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Major surface glycoprotein G (Attachment glycoprotein G) (Membrane-bound glycoprotein) (mG)

 GLYC_HRSVA              Reviewed;         298 AA.
P03423; Q77YB0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 89.
RecName: Full=Major surface glycoprotein G;
AltName: Full=Attachment glycoprotein G;
AltName: Full=Membrane-bound glycoprotein;
Short=mG;
Name=G;
Human respiratory syncytial virus A (strain A2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Pneumoviridae; Orthopneumovirus.
NCBI_TaxID=11259;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3858865; DOI=10.1073/pnas.82.12.4075;
Wertz G.W., Collins P.L., Huang Y., Gruber C., Levine S., Ball L.A.;
"Nucleotide sequence of the G protein gene of human respiratory
syncytial virus reveals an unusual type of viral membrane protein.";
Proc. Natl. Acad. Sci. U.S.A. 82:4075-4079(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=4069997; DOI=10.1093/nar/13.21.7795;
Satake M., Coligan J.E., Elango N., Norrby E., Venkatesan S.;
"Respiratory syncytial virus envelope glycoprotein (G) has a novel
structure.";
Nucleic Acids Res. 13:7795-7812(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=7747420; DOI=10.1006/viro.1995.1178;
Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
"A cold-passaged, attenuated strain of human respiratory syncytial
virus contains mutations in the F and L genes.";
Virology 208:478-484(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=9035372; DOI=10.1007/BF00366988;
Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L.,
Murphy B.R.;
"Acquisition of the ts phenotype by a chemically mutagenized cold-
passaged human respiratory syncytial virus vaccine candidate results
from the acquisition of a single mutation in the polymerase (L)
gene.";
Virus Genes 13:269-273(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=9557743;
Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
"Recombinant respiratory syncytial virus (RSV) bearing a set of
mutations from cold-passaged RSV is attenuated in chimpanzees.";
J. Virol. 72:4467-4471(1998).
[6]
OLIGOMERIZATION, AND PALMITOYLATION.
PubMed=1634876; DOI=10.1099/0022-1317-73-4-849;
Collins P.L., Mottet G.;
"Oligomerization and post-translational processing of glycoprotein G
of human respiratory syncytial virus: altered O-glycosylation in the
presence of brefeldin A.";
J. Gen. Virol. 73:849-863(1992).
[7]
ISOFORM SECRETED GLYCOPROTEIN G.
PubMed=8207828;
Roberts S.R., Lichtenstein D., Ball L.A., Wertz G.W.;
"The membrane-associated and secreted forms of the respiratory
syncytial virus attachment glycoprotein G are synthesized from
alternative initiation codons.";
J. Virol. 68:4538-4546(1994).
[8]
DISULFIDE BONDS.
PubMed=9194191; DOI=10.1002/pro.5560060619;
Gorman J.J., Ferguson B.L., Speelman D., Mills J.;
"Determination of the disulfide bond arrangement of human respiratory
syncytial virus attachment (G) protein by matrix-assisted laser
desorption/ionization time-of-flight mass spectrometry.";
Protein Sci. 6:1308-1315(1997).
[9]
HEPARIN-BINDING DOMAIN.
PubMed=10400758;
Feldman S.A., Hendry R.M., Beeler J.A.;
"Identification of a linear heparin binding domain for human
respiratory syncytial virus attachment glycoprotein G.";
J. Virol. 73:6610-6617(1999).
[10]
FUNCTION.
PubMed=10864656; DOI=10.1128/JVI.74.14.6442-6447.2000;
Feldman S.A., Audet S., Beeler J.A.;
"The fusion glycoprotein of human respiratory syncytial virus
facilitates virus attachment and infectivity via an interaction with
cellular heparan sulfate.";
J. Virol. 74:6442-6447(2000).
[11]
INTERACTION WITH HOST CX3CR1.
PubMed=11477410; DOI=10.1038/90675;
Tripp R.A., Jones L.P., Haynes L.M., Zheng H., Murphy P.M.,
Anderson L.J.;
"CX3C chemokine mimicry by respiratory syncytial virus G
glycoprotein.";
Nat. Immunol. 2:732-738(2001).
[12]
INTERACTION WITH SH.
PubMed=15659757; DOI=10.1099/vir.0.80563-0;
Rixon H.W., Brown G., Murray J.T., Sugrue R.J.;
"The respiratory syncytial virus small hydrophobic protein is
phosphorylated via a mitogen-activated protein kinase p38-dependent
tyrosine kinase activity during virus infection.";
J. Gen. Virol. 86:375-384(2005).
[13]
MUTAGENESIS OF SER-2; LYS-3; ASN-4; LYS-5; ASP-6 AND GLN-7,
INTERACTION WITH M PROTEIN, AND SUBCELLULAR LOCATION.
PubMed=15958665; DOI=10.1099/vir.0.80829-0;
Ghildyal R., Li D., Peroulis I., Shields B., Bardin P.G., Teng M.N.,
Collins P.L., Meanger J., Mills J.;
"Interaction between the respiratory syncytial virus G glycoprotein
cytoplasmic domain and the matrix protein.";
J. Gen. Virol. 86:1879-1884(2005).
[14]
INTERACTION WITH F.
PubMed=18036342; DOI=10.1016/j.bbrc.2007.11.042;
Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.;
"The RSV F and G glycoproteins interact to form a complex on the
surface of infected cells.";
Biochem. Biophys. Res. Commun. 366:308-313(2008).
[15]
FUNCTION.
PubMed=18842713; DOI=10.1128/JVI.01604-08;
Bukreyev A., Yang L., Fricke J., Cheng L., Ward J.M., Murphy B.R.,
Collins P.L.;
"The secreted form of respiratory syncytial virus G glycoprotein helps
the virus evade antibody-mediated restriction of replication by acting
as an antigen decoy and through effects on fc receptor-bearing
leukocytes.";
J. Virol. 82:12191-12204(2008).
-!- FUNCTION: Attaches the virion to the host cell membrane by
interacting with heparan sulfate, initiating the infection.
Interacts with host CX3CR1, the receptor for the CX3C chemokine
fractalkine, to modulate the immune response and facilitate
infection. Unlike the other paramyxovirus attachment proteins,
lacks both neuraminidase and hemagglutinating activities.
-!- FUNCTION: Secreted glycoprotein G helps RSV escape antibody-
dependent restriction of replication by acting as an antigen decoy
and by modulating the activity of leukocytes bearing Fcgamma
receptors.
-!- SUBUNIT: Homooligomer. Interacts (via N-terminus) with protein M.
Interacts with protein F; this interaction occurs on the surface
of infected cells. Interacts with protein SH. Interacts with host
CX3CR1; this interaction modulates host immune response.
{ECO:0000269|PubMed:11477410, ECO:0000269|PubMed:15659757,
ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:18036342}.
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000269|PubMed:15958665}. Host cell surface
{ECO:0000269|PubMed:15958665}.
-!- SUBCELLULAR LOCATION: Isoform Secreted glycoprotein G: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Membrane-bound glycoprotein G;
IsoId=P03423-1; Sequence=Displayed;
Name=Secreted glycoprotein G;
IsoId=P03423-2; Sequence=VSP_036039;
-!- DOMAIN: Contains a linear heparin binding domain essential for
virus attachment to the host.
-!- PTM: May carry 40-80 separate O-linked carbohydrate chains
distributed among the 91 serine and threonine residues.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:1634876}.
-!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M11486; AAB59857.1; -; Genomic_RNA.
EMBL; X03149; CAA26928.1; -; mRNA.
EMBL; U50362; AAB86663.1; -; Genomic_RNA.
EMBL; U50363; AAB86675.1; -; Genomic_RNA.
EMBL; U63644; AAC55969.1; -; Genomic_RNA.
EMBL; AF035006; AAC14901.1; -; Genomic_RNA.
PIR; A94048; MGNZ.
ProteinModelPortal; P03423; -.
SMR; P03423; -.
OrthoDB; VOG090001SX; -.
Proteomes; UP000007678; Genome.
Proteomes; UP000134464; Genome.
Proteomes; UP000181145; Genome.
Proteomes; UP000181262; Genome.
Proteomes; UP000181559; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR000925; G_prot.
Pfam; PF00802; Glycoprotein_G; 1.
1: Evidence at protein level;
Alternative initiation; Complete proteome; Disulfide bond;
Glycoprotein; Host-virus interaction; Membrane; Secreted;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral immunoevasion; Virion; Virus entry into host cell.
CHAIN 1 298 Major surface glycoprotein G.
/FTId=PRO_0000142855.
TOPO_DOM 1 37 Intravirion. {ECO:0000255}.
TRANSMEM 38 66 Helical.
TOPO_DOM 67 298 Virion surface. {ECO:0000255}.
REGION 184 198 Heparin-binding domain.
CARBOHYD 100 100 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 105 105 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 113 113 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 117 117 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 119 119 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 137 137 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 138 138 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 139 139 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 141 141 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 144 144 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 147 147 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 199 199 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 203 203 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 219 219 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 231 231 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 235 235 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 253 253 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 269 269 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 270 270 O-linked (GlcNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 275 275 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 282 282 O-linked (GalNAc...) threonine; by host.
{ECO:0000255}.
CARBOHYD 283 283 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 287 287 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
CARBOHYD 290 290 O-linked (GalNAc...) serine; by host.
{ECO:0000255}.
DISULFID 173 186 {ECO:0000269|PubMed:9194191}.
DISULFID 176 182 {ECO:0000269|PubMed:9194191}.
VAR_SEQ 1 47 Missing (in isoform Secreted glycoprotein
G). {ECO:0000305}.
/FTId=VSP_036039.
MUTAGEN 2 2 S->A: Complete loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
MUTAGEN 3 3 K->A: Partial loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
MUTAGEN 4 4 N->A: Partial loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
MUTAGEN 5 5 K->A: Partial loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
MUTAGEN 6 6 D->A: Complete loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
MUTAGEN 7 7 Q->AQ: Partial loss of interaction with
protein M. {ECO:0000269|PubMed:15958665}.
SEQUENCE 298 AA; 32586 MW; 993C3D2DD68BC634 CRC64;
MSKNKDQRTA KTLERTWDTL NHLLFISSCL YKLNLKSVAQ ITLSILAMII STSLIIAAII
FIASANHKVT PTTAIIQDAT SQIKNTTPTY LTQNPQLGIS PSNPSEITSQ ITTILASTTP
GVKSTLQSTT VKTKNTTTTQ TQPSKPTTKQ RQNKPPSKPN NDFHFEVFNF VPCSICSNNP
TCWAICKRIP NKKPGKKTTT KPTKKPTLKT TKKDPKPQTT KSKEVPTTKP TEEPTINTTK
TNIITTLLTS NTTGNPELTS QMETFHSTSS EGNPSPSQVS TTSEYPSQPS SPPNTPRQ


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