ID   GLYCO_SVCV              Reviewed;         509 AA.
AC   Q91DS0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   29-SEP-2021, entry version 76.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Spring viremia of carp virus (Rhabdovirus carpia).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Sprivivirus.
OX   NCBI_TaxID=696863;
OH   NCBI_TaxID=7962; Cyprinus carpio (Common carp).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Fijan reference;
RX   PubMed=11900842; DOI=10.1016/s0168-1702(01)00441-5;
RA   Hoffmann B., Schutze H., Mettenleiter T.C.;
RT   "Determination of the complete genomic sequence and analysis of the gene
RT   products of the virus of Spring Viremia of Carp, a fish rhabdovirus.";
RL   Virus Res. 84:89-100(2002).
CC   -!- FUNCTION: Attaches the virus to host receptors, inducing clathrin-
CC       dependent endocytosis of the virion. {ECO:0000250|UniProtKB:P03522}.
CC   -!- FUNCTION: In the endosome, the acidic pH induces conformational changes
CC       in the glycoprotein trimer, which trigger fusion between virus and
CC       endosomal membrane. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03522};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}.
CC       Host membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:P03522}. Note=The cytoplasmic
CC       domain sorts the protein to neurons dentrites instead of axons. When
CC       expressed in ex vivo polarized cells like epithelial cells, it sorts
CC       the protein to the basolateral side. {ECO:0000250|UniProtKB:P03522}.
CC   -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ318079; CAC51336.1; -; Genomic_RNA.
DR   SMR; Q91DS0; -.
DR   Proteomes; UP000007541; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
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   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..509
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000287249"
FT   TOPO_DOM        19..461
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        483..509
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   MOTIF           496..505
FT                   /note="basolateral targeting ex vivo"
FT                   /evidence="ECO:0000250|UniProtKB:P03522"
FT   LIPID           488
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
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:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..302
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        195..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        236..271
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  57443 MW;  5C7B8BF10494A30B CRC64;
     MSIISYIAFL LLIDSNLGIP IFVPSGRNIS WQPVIQPFDY QCPIHGNLPN TMGLSATKLT
     IKSPSVFSTD KVSGWICHAA EWKTTCDYRW YGPQYITHSI HPISPTIDEC RRIIQRIASG
     TDEDLGFPPQ SCGWASVTTV SNTNYRVVPH SVHLEPYGGH WIDHEFNGGE CREKVCEMKG
     NHSIWITEET VQHECAKHIE EVEGIMYGNV PRGDVMYANN FIIDRHHRVY RFGGSCQMKF
     CNKDGIKFAR GDWVEKTAGT LTTIHDNVPK CVDGTLVSGH RPGLDLIDTV FNLENVVEYT
     LCEGTKRKIN KQEKLTSVDL SYLAPRIGGF GSVFRVRNGT LERGSTTYIR IEVEGPIVDS
     LNGTDPRTNA SRVFWDDWEL DGNIYQGFNG VYKGKDGKIH IPLNMIESGI IDDELQHAFQ
     TDIIPHPHYD DDEIREDDIF FDNTGENGNP VDAVVEWVSG WGTSLKFFGM TLVALILIFL
     LIRCCVACTY LMKRSKRPAT ESHEMRSLV