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GLYC_BRSVR
ID   GLYC_BRSVR              Reviewed;         257 AA.
AC   P69350; O12584; O12865; Q84183;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
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   Bovine respiratory syncytial virus (strain Rb94) (BRS).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=11249;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9018058; DOI=10.1099/0022-1317-78-2-359;
RA   Prozzi D., Walravens K., Langedijk J.P., Daus F., Kramps J.A.,
RA   Letesson J.J.;
RT   "Antigenic and molecular analyses of the variability of bovine respiratory
RT   syncytial virus G glycoprotein.";
RL   J. Gen. Virol. 78:359-366(1997).
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. 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. {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=P69350-1; Sequence=Displayed;
CC       Name=Secreted glycoprotein G;
CC         IsoId=P69350-2; Sequence=VSP_036518;
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 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   EMBL; L27802; AAB47926.1; -; Genomic_RNA.
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..257
FT                   /note="Major surface glycoprotein G"
FT                   /id="PRO_0000142850"
FT   CHAIN           66..257
FT                   /note="Mature secreted glycoprotein G"
FT                   /id="PRO_0000451319"
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..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          70..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..166
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          204..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..257
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        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        85
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
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        105
FT                   /note="O-linked (GalNAc...) serine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
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...) 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_036518"
SQ   SEQUENCE   257 AA;  28388 MW;  D93E5347FA25FEFF CRC64;
     MSNHTHHLKF KTLKRAWKAS KYFIVGLSCL YKFNLKSLVQ TALTTLAMIT LTSLVITALI
     YISVGNAKAK PTSKPTIQQT QRPQNHTSPL FTEHNYKSTH TSIQSTTLSQ LLNIDTTRGT
     TYSHPTDETQ NRKIKSQSTL PATRQPPINP SGSNPPENHQ DHNNSQTLPY VPCSTCEGNL
     ACSSLCQIGL ERAPSRAPTI TLKKAPKPKT TKKPTKTTIH HRTSPEAKLQ PKNNTAAPQQ
     GILSSPEHHT NQSTTQI
 
 
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