GP_INSV
ID GP_INSV Reviewed; 1110 AA.
AC Q01260;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Impatiens necrotic spot virus (INSV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Tospoviridae; Orthotospovirus.
OX NCBI_TaxID=11612;
OH NCBI_TaxID=35939; Impatiens.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1585644; DOI=10.1016/0042-6822(92)90528-w;
RA Law M.D., Speck J., Moyer J.W.;
RT "The M RNA of impatiens necrotic spot Tospovirus (Bunyaviridae) has an
RT ambisense genomic organization.";
RL Virology 188:732-741(1992).
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. {ECO:0000250|UniProtKB:P36291}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including Glycoprotein N and Glycoprotein C.
CC {ECO:0000250|UniProtKB:P36291}.
CC -!- PTM: Glycosylated. Glycosylation is essential for proper subcellular
CC location. {ECO:0000250|UniProtKB:P36291}.
CC -!- SIMILARITY: Belongs to the tospovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M74904; AAA46242.1; -; Genomic_RNA.
DR PIR; B42544; B42544.
DR RefSeq; NP_619691.1; NC_003616.1.
DR SMR; Q01260; -.
DR PRIDE; Q01260; -.
DR GeneID; 956573; -.
DR KEGG; vg:956573; -.
DR Proteomes; UP000201303; 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 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT PROPEP 1..8
FT /evidence="ECO:0000255"
FT /id="PRO_0000036868"
FT CHAIN 9..1110
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036869"
FT CHAIN 9..459
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036870"
FT CHAIN 460..1110
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036871"
FT TOPO_DOM 1..321
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..1044
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1091..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..16
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT SITE 459..460
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1110 AA; 124868 MW; B0691F892BAC7F6F CRC64;
MALKETDAKI HVERGDHPEI YDEAYYDRSV DHKNEILDTL AEMLQNATGK TLRPTRDTQT
VLANNEVPQS SSGLSSTPTT ISIMDLPNPC LNASSLTCSI KGVSTFNVYY QVESNGVIYS
CISDTITKLG NCEGSSELPR SFETVPVVPI TKIDNKRKLS IGTKFYIIES LENYNYPIMY
NSRPTNGTVS LQSVKFSGDC KISKTNIVNS YTVSLTTPEK IMGYVVKREG SDMSHSIISF
SGSVSLTFTE ENMDGKHNLL CGDKSSKVPL VDKRVRDCII KYSKNIYKQT ACINFSWFRL
IMIALIVYFP IRYLVNKTSK TLFYGYDLLG LITYPILLLI NYLWSYFPLK CKVCGNLCLV
THECSKLCIC NKNKASEEHS EECPIITRTA EKNKKYNWAS IEWFHLIVNT KIGLSFLKAV
TETLIGFLIL SQMPMSMAQT AQCLDSCYYV PGCDRFVTNR YDKCPEKDQC FCAIKENSIV
ESNFLTNVVT EGPMDCIPYQ ECKGRITENA LVTFVKCRFG CEYASIFQSK PLDNGFLEYS
GDTLGLNAVN LHFMKRLRNG IIDFYNKTEK YGYISGDALK SNESDIPESI FPRKSLIFDS
VIDGKYRYMI EESLLSGGGT VFSLNDKSSS TAQKFVVYIK KVRIQYDVSE QYTTAPIQST
HTDFFSTCTG KCSDCRKEQP ITGYQDFCIT PTSYWGCEEV WCLAINEGAT CGFCRNVYDM
DQSFRIYSVI KSTIKSEVCI SGFVGAKCFT VSEEVPSESG YFQADILADF HNDGLTIGQL
IAHGPDSHVY AGNIARLNNP SKMFGHPQLS HQGDPIFSKK TLDTNDLSWD CSAIGKKTIT
IKSCGYDTYR FKTGLNQISD IPVQFTDQNS FYMEKIFSLG KLKIVLDLPS ELFKTVPKKP
ILSSVSLSCK GCFLCSQGLR CAASFISDIT FSARLTMKQC SLSTYQIAVK KGANKYNLTM
FCTSNPEKQK MIIEPEGDKS YSVEALVDSV AVLEPENIID QNDQHAHEEQ QYNSDTSVWS
FWDYVKSPFN FIASHFGSFF DTVRVVLLIL FVFALAYLCS IVATMCRGYV RNKSYKTKYI
EDTNDYSLVS TSSGKDTITR RRPPLDFSGI
