GP_TSWV
ID GP_TSWV Reviewed; 1135 AA.
AC O55647;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 84.
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 (TSWV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Tospoviridae; Orthotospovirus.
OX NCBI_TaxID=1933298;
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].
RA Ohnishi J., Kirita M., Hosokawa D., Tsuda S.;
RT "Sequence analysis for M RNA segment of tomato spotted wilt tospovirus
RT isolated in Japan.";
RL Nihon Shokubutsu Byori Gakkaiho 63:277-277(1997).
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; AB010996; BAA24894.1; -; Genomic_RNA.
DR PDB; 6Y9L; X-ray; 4.10 A; A/B/C/D=36-323.
DR PDB; 6YA0; X-ray; 2.86 A; A/B/C=36-323.
DR PDB; 6YA2; X-ray; 2.50 A; A/B/C=99-297.
DR PDBsum; 6Y9L; -.
DR PDBsum; 6YA0; -.
DR PDBsum; 6YA2; -.
DR SMR; O55647; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000036856"
FT CHAIN 36..484
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036857"
FT CHAIN 485..1135
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036858"
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"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:6YA2"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6YA0"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6YA2"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6YA2"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 207..220
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 236..251
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:6YA2"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:6YA0"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6YA2"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:6YA2"
SQ SEQUENCE 1135 AA; 127333 MW; BD9977103BE957F2 CRC64;
MRILKLLELV VKVSLFTIAL SSVLLAFLIF RATDAKVEII RGDHPEVYDD SAENEVPTAA
SIQRKAILET LTNLMLESQT PGTRQIREGE SIIPIFAESN TQKTISVSDL PNNCLNASSL
KCEIKGVSTY NVYYQVENNG VIYSCVSDSA EGLEKCDNSL NLPKRFSKVP VIPITKLDNK
RHFSVGTKFF ISESLTQDNY PITYNSYPTN GTVSLQTVKL SGDCKITKSN FANPYTVSIT
SPEKIMGYLI KKPGENVEHK VISFSGSASI TFTEEMLDGE HNLLCGDKSA KIPKTNKRVR
DCIIKYSKSI YKQTAGINFS WIRLILIALL IYFPIRWLVN KTTKPLFLWY DLIGLITYPI
LLLINCLWKY FPFKCSNCGN LCIITHECTK ICICNKSKAS KEHSSECPIL SKETDHGYNK
HKWTSMEWFH LIVNTKLSFS LLKFVTEILI GLIILSQMPM SMAQTTQCLS GCFYVPGCPF
LVTSKFEKCP EKDQCYCNVK EDKIIESIFG TNIVIEGPND CIENQNCAAH PSIDNLIKCR
LGCEYLDLFR NKPLYNGFSD YTGSSLGLTS VGLYEAKRLR NGIIDSYNRT DKISGMIAGD
SLNKNETSIP ENILPRQSLI FDSVVDGKYR YMIEQSLLGG GGTIFMLNDK TSETAKKFVI
YIKSVGIHYE VSEKYTTAPI QSTHTDFYST CTGNCDTCRK NQALTGFQDF CITPTSYWGC
EEAWCFAINE GATCGFCRNI YDMDKSYRIY SVLKSTIVAD VCISGILGGQ CSKITEEVPY
ENALFQADIQ ADLHNDGITI GELIAHGPDS HIYSGNIANL NDPVKMFGHP QLTHDGVPIF
TKKTLEGDDM SWDCAAIGKK SITIKTCGYD TYRFRSGLEQ ISDIPVSFKD FSSFFLEKAF
SLGKLKIVVD LPSDLFKVAP KRPSITSTSL NCNGCLLCGQ GLSCILEFFS DLTFSTAISI
DACSLSTYQL AVKKGSNKYN ITMFCSANPD KKKMTLYPEG NPDISVEVLV NNVIVEEPEN
IIDQNDEYAH EEQQYNSDSS AWGFWDYIKS PFNFIASYFG SFFDTIRVIL LIAFIFLVIY
FCSILTTICK GYVKNESYKS RSKIEDDDDS EIKAPMLMKD TMTRRRPPMD FSHLV
