ID   GP5_PRRSS               Reviewed;         201 AA.
AC   A0MD34;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   02-DEC-2020, entry version 28.
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 (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 GLYCOPROTEIN 4.
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: 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:19939927}.
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 host SIGLEC1; this interaction plays a role
CC       in virus entry into host cell (By similarity). Interacts with
CC       glycoprotein 4. {ECO:0000250, ECO:0000269|PubMed:19939927}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the arteriviridae GP5 protein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ489311; ABF66346.1; -; Genomic_RNA.
DR   PRIDE; A0MD34; -.
DR   Proteomes; UP000000937; 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   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Glycoprotein; Host-virus interaction; Membrane; Signal; Transmembrane;
KW   Transmembrane helix; 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_0000410887"
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        37
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
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"
SQ   SEQUENCE   201 AA;  22258 MW;  F1A9A4E671B95545 CRC64;
     MKCSHKLGHS LTPHSCFWWL FLLCTGLSWS FADGNGNNST YQYIYNLTIC ELNGTNWLSG
     HFEWAVETFV LYPVVTHILS LGFLTTSHFF DALGLGAVST AGFVGGRYVL SSVYGACAFA
     AFVCFVIRAA KNCMACRYAR TRFTNFIVDD RGGVHRWKSP IVVEKLGKAE IGGNLVTIKH
     VVLEGVKAQP LTRTSAEQWE A