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GLYC_HRSVL
ID   GLYC_HRSVL              Reviewed;         298 AA.
AC   P20895;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Major surface glycoprotein G;
DE   AltName: Full=Attachment glycoprotein G;
DE   AltName: Full=Membrane-bound glycoprotein;
DE            Short=mG;
DE   Contains:
DE     RecName: Full=Mature secreted glycoprotein G {ECO:0000305|PubMed:3373568};
DE              Short=Mature sG {ECO:0000305|PubMed:3373568};
GN   Name=G;
OS   Human respiratory syncytial virus A (strain Long).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=11260;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2441388; DOI=10.1073/pnas.84.16.5625;
RA   Johnson P.R., Spriggs M.K., Olmsted R.A., Collins P.L.;
RT   "The G glycoprotein of human respiratory syncytial viruses of subgroups A
RT   and B: extensive sequence divergence between antigenically related
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5625-5629(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 66-71 AND 75-80, SUBCELLULAR LOCATION (ISOFORM SECRETED
RP   GLYCOPROTEIN G), AND PROTEOLYTIC CLEAVAGE (ISOFORM SECRETED GLYCOPROTEIN
RP   G).
RX   PubMed=3373568; DOI=10.1128/jvi.62.7.2228-2233.1988;
RA   Hendricks D.A., McIntosh K., Patterson J.L.;
RT   "Further characterization of the soluble form of the G glycoprotein of
RT   respiratory syncytial virus.";
RL   J. Virol. 62:2228-2233(1988).
RN   [3]
RP   ALTERNATIVE INITIATION (ISOFORM SECRETED GLYCOPROTEIN G).
RX   PubMed=3585282; DOI=10.1099/0022-1317-68-6-1705;
RA   Hendricks D.A., Baradaran K., McIntosh K., Patterson J.L.;
RT   "Appearance of a soluble form of the G protein of respiratory syncytial
RT   virus in fluids of infected cells.";
RL   J. Gen. Virol. 68:1705-1714(1987).
CC   -!- FUNCTION: [Isoform Membrane-bound glycoprotein G]: Attaches the virion
CC       to the host cell membrane by interacting with heparan sulfate,
CC       initiating the infection. Interacts with host CX3CR1, the receptor for
CC       the CX3C chemokine fractalkine, to modulate the immune response and
CC       facilitate infection. Unlike the other paramyxovirus attachment
CC       proteins, lacks both neuraminidase and hemagglutinating activities.
CC       {ECO:0000250|UniProtKB:P03423}.
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:0000250|UniProtKB:P03423}.
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. Interacts with host CX3CR1; this
CC       interaction plays an important role in viral entry. Interacts with the
CC       host lectins CD209/DC-SIGN and CD209L/L-SIGN on dendritic cells; these
CC       interactions stimulate the phosphorylation of MAPK3/ERK1 and
CC       MAPK1/ERK2, which inhibits dendritic cell activation and could
CC       participate in the limited immunity against RSV reinfection.
CC       {ECO:0000250|UniProtKB:P03423}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion
CC       membrane {ECO:0000250|UniProtKB:P03423}; Single-pass type II membrane
CC       protein {ECO:0000250|UniProtKB:P03423}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P03423}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P03423}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Secreted glycoprotein G]: Secreted
CC       {ECO:0000269|PubMed:3373568}. Note=The protein is shed from infected
CC       cells before the appearance of progeny virus (PubMed:3373568). The
CC       initiation at the downstream methionine removes a portion of the
CC       transmembrane domain. The remaining hydrophobic portion of the sG
CC       protein is essential for translocating it into the lumen of the ER
CC       during translation and would likely maintain its membrane association
CC       until a proteolytic event releases the mature sG protein into the
CC       medium (Probable). {ECO:0000269|PubMed:3373568,
CC       ECO:0000305|PubMed:3373568}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Membrane-bound glycoprotein G;
CC         IsoId=P20895-1; Sequence=Displayed;
CC       Name=Secreted glycoprotein G;
CC         IsoId=P20895-2; Sequence=VSP_036524;
CC   -!- DOMAIN: [Isoform Membrane-bound glycoprotein G]: Contains a linear
CC       heparin binding domain essential for virus attachment to the host.
CC       {ECO:0000250|UniProtKB:P03423}.
CC   -!- PTM: [Isoform Secreted glycoprotein G]: Cleaved to give rise to the
CC       mature sG protein which lacks the transmembrane domain.
CC       {ECO:0000269|PubMed:3373568}.
CC   -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
CC       {ECO:0000305}.
CC   -!- CAUTION: A second site of cleavage between residues 74 and 75 has been
CC       described but has not been found in other strains.
CC       {ECO:0000269|PubMed:3373568}.
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DR   EMBL; M17212; AAA47411.1; -; Genomic_RNA.
DR   PIR; A32703; MGNZRL.
DR   PDB; 1KWD; NMR; -; A=172-187.
DR   PDB; 1KWE; NMR; -; A=172-187.
DR   PDBsum; 1KWD; -.
DR   PDBsum; 1KWE; -.
DR   SMR; P20895; -.
DR   BindingDB; P20895; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host cell membrane; Host membrane;
KW   Host-virus interaction; Membrane; Secreted; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..298
FT                   /note="Major surface glycoprotein G"
FT                   /id="PRO_0000142856"
FT   CHAIN           66..298
FT                   /note="Mature secreted glycoprotein G"
FT                   /id="PRO_0000451325"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          119..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..198
FT                   /note="Binding to host heparan sulfate"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   REGION          190..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..211
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            65..66
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:3373568"
FT   CARBOHYD        70
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        72
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        80
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        86
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        87
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        92
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   CARBOHYD        100
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="O-linked (GlcNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        173..186
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   DISULFID        176..182
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT   VAR_SEQ         1..47
FT                   /note="Missing (in isoform Secreted glycoprotein G)"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
FT                   /id="VSP_036524"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:1KWD"
SQ   SEQUENCE   298 AA;  32781 MW;  B79FEFA4B4A73B0E CRC64;
     MSKNKDQRTA KTLEKTWDTL NHLLFISSGL YKLNLKSIAQ ITLSILAMII STSLIITAII
     FIASANHKVT LTTAIIQDAT SQIKNTTPTY LTQDPQLGIS FSNLSEITSQ TTTILASTTP
     GVKSNLQPTT VKTKNTTTTQ TQPSKPTTKQ RQNKPPNKPN NDFHFEVFNF VPCSICSNNP
     TCWAICKRIP NKKPGKKTTT KPTKKPTFKT TKKDHKPQTT KPKEVPTTKP TEEPTINTTK
     TNIITTLLTN NTTGNPKLTS QMETFHSTSS EGNLSPSQVS TTSEHPSQPS SPPNTTRQ
 
 
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