WITH PIG SIGLEC1.
PubMed=20084110; DOI=10.1371/journal.ppat.1000730;
Van Breedam W., Van Gorp H., Zhang J.Q., Crocker P.R., Delputte P.L.,
Nauwynck H.J.;
"The M/GP(5) glycoprotein complex of porcine reproductive and
respiratory syndrome virus binds the sialoadhesin receptor in a sialic
acid-dependent manner.";
PLoS Pathog. 6:E1000730-E1000730(2010).
-!- FUNCTION: Major envelope protein present in abundant amounts in
the virion envelope. Mediates virion sialic acid-dependent
attachment the sialoadhesin receptor SIGLEC1. This attachment
induces virion internalization into alveolar macrophages
predominantly through clathrin-dependent endocytosis.
{ECO:0000269|PubMed:10073688, ECO:0000269|PubMed:17567703,
ECO:0000269|PubMed:20084110}.
-!- SUBUNIT: Heterodimer with the membrane protein; disulfide-linked.
This heterodimerization is required for transport to the Golgi
complex (By similarity). Interacts with glycoprotein 4 (By
similarity). Interacts with host SIGLEC1; this interaction plays a
role in virus entry into host cell. {ECO:0000250,
ECO:0000269|PubMed:17567703, ECO:0000269|PubMed:20084110}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:17913250}. Virion
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=GP5; Synonyms=Glycoprotein 5;
IsoId=Q04569-1; Sequence=Displayed;
Name=ORF5a; Synonyms=Protein ORF5a;
IsoId=P0DJZ4-1; Sequence=External;
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the arteriviridae GP5 protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M96262; AAA46278.1; -; Genomic_RNA.
EMBL; L04493; AAA47105.1; -; Genomic_RNA.
PIR; E45392; E45392.
PIR; F36861; F36861.
ProteinModelPortal; Q04569; -.
OrthoDB; VOG090002G2; -.
Proteomes; UP000006687; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR001332; Arteri_GP5.
Pfam; PF00951; Arteri_Gl; 1.
1: Evidence at protein level;
Alternative initiation;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Glycoprotein; Host-virus interaction; Membrane;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 201 Glycoprotein 5.
/FTId=PRO_0000080883.
TOPO_DOM 33 63 Virion surface. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
TRANSMEM 109 129 Helical. {ECO:0000255}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 24 24 Interchain (with C-8 in membrane
protein). {ECO:0000250}.
CONFLICT 24 24 C -> P (in Ref. 2; AAA47105).
{ECO:0000305}.
CONFLICT 97 97 A -> V (in Ref. 2; AAA47105).
{ECO:0000305}.
CONFLICT 103 103 F -> L (in Ref. 2; AAA47105).
{ECO:0000305}.
CONFLICT 158 158 K -> R (in Ref. 2; AAA47105).
{ECO:0000305}.
SEQUENCE 201 AA; 22429 MW; 85600B4F10A2F561 CRC64;
MRCSHKLGRF LTPHSCFWWL FLLCTGLSWS FADGNGDSST YQYIYNLTIC ELNGTDWLSS
HFGWAVETFV LYPVATHILS LGFLTTSHFF DALGLGAVST AGFVGGRYVL CSVYGACAFA
AFVCFVIRAA KNCMACRYAR TRFTNFIVDD RGRVHRWKSP IVVEKLGKAE VDGNLVTIKH
VVLEGVKAQP LTRTSAEQWE A


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