GLYC_HRSV1
ID GLYC_HRSV1 Reviewed; 292 AA.
AC P20896;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 18537).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11251;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2441388; DOI=10.1073/pnas.84.16.5625;
RA Johnson P.R., Spriggs M.K., Olmsted R.A., Collins P.L.;
RT "The G glycoprotein of human respiratory syncytial viruses of subgroups A
RT and B: extensive sequence divergence between antigenically related
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5625-5629(1987).
RN [2]
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).
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=P20896-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=P20896-2; Sequence=VSP_036525;
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; M17213; AAA47412.1; -; Genomic_RNA.
DR PIR; B32703; MGNZ18.
DR SMR; P20896; -.
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 1: Evidence at protein level;
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..292
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142857"
FT CHAIN 66..292
FT /note="Mature secreted glycoprotein G"
FT /id="PRO_0000451326"
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..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 92..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:0000269|PubMed:10400758"
FT REGION 189..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..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 241..292
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="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
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 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 271
FT /note="O-linked (GlcNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
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_036525"
SQ SEQUENCE 292 AA; 32306 MW; BC8C59F69CA7AFC2 CRC64;
MSKHKNQRTA RTLEKTWDTL NHLIVISSCL YRLNLKSIAQ IALSVLAMII STSLIIAAII
FIISANHKVT LTTVTVQTIK NHTEKNISTY LTQVPPERVN SSKQPTTTSP IHTNSATISP
NTKSETHHTT AQTKGRITTS TQTNKPSTKS RSKNPPKKPK DDYHFEVFNF VPCSICGNNQ
LCKSICKTIP SNKPKKKPTI KPTNKPTTKT TNKRDPKTPA KMPKKEIITN PAKKPTLKTT
ERDTSISQST VLDTITPKYT IQQQSLHSTT SENTPSSTQI PTASEPSTLN PN
