ID   GLYCO_IHNVO             Reviewed;         508 AA.
AC   Q82706;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glycoprotein;
DE   AltName: Full=Spike glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Infectious hematopoietic necrosis virus (strain Oregon69) (IHNV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC   Novirhabdovirus.
OX   NCBI_TaxID=429315;
OH   NCBI_TaxID=8028; Salmo.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8683214; DOI=10.1099/0022-1317-77-6-1259;
RA   Schutze H., Enzmann P.J., Mundt E., Mettenleiter T.C.;
RT   "Identification of the non-virion (NV) protein of fish rhabdoviruses viral
RT   haemorrhagic septicaemia virus and infectious haematopoietic necrosis
RT   virus.";
RL   J. Gen. Virol. 77:1259-1263(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7595355; DOI=10.1099/0022-1317-76-10-2519;
RA   Schutze H., Enzmann P.J., Kuchling R., Mundt E., Niemann H.,
RA   Mettenleiter T.C.;
RT   "Complete genomic sequence of the fish rhabdovirus infectious
RT   haematopoietic necrosis virus.";
RL   J. Gen. Virol. 76:2519-2527(1995).
CC   -!- FUNCTION: Binds to specific receptor at cellular surface, bringing
CC       about the attachment of the virus particle to the cell. Plays a major
CC       role in the determination of host range restriction and virulence.
CC       Class I viral fusion protein. Responsible for penetration of the viral
CC       nucleocapsid into the cell cytoplasm by mediating the fusion of the
CC       membrane of the endocytosed virus particle with the endosomal membrane.
CC       Low pH in endosomes induce an irreversible conformational change in G,
CC       releasing a fusion hydrophobic peptide (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the novirhabdovirus glycoprotein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X89213; CAA61498.1; -; Genomic_RNA.
DR   Proteomes; UP000007211; 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   InterPro; IPR002417; Spike_prot.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
DR   PRINTS; PR00796; SPIKEPROTEIN.
PE   3: Inferred from homology;
KW   Glycoprotein; Host-virus interaction; Membrane; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..508
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000282899"
FT   TOPO_DOM        21..461
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        483..508
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   508 AA;  56629 MW;  FFD518E5BFF6A260 CRC64;
     MDTTITTPLI LILITCGANS QTVKPDTASE SDQPTWSNPL FTYPEGCTLD KLSKVNASQL
     RCPRIFDDEN RGLIAYPTSI RSLSVGNDLG DIHTQGNHIH KVLYRTICST GFFGGQTIEK
     ALVEMKLSTK EAGAYDTTTA AALYFPAPRC QWYTDNVQND LIFYYTTQKS VLRDPYTRDF
     LDSDFIGGKC TKSPCQTHWS NVVWMGDAGI PACDSSQEIK GHLFVDKISN RVVKATSYGH
     HPWGLHQACM IEFCGKQWIR TDLGDLISVE YNSGAEILSF PKCEDKTVGM RGNLDDFAYL
     DDLVKASESR EECLEAHAEI ISTNSVTPYL LSKFRSPHPG INDVYAMHKG SIYHGMCMTV
     AVDEVSKDRT TYRAHRATSF TKWERPFGDE WEGFHGLHGN NTTIIPDLEK YVAQYKTSMM
     EPMSIKSVPH PSILALYNET DVSGISIRKL DSFDLQSLHW SFWPTISALG GIPFALLLAV
     AACCCWSGRP PTPSASQSIP MYHLANRS