GLYCO_ISFV
ID GLYCO_ISFV Reviewed; 523 AA.
AC Q5K2K4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Isfahan virus (ISFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=290008;
OH NCBI_TaxID=10045; Gerbillinae (gerbils).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15614433; DOI=10.1007/s00705-004-0452-2;
RA Marriott A.C.;
RT "Complete genome sequences of Chandipura and Isfahan vesiculoviruses.";
RL Arch. Virol. 150:671-680(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: Homotrimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Glycosylated by host. Palmitoylated by host on Cys-497 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AJ810084; CAH17547.1; -; Genomic_RNA.
DR RefSeq; YP_007641385.1; NC_020806.1.
DR SMR; Q5K2K4; -.
DR GeneID; 14857915; -.
DR KEGG; vg:14857915; -.
DR Proteomes; UP000204017; 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.
DR InterPro; IPR001903; Rhabd_glycop.
DR Pfam; PF00974; Rhabdo_glycop; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..523
FT /note="Glycoprotein"
FT /id="PRO_0000287247"
FT TOPO_DOM 21..475
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..523
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT LIPID 497
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 44..307
FT /evidence="ECO:0000250"
FT DISULFID 79..112
FT /evidence="ECO:0000250"
FT DISULFID 88..134
FT /evidence="ECO:0000250"
FT DISULFID 173..178
FT /evidence="ECO:0000250"
FT DISULFID 198..243
FT /evidence="ECO:0000250"
FT DISULFID 238..276
FT /evidence="ECO:0000250"
SQ SEQUENCE 523 AA; 58343 MW; E1D68DC6B54C0522 CRC64;
MTSVLFMVGV LLGAFGSTHC SIQIVFPSET KLVWKPVLKG TRYCPQSAEL NLEPDLKTMA
FDSKVPIGIT PSNSDGYLCH AAKWVTTCDF RWYGPKYITH SVHSLRPTVS DCKAAVEAYN
AGTLMYPGFP PESCGYASIT DSEFYVMLVT PHPVGVDDYR GHWVDPLFPT SECNSNFCET
VHNATMWIPK DLKTHDVCSQ DFQTIRVSVM YPQTKPTKGA DLTLKSKFHA HMKGDRVCKM
KFCNKNGLRL GNGEWIEVGD EVMLDNSKLL SLFPDCLVGS VVKSTLLSEG VQTALWETDR
LLDYSLCQNT WEKIDRKEPL SAVDLSYLAP RSPGKGMAYI VANGSLMSAP ARYIRVWIDS
PILKEIKGKK ESASGIDTVL WEQWLPFNGM ELGPNGLIKT KSGYKFPLYL LGMGIVDQDL
QELSSVNPVD HPHVPIAQAF VSEGEEVFFG DTGVSKNPIE LISGWFSDWK ETAAALGFAA
ISVILIIGLM RLLPLLCRRR KQKKVIYKDV ELNSFDPRQA FHR