ID   GLYCO_TIBVC             Reviewed;         662 AA.
AC   D8V075;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   29-SEP-2021, entry version 26.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Tibrogargan virus (strain CS132) (TIBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Tibrovirus.
OX   NCBI_TaxID=1559361;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=469753; Culicoides brevitarsis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=CS132;
RX   PubMed=21593274; DOI=10.1099/vir.0.026120-0;
RA   Gubala A., Davis S., Weir R., Melville L., Cowled C., Boyle D.;
RT   "Tibrogargan and Coastal Plains rhabdoviruses: genomic characterization,
RT   evolution of novel genes and seroprevalence in Australian livestock.";
RL   J. Gen. Virol. 92:2160-2170(2011).
CC   -!- FUNCTION: Attaches the virus to host receptors, inducing clathrin-
CC       dependent endocytosis of the virion. {ECO:0000250|UniProtKB:P03522}.
CC   -!- FUNCTION: In the endosome, the acidic pH induces conformational changes
CC       in the glycoprotein trimer, which trigger fusion between virus and
CC       endosomal membrane. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03522};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}.
CC       Host membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:P03522}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Glycoprotein;
CC         IsoId=D8V075-1; Sequence=Displayed;
CC       Name=Uncharacterized protein U4;
CC         IsoId=D8V076-1; Sequence=External;
CC   -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; GQ294472; ADG86352.1; -; Viral_cRNA.
DR   RefSeq; YP_007641373.1; NC_020804.1.
DR   GeneID; 14857903; -.
DR   KEGG; vg:14857903; -.
DR   Proteomes; UP000029770; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR001903; Rhabd_glycop.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Clathrin-mediated endocytosis of virus by host;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..662
FT                   /note="Glycoprotein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432050"
FT   TOPO_DOM        17..579
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        580..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        606..662
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..338
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        202..259
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   662 AA;  76840 MW;  7E1E74D38092FAEF CRC64;
     MEAITIEIII IILTISYPIL VAPQLLYNYP FNCKKGPKMT LDGLTCPLDF NTFNLDSKDN
     MEAGTMCRPN PLSKDIEDGF LCYKDTWVTT CEETWYFSKT VKNHIIHEHI TKDECFEALA
     TYKLGKHVEP FFPAPSCYWS ATNEERATFV NIQPHGVLLD PYSGKIKDPL IDSDNCDNDF
     CVTRSHQTHW LRNRKPDIME RCNNETWECH PIKIYYGWVS KKKNQETSTT FNYVQTGLVI
     ESQYIGHVLM ADLCIMTFCN RDGYLFPDGS WWEIKYSLYH AFTKDHTVLN NAHKCGDRTH
     GDHLTEFQRD KKVGYEDLEI NLEGLEMRQK SRSINMMCLN RLAEIRNTHH INVLDMSYLT
     PKHPGRGLAY YFSQDQKNSS KYHVKVLDCD YKLIHIHDAD IKGFVNITKY PEPNVTILGL
     KDNLTFADLG ISRCQDLTPL NGSRNISCEE SSGPLHSDDS RLSNGKRFWT RHSFQGANFH
     EHPGVRIGVN GITYDIRKQI LRFPSTSNLL WDLPSYYSTK HRVHFFQHPT KHEIRKNFTG
     SDSRDIDVLD DLINRHINRT DFPTRIRNWI GNIEDKVEHF FSNVGGTIKT IISLVLFVIG
     TLISIKVWKK CKRHPQKTKK VAQLKLNDYE KTYNQRDTSN NNNDDLYETI ENGGTVYSPF
     HV