GLYC_BRSVA
ID GLYC_BRSVA Reviewed; 263 AA.
AC P62648; Q77KZ8; Q8V689;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 A51908) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11247;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8376974; DOI=10.1099/0022-1317-74-9-2001;
RA Mallipeddi S.K., Samal S.K.;
RT "Sequence variability of the glycoprotein gene of bovine respiratory
RT syncytial virus.";
RL J. Gen. Virol. 74:2001-2004(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A51908, and ATCC 51908;
RX PubMed=11724268; DOI=10.1023/a:1011888019966;
RA Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT genome sequence of BRSV strain A51908.";
RL Virus Genes 23:157-164(2001).
RN [3]
RP FUNCTION (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G), AND INTERACTION WITH HOST
RP HEPARATE SULFATE (ISOFORM MEMBRANE-BOUND GLYCOPROTEIN G).
RX PubMed=11172105; DOI=10.1099/0022-1317-82-3-631;
RA Karger A., Schmidt U., Buchholz U.J.;
RT "Recombinant bovine respiratory syncytial virus with deletions of the G or
RT SH genes: G and F proteins bind heparin.";
RL J. Gen. Virol. 82:631-640(2001).
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=P62648-1; Sequence=Displayed;
CC Name=Secreted glycoprotein G;
CC IsoId=P62648-2; Sequence=VSP_036515;
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; AF295543; AAL49398.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49409.1; -; Genomic_RNA.
DR PIR; JQ2284; JQ2284.
DR Proteomes; UP000007616; 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 1: Evidence at protein level;
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..263
FT /note="Major surface glycoprotein G"
FT /id="PRO_0000142847"
FT CHAIN 66..263
FT /note="Mature secreted glycoprotein G"
FT /id="PRO_0000451316"
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..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 69..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:0000269|PubMed:11172105"
FT REGION 223..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..144
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 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 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 231
FT /note="O-linked (GalNAc...) threonine; 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_036515"
FT VARIANT 8
FT /note="P -> L (in strain: ATCC 51908)"
FT VARIANT 24
FT /note="I -> T"
FT VARIANT 45
FT /note="S -> T (in strain: ATCC 51908)"
FT VARIANT 77
FT /note="T -> I (in strain: ATCC 51908)"
FT VARIANT 88..91
FT /note="PLLP -> SPFF (in strain: ATCC 51908)"
FT VARIANT 96
FT /note="H -> Y (in strain: ATCC 51908)"
FT VARIANT 103
FT /note="T -> I (in strain: ATCC 51908)"
FT VARIANT 111
FT /note="P -> L (in strain: ATCC 51908)"
FT VARIANT 114
FT /note="I -> T (in strain: ATCC 51908)"
FT VARIANT 118..119
FT /note="SG -> RE (in strain: ATCC 51908)"
FT VARIANT 123..128
FT /note="GHPINR -> SHSINE (in strain: ATCC 51908)"
FT VARIANT 140..141
FT /note="PL -> LP (in strain: ATCC 51908)"
FT VARIANT 146
FT /note="L -> P (in strain: ATCC 51908)"
FT VARIANT 151..152
FT /note="LE -> SG (in strain: ATCC 51908)"
FT VARIANT 170
FT /note="H -> Y (in strain: ATCC 51908)"
FT VARIANT 180
FT /note="P -> L (in strain: ATCC 51908)"
FT VARIANT 183..184
FT /note="SP -> LS (in strain: ATCC 51908)"
FT VARIANT 190
FT /note="L -> P (in strain: ATCC 51908)"
FT VARIANT 205
FT /note="A -> T (in strain: ATCC 51908)"
FT VARIANT 220
FT /note="Y -> H (in strain: ATCC 51908)"
FT VARIANT 231..233
FT /note="TKK -> PKN (in strain: ATCC 51908)"
FT VARIANT 237
FT /note="T -> A (in strain: ATCC 51908)"
FT VARIANT 249
FT /note="Q -> H (in strain: ATCC 51908)"
SQ SEQUENCE 263 AA; 28964 MW; A630883D51ED02D5 CRC64;
MSNHTHHPKF KTLKRAWKAS KYFIVGLSCL YKFNLKSLVQ TALTSLAMIT LTSLVITAII
YISVGNAKAK PTSKPTTQQT QQPQNHTPLL PTEHNHKSTH TSTQSTTLSQ PPNIDTTSGT
TYGHPINRTQ NRKIKSQSTP LATRKLPINP LESNPPENHQ DHNNSQTLPH VPCSTCEGNP
ACSPLCQIGL ERAPSRAPTI TLKKAPKPKT TKKPTKTTIY HRTSPEAKLQ TKKNTATPQQ
GILSSPEHQT NQSTTQISQH TSI
