GP5_PRRSL
ID GP5_PRRSL Reviewed; 201 AA.
AC Q04569;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 07-OCT-2020, entry version 76.
DE RecName: Full=Glycoprotein 5;
DE Short=Protein GP5;
DE AltName: Full=G(L);
DE Flags: Precursor;
GN Name=GP5; ORFNames=5;
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 CHARACTERIZATION.
RC STRAIN=FL-12;
RX PubMed=16571816; DOI=10.1128/jvi.80.8.3994-4004.2006;
RA Ansari I.H., Kwon B., Osorio F.A., Pattnaik A.K.;
RT "Influence of N-linked glycosylation of porcine reproductive and
RT respiratory syndrome virus GP5 on virus infectivity, antigenicity, and
RT ability to induce neutralizing antibodies.";
RL J. Virol. 80:3994-4004(2006).
RN [4]
RP FUNCTION.
RX PubMed=10073688; DOI=10.1099/0022-1317-80-2-297;
RA Nauwynck H.J., Duan X., Favoreel H.W., Van Oostveldt P., Pensaert M.B.;
RT "Entry of porcine reproductive and respiratory syndrome virus into porcine
RT alveolar macrophages via receptor-mediated endocytosis.";
RL J. Gen. Virol. 80:297-305(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH PIG SIGLEC1.
RX PubMed=17567703; DOI=10.1128/jvi.00569-07;
RA Delputte P.L., Van Breedam W., Delrue I., Oetke C., Crocker P.R.,
RA Nauwynck H.J.;
RT "Porcine arterivirus attachment to the macrophage-specific receptor
RT sialoadhesin is dependent on the sialic acid-binding activity of the N-
RT terminal immunoglobulin domain of sialoadhesin.";
RL J. Virol. 81:9546-9550(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17913250; DOI=10.1016/j.jviromet.2007.08.018;
RA Matanin B.M., Huang Y., Meng X.J., Zhang C.;
RT "Purification of the major envelop protein GP5 of porcine reproductive and
RT respiratory syndrome virus (PRRSV) from native virions.";
RL J. Virol. Methods 147:127-135(2008).
RN [7]
RP FUNCTION, AND INTERACTION WITH PIG SIGLEC1.
RX PubMed=20084110; DOI=10.1371/journal.ppat.1000730;
RA Van Breedam W., Van Gorp H., Zhang J.Q., Crocker P.R., Delputte P.L.,
RA Nauwynck H.J.;
RT "The M/GP(5) glycoprotein complex of porcine reproductive and respiratory
RT syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent
RT manner.";
RL PLoS Pathog. 6:E1000730-E1000730(2010).
RN [8]
RP INTERACTION WITH PIG B4GALT5.
RX PubMed=29546034; DOI=10.3389/fcimb.2018.00048;
RA Zhang L., Ren J., Shi P., Lu D., Zhao C., Su Y., Zhang L., Huang J.;
RT "The immunological regulation roles of porcine beta-1, 4
RT Galactosyltransferase V (B4GALT5) in PRRSV Infection.";
RL Front. Cell. Infect. Microbiol. 8:48-48(2018).
CC -!- FUNCTION: Major envelope protein present in abundant amounts in the
CC virion envelope. Mediates virion sialic acid-dependent attachment the
CC sialoadhesin receptor SIGLEC1. This attachment induces virion
CC internalization into alveolar macrophages predominantly through
CC clathrin-dependent endocytosis. {ECO:0000269|PubMed:10073688,
CC ECO:0000269|PubMed:17567703, ECO:0000269|PubMed:20084110}.
CC -!- SUBUNIT: Heterodimer with the membrane protein; disulfide-linked. This
CC heterodimerization is required for transport to the Golgi complex (By
CC similarity). Interacts with glycoprotein 4 (By similarity). Interacts
CC with host SIGLEC1; this interaction plays a role in virus entry into
CC host cell. Interacts with host B4GALT5 (PubMed:29546034). {ECO:0000250,
CC ECO:0000269|PubMed:17567703, ECO:0000269|PubMed:20084110,
CC ECO:0000269|PubMed:29546034}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:17913250}. Virion
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=GP5; Synonyms=Glycoprotein 5;
CC IsoId=Q04569-1; Sequence=Displayed;
CC Name=ORF5a; Synonyms=Protein ORF5a;
CC IsoId=P0DJZ4-1; Sequence=External;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arteriviridae GP5 protein family.
CC {ECO:0000305}.
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DR EMBL; M96262; AAA46278.1; -; Genomic_RNA.
DR EMBL; L04493; AAA47105.1; -; Genomic_RNA.
DR PIR; E45392; E45392.
DR PIR; F36861; F36861.
DR Proteomes; UP000006687; Genome.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR001332; Arteri_GP5.
DR Pfam; PF00951; Arteri_Gl; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Clathrin-mediated endocytosis of virus by host;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..201
FT /note="Glycoprotein 5"
FT /id="PRO_0000080883"
FT TOPO_DOM 33..63
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 24
FT /note="Interchain (with C-8 in membrane protein)"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="C -> P (in Ref. 2; AAA47105)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="A -> V (in Ref. 2; AAA47105)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="F -> L (in Ref. 2; AAA47105)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="K -> R (in Ref. 2; AAA47105)"
FT /evidence="ECO:0000305"
SQ 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
