ID C1ILQ3_HRSV Unreviewed; 117 AA. AC C1ILQ3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 12-AUG-2020, entry version 25. 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 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|ARBA:ARBA00002164, 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: Cell surface {ECO:0000256|ARBA:ARBA00004241}. CC Host cell surface {ECO:0000256|ARBA:ARBA00004426, CC ECO:0000256|RuleBase:RU363027}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. Secreted CC {ECO:0000256|RuleBase:RU363027}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004182, ECO:0000256|RuleBase:RU363027}. CC -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family. CC {ECO:0000256|ARBA:ARBA00007101, 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: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 1..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..27 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..117 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACF28511.1" FT NON_TER 117 FT /evidence="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 //