ID GLYC_ORSVW Reviewed; 263 AA.
AC Q86695;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Major surface glycoprotein G;
DE AltName: Full=Attachment glycoprotein G;
GN Name=G;
OS Ovine respiratory syncytial virus (strain WSU 83-1578) (ORSV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae;
OC Ovine respiratory syncytial virus.
OX NCBI_TaxID=79699;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8277288; DOI=10.1099/0022-1317-74-12-2787;
RA Mallipeddi S.K., Samal S.K.;
RT "Analysis of the ovine respiratory syncytial virus (RSV) G glycoprotein
RT gene defines a subgroup of ungulate RSV.";
RL J. Gen. Virol. 74:2787-2791(1993).
CC -!- FUNCTION: Attaches the virion to the host cell membrane by interacting
CC with heparan sulfate, initiating the infection. Interacts with host
CC CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate
CC the immune response and facilitate infection. Unlike the other
CC paramyxovirus attachment proteins, lacks both neuraminidase and
CC hemagglutinating activities (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Secreted glycoprotein G helps RSV escape antibody-dependent
CC restriction of replication by acting as an antigen decoy and by
CC modulating the activity of leukocytes bearing Fcgamma receptors.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminus) with protein M.
CC Interacts with protein F; this interaction occurs on the surface of
CC infected cells. Interacts with protein SH. Interacts with host CX3CR1;
CC this interaction modulates host immune response (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane. Host cell surface {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted glycoprotein G]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Membrane-bound glycoprotein G;
CC IsoId=Q86695-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=Q86695-2; Sequence=VSP_036521;
CC -!- DOMAIN: Contains a linear heparin binding domain essential for virus
CC attachment to the host.
CC -!- PTM: May carry a lot of separate O-linked carbohydrate chains
CC distributed among serine and threonine residues. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
CC {ECO:0000305}.
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DR EMBL; AH004456; AAB29551.1; -; Genomic_RNA.
DR PIR; JQ2388; JQ2388.
DR GlyCosmos; Q86695; 4 sites, No reported glycans.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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 GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW.
DR InterPro; IPR000925; G_prot.
DR Pfam; PF00802; Glycoprotein_G; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Secreted; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW Virion; Virus entry into host cell.
FT CHAIN 1..263
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142853"
FT TOPO_DOM 1..37
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..263
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 173..186
FT /evidence="ECO:0000250"
FT DISULFID 176..182
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform Secreted glycoprotein G)"
FT /evidence="ECO:0000305"
FT /id="VSP_036521"
SQ SEQUENCE 263 AA; 29226 MW; 81A649C6047B3B71 CRC64;
MSNHTHHFEF KTLKKAWKAS KYFIVGLSCL YKLNLKSLVQ MALSALAMIT LVSLTITAII
YISTGNTKAK PMPTPTIQIT QQFQNHTSLP PTEHNHNSTH SPTQGTTSPH TFAVDVTEGT
RYYHLTLKTQ GGKTKGPPTP HATRKPPISS QKSNPSEIQQ DYSDFQILPY VPCNICEGDS
ACLSLCQDRS ESILDKALTT TPKKTPKPMT TKKPTKTSTH HRTSLRNKLY IKTNMTTPPH
GLISTAKHNK NQSTVQNPRH TLA
//
