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Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]

 GP_TSWV1                Reviewed;        1135 AA.
P36291;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=Envelopment polyprotein;
AltName: Full=M polyprotein;
Contains:
RecName: Full=Glycoprotein N {ECO:0000305|PubMed:18973913};
Short=Gn;
AltName: Full=Glycoprotein G1;
Contains:
RecName: Full=Glycoprotein C {ECO:0000305|PubMed:18973913};
Short=Gc;
AltName: Full=Glycoprotein G2;
Flags: Precursor;
Name=GP;
Tomato spotted wilt virus (strain Brazilian Br-01) (TSWV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses; Bunyavirales;
Tospoviridae; Orthotospovirus.
NCBI_TaxID=36413;
NCBI_TaxID=133901; Frankliniella occidentalis (Western flower thrips).
NCBI_TaxID=163899; Scirtothrips dorsalis.
NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
NCBI_TaxID=161014; Thrips tabaci.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1431808; DOI=10.1099/0022-1317-73-11-2795;
Kormelink R., de Haan P., Meurs C., Peters D., Goldbach R.;
"The nucleotide sequence of the M RNA segment of tomato spotted wilt
virus, a bunyavirus with two ambisense RNA segments.";
J. Gen. Virol. 73:2795-2804(1992).
[2]
ERRATUM.
PubMed=8468562;
Kormelink R., de Haan P., Meurs C., Peters D., Goldbach R.;
J. Gen. Virol. 74:790-790(1993).
[3]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, POST-TRANSLATIONAL
MODIFICATIONS, AND SUBCELLULAR LOCATION.
PubMed=11134314; DOI=10.1128/JVI.75.2.1004-1012.2001;
Kikkert M., Verschoor A., Kormelink R., Rottier P., Goldbach R.;
"Tomato spotted wilt virus glycoproteins exhibit trafficking and
localization signals that are functional in mammalian cells.";
J. Virol. 75:1004-1012(2001).
[4]
SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
(GLYCOPROTEIN C).
PubMed=18632951; DOI=10.1099/vir.0.2008/001164-0;
Ribeiro D., Foresti O., Denecke J., Wellink J., Goldbach R.,
Kormelink R.J.;
"Tomato spotted wilt virus glycoproteins induce the formation of
endoplasmic reticulum- and Golgi-derived pleomorphic membrane
structures in plant cells.";
J. Gen. Virol. 89:1811-1818(2008).
[5]
INTERACTION WITH NUCLEOPROTEIN (GLYCOPROTEIN N), AND INTERACTION WITH
NUCLEOPROTEIN (GLYCOPROTEIN C).
PubMed=18973913; DOI=10.1016/j.virol.2008.09.028;
Ribeiro D., Borst J.W., Goldbach R., Kormelink R.;
"Tomato spotted wilt virus nucleocapsid protein interacts with both
viral glycoproteins Gn and Gc in planta.";
Virology 383:121-130(2009).
-!- FUNCTION: Glycoprotein N: Together with Glycoprotein C are present
at the surface of the virion. They are able to attach the virion
to a cell receptor and to promote fusion of membranes after
endocytosis of the virion (By similarity). {ECO:0000250}.
-!- FUNCTION: Glycoprotein C: Together with Glycoprotein N are present
at the surface of the virion. They are able to attach the virion
to a cell receptor and to promote fusion of membranes after
endocytosis of the virion (By similarity). {ECO:0000250}.
-!- SUBUNIT: Glycoprotein N: Interacts with Glycoprotein C and
nucleoprotein. Glycoprotein C: Interacts with Glycoprotein N and
nucleoprotein. {ECO:0000269|PubMed:18973913}.
-!- SUBCELLULAR LOCATION: Glycoprotein N: Virion membrane
{ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18632951}. Host Golgi apparatus membrane
{ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18632951}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18632951}. Note=Glycoprotein C alone is
retained in the membrane of the endoplasmic reticulum, but not
transported to the Golgi. Coexpression of Glycoprotein C and
Glycoprotein N results in efficient transport of Glycoprotein C to
the Golgi complex, indicating that their interaction is essential
for proper targeting to this organelle, where virion budding
occurs. {ECO:0000269|PubMed:18632951}.
-!- SUBCELLULAR LOCATION: Glycoprotein C: Virion membrane
{ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18632951}. Host Golgi apparatus membrane
{ECO:0000269|PubMed:18632951}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18632951}. Note=Glycoprotein G2 is retained in
the Golgi complex and probably contains a Golgi retention signal.
{ECO:0000269|PubMed:18632951}.
-!- DOMAIN: The cell attachment site present in these glycoproteins
may help in the adhesion of virus to cells.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
including Glycoprotein N and Glycoprotein C.
{ECO:0000269|PubMed:11134314}.
-!- PTM: Glycosylated. Glycosylation is essential for proper
subcellular location.
-!- SIMILARITY: Belongs to the tospovirus envelope glycoprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S48091; AAB24089.1; -; Genomic_RNA.
PIR; JQ1928; JQ1928.
ProteinModelPortal; P36291; -.
KEGG; vg:956579; -.
OrthoDB; VOG090000BP; -.
Proteomes; UP000006674; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR005167; Bunya_G1.
InterPro; IPR014414; M_poly_TospoV.
Pfam; PF03557; Bunya_G1; 1.
PIRSF; PIRSF003960; M_poly_TospoV; 1.
1: Evidence at protein level;
Complete proteome;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
Host-virus interaction; Membrane; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 1135 Envelopment polyprotein.
/FTId=PRO_0000036859.
CHAIN 36 484 Glycoprotein N.
/FTId=PRO_0000036860.
CHAIN 485 1135 Glycoprotein C.
/FTId=PRO_0000036861.
TOPO_DOM 36 345 Lumenal. {ECO:0000255}.
TRANSMEM 346 366 Helical. {ECO:0000255}.
TOPO_DOM 367 484 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 485 1067 Lumenal. {ECO:0000255}.
TRANSMEM 1068 1088 Helical. {ECO:0000255}.
TOPO_DOM 1089 1135 Cytoplasmic. {ECO:0000255}.
MOTIF 41 43 Cell attachment site. {ECO:0000255}.
SITE 484 485 Cleavage; by host signal peptidase.
{ECO:0000250}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 980 980 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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


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