GLYCO_COCAV
ID GLYCO_COCAV Reviewed; 512 AA.
AC O56677;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 29-SEP-2021, entry version 71.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Cocal virus (COCV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=50713;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=50557; Insecta.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9696127; DOI=10.1016/s0168-1702(98)00006-9;
RA Bhella R.S., Nichol S.T., Wanas E., Ghosh H.P.;
RT "Structure, expression and phylogenetic analysis of the glycoprotein gene
RT of Cocal virus.";
RL Virus Res. 54:197-205(1998).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AF045556; AAC02712.1; -; Genomic_RNA.
DR RefSeq; YP_009177650.1; NC_028255.1.
DR SMR; O56677; -.
DR GeneID; 26131813; -.
DR KEGG; vg:26131813; -.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..512
FT /note="Glycoprotein"
FT /id="PRO_0000287246"
FT TOPO_DOM 18..468
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..512
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 41..301
FT /evidence="ECO:0000250"
FT DISULFID 76..109
FT /evidence="ECO:0000250"
FT DISULFID 85..131
FT /evidence="ECO:0000250"
FT DISULFID 170..175
FT /evidence="ECO:0000250"
FT DISULFID 194..241
FT /evidence="ECO:0000250"
FT DISULFID 236..270
FT /evidence="ECO:0000250"
SQ SEQUENCE 512 AA; 58030 MW; 9A3AEF403930D8B8 CRC64;
MNFLLLTFIV LPLCSHAKFS IVFPQSQKGN WKNVPSSYHY CPSSSDQNWH NDLLGITMKV
KMPKTHKAIQ ADGWMCHAAK WITTCDFRWY GPKYITHSIH SIQPTSEQCK ESIKQTKQGT
WMSPGFPPQN CGYATVTDSV AVVVQATPHH VLVDEYTGEW IDSQFPNGKC ETEECETVHN
STVWYSDYKV TGLCDATLVD TEITFFSEDG KKESIGKPNT GYRSNYFAYE KGDKVCKMNY
CKHAGVRLPS GVWFEFVDQD VYAAAKLPEC PVGATISAPT QTSVDVSLIL DVERILDYSL
CQETWSKIRS KQPVSPVDLS YLAPKNPGTG PAFTIINGTL KYFETRYIRI DIDNPIISKM
VGKISGSQTE RELWTEWFPY EGVEIGPNGI LKTPTGYKFP LFMIGHGMLD SDLHKTSQAE
VFEHPHLAEA PKQLPEEETL FFGDTGISKN PVELIEGWFS SWKSTVVTFF FAIGVFILLY
VVARIVIAVR YRYQGSNNKR IYNDIEMSRF RK