GLYCO_IHNVR
ID GLYCO_IHNVR Reviewed; 508 AA.
AC P07923;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Glycoprotein;
DE AltName: Full=Spike glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Infectious hematopoietic necrosis virus (strain Round Butte) (IHNV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=11291;
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3033264; DOI=10.1128/jvi.61.5.1342-1349.1987;
RA Koener J.F., Passavant C.W., Kurath G., Leong J.-A.;
RT "Nucleotide sequence of a cDNA clone carrying the glycoprotein gene of
RT infectious hematopoietic necrosis virus, a fish rhabdovirus.";
RL J. Virol. 61:1342-1349(1987).
RN [2]
RP SEQUENCE REVISION.
RA Leong J.-A.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; M16023; AAB59926.1; -; Genomic_RNA.
DR PIR; A29532; VGVNFR.
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 CHAIN 21..508
FT /note="Glycoprotein"
FT /id="PRO_0000040991"
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; 56800 MW; CF65376C626FE89B CRC64;
MDTMITTPLI LILITCGANS QTVKPDTASE SDQPTWSNPL FTYPEGCTLD KLSKVNASQL
RCPRIFDDEN RGLIAYPTSI RSLSVGNDLG EIHTQGNHIH KVLYRTICST GFFGGQTIEK
ALVEMKLSTK EAGAYDTTTA AALYFPAPRC QWYTDNVQND LIFYYTTQKS VLRDPYTRDF
LDSDFIGGKC TKSPCQTHWS NVVWMGDAGI PACDSSQEIK AHLFVDKISN RVVKATSYGH
HPWGLHRACM IEFCGKQWIR TDLGDLISVE YNSGAEILSF PKCEDKTMGM RGNLDDFAYL
DDLVKASESR EECLEAHAEI ISTNSVTPYL LSKFRSPHPG INDVYAMHKG SIYHGMCMTV
AVDEVSKDRT TYRAHRATSF TKWERPFGDE WEGFHGLHGN NTTIIPDLEK YVAQYKTSMM
EPMSIKSVPH PSILAFYNET DLSGISIRKL DSFDLQSLHW SFWPTISALG GIPLVLLLAV
AACCCWSGRP PTPSAPQSIP MYHLANRS