GLYC_BRSVL
ID GLYC_BRSVL Reviewed; 257 AA.
AC O09495;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, 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 Bovine respiratory syncytial virus (strain Lelystad) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=82823;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9018058; DOI=10.1099/0022-1317-78-2-359;
RA Prozzi D., Walravens K., Langedijk J.P., Daus F., Kramps J.A.,
RA Letesson J.J.;
RT "Antigenic and molecular analyses of the variability of bovine respiratory
RT syncytial virus G glycoprotein.";
RL J. Gen. Virol. 78:359-366(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. 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. {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=O09495-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=O09495-2; Sequence=VSP_036517;
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 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; U33539; AAB50935.1; -; mRNA.
DR SMR; O09495; -.
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 2: Evidence at transcript 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..257
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142849"
FT CHAIN 66..257
FT /note="Mature secreted glycoprotein G"
FT /id="PRO_0000451318"
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..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..166
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 204..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..257
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 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 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
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 105
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
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...) 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_036517"
SQ SEQUENCE 257 AA; 28354 MW; E8DF5710FB21ACDA CRC64;
MSNHTHHLKL KTLKRAWKAS KYFIVGLSCL YKFNLKSLVQ TALTTLAMIT LTSLVITAII
YISVGNAKAK PTSKPTIQQT QRPQNHTSPL FTEHNYKSTH TSIQSTTLSQ LLNIDTTRGT
TYSHPTDETQ NRKIKSQSTL PATRQPPINP SGSNPPENHQ DHNNSQTLPY VPCSTCEGNL
ACSSLCQIGL ERAPSRAPTI TLKKAPKPKT TKKPTKTTIH HRTSPEAKLQ PKNNTAAPQQ
GILSSPEHHT NQSTTQI
