ID   GLYCO_LNYV3             Reviewed;         551 AA.
AC   Q9DIC6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-NOV-2023, entry version 62.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Lettuce necrotic yellows virus (isolate 318) (LNYV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC   Cytorhabdovirus; Cytorhabdovirus lactucanecante.
OX   NCBI_TaxID=928304;
OH   NCBI_TaxID=43191; Embergeria.
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=43208; Reichardia tingitana.
OH   NCBI_TaxID=255580; Sonchus hydrophilus.
OH   NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16313992; DOI=10.1016/j.virusres.2005.10.024;
RA   Dietzgen R.G., Callaghan B., Wetzel T., Dale J.L.;
RT   "Completion of the genome sequence of Lettuce necrotic yellows virus, type
RT   species of the genus Cytorhabdovirus.";
RL   Virus Res. 118:16-22(2006).
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 cytorhabdovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ251533; CAC18651.1; -; Genomic_RNA.
DR   EMBL; AJ867584; CAI30425.1; -; Genomic_RNA.
DR   RefSeq; YP_425091.1; NC_007642.1.
DR   GeneID; 3844361; -.
DR   KEGG; vg:3844361; -.
DR   Proteomes; UP000008592; Segment.
DR   GO; GO:0016020; C: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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..551
FT                   /note="Glycoprotein"
FT                   /id="PRO_5000065805"
FT   TOPO_DOM        26..503
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        525..551
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  62317 MW;  838FA34080A37F98 CRC64;
     MVSKITLLCF AITCDVLISM GTVQGVFNHS VGPLAVCSPD MEDARAYTEN CYRRCSRNKE
     PSTHGYVWLY SDTAPKGGPV VTRCNKVRVK QVFTETWSFS FIKGTPTRMT LDVTEAECVA
     VMRSQCPTHN CNIKAPSELP EEYHYASDTE VVQDYLEILS MPSGLDYMEE NLRITPSQSK
     FSFQLTDGKG QEGQYIYFWD TKYDDTKCPF DSFQSHGCDK YDSPLDLINC RESRFVIPSI
     ANSTTLVGAC QGLQKSTTGL IYKWDDRPDS IANDSKRIAL TKNDQTAGNV ATLRVLVADS
     LNAVDEDLCH TQCEMLDFIL RSDRKREVLT RIGGSYLVVS KTSYIRQCRP LVGCRIVKPH
     YFCGNPNRVA IICHGKVWYW DPLKSYVDEG MNCERRVAGT KLVFAVGNHE YAIDDDMHVE
     LPEHETYGIS HDLLASSEDR ISKDIVDPTE LRNSWQSHIA KEGRMSIEPL SQDKQVSHWD
     AEFSNPLTWL TSAGGWILDM SHKVTLWATV FLTLGALVAG AKVWEIMRKA NRKSQYKRTN
     TEPHDSQATW I
//