GLYCO_IHNVW
ID GLYCO_IHNVW Reviewed; 508 AA.
AC Q82683;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 76.
DE RecName: Full=Glycoprotein;
DE AltName: Full=Spike glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Infectious hematopoietic necrosis virus (strain WRAC) (IHNV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=429314;
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8578857; DOI=10.1016/0168-1702(95)00056-v;
RA Morzunov S.P., Winton J.R., Nichol S.T.;
RT "The complete genome structure and phylogenetic relationship of infectious
RT hematopoietic necrosis virus.";
RL Virus Res. 38:175-192(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}.
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DR EMBL; L40883; AAC42153.1; -; Genomic_RNA.
DR RefSeq; NP_042679.1; NC_001652.1.
DR GeneID; 1489848; -.
DR KEGG; vg:1489848; -.
DR Proteomes; UP000007212; 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; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..508
FT /note="Glycoprotein"
FT /id="PRO_0000282900"
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; 56755 MW; 14E2A706463F3B50 CRC64;
MDTMITTPLI LILITCGANS QTVKPDTASE SDQPTWSNPL FTYPEGCTLD KLSKVNASQL
RCPRIFDDEN RGLIAYPTSI RSLSVGNDLG DIHTQGNHIH KVLYRTICST GFFGGQTIEK
ALVKMKLSTK EAGAYDTTTA AALYFPAPRC QWYTDNVQND LIFYYTTQKS VLRDPYTRDF
LDSDFIGGKC TKSPCQTHWS NVVWMGDAGI PACDSSQEIK AHLFVDKISN RVVKATSYGH
HPWGLHQACM IEFCGQQWIR TDLGDLISVV YNSGSEILSF PKCEDKTVGM RGNLDDFAYL
DDLVKASESR EECLEAHAEI ISTNSVTPYL LSKFRSPHPG INDVYAMHKG SIYHGMCMTV
AVDEVSKDRT TYRAHRATSF TKWERPFGDE WEGFHGLHGN NTTIIPDLEK YVAQYKMSMM
EPMSIKSVPH PSILALYNET DVSGISIRKL DSFDLQSLHW SFWPTISALG GIPFVLLLAV
AACCCWSGRP PTPSVPQSIP MYHLANRS