GLYCO_RABVN
ID GLYCO_RABVN Reviewed; 524 AA.
AC Q9IPJ6; Q75T09; Q787B5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 58.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Rabies virus (strain Nishigahara RCEH) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11298;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Nishigahara, and RC_HL;
RX PubMed=11270607; DOI=10.1111/j.1348-0421.2001.tb01274.x;
RA Ito N., Kakemizu M., Ito K.A., Yamamoto A., Yoshida Y., Sugiyama M.,
RA Minamoto N.;
RT "A comparison of complete genome sequences of the attenuated RC-HL strain
RT of rabies virus used for production of animal vaccine in Japan, and the
RT parental Nishigahara strain.";
RL Microbiol. Immunol. 45:51-58(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Ni-CE;
RX PubMed=17010466; DOI=10.1016/j.virusres.2006.08.011;
RA Shimizu K., Ito N., Mita T., Yamada K., Hosokawa-Muto J., Sugiyama M.,
RA Minamoto N.;
RT "Involvement of nucleoprotein, phosphoprotein, and matrix protein genes of
RT rabies virus in virulence for adult mice.";
RL Virus Res. 123:154-160(2007).
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; AB044824; BAA96805.1; -; Genomic_RNA.
DR EMBL; AB009663; BAA24086.2; -; Genomic_RNA.
DR EMBL; AB128149; BAD04913.1; -; Genomic_RNA.
DR SMR; Q9IPJ6; -.
DR ABCD; Q9IPJ6; 2 sequenced antibodies.
DR Proteomes; UP000006366; Genome.
DR Proteomes; UP000007309; Genome.
DR Proteomes; UP000007310; 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 Glycoprotein; Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..524
FT /note="Glycoprotein"
FT /id="PRO_0000295802"
FT TOPO_DOM 20..459
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..524
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT LIPID 480
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 16
FT /note="S -> L (in strain: RC_HL)"
FT VARIANT 69
FT /note="Y -> R (in strain: Ni-CE)"
FT VARIANT 70
FT /note="I -> T (in strain: RC_HL)"
FT VARIANT 183
FT /note="V -> R (in strain: RC_HL)"
FT VARIANT 201
FT /note="S -> I (in strain: Ni-CE and RC_HL)"
FT VARIANT 219
FT /note="A -> V (in strain: RC_HL)"
FT VARIANT 224
FT /note="K -> T (in strain: RC_HL)"
FT VARIANT 229
FT /note="V -> I (in strain: RC_HL)"
FT VARIANT 261
FT /note="A -> S (in strain: RC_HL)"
FT VARIANT 274
FT /note="D -> N (in strain: RC_HL)"
FT VARIANT 287
FT /note="I -> L (in strain: RC_HL)"
FT VARIANT 322
FT /note="Y -> H (in strain: RC_HL)"
FT VARIANT 458
FT /note="E -> K (in strain: RC_HL)"
FT VARIANT 471
FT /note="M -> V (in strain: RC_HL)"
FT VARIANT 511
FT /note="P -> N (in strain: RC_HL)"
SQ SEQUENCE 524 AA; 58427 MW; 7C2D8378DB1A9628 CRC64;
MVPQALLLVP ILGFSSCFGK FPIYTIPDTL GPWSPIDIHH LSCPNNLVVE DEGCTNLSGF
SYMELKVGYI SAIKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
MAGDPRYEES LHSPYPDYHW LRTVKTTKES LVIISPSVAD LDPYDNSLHS RVFPSGKCSG
ITVSSVYCST NHDYTVWMPE SLRLGTSCDI FTNSRGKRAS KGSKTCGFVD ERGLYKSLKG
ACKLKLCGVL GLRLMDGTWV AMQTSNETKW CPPDQLVNLH DLRSDEIEHL VIEELVKKRE
ECLDALESII TTKSVSFRRL SYLRKLVPGF GKAYTIFNKT LMEAEAHYKS VRTWNEIIPS
KGCLRVGGRC HPHVNGVFFN GIILGPDGHV LIPEMQSSLL QQHIELLESS VIPLMHPLAD
PFTVFKDGDE TEDFIEVHLP DVHEQVSGVD LGLPNWGEYV LLSAGTLIAL MLIIFLMTCC
RKVDRPESTQ RSLRGTGRNV SVTSQSGKFI PSWESYKSGG ETGL
