GP3_EAVBU
ID GP3_EAVBU Reviewed; 163 AA.
AC P28993;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 29-SEP-2021, entry version 76.
DE RecName: Full=Glycoprotein 3;
DE Short=Protein GP3;
GN Name=GP3; ORFNames=3;
OS Equine arteritis virus (strain Bucyrus) (EAV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Equarterivirinae;
OC Alphaarterivirus; Alphaarterivirus equid.
OX NCBI_TaxID=299386;
OH NCBI_TaxID=9788; Equidae (horses).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1851863; DOI=10.1128/jvi.65.6.2910-2920.1991;
RA den Boon J.A., Snijder E.J., Chirnside E.D., de Vries A.A.F.,
RA Horzinek M.C., Spaan W.J.M.;
RT "Equine arteritis virus is not a togavirus but belongs to the
RT coronaviruslike superfamily.";
RL J. Virol. 65:2910-2920(1991).
RN [2]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12368326; DOI=10.1128/jvi.76.21.10829-10840.2002;
RA Wieringa R., de Vries A.A., Raamsman M.J., Rottier P.J.;
RT "Characterization of two new structural glycoproteins, GP(3) and GP(4), of
RT equine arteritis virus.";
RL J. Virol. 76:10829-10840(2002).
RN [3]
RP SUBUNIT.
RX PubMed=12743278; DOI=10.1128/jvi.77.11.6216-6226.2003;
RA Wieringa R., de Vries A.A., Rottier P.J.;
RT "Formation of disulfide-linked complexes between the three minor envelope
RT glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.";
RL J. Virol. 77:6216-6226(2003).
RN [4]
RP FUNCTION OF GP2B-GP3-GP4 HETEROTRIMER.
RX PubMed=18570963; DOI=10.1016/j.virol.2008.04.041;
RA Nitschke M., Korte T., Tielesch C., Ter-Avetisyan G., Tunnemann G.,
RA Cardoso M.C., Veit M., Herrmann A.;
RT "Equine arteritis virus is delivered to an acidic compartment of host cells
RT via clathrin-dependent endocytosis.";
RL Virology 377:248-254(2008).
RN [5]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-28 AND ASN-29, REGION, AND
RP MUTAGENESIS OF ASN-28; ASN-29 AND 137-LEU--SER-163.
RX PubMed=24142700; DOI=10.1074/jbc.m113.505420;
RA Matczuk A.K., Kunec D., Veit M.;
RT "Co-translational processing of glycoprotein 3 from equine arteritis virus:
RT N-glycosylation adjacent to the signal peptide prevents cleavage.";
RL J. Biol. Chem. 288:35396-35405(2013).
CC -!- FUNCTION: Minor envelope protein. Part of the glycoproteins
CC heterotrimer GP2b-GP3-GP4 which is probably responsible for the
CC attachment to target host cell. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis.
CC {ECO:0000269|PubMed:18570963}.
CC -!- SUBUNIT: Heterotrimer of GP2b, GP3, and GP4; disulfide-linked
CC (Probable). The GP2b-GP3-GP4 complex associates with the E protein (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane;
CC Peripheral membrane protein. Host Golgi apparatus membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Secreted
CC {ECO:0000250}. Note=Only a small fraction of GP3 synthesized in
CC infected cells ends up in virions. The signal sequence functions as an
CC uncleaved signal when glycosylated at Asn-28 and Asn-29. When the
CC protein is not glycosylated at these sites, the signal sequence is
CC cleaved (PubMed:24142700). {ECO:0000269|PubMed:24142700}.
CC -!- PTM: N-glycosylation for overlapping sequons occurs at both Asn-28 and
CC Asn-29, and blocks cleavage of the signal peptide between Gly-26 and
CC Ser-27. {ECO:0000269|PubMed:24142700}.
CC -!- SIMILARITY: Belongs to the arteriviridae GP3 protein family.
CC {ECO:0000305}.
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DR EMBL; X53459; CAA37542.1; -; Genomic_RNA.
DR PIR; D39925; D39925.
DR RefSeq; NP_065657.1; NC_002532.2.
DR SMR; P28993; -.
DR iPTMnet; P28993; -.
DR GeneID; 921346; -.
DR KEGG; vg:921346; -.
DR Proteomes; UP000000353; 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:0016020; C: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; IPR004310; EAV_Gp3.
DR Pfam; PF03076; GP3; 1.
PE 1: Evidence at protein level;
KW Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW Secreted; Signal; 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..26
FT /note="Not cleaved"
FT /evidence="ECO:0000255"
FT CHAIN 27..163
FT /note="Glycoprotein 3"
FT /id="PRO_0000080878"
FT REGION 142..158
FT /note="Important for peripheral membrane localization"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:24142700"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:24142700"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 28
FT /note="N->H: Not glycosylated, no cleavage of the signal
FT peptide. Not glycosylated, allows cleavage of the signal
FT peptide; when associated with H-29."
FT /evidence="ECO:0000269|PubMed:24142700"
FT MUTAGEN 28
FT /note="N->Q: Not glycosylated, no cleavage of the signal
FT peptide. Not glycosylated; allows cleavage of the signal
FT peptide; when associated with Q-29."
FT /evidence="ECO:0000269|PubMed:24142700"
FT MUTAGEN 29
FT /note="N->H: Not glycosylated, no cleavage of the signal
FT peptide. Not glycosylated; allows cleavage of the signal
FT peptide; when associated with H-28."
FT /evidence="ECO:0000269|PubMed:24142700"
FT MUTAGEN 29
FT /note="N->Q: Not glycosylated, no cleavage of the signal
FT peptide. Not glycosylated; allows cleavage of the signal
FT peptide; when associated with Q-28."
FT /evidence="ECO:0000269|PubMed:24142700"
FT MUTAGEN 137..163
FT /note="Missing: Allows secretion of the protein. No effect
FT in inhibition of signal peptide cleavage by adjacent
FT carbohydrates."
FT /evidence="ECO:0000269|PubMed:24142700"
SQ SEQUENCE 163 AA; 18054 MW; 8B472DACC39FB2E8 CRC64;
MGRAYSGPVA LLCFFLYFCF ICGSVGSNNT TICMHTTSDT SVHLFYAANV TFPSHFQRHF
AAAQDFVVHT GYEYAGVTML VHLFANLVLT FPSLVNCSRP VNVFANASCV QVVCSHTNST
TGLGQLSFSF VDEDLRLHIR PTLICWFALL LVHFLPMPRC RGS
