GLYC_HRSV5
ID GLYC_HRSV5 Reviewed; 298 AA.
AC P27024;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 rsb6190).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11255;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1895054; DOI=10.1099/0022-1317-72-9-2091;
RA Cane P.A., Matthews D.A., Pringle C.R.;
RT "Identification of variable domains of the attachment (G) protein of
RT subgroup A respiratory syncytial viruses.";
RL J. Gen. Virol. 72:2091-2096(1991).
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=P27024-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=P27024-2; Sequence=VSP_036529;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; JQ1207; JQ1207.
DR SMR; P27024; -.
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; Secreted; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW Virion; Virus entry into host cell.
FT CHAIN 1..298
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142861"
FT CHAIN 66..298
FT /note="Mature secreted glycoprotein G"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT /id="PRO_0000451330"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 132..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:0000250|UniProtKB:P03423"
FT REGION 192..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..211
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..298
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 80
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
FT CARBOHYD 87
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03423"
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 103
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
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 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 250
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 294
FT /note="N-linked (GlcNAc...) asparagine; 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_036529"
SQ SEQUENCE 298 AA; 32769 MW; 4D74E854D34D7BA5 CRC64;
MSKTKDQRTA KTLEKTWDTL NHLLFISSCL YKLNLKSIAQ ITLSILAMII STSLIIAAII
FIASANNKVT LTTAIIQDAT SQIKNTTPTY LTQNPQLGIS FFNLSGTTSQ TTAILALTTP
SVESILQSTT VKTKNTTTTQ IQPSKPTTKQ RQNKPPNKPN NDFHFEVFNF VPCSICSNNP
TCWAICKRIP SKKPGKKTTT KPTKKPTIKT TKKDHKPQTT KPKEAPSTKP TEKPTINITK
PNIRTTLLTN STTGNLEHTS QEETLHSTSS EGNTSPSQVY TTSEYLSQPT SPSNITNQ
