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GLYC_HRSV2
ID   GLYC_HRSV2              Reviewed;         297 AA.
AC   P27021;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 73.
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:0000250|UniProtKB:P20895};
DE              Short=Mature sG {ECO:0000250|UniProtKB:P20895};
GN   Name=G;
OS   Human respiratory syncytial virus A (strain rsb642).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=11252;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1895054; DOI=10.1099/0022-1317-72-9-2091;
RA   Cane P.A., Matthews D.A., Pringle C.R.;
RT   "Identification of variable domains of the attachment (G) protein of
RT   subgroup A respiratory syncytial viruses.";
RL   J. Gen. Virol. 72:2091-2096(1991).
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:0000250|UniProtKB:P20895}. Note=The protein is shed from infected
CC       cells before the appearance of progeny virus. The initiation at the
CC       downstream methionine removes a portion of the transmembrane domain.
CC       The remaining hydrophobic portion of the sG protein is essential for
CC       translocating it into the lumen of the ER during translation and would
CC       likely maintain its membrane association until a proteolytic event
CC       releases the mature sG protein into the medium.
CC       {ECO:0000250|UniProtKB:P20895}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Membrane-bound glycoprotein G;
CC         IsoId=P27021-1; Sequence=Displayed;
CC       Name=Secreted glycoprotein G;
CC         IsoId=P27021-2; Sequence=VSP_036526;
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:0000250|UniProtKB:P20895}.
CC   -!- PTM: [Isoform Membrane-bound glycoprotein G]: N- and O-glycosylated.
CC       May carry 30-40 separate O-linked carbohydrate chains distributed among
CC       the 91 serine and threonine residues. {ECO:0000250|UniProtKB:P03423}.
CC   -!- PTM: [Isoform Membrane-bound glycoprotein G]: Palmitoylated.
CC       {ECO:0000250|UniProtKB:P03423}.
CC   -!- SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.
CC       {ECO:0000305}.
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DR   PIR; JQ1204; JQ1204.
DR   SMR; P27021; -.
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   3: Inferred from homology;
KW   Alternative initiation; Disulfide bond; Glycoprotein; Host cell membrane;
KW   Host membrane; 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..297
FT                   /note="Major surface glycoprotein G"
FT                   /id="PRO_0000142858"
FT   CHAIN           66..297
FT                   /note="Mature secreted glycoprotein G"
FT                   /id="PRO_0000451327"
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..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          133..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          191..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            65..66
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P03423"
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        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        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        144
FT                   /note="N-linked (GlcNAc...) asparagine; 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        251
FT                   /note="N-linked (GlcNAc...) asparagine; 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        290
FT                   /note="O-linked (GalNAc...) serine; 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_036526"
SQ   SEQUENCE   297 AA;  32745 MW;  FC72A7F3A8EBF67C CRC64;
     MSKNKDQRTA KTLERTWDTL NHLLFISSCL YKLNLKSVAQ ITLSILAMII STSLIIAAII
     FIASANHRVT STTTIIQDAT NQIKNTTPTY LTQNPQLGIS PSNPSEITSL ITTILDPTTP
     GVKLTLQSTT VRIKNTTTTQ AQPNKSTTKQ RQNKPPSKPN NDFHFEVFNF VPCSICSNNP
     TCWAICKRIP NKKPGKRTTT KPTKKPTLKT TKKDPKPQTT KSEEVPTTKL TEEPTINTTK
     TNIITTPLTS NTARNPELTS QMETFHSTSS EGNPSPSQVS ITSEYPPQPS SPPNTPR
 
 
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