GP_TSWV1
ID GP_TSWV1 Reviewed; 1135 AA.
AC P36291;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000305|PubMed:18973913};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000305|PubMed:18973913};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Tomato spotted wilt virus (strain Brazilian Br-01) (TSWV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Tospoviridae; Orthotospovirus.
OX NCBI_TaxID=36413;
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=1431808; DOI=10.1099/0022-1317-73-11-2795;
RA Kormelink R., de Haan P., Meurs C., Peters D., Goldbach R.;
RT "The nucleotide sequence of the M RNA segment of tomato spotted wilt virus,
RT a bunyavirus with two ambisense RNA segments.";
RL J. Gen. Virol. 73:2795-2804(1992).
RN [2]
RP ERRATUM OF PUBMED:1431808.
RX PubMed=8468562; DOI=10.1099/0022-1317-74-4-790;
RA Kormelink R., de Haan P., Meurs C., Peters D., Goldbach R.;
RL J. Gen. Virol. 74:790-790(1993).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, POST-TRANSLATIONAL MODIFICATIONS,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11134314; DOI=10.1128/jvi.75.2.1004-1012.2001;
RA Kikkert M., Verschoor A., Kormelink R., Rottier P., Goldbach R.;
RT "Tomato spotted wilt virus glycoproteins exhibit trafficking and
RT localization signals that are functional in mammalian cells.";
RL J. Virol. 75:1004-1012(2001).
RN [4]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
RP (GLYCOPROTEIN C).
RX PubMed=18632951; DOI=10.1099/vir.0.2008/001164-0;
RA Ribeiro D., Foresti O., Denecke J., Wellink J., Goldbach R.,
RA Kormelink R.J.;
RT "Tomato spotted wilt virus glycoproteins induce the formation of
RT endoplasmic reticulum- and Golgi-derived pleomorphic membrane structures in
RT plant cells.";
RL J. Gen. Virol. 89:1811-1818(2008).
RN [5]
RP INTERACTION WITH NUCLEOPROTEIN (GLYCOPROTEIN N), AND INTERACTION WITH
RP NUCLEOPROTEIN (GLYCOPROTEIN C).
RX PubMed=18973913; DOI=10.1016/j.virol.2008.09.028;
RA Ribeiro D., Borst J.W., Goldbach R., Kormelink R.;
RT "Tomato spotted wilt virus nucleocapsid protein interacts with both viral
RT glycoproteins Gn and Gc in planta.";
RL Virology 383:121-130(2009).
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:0000269|PubMed:18973913}.
CC -!- SUBUNIT: [Glycoprotein C]: Interacts with Glycoprotein N and
CC nucleoprotein. {ECO:0000269|PubMed:18973913}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18632951}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18632951}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18632951}. Note=Glycoprotein C alone is retained in
CC the membrane of the endoplasmic reticulum, but not transported to the
CC 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:0000269|PubMed:18632951}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18632951}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18632951}. Note=Glycoprotein G2 is retained in the
CC Golgi complex and probably contains a Golgi retention signal.
CC {ECO:0000269|PubMed:18632951}.
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 N and Glycoprotein C.
CC {ECO:0000269|PubMed:11134314}.
CC -!- PTM: Glycosylated. Glycosylation is essential for proper subcellular
CC location.
CC -!- SIMILARITY: Belongs to the tospovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; S48091; AAB24089.1; -; Genomic_RNA.
DR PIR; JQ1928; JQ1928.
DR PDB; 6Y9M; X-ray; 3.40 A; A/B/C/D=36-319.
DR PDBsum; 6Y9M; -.
DR SMR; P36291; -.
DR Proteomes; UP000006674; Genome.
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; Reference proteome; Signal;
KW Transmembrane; 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_0000036859"
FT CHAIN 36..484
FT /note="Glycoprotein N"
FT /id="PRO_0000036860"
FT CHAIN 485..1135
FT /note="Glycoprotein C"
FT /id="PRO_0000036861"
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 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 HELIX 112..115
FT /evidence="ECO:0007829|PDB:6Y9M"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6Y9M"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 207..220
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6Y9M"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:6Y9M"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6Y9M"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:6Y9M"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:6Y9M"
SQ SEQUENCE 1135 AA; 127318 MW; AC1A3FFFE84044FB CRC64;
MRILKLLELV VKVSLFTIAL SSVLLAFLIF RATDAKVEII RGDHPEIYDD SAENEVPTAA
SIQREAILET LTNLMLESRT PGTRQIREEK STIPISAEPT TQKTISVLDL PNNCLNASSL
KCEIKGISTY NVYYQVENNG VIYSCVSDSA EGLEKCDNSL NLPKRFSKVP VIPITKLDKK
RHFSVGGKFF ISESLTQDNY PITYNSYPTN GTVSLQTVKL SGDCKITKSN FANPYTVSIT
SPEKIMGYLI KKPGENVEHK VISFSGSASI TFTEEMLDGE HNLLCGDKSA KIPKTNKRVR
DCIIKYSKSI YKQTACINFS WIRLILIALL IYFPIRWLVN KTTKPLFLWY DLMGLITYPV
LLLINCLWKY FPLKCSNCGN LCIVTHECTK VCICNKSKAS KEHSSECPIL SKEADHDYNK
HKWTSMEWFH LIVNTKLSLS LLKFVTEILI GLVILSQMPM SMAQTTQCLS GCFYVPGCPF
LVTSKFEKCS EKDQCYCNVK EDKIIESIFG TNIVIEGPND CIENQNCIAR PSIDNLIKCR
LGCEYLDLFR NKPLYNGFSD YTGSSLGLTS VGLYEAKRLR NGIIDSYNRQ GKISGMVAGD
SLNKNETSIP ENILPRQSLI FDSVVDGKYR YMIEQSLLGG GGTIFMLNDK TSETAKKFVI
YIKSVGIHYE VSEKYTTAPI QSTHTDFYST CTGNCDTCRK NQALTGFQDF CVTPTSYWGC
EEAWCFAINE GATCGFCRNI YDMDKSYRIY SVLKSTIVAD VCISGILGGQ CSRITEEVPY
ENTLFQADIQ ADLHNDGITI GELIAHGPDS HIYSGNIANL NDPVKMFGHP QLTHDGVPIF
TKKTLEGDDM SWDCAAIGKK SVTIKTCGYD TYRFRSGLEQ ISDIPVSFKD FSSFFLAKSF
SLGKLKMVVD LPSDLFKVAP KKPSITSTSL NCNGCLLCGQ GLSCLLEFFS DLTFSTAISI
DACSLSTYQL AVKKGSNKYN ITMFCSANPD KKKMTLYPEG NPDISVEVLV NNVIVEEPEN
IIDQNDEYAH EEQQYNSDSS AWGFWDYIKS PFNFIASYFG SFFDTIRVVL LIAFIFLVTY
FCSILTSICK GYVKNESYKS RSKIEDDDEP EIKAPMLMKD TMTRRRPPMD FSHLV
