VGLG_VSIVM
ID VGLG_VSIVM Reviewed; 423 AA.
AC P0C2X0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=Glycoprotein G;
DE Flags: Fragment;
GN Name=G;
OS Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11279;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-423, AND SUBUNIT.
RX PubMed=16840692; DOI=10.1126/science.1127683;
RA Roche S., Bressanelli S., Rey F.A., Gaudin Y.;
RT "Crystal structure of the low-pH form of the vesicular stomatitis virus
RT glycoprotein G.";
RL Science 313:187-191(2006).
CC -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC clathrin-dependent endocytosis of the virion. In the endosome, the
CC acidic pH induces conformational changes in the glycoprotein trimer,
CC which trigger fusion between virus and endosomal membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16840692}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Glycosylated by host. Palmitoylated by host (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC {ECO:0000305}.
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DR PDB; 5I2M; X-ray; 2.40 A; A/B/C=1-422.
DR PDB; 5I2S; X-ray; 3.00 A; A=1-422.
DR PDB; 5OY9; X-ray; 3.60 A; A=1-410.
DR PDBsum; 5I2M; -.
DR PDBsum; 5I2S; -.
DR PDBsum; 5OY9; -.
DR SMR; P0C2X0; -.
DR TCDB; 1.G.5.1.1; the viral pore-forming membrane fusion protein-5 (vmfp5) family.
DR ABCD; P0C2X0; 14 sequenced antibodies.
DR EvolutionaryTrace; P0C2X0; -.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR001903; Rhabd_glycop.
DR Pfam; PF00974; Rhabdo_glycop; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Clathrin-mediated endocytosis of virus by host;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate; Transmembrane;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN <1..>423
FT /note="Glycoprotein G"
FT /id="PRO_0000287253"
FT TOPO_DOM <1..>423
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 24..284
FT DISULFID 59..92
FT DISULFID 68..114
FT DISULFID 153..158
FT DISULFID 177..224
FT DISULFID 219..253
FT NON_TER 1
FT NON_TER 423
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:5I2M"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:5I2M"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5I2S"
FT STRAND 56..70
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 118..131
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5I2M"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5I2S"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 264..293
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 309..319
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 322..347
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:5I2M"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5I2M"
FT HELIX 384..399
FT /evidence="ECO:0007829|PDB:5I2M"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:5I2S"
SQ SEQUENCE 423 AA; 47396 MW; 7ABF5EA3C2DE0E5B CRC64;
KFTIVFPHNQ KGNWKNVPSN YHYCPSSSDL NWHNDLIGTA IQVKMPKSHK AIQADGWMCH
ASKWVTTCDF RWYGPKYITQ SIRSFTPSVE QCKESIEQTK QGTWLNPGFP PQSCGYATVT
DAEAVIVQVT PHHVLVDEYT GEWVDSQFIN GKCSNYICPT VHNSTTWHSD YKVKGLCDSN
LISMDITFFS EDGELSSLGK EGTGFRSNYF AYETGGKACK MQYCKHWGVR LPSGVWFEMA
DKDLFAAARF PECPEGSSIS APSQTSVDVS LIQDVERILD YSLCQETWSK IRAGLPISPV
DLSYLAPKNP GTGPAFTIIN GTLKYFETRY IRVDIAAPIL SRMVGMISGT TTERELWDDW
APYEDVEIGP NGVLRTSSGY KFPLYMIGHG MLDSDLHLSS KAQVFEHPHI QDAASQLPDD
ESL
