ID   GP3_PRRSL               Reviewed;         265 AA.
AC   Q04567;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Glycoprotein 3;
DE            Short=Protein GP3;
GN   Name=GP3; ORFNames=3;
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.
CC   -!- SUBUNIT: Heterotrimer of GP2a, GP3, and GP4 (By similarity). The GP2a-
CC       GP3-GP4 complex associates with the E protein (Probable). {ECO:0000250,
CC       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 GP3
CC       synthesized in infected cells ends up in virions. The transmembrane
CC       region probably functions as an uncleaved signal (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arteriviridae GP3 protein family.
CC       {ECO:0000305}.
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DR   EMBL; M96262; AAA46276.1; -; Genomic_RNA.
DR   EMBL; L04493; AAA47103.1; -; Genomic_RNA.
DR   PIR; C45392; C45392.
DR   PIR; D36861; D36861.
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   InterPro; IPR002556; Arteri_GP3.
DR   Pfam; PF01606; Arteri_env; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW   Host membrane; Membrane; Reference proteome; Secreted; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..265
FT                   /note="Glycoprotein 3"
FT                   /id="PRO_0000080879"
FT   TRANSMEM        8..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          239..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        3..5
FT                   /note="HQC -> RQR (in Ref. 2; AAA47103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="H -> P (in Ref. 2; AAA47103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  30583 MW;  B35A13D7EEB5D51C CRC64;
     MAHQCARFHF FLCGFICYLV HSALASNSSS TLCFWFPLAH GNTSFELTIN YTICMPCSTS
     QAARQRLEPG RNMWCKIGHD RCEERDHDEL LMSIPSGYDN LKLEGYYAWL AFLSFSYAAQ
     FHPELFGIGN VSRVFVDKRH QFICAEHDGH NSTVSTGHNI SALYAAYYHH QIDGGNWFHL
     EWLRPLFSSW LVLNISWFLR RSPVSPVSRR IYQILRPTRP RLPVSWSFRT SIVSDLTGSQ
     QRKRKFPSES RPNVVKPSVL PSTSR