GLYC_HRSVA
ID GLYC_HRSVA Reviewed; 298 AA.
AC P03423; Q77YB0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Major surface glycoprotein G;
DE AltName: Full=Attachment glycoprotein G;
DE AltName: Full=Membrane-bound glycoprotein;
DE Short=mG;
DE Contains:
DE RecName: Full=Mature secreted glycoprotein G {ECO:0000250|UniProtKB:P20895};
DE Short=Mature sG {ECO:0000250|UniProtKB:P20895};
GN Name=G;
OS Human respiratory syncytial virus A (strain A2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11259;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND GLYCOSYLATION (MEMBRANE-BOUND
RP GLYCOPROTEIN G).
RX PubMed=3858865; DOI=10.1073/pnas.82.12.4075;
RA Wertz G.W., Collins P.L., Huang Y., Gruber C., Levine S., Ball L.A.;
RT "Nucleotide sequence of the G protein gene of human respiratory syncytial
RT virus reveals an unusual type of viral membrane protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4075-4079(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND GLYCOSYLATION (MEMBRANE-BOUND
RP GLYCOPROTEIN G).
RX PubMed=4069997; DOI=10.1093/nar/13.21.7795;
RA Satake M., Coligan J.E., Elango N., Norrby E., Venkatesan S.;
RT "Respiratory syncytial virus envelope glycoprotein (G) has a novel
RT structure.";
RL Nucleic Acids Res. 13:7795-7812(1985).
RN [3]
RP PROTEIN SEQUENCE OF 66-93, ALTERNATIVE INITIATION (ISOFORM SECRETED
RP GLYCOPROTEIN G), GLYCOSYLATION AT THR-70; THR-72; THR-80; THR-86; THR-87
RP AND THR-92, AND PROTEOLYTIC CLEAVAGE (ISOFORM SECRETED GLYCOPROTEIN G).
RX PubMed=8207828; DOI=10.1128/jvi.68.7.4538-4546.1994;
RA Roberts S.R., Lichtenstein D., Ball L.A., Wertz G.W.;
RT "The membrane-associated and secreted forms of the respiratory syncytial
RT virus attachment glycoprotein G are synthesized from alternative initiation
RT codons.";
RL J. Virol. 68:4538-4546(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=7747420; DOI=10.1006/viro.1995.1178;
RA Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
RT "A cold-passaged, attenuated strain of human respiratory syncytial virus
RT contains mutations in the F and L genes.";
RL Virology 208:478-484(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9035372; DOI=10.1007/bf00366988;
RA Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.;
RT "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged
RT human respiratory syncytial virus vaccine candidate results from the
RT acquisition of a single mutation in the polymerase (L) gene.";
RL Virus Genes 13:269-273(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9557743; DOI=10.1128/jvi.72.5.4467-4471.1998;
RA Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
RT "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations
RT from cold-passaged RSV is attenuated in chimpanzees.";
RL J. Virol. 72:4467-4471(1998).
RN [7]
RP FUNCTION (MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=3655746; DOI=10.1099/0022-1317-68-9-2521;
RA Levine S., Klaiber-Franco R., Paradiso P.R.;
RT "Demonstration that glycoprotein G is the attachment protein of respiratory
RT syncytial virus.";
RL J. Gen. Virol. 68:2521-2524(1987).
RN [8]
RP SUBCELLULAR LOCATION (MEMBRANE-BOUND GLYCOPROTEIN G), GLYCOSYLATION, AND
RP TOPOLOGY.
RX PubMed=2164608; DOI=10.1128/jvi.64.8.4007-4012.1990;
RA Collins P.L.;
RT "O glycosylation of glycoprotein G of human respiratory syncytial virus is
RT specified within the divergent ectodomain.";
RL J. Virol. 64:4007-4012(1990).
RN [9]
RP PALMITOYLATION, SUBUNIT (MEMBRANE-BOUND GLYCOPROTEIN G), AND GLYCOSYLATION
RP (MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=1634876; DOI=10.1099/0022-1317-73-4-849;
RA Collins P.L., Mottet G.;
RT "Oligomerization and post-translational processing of glycoprotein G of
RT human respiratory syncytial virus: altered O-glycosylation in the presence
RT of brefeldin A.";
RL J. Gen. Virol. 73:849-863(1992).
RN [10]
RP DISULFIDE BONDS.
RX PubMed=9194191; DOI=10.1002/pro.5560060619;
RA Gorman J.J., Ferguson B.L., Speelman D., Mills J.;
RT "Determination of the disulfide bond arrangement of human respiratory
RT syncytial virus attachment (G) protein by matrix-assisted laser
RT desorption/ionization time-of-flight mass spectrometry.";
RL Protein Sci. 6:1308-1315(1997).
RN [11]
RP DOMAIN (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G), FUNCTION (MEMBRANE-BOUND
RP GLYCOPROTEIN G), AND INTERACTION WITH HOST HEPARATE SULFATE (ISOFORM
RP MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=10400758; DOI=10.1128/jvi.73.8.6610-6617.1999;
RA Feldman S.A., Hendry R.M., Beeler J.A.;
RT "Identification of a linear heparin binding domain for human respiratory
RT syncytial virus attachment glycoprotein G.";
RL J. Virol. 73:6610-6617(1999).
RN [12]
RP FUNCTION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=10864656; DOI=10.1128/jvi.74.14.6442-6447.2000;
RA Feldman S.A., Audet S., Beeler J.A.;
RT "The fusion glycoprotein of human respiratory syncytial virus facilitates
RT virus attachment and infectivity via an interaction with cellular heparan
RT sulfate.";
RL J. Virol. 74:6442-6447(2000).
RN [13]
RP INTERACTION WITH HOST CX3CR1 (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G), AND
RP FUNCTION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=11477410; DOI=10.1038/90675;
RA Tripp R.A., Jones L.P., Haynes L.M., Zheng H., Murphy P.M., Anderson L.J.;
RT "CX3C chemokine mimicry by respiratory syncytial virus G glycoprotein.";
RL Nat. Immunol. 2:732-738(2001).
RN [14]
RP INTERACTION WITH SH (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=15659757; DOI=10.1099/vir.0.80563-0;
RA Rixon H.W., Brown G., Murray J.T., Sugrue R.J.;
RT "The respiratory syncytial virus small hydrophobic protein is
RT phosphorylated via a mitogen-activated protein kinase p38-dependent
RT tyrosine kinase activity during virus infection.";
RL J. Gen. Virol. 86:375-384(2005).
RN [15]
RP MUTAGENESIS OF SER-2; LYS-3; ASN-4; LYS-5; ASP-6 AND GLN-7, INTERACTION
RP WITH M PROTEIN (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G), AND SUBCELLULAR
RP LOCATION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=15958665; DOI=10.1099/vir.0.80829-0;
RA Ghildyal R., Li D., Peroulis I., Shields B., Bardin P.G., Teng M.N.,
RA Collins P.L., Meanger J., Mills J.;
RT "Interaction between the respiratory syncytial virus G glycoprotein
RT cytoplasmic domain and the matrix protein.";
RL J. Gen. Virol. 86:1879-1884(2005).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH F1; F2 AND G GLYCOPROTEIN (ISOFORM
RP MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=18036342; DOI=10.1016/j.bbrc.2007.11.042;
RA Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.;
RT "The RSV F and G glycoproteins interact to form a complex on the surface of
RT infected cells.";
RL Biochem. Biophys. Res. Commun. 366:308-313(2008).
RN [17]
RP FUNCTION (ISOFORM SECRETED GLYCOPROTEIN G).
RX PubMed=18842713; DOI=10.1128/jvi.01604-08;
RA Bukreyev A., Yang L., Fricke J., Cheng L., Ward J.M., Murphy B.R.,
RA Collins P.L.;
RT "The secreted form of respiratory syncytial virus G glycoprotein helps the
RT virus evade antibody-mediated restriction of replication by acting as an
RT antigen decoy and through effects on fc receptor-bearing leukocytes.";
RL J. Virol. 82:12191-12204(2008).
RN [18]
RP INTERACTION WITH HOST CD209 AND CD209L (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN
RP G).
RX PubMed=22090124; DOI=10.1128/jvi.06096-11;
RA Johnson T.R., McLellan J.S., Graham B.S.;
RT "Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-
RT SIGN to activate ERK1 and ERK2.";
RL J. Virol. 86:1339-1347(2012).
RN [19]
RP FUNCTION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G), AND INTERACTION WITH HOST
RP CX3CR1 (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=26658574; DOI=10.1371/journal.ppat.1005318;
RA Johnson S.M., McNally B.A., Ioannidis I., Flano E., Teng M.N., Oomens A.G.,
RA Walsh E.E., Peeples M.E.;
RT "Respiratory Syncytial Virus Uses CX3CR1 as a Receptor on Primary Human
RT Airway Epithelial Cultures.";
RL PLoS Pathog. 11:E1005318-E1005318(2015).
RN [20]
RP FUNCTION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=26107373; DOI=10.1371/journal.pone.0130517;
RA Jeong K.I., Piepenhagen P.A., Kishko M., DiNapoli J.M., Groppo R.P.,
RA Zhang L., Almond J., Kleanthous H., Delagrave S., Parrington M.;
RT "CX3CR1 Is Expressed in Differentiated Human Ciliated Airway Cells and Co-
RT Localizes with Respiratory Syncytial Virus on Cilia in a G Protein-
RT Dependent Manner.";
RL PLoS ONE 10:e0130517-e0130517(2015).
RN [21]
RP SUBCELLULAR LOCATION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=28939853; DOI=10.1038/s41467-017-00732-z;
RA Vanover D., Smith D.V., Blanchard E.L., Alonas E., Kirschman J.L.,
RA Lifland A.W., Zurla C., Santangelo P.J.;
RT "RSV glycoprotein and genomic RNA dynamics reveal filament assembly prior
RT to the plasma membrane.";
RL Nat. Commun. 8:667-667(2017).
RN [22] {ECO:0007744|PDB:5WN9, ECO:0007744|PDB:5WNA, ECO:0007744|PDB:5WNB}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 161-197.
RX PubMed=29523582; DOI=10.1126/sciimmunol.aar3534;
RA Fedechkin S.O., George N.L., Wolff J.T., Kauvar L.M., DuBois R.M.;
RT "Structures of respiratory syncytial virus G antigen bound to broadly
RT neutralizing antibodies.";
RL Sci. Immunol. 3:0-0(2018).
RN [23] {ECO:0007744|PDB:6UVO}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 157-197.
RX PubMed=31852779; DOI=10.1128/jvi.01879-19;
RA Fedechkin S.O., George N.L., Nunez Castrejon A.M., Dillen J.R.,
RA Kauvar L.M., DuBois R.M.;
RT "Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing
RT Epitopes.";
RL J. Virol. 94:0-0(2020).
CC -!- FUNCTION: [Isoform Membrane-bound glycoprotein G]: Attaches the virion
CC to the host cell membrane by interacting with heparan sulfate,
CC initiating the infection (PubMed:3655746, PubMed:10400758,
CC PubMed:10864656). Interacts with host CX3CR1, the receptor for the CX3C
CC chemokine fractalkine, to modulate the immune response and facilitate
CC infection (PubMed:26658574, PubMed:11477410, PubMed:26107373). Unlike
CC the other paramyxovirus attachment proteins, lacks both neuraminidase
CC and hemagglutinating activities (Probable).
CC {ECO:0000269|PubMed:10400758, ECO:0000269|PubMed:10864656,
CC ECO:0000269|PubMed:11477410, ECO:0000269|PubMed:26107373,
CC ECO:0000269|PubMed:26658574, ECO:0000269|PubMed:3655746, ECO:0000305}.
CC -!- FUNCTION: [Isoform Secreted glycoprotein G]: Helps the virus escape
CC antibody-dependent restriction of replication by acting as an antigen
CC decoy and by modulating the activity of leukocytes bearing Fc-gamma
CC receptors. {ECO:0000269|PubMed:18842713}.
CC -!- SUBUNIT: [Isoform Membrane-bound glycoprotein G]: Homooligomer
CC (PubMed:1634876). Interacts (via N-terminus) with protein M
CC (PubMed:15958665). Part of a complex composed of F1, F2 and G
CC glycoproteins (PubMed:18036342). Interacts with protein SH
CC (PubMed:15659757). Interacts with host heparate sulfate; this
CC interaction probably participates in the viral attachment to the host
CC cell (PubMed:10400758). Interacts with host CX3CR1; this interaction
CC plays an important role in viral entry (PubMed:11477410,
CC PubMed:26658574). Interacts with the host lectins CD209/DC-SIGN and
CC CD209L/L-SIGN on dendritic cells; these interactions stimulate the
CC phosphorylation of MAPK3/ERK1 and MAPK1/ERK2, which inhibits dendritic
CC cell activation and could participate in the limited immunity against
CC RSV reinfection (PubMed:22090124). {ECO:0000269|PubMed:10400758,
CC ECO:0000269|PubMed:11477410, ECO:0000269|PubMed:15659757,
CC ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:1634876,
CC ECO:0000269|PubMed:18036342, ECO:0000269|PubMed:22090124,
CC ECO:0000269|PubMed:26658574}.
CC -!- SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion
CC membrane {ECO:0000269|PubMed:15958665}; Single-pass type II membrane
CC protein {ECO:0000303|PubMed:2164608}. Host cell membrane
CC {ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:28939853}; Single-pass
CC type II membrane protein {ECO:0000303|PubMed:2164608}.
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted glycoprotein G]: Secreted
CC {ECO:0000250|UniProtKB:P20895}. Note=The protein is shed from infected
CC cells before the appearance of progeny virus (By similarity). The
CC initiation at the downstream methionine removes a portion of the
CC transmembrane domain. The remaining hydrophobic portion of the sG
CC protein is essential for translocating it into the lumen of the ER
CC during translation and would likely maintain its membrane association
CC until a proteolytic event releases the mature sG protein into the
CC medium (By similarity). {ECO:0000250|UniProtKB:P20895}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Membrane-bound glycoprotein G;
CC IsoId=P03423-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G; Synonyms=sG;
CC IsoId=P03423-2; Sequence=VSP_036039;
CC -!- DOMAIN: [Isoform Membrane-bound glycoprotein G]: Contains a linear
CC heparin binding domain essential for virus attachment to the host.
CC {ECO:0000269|PubMed:10400758}.
CC -!- PTM: [Isoform Secreted glycoprotein G]: Cleaved to give rise to the
CC mature sG protein which lacks the transmembrane domain.
CC {ECO:0000250|UniProtKB:P20895}.
CC -!- PTM: [Isoform Membrane-bound glycoprotein G]: N- and O-glycosylated
CC (PubMed:4069997). May carry 30-40 separate O-linked carbohydrate chains
CC distributed among the 91 serine and threonine residues (PubMed:1634876,
CC PubMed:3858865, PubMed:2164608). {ECO:0000269|PubMed:1634876,
CC ECO:0000269|PubMed:2164608, ECO:0000269|PubMed:3858865,
CC ECO:0000269|PubMed:4069997}.
CC -!- PTM: [Isoform Membrane-bound glycoprotein G]: Palmitoylated.
CC {ECO:0000269|PubMed:1634876}.
CC -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
CC {ECO:0000305}.
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DR EMBL; M11486; AAB59857.1; -; Genomic_RNA.
DR EMBL; X03149; CAA26928.1; -; mRNA.
DR EMBL; U50362; AAB86663.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86675.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55969.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14901.1; -; Genomic_RNA.
DR PIR; A94048; MGNZ.
DR PDB; 5WN9; X-ray; 1.55 A; A=168-196.
DR PDB; 5WNA; X-ray; 2.40 A; A/B=161-197.
DR PDB; 5WNB; X-ray; 2.40 A; A/B=162-172.
DR PDB; 6UVO; X-ray; 2.90 A; D=157-197.
DR PDB; 7T8W; X-ray; 3.10 A; D=157-197.
DR PDBsum; 5WN9; -.
DR PDBsum; 5WNA; -.
DR PDBsum; 5WNB; -.
DR PDBsum; 6UVO; -.
DR PDBsum; 7T8W; -.
DR SMR; P03423; -.
DR ABCD; P03423; 2 sequenced antibodies.
DR Proteomes; UP000007678; Genome.
DR Proteomes; UP000134464; Genome.
DR Proteomes; UP000181145; Genome.
DR Proteomes; UP000181262; Genome.
DR Proteomes; UP000181559; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000925; G_prot.
DR Pfam; PF00802; Glycoprotein_G; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix;
KW Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW Viral immunoevasion; Virion; Virus entry into host cell.
FT CHAIN 1..298
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142855"
FT CHAIN 66..298
FT /note="Mature secreted glycoprotein G"
FT /id="PRO_0000451323"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31852779"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..298
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31852779"
FT REGION 125..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..198
FT /note="Binding to host heparan sulfate"
FT /evidence="ECO:0000305|PubMed:10400758"
FT REGION 190..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 65..66
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:8207828"
FT CARBOHYD 70
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 72
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 80
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 87
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 92
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000305|PubMed:8207828"
FT CARBOHYD 100
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
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 CARBOHYD 253
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="O-linked (GlcNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 173..186
FT /evidence="ECO:0000269|PubMed:9194191"
FT DISULFID 176..182
FT /evidence="ECO:0000269|PubMed:9194191"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform Secreted glycoprotein G)"
FT /evidence="ECO:0000269|PubMed:8207828"
FT /id="VSP_036039"
FT MUTAGEN 2
FT /note="S->A: Complete loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT MUTAGEN 3
FT /note="K->A: Partial loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT MUTAGEN 4
FT /note="N->A: Partial loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT MUTAGEN 5
FT /note="K->A: Partial loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT MUTAGEN 6
FT /note="D->A: Complete loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT MUTAGEN 7
FT /note="Q->AQ: Partial loss of interaction with protein M."
FT /evidence="ECO:0000269|PubMed:15958665"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:5WNA"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5WN9"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5WNA"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:5WN9"
SQ 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
