ID   GLYCO_NCMV              Reviewed;         483 AA.
AC   Q9JGT4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Northern cereal mosaic virus (NCMV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC   Cytorhabdovirus.
OX   NCBI_TaxID=1985704;
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10963343; DOI=10.1007/s007050070096;
RA   Tanno F., Nakatsu A., Toriyama S., Kojima M.;
RT   "Complete nucleotide sequence of Northern cereal mosaic virus and its
RT   genome organization.";
RL   Arch. Virol. 145:1373-1384(2000).
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: Glycosylatedby host. Glycosylation is crucial for glycoprotein
CC       export at the cell surface (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytorhabdovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AB030277; BAA95351.1; -; Genomic_RNA.
DR   PRIDE; Q9JGT4; -.
DR   Proteomes; UP000007785; Genome.
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.
PE   3: Inferred from homology;
KW   Glycoprotein; Host-virus interaction; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..483
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299234"
FT   TOPO_DOM        22..442
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        464..483
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   483 AA;  54118 MW;  2A57C312429BF3A3 CRC64;
     MQKLSLVWII TLSVSVITGD GLSILSCNKT DEVPTVTQCF KSCSDTILGE QVKVSILSQE
     DPTSIVVGRC IWRIMKQSFT ETWTFSRLIS AKEITWEPAT TQECNGAFHN LCKNKAGCVS
     EDLEIEPEFS WARTEIREVK HLSIETLTMS AYLHQGAGKV LIDGVAVPIS KKTHNNGDFT
     YVWDDVPISE VCPWKHPISH LSCYKDKEDL DDIYCPSQGI SLVNYTKVDT SCPEQIYTDV
     GGLVFKLGKV DFNDWYPYVI ESSDVAVKET ISSINMALKM RESVHCHQDC LEIRRRVTYV
     DGFYYDPLPP AKCRLIGNCS VDSGSVTCNN GTLVWATCGG RRVWIDLKSG RDVKNAVCEK
     GGRSRISKNQ FEGVLNEFHL NNSKFGNILR ANEIHSVILK DNEVMDFARV VKSASERSGN
     FSEGTLINVR QLFRPMINFL RGIEHEIKVV AFSVLALIVG YIIIRIRTVT VAKAKSLESI
     AMI