GP2B_EAVBU
ID GP2B_EAVBU Reviewed; 227 AA.
AC P28992;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 23-FEB-2022, entry version 78.
DE RecName: Full=Glycoprotein 2b;
DE Short=Protein GP2b;
DE AltName: Full=GP(S);
DE Flags: Precursor;
GN Name=GP2b; ORFNames=2b;
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 SUBUNIT, AND SUBCELLULAR LOCATION.
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 [3]
RP DISULFIDE BONDS.
RX PubMed=14645556; DOI=10.1128/jvi.77.24.12996-13004.2003;
RA Wieringa R., De Vries A.A., Post S.M., Rottier P.J.;
RT "Intra- and intermolecular disulfide bonds of the GP2b glycoprotein of
RT equine arteritis virus: relevance for virus assembly and infectivity.";
RL J. Virol. 77:12996-13004(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).
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|PubMed:12743278};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:12743278}. Host
CC endoplasmic reticulum membrane {ECO:0000305|PubMed:12743278}; Single-
CC pass type I membrane protein {ECO:0000305|PubMed:12743278}. Host Golgi
CC apparatus membrane {ECO:0000305|PubMed:12743278}; Single-pass type I
CC membrane protein {ECO:0000305|PubMed:12743278}. Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: Translated from a subgenomic RNA (sgRNA2).
CC -!- SIMILARITY: Belongs to the arteriviridae GP2b 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; X53459; CAA37541.1; -; Genomic_RNA.
DR PIR; C39925; C39925.
DR RefSeq; NP_065656.1; NC_002532.2.
DR GeneID; 921344; -.
DR KEGG; vg:921344; -.
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: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; IPR001913; Equi_arteri_GP2b.
DR Pfam; PF01309; EAV_GS; 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; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..227
FT /note="Glycoprotein 2b"
FT /id="PRO_0000080876"
FT TOPO_DOM 29..177
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..227
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 48..137
FT /evidence="ECO:0000305|PubMed:14645556"
FT DISULFID 102
FT /note="Interchain (with GP4)"
FT /evidence="ECO:0000305|PubMed:14645556"
SQ SEQUENCE 227 AA; 25579 MW; 6E60BEA76C06D0B3 CRC64;
MQRFSFSCYL HWLLLLCFFS GSLLPSAAAW WRGVHEVRVT DLFKDLQCDN LRAKDAFPSL
GYALSIGQSR LSYMLQDWLL AAHRKEVMPS NIMPMPGLTP DCFDHLESSS YAPFINAYRQ
AILSQYPQEL QLEAINCKLL AVVAPALYHN YHLANLTGPA TWVVPTVGQL HYYASSSIFA
SSVEVLAAII LLFACIPLVT RVYISFTRLM SPSRRTSSGT LPRRKIL
