UniProtKB - P03423 (GLYC_HRSVA)
Major surface glycoprotein G
G
Functioni
Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection (PubMed:3655746, PubMed:10400758, PubMed:10864656).
Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection (PubMed:26658574, PubMed:11477410, PubMed:26107373).
Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities (Probable).
Curated6 PublicationsHelps the virus escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fc-gamma receptors.
1 PublicationGO - Biological processi
- adhesion receptor-mediated virion attachment to host cell Source: UniProtKB-KW
- mitigation of host immune response by virus Source: UniProtKB-KW
- viral entry into host cell Source: UniProtKB-KW
Keywordsi
Biological process | Host-virus interaction, Viral attachment to host adhesion receptor, Viral attachment to host cell, Viral immunoevasion, Virus entry into host cell |
Names & Taxonomyi
Protein namesi | Recommended name: Major surface glycoprotein GAlternative name(s): Attachment glycoprotein G Membrane-bound glycoprotein Short name: mG Cleaved into the following chain: |
Gene namesi | Name:G |
Organismi | Human respiratory syncytial virus A (strain A2) |
Taxonomic identifieri | 11259 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Haploviricotina › Monjiviricetes › Mononegavirales › Pneumoviridae › Orthopneumovirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion membrane 1 Publication; Single-pass type II membrane protein 1 Publication
- Host cell membrane 2 Publications; Single-pass type II membrane protein 1 Publication
- Secreted By similarity Note: The protein is shed from infected cells before the appearance of progeny virus (By similarity). The initiation at the downstream methionine removes a portion of the transmembrane domain. The remaining hydrophobic portion of the sG protein is essential for translocating it into the lumen of the ER during translation and would likely maintain its membrane association until a proteolytic event releases the mature sG protein into the medium (By similarity).By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 42 | Cytoplasmic1 PublicationAdd BLAST | 42 | |
Transmembranei | 43 – 63 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 64 – 298 | Extracellular1 PublicationAdd BLAST | 235 |
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Secreted, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | S → A: Complete loss of interaction with protein M. 1 Publication | 1 | |
Mutagenesisi | 3 | K → A: Partial loss of interaction with protein M. 1 Publication | 1 | |
Mutagenesisi | 4 | N → A: Partial loss of interaction with protein M. 1 Publication | 1 | |
Mutagenesisi | 5 | K → A: Partial loss of interaction with protein M. 1 Publication | 1 | |
Mutagenesisi | 6 | D → A: Complete loss of interaction with protein M. 1 Publication | 1 | |
Mutagenesisi | 7 | Q → AQ: Partial loss of interaction with protein M. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000142855 | 1 – 298 | Major surface glycoprotein GAdd BLAST | 298 | |
ChainiPRO_0000451323 | 66 – 298 | Mature secreted glycoprotein GAdd BLAST | 233 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 70 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 72 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 80 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 86 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 87 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 92 | O-linked (GalNAc...) threonine; by host1 Publication | 1 | |
Glycosylationi | 100 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 105 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 113 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 117 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 119 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 135 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 137 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 138 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 139 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 141 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 144 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 147 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Disulfide bondi | 173 ↔ 186 | 1 Publication | ||
Disulfide bondi | 176 ↔ 182 | 1 Publication | ||
Glycosylationi | 199 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 203 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 219 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 231 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 235 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 237 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 251 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 253 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 269 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 270 | O-linked (GlcNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 275 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 282 | O-linked (GalNAc...) threonine; by hostSequence analysis | 1 | |
Glycosylationi | 283 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 287 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 | |
Glycosylationi | 290 | O-linked (GalNAc...) serine; by hostSequence analysis | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 65 – 66 | Cleavage1 Publication | 2 |
Keywords - PTMi
Disulfide bond, GlycoproteinInteractioni
Subunit structurei
Homooligomer (PubMed:1634876).
Interacts (via N-terminus) with protein M (PubMed:15958665).
Part of a complex composed of F1, F2 and G glycoproteins (PubMed:18036342).
Interacts with protein SH (PubMed:15659757).
Interacts with host heparate sulfate; this interaction probably participates in the viral attachment to the host cell (PubMed:10400758).
Interacts with host CX3CR1; this interaction plays an important role in viral entry (PubMed:11477410, PubMed:26658574).
Interacts with the host lectins CD209/DC-SIGN and CD209L/L-SIGN on dendritic cells; these interactions stimulate the phosphorylation of MAPK3/ERK1 and MAPK1/ERK2, which inhibits dendritic cell activation and could participate in the limited immunity against RSV reinfection (PubMed:22090124).
8 PublicationsStructurei
Secondary structure
3D structure databases
SMRi | P03423 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 125 – 161 | DisorderedSequence analysisAdd BLAST | 37 | |
Regioni | 187 – 198 | Binding to host heparan sulfate1 PublicationAdd BLAST | 12 | |
Regioni | 190 – 298 | DisorderedSequence analysisAdd BLAST | 109 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 125 – 159 | Polar residuesSequence analysisAdd BLAST | 35 | |
Compositional biasi | 221 – 288 | Polar residuesSequence analysisAdd BLAST | 68 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
InterProi | View protein in InterPro IPR000925, G_prot |
Pfami | View protein in Pfam PF00802, Glycoprotein_G, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative initiation. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MSKNKDQRTA KTLERTWDTL NHLLFISSCL YKLNLKSVAQ ITLSILAMII
60 70 80 90 100
STSLIIAAII FIASANHKVT PTTAIIQDAT SQIKNTTPTY LTQNPQLGIS
110 120 130 140 150
PSNPSEITSQ ITTILASTTP GVKSTLQSTT VKTKNTTTTQ TQPSKPTTKQ
160 170 180 190 200
RQNKPPSKPN NDFHFEVFNF VPCSICSNNP TCWAICKRIP NKKPGKKTTT
210 220 230 240 250
KPTKKPTLKT TKKDPKPQTT KSKEVPTTKP TEEPTINTTK TNIITTLLTS
260 270 280 290
NTTGNPELTS QMETFHSTSS EGNPSPSQVS TTSEYPSQPS SPPNTPRQ
The sequence of this isoform differs from the canonical sequence as follows:
1-47: Missing.
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_036039 | 1 – 47 | Missing in isoform Secreted glycoprotein G. 1 PublicationAdd BLAST | 47 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M11486 Genomic RNA Translation: AAB59857.1 X03149 mRNA Translation: CAA26928.1 U50362 Genomic RNA Translation: AAB86663.1 U50363 Genomic RNA Translation: AAB86675.1 U63644 Genomic RNA Translation: AAC55969.1 AF035006 Genomic RNA Translation: AAC14901.1 |
PIRi | A94048, MGNZ |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M11486 Genomic RNA Translation: AAB59857.1 X03149 mRNA Translation: CAA26928.1 U50362 Genomic RNA Translation: AAB86663.1 U50363 Genomic RNA Translation: AAB86675.1 U63644 Genomic RNA Translation: AAC55969.1 AF035006 Genomic RNA Translation: AAC14901.1 |
PIRi | A94048, MGNZ |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5WN9 | X-ray | 1.55 | A | 168-196 | [»] | |
5WNA | X-ray | 2.40 | A/B | 161-197 | [»] | |
5WNB | X-ray | 2.40 | A/B | 162-172 | [»] | |
6UVO | X-ray | 2.90 | D | 157-197 | [»] | |
SMRi | P03423 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protocols and materials databases
ABCDi | P03423, 2 sequenced antibodies |
Family and domain databases
InterProi | View protein in InterPro IPR000925, G_prot |
Pfami | View protein in Pfam PF00802, Glycoprotein_G, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GLYC_HRSVA | |
Accessioni | P03423Primary (citable) accession number: P03423 Secondary accession number(s): Q77YB0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | February 23, 2022 | |
This is version 111 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families