ID   GLYCO_MOKV              Reviewed;         522 AA.
AC   P0C572;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   29-SEP-2021, entry version 51.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Mokola virus (MOKV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=12538;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH   NCBI_TaxID=269271; Chodsigoa caovansunga (Van Sung's shrew).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9989; Rodentia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9225031; DOI=10.1099/0022-1317-78-7-1571;
RA   Le Mercier P., Jacob Y., Tordo N.;
RT   "The complete Mokola virus genome sequence: structure of the RNA-dependent
RT   RNA polymerase.";
RL   J. Gen. Virol. 78:1571-1576(1997).
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. There is convincing in vitro evidence
CC       that the muscular form of the nicotinic acetylcholine receptor (nAChR),
CC       the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin
CC       receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus
CC       entry into cells (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts with matrix protein (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Glycosylated and palmitoylated by host. Glycosylation is crucial
CC       for glycoprotein export at the cell surface (By similarity).
CC       {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Primary surface antigen capable of inducing and reacting
CC       with virus-neutralizing antibodies. Almost all human and veterinary
CC       vaccines are based on the functional aspects of the G protein.
CC   -!- MISCELLANEOUS: Arg-352 is highly involved in rabies virus
CC       pathogenicity. Its mutation dramatically attenuates the virus (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyssavirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; Y09762; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   RefSeq; YP_142353.1; NC_006429.1.
DR   PDB; 6TMR; X-ray; 2.89 A; A=20-455.
DR   PDBsum; 6TMR; -.
DR   SMR; P0C572; -.
DR   GeneID; 3159473; -.
DR   KEGG; vg:3159473; -.
DR   Proteomes; UP000006826; 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   InterPro; IPR001903; Rhabd_glycop.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..522
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295797"
FT   TOPO_DOM        20..455
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        477..522
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   STRAND          23..28
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          77..91
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          97..106
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           110..121
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          152..156
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   TURN            163..166
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          195..201
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          211..221
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          249..253
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           282..311
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           317..323
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          326..337
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   STRAND          340..351
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           354..356
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           393..396
FT                   /evidence="ECO:0007829|PDB:6TMR"
FT   HELIX           399..409
FT                   /evidence="ECO:0007829|PDB:6TMR"
SQ   SEQUENCE   522 AA;  58902 MW;  3517ECC0F10C23A4 CRC64;
     MNIPCFVVIL SLATTHSLGE FPLYTIPEKI EKWTPIDMIH LSCPNNLLSE EEGCNAESSF
     TYFELKSGYL AHQKVPGFTC TGVVNEAETY TNFVGYVTTT FKRKHFRPTV AACRDAYNWK
     VSGDPRYEES LHTPYPDSSW LRTVTTTKES LLIISPSIVE MDIYGRTLHS PMFPSGVCSN
     VYPSVPSCET NHDYTLWLPE DPSLSLVCDI FTSSNGKKAM NGSRICGFKD ERGFYRSLKG
     ACKLTLCGRP GIRLFDGTWV SFTKPDVHVW CTPNQLINIH NDRLDEIEHL IVEDIIKKRE
     ECLDTLETIL MSQSVSFRRL SHFRKLVPGY GKAYTILNGS LMETNVYYKR VDKWADILPS
     KGCLKVGQQC MEPVKGVLFN GIIKGPDGQI LIPEMQSEQL KQHMDLLKAA VFPLRHPLIS
     REAVFKKDGD ADDFVDLHMP DVHKSVSDVD LGLPHWGFWM LIGATIVAFV VLVCLLRVCC
     KRVRRRRSGR ATQEIPLSFP SAPVPRAKVV SSWESYKGLP GT