GLYC_HRSVB
ID GLYC_HRSVB Reviewed; 299 AA.
AC O36633;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 B (strain B1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=79692;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=B1;
RX PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA Sidhu M.S.;
RT "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT viral replication in vitro: clinical evaluation and molecular
RT characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
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. Interacts with host CX3CR1, the receptor for
CC the CX3C chemokine fractalkine, to modulate the immune response and
CC facilitate infection. Unlike the other paramyxovirus attachment
CC proteins, lacks both neuraminidase and hemagglutinating activities.
CC {ECO:0000250|UniProtKB:P03423}.
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:0000250|UniProtKB:P03423}.
CC -!- SUBUNIT: [Isoform Membrane-bound glycoprotein G]: Homooligomer.
CC Interacts (via N-terminus) with protein M. Part of a complex composed
CC of F1, F2 and G glycoproteins. Interacts with protein SH. Interacts
CC with host heparate sulfate; this interaction probably participates in
CC the viral attachment to the host cell. Interacts with host CX3CR1; this
CC interaction plays an important role in viral entry. Interacts with the
CC host lectins CD209/DC-SIGN and CD209L/L-SIGN on dendritic cells; these
CC interactions stimulate the phosphorylation of MAPK3/ERK1 and
CC MAPK1/ERK2, which inhibits dendritic cell activation and could
CC participate in the limited immunity against RSV reinfection.
CC {ECO:0000250|UniProtKB:P03423}.
CC -!- SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion
CC membrane {ECO:0000250|UniProtKB:P03423}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:P03423}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03423}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P03423}.
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. The initiation at the
CC downstream methionine removes a portion of the transmembrane domain.
CC The remaining hydrophobic portion of the sG protein is essential for
CC translocating it into the lumen of the ER during translation and would
CC likely maintain its membrane association until a proteolytic event
CC releases the mature sG protein into the medium.
CC {ECO:0000250|UniProtKB:P20895}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Membrane-bound glycoprotein G;
CC IsoId=O36633-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=O36633-2; Sequence=VSP_036523;
CC -!- DOMAIN: [Isoform Membrane-bound glycoprotein G]: Contains a linear
CC heparin binding domain essential for virus attachment to the host.
CC {ECO:0000250|UniProtKB:P03423}.
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 May carry 30-40 separate O-linked carbohydrate chains distributed among
CC the 91 serine and threonine residues. {ECO:0000250|UniProtKB:P03423}.
CC -!- PTM: [Isoform Membrane-bound glycoprotein G]: Palmitoylated.
CC {ECO:0000250|UniProtKB:P03423}.
CC -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
CC {ECO:0000305}.
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DR EMBL; AF013254; AAB82435.1; -; Genomic_RNA.
DR RefSeq; NP_056862.1; NC_001781.1.
DR SMR; O36633; -.
DR PRIDE; O36633; -.
DR GeneID; 1489824; -.
DR KEGG; vg:1489824; -.
DR Proteomes; UP000002472; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; 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; Host cell membrane;
KW Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral immunoevasion; Virion;
KW Virus entry into host cell.
FT CHAIN 1..299
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000365795"
FT CHAIN 66..299
FT /note="Mature secreted glycoprotein G"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT /id="PRO_0000451324"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..66
FT /note="Helical"
FT TOPO_DOM 67..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 89..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..198
FT /note="Binding to host heparan sulfate"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT REGION 189..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 297..299
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 89..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 65..66
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 70
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 72
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 100
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 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 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 232
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 173..186
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT DISULFID 176..182
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform Secreted glycoprotein G)"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT /id="VSP_036523"
SQ SEQUENCE 299 AA; 32967 MW; 7532BF3B3CA05D6F CRC64;
MSKHKNQRTA RTLEKTWDTL NHLIVISSCL YRLNLKSIAQ IALSVLAMII STSLIIAAII
FIISANHKVT LTTVTVQTIK NHTEKNITTY LTQVPPERVS SSKQPTTTSP IHTNSATTSP
NTKSETHHTT AQTKGRTTTS TQTNKPSTKP RLKNPPKKPK DDYHFEVFNF VPCSICGNNQ
LCKSICKTIP SNKPKKKPTI KPTNKPTTKT TNKRDPKTPA KTTKKETTTN PTKKPTLTTT
ERDTSTSQST VLDTTTLEHT IQQQSLHSTT PENTPNSTQT PTASEPSTSN STQNTQSHA
