ID   GP2A_PRRSS              Reviewed;         249 AA.
AC   A0MD30;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   23-FEB-2022, entry version 29.
DE   RecName: Full=Glycoprotein 2a;
DE            Short=Protein GP2a;
DE   AltName: Full=GP2;
DE   Flags: Precursor;
GN   Name=GP2a; ORFNames=2a;
OS   Porcine reproductive and respiratory syndrome virus (isolate Pig/United
OS   States/SD 01-08/2001) (PRRSV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Arnidovirineae; Arteriviridae; unclassified Arteriviridae.
OX   NCBI_TaxID=857306;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Infectious clone SD 01-08;
RX   PubMed=17037606; DOI=10.1007/978-0-387-33012-9_110;
RA   Fang Y., Faaberg K.S., Rowland R.R., Christopher-Hennings J.,
RA   Pattnaik A.K., Osorio F., Nelson E.A.;
RT   "Construction of a full-length cDNA infectious clone of a European-like
RT   Type 1 PRRSV isolated in the U.S.";
RL   Adv. Exp. Med. Biol. 581:605-608(2006).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH PIG CD163.
RC   STRAIN=FL-12;
RX   PubMed=19939927; DOI=10.1128/jvi.01774-09;
RA   Das P.B., Dinh P.X., Ansari I.H., de Lima M., Osorio F.A., Pattnaik A.K.;
RT   "The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and
RT   respiratory syndrome virus interact with the receptor CD163.";
RL   J. Virol. 84:1731-1740(2010).
CC   -!- FUNCTION: Minor envelope protein. Along with GP4, serves as the viral
CC       attachment protein responsible for mediating interactions with CD163
CC       thereby playing a role in virus entry into susceptible host cells.
CC       {ECO:0000269|PubMed:19939927}.
CC   -!- SUBUNIT: Heterotrimer of GP2a, GP3, and GP4 (By similarity). The GP2a-
CC       GP3-GP4 complex associates with the E protein (By similarity).
CC       Interacts with host CD163; this interaction plays a role in virus entry
CC       into host cell. {ECO:0000250, ECO:0000269|PubMed:19939927}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC       Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane
CC       protein {ECO:0000250}. Secreted {ECO:0000250}.
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DR   EMBL; DQ489311; ABF66342.1; -; Genomic_RNA.
DR   Proteomes; UP000000937; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR003434; Arteri_GP2a.
DR   Pfam; PF02340; PRRSV_Env; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW   Host membrane; Host-virus interaction; Membrane; Secreted; Signal;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..249
FT                   /note="Glycoprotein 2a"
FT                   /id="PRO_0000410890"
FT   TOPO_DOM        36..207
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..249
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   249 AA;  28561 MW;  2CC59FDFD5F2C389 CRC64;
     MQWGHCGVKS ASCSWMPSLS FLSVWLILSF SLPYCLGSPS QDGYWSFFSE WFAPRFSVRA
     LPFTLPNYRR SYESLLPNCR PDVPQFAFKH PLGILWHMRV SHLIDEMVSR RIYQTMEHSG
     QAAWKYVVGE ATLTKLSKLD IVTHFQHLAA VEADSCRFLS SRLVMLKNLA VGNVSLQYNT
     TLDRVELIFP TPGTRPKLTD FRQWLISVHA SIFSSVASSV TLFIVLWLRI PALRYVFGFH
     WPTATHHSS