ID   GP3_PRRSS               Reviewed;         265 AA.
AC   A0MD32;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   23-FEB-2022, entry version 28.
DE   RecName: Full=Glycoprotein 3;
DE            Short=Protein GP3;
GN   Name=GP3; ORFNames=3;
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).
CC   -!- FUNCTION: Minor envelope protein. {ECO:0000250}.
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: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}. Note=Only a small
CC       fraction of GP3 synthesized in infected cells ends up in virions. The
CC       transmembrane region probably functions as an uncleaved signal (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arteriviridae GP3 protein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ489311; ABF66344.1; -; Genomic_RNA.
DR   PRIDE; A0MD32; -.
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   InterPro; IPR002556; Arteri_GP3.
DR   Pfam; PF01606; Arteri_env; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW   Host membrane; Membrane; Secreted; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   CHAIN           1..265
FT                   /note="Glycoprotein 3"
FT                   /id="PRO_0000410891"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          241..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   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   265 AA;  30647 MW;  D155FE4599EAFD59 CRC64;
     MAHQCACFHF FLCGFICYLV HSALAANSSS TLCFWFPLAH GNTSFELTIN YTICMPCLTS
     QAARQRLEPG RNMWCRIGHD RCEERDHDEL LMSIPSGYDN LKLEGYYAWL AFLSFSYAAQ
     FHPELFGIGN VSRVFVDKRH QFICAEHGGL NSTLSTEHNI SALYAVYYHH QIDGGNWFHL
     EWLRPLFSSW LVLNISWFLR RSPVSPVSRR IYQILRPTRP RLPVSWSFRT SIVPGLTRPQ
     QRKVKFPPES RPNAVKPSVF PNTSR