GP_TSWVD
ID GP_TSWVD Reviewed; 1135 AA.
AC Q9IKB7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P36291};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P36291};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Tomato spotted wilt virus (isolate D) (TSWV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Tospoviridae; Orthotospovirus.
OX NCBI_TaxID=267288;
OH NCBI_TaxID=133901; Frankliniella occidentalis (Western flower thrips) (Euthrips occidentalis).
OH NCBI_TaxID=163899; Scirtothrips dorsalis (Chilli thrips).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=161014; Thrips tabaci.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11204788; DOI=10.1094/mpmi.2001.14.2.242;
RA Hoffmann K., Qiu W.P., Moyer J.W.;
RT "Overcoming host- and pathogen-mediated resistance in tomato and tobacco
RT maps to the M RNA of Tomato spotted wilt virus.";
RL Mol. Plant Microbe Interact. 14:242-249(2001).
CC -!- FUNCTION: [Glycoprotein N]: Together with Glycoprotein C are present at
CC the surface of the virion. They are able to attach the virion to a cell
CC receptor and to promote fusion of membranes after endocytosis of the
CC virion (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Glycoprotein C]: Together with Glycoprotein N are present at
CC the surface of the virion. They are able to attach the virion to a cell
CC receptor and to promote fusion of membranes after endocytosis of the
CC virion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: [Glycoprotein N]: Interacts with Glycoprotein C and
CC nucleoprotein. {ECO:0000250|UniProtKB:P36291}.
CC -!- SUBUNIT: [Glycoprotein C]: Interacts with Glycoprotein N and
CC nucleoprotein. {ECO:0000250|UniProtKB:P36291}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P36291}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P36291}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P36291}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P36291}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P36291}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P36291}. Note=Glycoprotein C alone is retained
CC in the membrane of the endoplasmic reticulum, but not transported to
CC the Golgi. Coexpression of Glycoprotein C and Glycoprotein N results in
CC efficient transport of Glycoprotein C to the Golgi complex, indicating
CC that their interaction is essential for proper targeting to this
CC organelle, where virion budding occurs. {ECO:0000250|UniProtKB:P36291}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P36291}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P36291}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P36291}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P36291}. Note=Glycoprotein G2 is retained in the
CC Golgi complex and probably contains a Golgi retention signal.
CC {ECO:0000250|UniProtKB:P36291}.
CC -!- DOMAIN: The cell attachment site present in these glycoproteins may
CC help in the adhesion of virus to cells.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including glycoprotein G1 and glycoprotein G2. {ECO:0000250}.
CC -!- PTM: Glycosylated. Glycosylation is essential for proper subcellular
CC location (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tospovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AF208497; AAF80979.1; -; Genomic_RNA.
DR SMR; Q9IKB7; -.
DR PRIDE; Q9IKB7; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
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; IPR005167; Bunya_G1.
DR InterPro; IPR014414; M_poly_TospoV.
DR Pfam; PF03557; Bunya_G1; 1.
DR PIRSF; PIRSF003960; M_poly_TospoV; 1.
PE 3: Inferred from homology;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1135
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036862"
FT CHAIN 36..484
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036863"
FT CHAIN 485..1135
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036864"
FT TOPO_DOM 36..345
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..1067
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1068..1088
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1089..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 41..43
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT SITE 484..485
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1135 AA; 127554 MW; 53F271999CABEC33 CRC64;
MRILKLLELV VKVSLFTIAL SSVLLAFLTF RATDAKVEII RGDHPEIYDD SAENEVPTAA
SIQREAILET LTNLVLESRT PGTRQIREEK LTIPISTEPA TQKTISVLDL PNNCLNASSL
KCEIKGISTY NVYYQVENNG VIYSSVSDSA EGLEKCDNSL NLPKRFSKVP VIPITKLDNK
RHFSVGTNFF IPESLTQDNY PITYNSYPTN GTVSLQTVKL SGDCKITKSN FANPYTVSIT
SPEKIMGYLI KKPGENVEHK VIAFSGSASI TFTEEMLDGE HNLLCGDKSA KIPKTNKRVR
DCIIKYSKSI YKQTACINFS WIRLILIALL IYFPIRWLVN KTTKPLFLWY DLMGLITYPV
LLLINCLWKY FPFKCSNCGN LCIVTRECTK VCICNKSKAS KEHSSECPIL SKEADHDYNK
HKWTSMEWFH LIVNTKLSLS LLKFVTEILI GLVILSQIPM SMAQTTQCLS GCFYVPGCPF
LVTSKFEKCP EKDQCYCNVK EDKIIESIFG TNIVIEGPND CIENQNCIAR PSIDNLIKCR
LGCEYLDLFQ NKPLYNGFSD YTESSLGLTS VGLYEAKRLR NGIIDSYNRT DKISGMIAGD
SLDKNETSIP ENILPRQSLI FDSVVDGKYR YMIEQSLLGG GGTIFMLNDK TSETAKKFVI
YIKSVGIHHE VSEEYTTAPI QSTHTDFYPT CIGNCDTCRK NQALTGFQDF CITPTSYWGC
EEAWCFAINE GATCGFCRNI YDIDKSYRIY SVLKSTIVAD VCISGILGGQ CSRITEEVPY
ENTLFQADIQ SDLHNDGITI GELIAHGPDS HIYSGNIANL NDPVKMFGHP QLTHDGVPIF
TKKTLEGDDM SWDCAATGKK SVTIKTCGYD TYRFRSGLEQ ISDIPVSFKD FSSFFLEKSF
SLGELKIVVD LPSDLFKVVP KKPSITSTSL NCNGCLLCGQ GLSCILEFFS DLTFSTAISI
DACSLSTYQL AVKKGSNKYN ITMFCSANPD KKKMTLYPEG NPDIPVEVLV NNVIIEEPEN
IIDQNDEYAH EEQQYNSDSS AWGFWDYIKS PFNFIASYFG SFFDTIRVVL LIAFIFLVIY
FCSILTSICK GYVKHKSYKS RSKIEDDDEP EIKAPMLMKD TMTRRRPPMD FSHLV
