ID D4P018_HRSV Unreviewed; 86 AA. AC D4P018; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-NOV-2024, entry version 37. DE RecName: Full=Major surface glycoprotein G {ECO:0000256|ARBA:ARBA00021662, ECO:0000256|RuleBase:RU363027}; DE AltName: Full=Attachment glycoprotein G {ECO:0000256|ARBA:ARBA00032570, ECO:0000256|RuleBase:RU363027}; DE Flags: Fragment; GN Name=G {ECO:0000256|RuleBase:RU363027, ECO:0000313|EMBL:ADD62634.1}; OS Human respiratory syncytial virus. OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus; OC Orthopneumovirus hominis. OX NCBI_TaxID=11250 {ECO:0000313|EMBL:ADD62634.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ADD62634.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Chongqing/A/06/23 {ECO:0000313|EMBL:ADD62634.1}; RX PubMed=20147636; DOI=10.1128/JCM.02258-09; RA Zhang Z.Y., Du L.N., Chen X., Zhao Y., Liu E.M., Yang X.Q., Zhao X.D.; RT "Genetic variability of respiratory syncytial viruses (RSV) prevalent in RT Southwestern China from 2006 to 2009: emergence of subgroup B and A RSV as RT dominant strains."; RL J. Clin. Microbiol. 48:1201-1207(2010). RN [2] {ECO:0000313|EMBL:ADD62634.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Chongqing/A/06/23 {ECO:0000313|EMBL:ADD62634.1}; RA Zhang Z.-Y., Du L.-N., Chen X., Zhao Y., Liu E.-M., Yang X.-Q., Zhao X.-D.; RL Submitted (JAN-2010) 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|ARBA:ARBA00045557}. 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:0000256|RuleBase:RU363027}. CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminus) with protein M. Part CC of a complex composed of F1, F2 and G glycoproteins. Interacts with CC protein SH. Interacts with host heparate sulfate; this interaction CC probably participates in the viral attachment to the host cell. CC Interacts with host CX3CR1; this interaction plays an important role in CC viral entry. Interacts with the host lectins CD209/DC-SIGN and CC CD209L/L-SIGN on dendritic cells; these interactions stimulate the CC phosphorylation of MAPK3/ERK1 and MAPK1/ERK2, which inhibits dendritic CC cell activation and could participate in the limited immunity against CC RSV reinfection. {ECO:0000256|ARBA:ARBA00046352}. 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:0000256|RuleBase:RU363027}. CC -!- SUBCELLULAR LOCATION: Host cell membrane CC {ECO:0000256|ARBA:ARBA00004336}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004336}. Secreted CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU363027}. Virion CC membrane {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane CC protein {ECO:0000256|ARBA:ARBA00004208}. 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; GU550449; ADD62634.1; -; mRNA. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. DR InterPro; IPR000925; G_prot. DR Pfam; PF00802; Glycoprotein_G; 1. PE 2: Evidence at transcript level; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, KW ECO:0000256|RuleBase:RU363027}; Membrane {ECO:0000256|ARBA:ARBA00022870}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU363027}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804, KW ECO:0000256|RuleBase:RU363027}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, KW ECO:0000256|RuleBase:RU363027}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU363027}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296, KW ECO:0000256|RuleBase:RU363027}. FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..86 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADD62634.1" SQ SEQUENCE 86 AA; 9381 MW; B5C94E56BDB6891B CRC64; KKDPKPQTTK PKEVLTTKPT EKPTIDTTKT NIKTTLLTSN TTGNPEHTSQ EETLHSTTSE GNLSPSQVYT TSEYLSQSPS SSNTTK //