ID A4V922_HRSV Unreviewed; 115 AA. AC A4V922; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 22-APR-2020, entry version 27. DE RecName: Full=Major surface glycoprotein G {ECO:0000256|RuleBase:RU363027}; DE AltName: Full=Attachment glycoprotein G {ECO:0000256|RuleBase:RU363027}; DE Flags: Fragment; GN Name=G {ECO:0000256|RuleBase:RU363027, ECO:0000313|EMBL:CAL64794.1}; OS Human respiratory syncytial virus (strain RSP140/Sweden/02-03). OC Viruses; Riboviria; Negarnaviricota; Haploviricotina; Monjiviricetes; OC Mononegavirales; Pneumoviridae; Orthopneumovirus. OX NCBI_TaxID=410248 {ECO:0000313|EMBL:CAL64794.1}; RN [1] {ECO:0000313|EMBL:CAL64794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RSP140/Sweden/02-03 {ECO:0000313|EMBL:CAL64794.1}; RX PubMed=18041002; DOI=10.1002/jmv.21066; RA Rotzen Ostlund M., Tiveljung Lindell A., Stenler S., Riedel H.M., RA Zweygberg Wirgart B., Grillner L.; RT "Molecular Epidemiology and Genetic Variability of Respiratory Syncytial RT Virus (RSV) in Stockholm, 2002-2003."; RL J. Med. Virol. 80:159-167(2008). CC -!- FUNCTION: Attaches the virion to the host cell membrane by interacting CC with heparan sulfate, initiating the infection. Interacts with host CC CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate CC the immune response and facilitate infection. Unlike the other CC paramyxovirus attachment proteins, lacks both neuraminidase and CC hemagglutinating activities. {ECO:0000256|RuleBase:RU363027}. CC -!- FUNCTION: Secreted glycoprotein G helps RSV escape antibody-dependent CC restriction of replication by acting as an antigen decoy and by CC modulating the activity of leukocytes bearing Fcgamma receptors. CC {ECO:0000256|RuleBase:RU363027}. CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminus) with protein M. CC Interacts with protein F; this interaction occurs on the surface of CC infected cells. Interacts with protein SH. Interacts with host CX3CR1; CC this interaction modulates host immune response. CC {ECO:0000256|RuleBase:RU363027}. CC -!- SUBCELLULAR LOCATION: Host cell surface CC {ECO:0000256|RuleBase:RU363027}. Secreted CC {ECO:0000256|RuleBase:RU363027}. Virion membrane CC {ECO:0000256|RuleBase:RU363027}. CC -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family. CC {ECO:0000256|RuleBase:RU363027}. 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; AM409217; CAL64794.1; -; Genomic_RNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030683; P:mitigation of host immune response by virus; IEA:UniProtKB-KW. 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 Host-virus interaction {ECO:0000256|RuleBase:RU363027}; KW Secreted {ECO:0000256|RuleBase:RU363027}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU363027}; KW Viral immunoevasion {ECO:0000256|RuleBase:RU363027}; KW Virion {ECO:0000256|RuleBase:RU363027}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU363027}. FT REGION 41..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 41..98 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAL64794.1" FT NON_TER 115 FT /evidence="ECO:0000313|EMBL:CAL64794.1" SQ SEQUENCE 115 AA; 12743 MW; 717C72E8088A823C CRC64; STSLIIAAII FIISANHKVT LTTVTVQTIK NHTEKNITTY FTQVSPERVS PSKQPTTTPP IHTNSATISP NTKSETHHTT AQTKSRTTTP TQNNKPSTKP RPKNPPKKPK DDYHF //