GLYC_BRSVC
ID GLYC_BRSVC Reviewed; 257 AA.
AC P22261;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Copenhagen) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11248;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2214024; DOI=10.1128/jvi.64.11.5559-5569.1990;
RA Lerch R.A., Anderson K., Wertz G.W.;
RT "Nucleotide sequence analysis and expression from recombinant vectors
RT demonstrate that the attachment protein G of bovine respiratory syncytial
RT virus is distinct from that of human respiratory syncytial virus.";
RL J. Virol. 64:5559-5569(1990).
RN [2]
RP STRUCTURE BY NMR OF 158-189.
RC STRAIN=391-2;
RX PubMed=8942628; DOI=10.1021/bi9621627;
RA Doreleijers J.F., Langedijk J.P.M., Haard K., Boelens R., Rullmann J.A.,
RA Schaaper W.M., van Oirschot J.T., Kaptein R.;
RT "Solution structure of the immunodominant region of protein G of bovine
RT respiratory syncytial virus.";
RL Biochemistry 35:14684-14688(1996).
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=P22261-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=P22261-2; Sequence=VSP_036516;
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}.
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 EMBL; M58307; AAA42810.1; -; mRNA.
DR PIR; A36408; MGNZBR.
DR PDB; 1BRV; NMR; -; A=158-189.
DR PDBsum; 1BRV; -.
DR BMRB; P22261; -.
DR SMR; P22261; -.
DR EvolutionaryTrace; P22261; -.
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 3D-structure; Alternative initiation; Disulfide bond; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Membrane;
KW Secreted; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral immunoevasion; Virion;
KW Virus entry into host cell.
FT CHAIN 1..257
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142848"
FT CHAIN 66..257
FT /note="Mature secreted glycoprotein G"
FT /id="PRO_0000451317"
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 71..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..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 197..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
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 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
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 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_036516"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1BRV"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:1BRV"
SQ SEQUENCE 257 AA; 28570 MW; 0B86D541FBA0657D CRC64;
MSNHTHHLKF KTLKRAWKAS KYFIVGLSCL YKFNLKSLVQ TALSTLAMIT LTSLVITAII
YISVGNAKAK PTSKPTIQQT QQPQNHTSPF FTEHNYKSTH TSIQSTTLSQ LLNIDTTRGI
TYGHSTNETQ NRKIKGQSTL PATRKPPINP SGSIPPENHQ DHNNFQTLPY VPCSTCEGNL
ACLSLCHIET ERAPSRAPTI TLKKTPKPKT TKKPTKTTIH HRTSPETKLQ PKNNTATPQQ
GILSSTEHHT NQSTTQI
