GLYC_EMARV
ID GLYC_EMARV Reviewed; 646 AA.
AC Q6Q304;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 02-DEC-2020, entry version 43.
DE RecName: Full=Envelope glycoprotein;
DE Short=GP;
DE Contains:
DE RecName: Full=Glycoprotein G2;
DE Contains:
DE RecName: Full=Glycoprotein G1;
DE Flags: Precursor;
OS European mountain ash ringspot-associated virus (isolate Sorbus aucuparia)
OS (EMARAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Fimoviridae; Emaravirus.
OX NCBI_TaxID=1980426;
OH NCBI_TaxID=483436; Eriophyes pyri (pearleaf blister mite).
OH NCBI_TaxID=36599; Sorbus aucuparia (European mountain ash) (Rowan).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15449143; DOI=10.1007/s00705-004-0397-5;
RA Benthack W., Mielke N., Buttner C., Muhlbach H.P.;
RT "Double-stranded RNA pattern and partial sequence data indicate plant virus
RT infection associated with the ringspot disease of European mountain ash
RT (Sorbus aucuparia L.).";
RL Arch. Virol. 150:37-52(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17374780; DOI=10.1099/vir.0.82715-0;
RA Mielke N., Muehlbach H.P.;
RT "A novel, multipartite, negative-strand RNA virus is associated with the
RT ringspot disease of European mountain ash (Sorbus aucuparia L.).";
RL J. Gen. Virol. 88:1337-1346(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mielke N., Muehlbach H.-P.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycoprotein G2 and glycoprotein G1 interact with each other
CC and are present at the surface of the virion. They are able to attach
CC the virion to a cell receptor and to promote fusion of membranes after
CC endocytosis of the virion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: G2 and G1 interact with each other. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000305}.
CC Host Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000305}.
CC Host Golgi apparatus membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including glycoprotein G1 and glycoprotein G2.
CC -!- PTM: Glycosylated. Glycosylation is essential for proper subcellular
CC location.
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DR EMBL; AY563041; AAS73288.2; -; mRNA.
DR RefSeq; YP_003104765.1; NC_013106.1.
DR GeneID; 8355988; -.
DR KEGG; vg:8355988; -.
DR Proteomes; UP000006676; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
PE 2: Evidence at transcript level;
KW Glycoprotein; Host Golgi apparatus; Host membrane; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Virion.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..646
FT /note="Envelope glycoprotein"
FT /id="PRO_0000395601"
FT CHAIN 26..197
FT /note="Glycoprotein G2"
FT /id="PRO_0000395602"
FT CHAIN 198..646
FT /note="Glycoprotein G1"
FT /id="PRO_0000395603"
FT TOPO_DOM 26..119
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..588
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 197..198
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 74280 MW; 21849E40CA7824FE CRC64;
MLSVAQSSAL FLLQAICILY ITKLTIPTPV SEINLVRQSD CVCVPIISRS GTDYITCFNN
CQIEPINTKL YNSTCTKMVN ITLVRCNNEV YVMTLPNLVS NRSHSWEVLI NYLLRFISAI
IVYLLLSISK QGIFLFFSIV HYSFKFIKNK KSCNICGNDF YFIHIDCPKP DFTKRSDFHM
MFYIILFLSL FFVVTHADDN VYNYYEHGDL TEIQLLDKEH YSQDFVSDGF LYNFYVENSH
LIYDISNIST ITRPVKHNEV TSTWSCDGSS GCYKDHVGKY NKKPDYVLKK VHDGFSCFFT
TATICGTCKS EHIAIGDHVR VINVKPYIHI VVKTANKTDK IVIDEFNKFI HEPYYIKPIT
QIHIDQHDFL VTGSKVYQGT FCERPSKSCF GPNYITSDKT VTLHEPKIRD TFTHDREYII
DYCDYPSNSD LESLELTDMV HHSDKIYSPY DFGLISIGIP KLGYLAGGFC ESLVSVKKIE
VYGCYDCQNG VKISVTYESS DSCHTLICKH DSTTHRYFVQ QHTTTLNFHS FMSKKDTIIE
CNQMRKALNL DESSETSVYF ESNGVKGSAK EPVNFDFIKN LLYIDYKKII FVFLVAIISI
GIFLRSPYML LSSILKFRKR RKVVATNRSE QLVMDDDVDV FIGPPS
