ID   GLYCO_ARV               Reviewed;         660 AA.
AC   Q89669;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 68.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Adelaide River virus (ARV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Ephemerovirus.
OX   NCBI_TaxID=31612;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH   NCBI_TaxID=58271; Culicoides.
OH   NCBI_TaxID=9970; Syncerus caffer (African buffalo).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
RX   PubMed=8337841; DOI=10.1006/viro.1993.1423;
RA   Wang Y., Walker P.J.;
RT   "Adelaide river rhabdovirus expresses consecutive glycoprotein genes as
RT   polycistronic mRNAs: new evidence of gene duplication as an evolutionary
RT   process.";
RL   Virology 195:719-731(1993).
CC   -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC       endocytosis of the virion. In the endosome, the acidic pH induces
CC       conformational changes in the glycoprotein trimer, which trigger fusion
CC       between virus and cell membrane (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts with matrix protein (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Glycosylated by host. Glycosylation is crucial for glycoprotein
CC       export at the cell surface (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ephemerovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; L09206; AAA02762.1; -; Genomic_RNA.
DR   EMBL; L09207; AAA02764.1; -; mRNA.
DR   PIR; T02768; T02768.
DR   RefSeq; YP_009177242.1; NC_028246.1.
DR   GeneID; 26123212; -.
DR   KEGG; vg:26123212; -.
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: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; IPR001903; Rhabd_glycop.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Host-virus interaction; Membrane; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..660
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299235"
FT   TOPO_DOM        23..558
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        559..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        580..660
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   660 AA;  77206 MW;  E0A48EC3DEC0960D CRC64;
     MATFKVLVLM ILWITSIFNV RCEKFVTIPV NCSGEVDIDK MDVMCPNRYN LLSTNHLMEG
     EEVETFCRPS LRENDLLDGY LCRKQKWEVT CTETWYFVTD VKYQIIEVIP TENECMEERE
     RKLKGEYIPP YYPPTNCVWN AIDTQERTFI TLIEHPVIED PVTMTLMDSK FTKPCNPKHN
     EVTICDTYNP LIKWISKETS GLNLHCQIKS WECIPVKLHH SHRNMMEALY LESPDFGIVD
     ASKICNLTFC GYNGILLDNG EWWSIYRSGF THGFLDNHIL KNRRIEECKE KKPGYKLAKL
     DTTYIDLEFE IELEHEKCLG TLEKLQNGEY VTPLDLSYLS PSNPGKHYAY RLEYINTTEH
     KCVQLGFTYE GGDCRKMLDE RDDHGAYYNW TTIKLQRVIR AVCYYHTFSM NLDESKHKYY
     DQDNRSIQID EKFISEVLKS TPLIDRHEKY EGNLSWNGII IESKNGHEKN VIVPSASQYN
     HVMINKILKR LDTVMYDSYK FDSESGSISY NKIVPIVRED NLQNAHRVDV IQYIKDKGSY
     IINGFTGWFS SLGKLMRWTI WGVGLFFSIF TLYKIIMILR KHSNDNVRKE FKETAGKVMI
     GQPIDTKSMS RTSIKANNKG KFDKVKDLFT PRSKTISHLT TDTLKEHTDG TYEELHFFNV