ID   GLYCO_MMVR              Reviewed;         591 AA.
AC   Q6E0W7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   23-FEB-2022, entry version 52.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Maize mosaic virus (isolate Maize/United States/Reed/2005) (MMV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Nucleorhabdovirus.
OX   NCBI_TaxID=928305;
OH   NCBI_TaxID=300124; Rottboellia.
OH   NCBI_TaxID=4554; Setaria.
OH   NCBI_TaxID=4558; Sorghum bicolor (Sorghum) (Sorghum vulgare).
OH   NCBI_TaxID=4577; Zea mays (Maize).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16005085; DOI=10.1016/j.jviromet.2005.05.013;
RA   Reed S.E., Tsai C.W., Willie K.J., Redinbaugh M.G., Hogenhout S.A.;
RT   "Shotgun sequencing of the negative-sense RNA genome of the rhabdovirus
RT   Maize mosaic virus.";
RL   J. Virol. Methods 129:91-96(2005).
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 nucleorhabdovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY618418; AAT66756.1; -; Genomic_RNA.
DR   RefSeq; YP_052854.1; NC_005975.1.
DR   GeneID; 2886116; -.
DR   KEGG; vg:2886116; -.
DR   Proteomes; UP000008593; 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..591
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299238"
FT   TOPO_DOM        22..552
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..591
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   591 AA;  65917 MW;  21FCB20C8FA7F251 CRC64;
     MSLIHLIYFP TILSLILGTE GTPALTYGNL ADNQHGNEEQ GDVDMYPLYE CSKKGAGVSS
     NNWYGACRGA CSMTKNTTDV HMEIYYRNDS VGWIDVLSIQ TTEIWKHSHV TWYGECEHNT
     KYGSSNTAPV SVILERLEFL HNGMSSWPYG HSIHVHDTIS SPDCSYFDDV SRSGWRLIIS
     KRALELKSDI AGEGYIVDPD VGYVYPVADG IGKGRTWHVW KASSVPSSGC YFKSAGITNC
     TLLMDTFLYS CPSLNIAFSA RVGKHIKSTC VGDMNISTDG VTYQTLGSTD QGSISTQLVS
     LWHQSQEALI QQLILTINEA LGKIETSYCE STCDLTEMLI SQHTEHPMVI ETPVGPWLPY
     SIDGKVSVLP CQGGQDLVVI KPIEICASPF MLKVKSLKSL DTYWWVPTDS HVAPFTQCSN
     RDDEEMIIKI QRKKPLIFEF WRGAYKLDYP YNSSGIWLDN PGGHIHRSSK WFPTLDSLSY
     SSPINLPLIS KGIRKHIQAI VSTTEITSGG NVTSWTHSIS TIAEAMFDSA AIAAGRVVMW
     WYTLEESVKR YLTVAFGLVL TVITIWAMSK LFFRSSPTYA RAPTNIEWVR S