ID C1ILQ3_HRSV Unreviewed; 117 AA. AC C1ILQ3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 31-JUL-2019, entry version 22. 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}; OS Human respiratory syncytial virus. OC Viruses; Riboviria; Negarnaviricota; Haploviricotina; Monjiviricetes; OC Mononegavirales; Pneumoviridae; Orthopneumovirus. OX NCBI_TaxID=11250 {ECO:0000313|EMBL:ACF28511.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ACF28511.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KOL/117/05/B {ECO:0000313|EMBL:ACF28511.1}; RA Agrawal A.S., Naik T.N., Sarkar M.; RT "Surface Glycoprotein G encoding gene of Human Respiratory Syncytial RT Virus(HRSV), B Subgroup."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Attaches the virion to the host cell membrane by CC interacting with heparan sulfate, initiating the infection. CC Interacts with host CX3CR1, the receptor for the CX3C chemokine CC fractalkine, to modulate the immune response and facilitate CC infection. Unlike the other paramyxovirus attachment proteins, CC lacks both neuraminidase and hemagglutinating activities. CC {ECO:0000256|RuleBase:RU363027}. CC -!- FUNCTION: Secreted glycoprotein G helps RSV escape antibody- CC dependent restriction of replication by acting as an antigen decoy CC and by modulating the activity of leukocytes bearing Fcgamma CC receptors. {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 CC of infected cells. Interacts with protein SH. Interacts with host CC CX3CR1; 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; EU604793; ACF28511.1; -; Viral_cRNA. 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:evasion or tolerance by virus of host immune response; 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 1 117 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 13 27 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 28 117 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACF28511.1}. FT NON_TER 117 117 {ECO:0000313|EMBL:ACF28511.1}. SQ SEQUENCE 117 AA; 12755 MW; 3385331A1E137A6F CRC64; KKPTTKPTNK PPTKTTNKRD PKTPAKTPKK ETTINPTKKP TPKTTERDTS TPQSTVLDTT TSKHTERDTS TSQSIVLDTT TSKHTIQQQS LYSTTPENTP NSTKTPTASE PSTSNST //