GP_RVFVZ
ID GP_RVFVZ Reviewed; 1197 AA.
AC P21401; A2T075;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=NSm-Gn protein {ECO:0000303|PubMed:26038497};
DE AltName: Full=p78;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000303|PubMed:22710362};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000303|PubMed:22710362};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Rift valley fever virus (strain ZH-548 M12) (RVFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX NCBI_TaxID=11589;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=297284; Bos taurus x Bison bison (beefalo).
OH NCBI_TaxID=9837; Camelus bactrianus (Bactrian camel).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2705307; DOI=10.1016/0042-6822(89)90171-2;
RA Takehara K., Min M.K., Battles J.K., Sugiyama K., Emery V.C.,
RA Dalrymple J.M., Bishop D.H.L.;
RT "Identification of mutations in the M RNA of a candidate vaccine strain of
RT Rift Valley fever virus.";
RL Virology 169:452-457(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17192303; DOI=10.1128/JVI.02095-06;
RA Bird B.H., Khristova M.L., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Complete genome analysis of 33 ecologically and biologically diverse Rift
RT Valley fever virus strains reveals widespread virus movement and low
RT genetic diversity due to recent common ancestry.";
RL J. Virol. 81:2805-2816(2007).
RN [3]
RP SUBCELLULAR LOCATION (NSM-GN PROTEIN).
RX PubMed=3046119; DOI=10.1016/0042-6822(88)90174-2;
RA Wasmoen T.L., Kakach L.T., Collett M.S.;
RT "Rift Valley fever virus M segment: cellular localization of M segment-
RT encoded proteins.";
RL Virology 166:275-280(1988).
RN [4]
RP GLYCOSYLATION (GLYCOPROTEIN N), AND GLYCOSYLATION (GLYCOPROTEIN D).
RX PubMed=2728348; DOI=10.1016/0042-6822(89)90442-x;
RA Kakach L.T., Suzich J.A., Collett M.S.;
RT "Rift Valley fever virus M segment: phlebovirus expression strategy and
RT protein glycosylation.";
RL Virology 170:505-510(1989).
RN [5]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
RP (GLYCOPROTEIN C).
RX PubMed=12414959; DOI=10.1128/jvi.76.23.12200-12210.2002;
RA Gerrard S.R., Nichol S.T.;
RT "Characterization of the Golgi retention motif of Rift Valley fever virus
RT G(N) glycoprotein.";
RL J. Virol. 76:12200-12210(2002).
RN [6]
RP PROTEOLYTIC CLEAVAGE (ENVELOPMENT POLYPROTEIN).
RX PubMed=16963099; DOI=10.1016/j.virol.2006.08.002;
RA Gerrard S.R., Nichol S.T.;
RT "Synthesis, proteolytic processing and complex formation of N-terminally
RT nested precursor proteins of the Rift Valley fever virus glycoproteins.";
RL Virology 357:124-133(2007).
RN [7]
RP STRUCTURE BY ELECTRON CRYOMICROSCOPY OF THE VIRAL PARTICLE, FUNCTION
RP (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=18715915; DOI=10.1128/jvi.01191-08;
RA Freiberg A.N., Sherman M.B., Morais M.C., Holbrook M.R., Watowich S.J.;
RT "Three-dimensional organization of Rift Valley fever virus revealed by
RT cryoelectron tomography.";
RL J. Virol. 82:10341-10348(2008).
RN [8]
RP INTERACTION WITH PROTEIN N AND POLYMERASE L (GLYCOPROTEIN N), FUNCTION
RP (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION (GLYCOPROTEIN N).
RX PubMed=21445316; DOI=10.1371/journal.pone.0018070;
RA Piper M.E., Sorenson D.R., Gerrard S.R.;
RT "Efficient cellular release of Rift Valley fever virus requires genomic
RT RNA.";
RL PLoS ONE 6:E18070-E18070(2011).
RN [9]
RP GLYCOSYLATION (GLYCOPROTEIN N), GLYCOSYLATION (GLYCOPROTEIN C), FUNCTION
RP (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
RA Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
RA Helenius A.;
RT "DC-SIGN as a receptor for phleboviruses.";
RL Cell Host Microbe 10:75-88(2011).
RN [10]
RP REVIEW.
RX PubMed=22710362; DOI=10.1016/j.antiviral.2012.06.001;
RA Ikegami T.;
RT "Molecular biology and genetic diversity of Rift Valley fever virus.";
RL Antiviral Res. 95:293-310(2012).
RN [11]
RP FUNCTION (ISOFORM NSM PROTEIN), AND SUBCELLULAR LOCATION (ISOFORM NSM
RP PROTEIN).
RX PubMed=23097454; DOI=10.1128/jvi.02192-12;
RA Terasaki K., Won S., Makino S.;
RT "The C-terminal region of Rift Valley fever virus NSm protein targets the
RT protein to the mitochondrial outer membrane and exerts antiapoptotic
RT function.";
RL J. Virol. 87:676-682(2013).
RN [12]
RP FUNCTION (ISOFORM NSM PROTEIN), FUNCTION (NSM-GN PROTEIN), AND ALTERNATIVE
RP INITIATION.
RX PubMed=26038497; DOI=10.1038/emi.2014.71;
RA Kreher F., Tamietti C., Gommet C., Guillemot L., Ermonval M.,
RA Failloux A.B., Panthier J.J., Bouloy M., Flamand M.;
RT "The Rift Valley fever accessory proteins NSm and P78/NSm-GN are distinct
RT determinants of virus propagation in vertebrate and invertebrate hosts.";
RL Emerg. Microbes Infect. 3:E71-E71(2014).
RN [13]
RP FUNCTION (NSM-GN PROTEIN), AND SUBCELLULAR LOCATION (NSM-GN PROTEIN).
RC STRAIN=ZH-501;
RX PubMed=24489907; DOI=10.1371/journal.pone.0087385;
RA Weingartl H.M., Zhang S., Marszal P., McGreevy A., Burton L., Wilson W.C.;
RT "Rift Valley fever virus incorporates the 78 kDa glycoprotein into virions
RT matured in mosquito C6/36 cells.";
RL PLoS ONE 9:E87385-E87385(2014).
RN [14]
RP INTERACTION WITH HOST LRP1.
RX PubMed=34559985; DOI=10.1016/j.cell.2021.09.001;
RA Ganaie S.S., Schwarz M.M., McMillen C.M., Price D.A., Feng A.X., Albe J.R.,
RA Wang W., Miersch S., Orvedahl A., Cole A.R., Sentmanat M.F., Mishra N.,
RA Boyles D.A., Koenig Z.T., Kujawa M.R., Demers M.A., Hoehl R.M., Moyle A.B.,
RA Wagner N.D., Stubbs S.H., Cardarelli L., Teyra J., McElroy A., Gross M.L.,
RA Whelan S.P.J., Doench J., Cui X., Brett T.J., Sidhu S.S., Virgin H.W.,
RA Egawa T., Leung D.W., Amarasinghe G.K., Hartman A.L.;
RT "Lrp1 is a host entry factor for Rift Valley fever virus.";
RL Cell 184:5163-5178.e24(2021).
RN [15]
RP INTERACTION WITH HOST E3 UBIQUITIN-PROTEIN LIGASE UBR4 (GLYCOPROTEIN N).
RC STRAIN=MP12, and ZH548;
RX PubMed=35032865; DOI=10.1016/j.virol.2021.12.010;
RA Bracci N., de la Fuente C., Saleem S., Pinkham C., Narayanan A.,
RA Garcia-Sastre A., Balaraman V., Richt J.A., Wilson W., Kehn-Hall K.;
RT "Rift Valley fever virus Gn V5-epitope tagged virus enables identification
RT of UBR4 as a Gn interacting protein that facilitates Rift Valley fever
RT virus production.";
RL Virology 567:65-76(2022).
RN [16] {ECO:0007744|PDB:6I9I}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 154-469 IN COMPLEX WITH A
RP NEUTRALIZING ANTIBODY.
RX PubMed=30590046; DOI=10.1016/j.celrep.2018.12.001;
RA Allen E.R., Krumm S.A., Raghwani J., Halldorsson S., Elliott A.,
RA Graham V.A., Koudriakova E., Harlos K., Wright D., Warimwe G.M.,
RA Brennan B., Huiskonen J.T., Dowall S.D., Elliott R.M., Pybus O.G.,
RA Burton D.R., Hewson R., Doores K.J., Bowden T.A.;
RT "A Protective Monoclonal Antibody Targets a Site of Vulnerability on the
RT Surface of Rift Valley Fever Virus.";
RL Cell Rep. 25:3750-3758.E4(2018).
RN [17] {ECO:0007744|PDB:6F8P, ECO:0007744|PDB:6F9B, ECO:0007744|PDB:6F9C, ECO:0007744|PDB:6F9D, ECO:0007744|PDB:6F9E, ECO:0007744|PDB:6F9F}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 154-469 AND 691-1118, FUNCTION
RP (GLYCOPROTEIN N), FUNCTION (GLYCOPROTEIN C), SUBUNIT (GLYCOPROTEIN N),
RP SUBUNIT (GLYCOPROTEIN C), AND DISULFIDE BONDS.
RX PubMed=29367607; DOI=10.1038/s41467-017-02789-2;
RA Halldorsson S., Li S., Li M., Harlos K., Bowden T.A., Huiskonen J.T.;
RT "Shielding and activation of a viral membrane fusion protein.";
RL Nat. Commun. 9:349-349(2018).
CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that
CC interacts with glycoprotein C (PubMed:18715915). It shields the
CC hydrophobic fusion loops of the glycoprotein C, preventing premature
CC fusion (PubMed:29367607). The glycoprotein protrusions are arranged on
CC an icosahedral lattice, with T=12 triangulation (PubMed:18715915,
CC PubMed:29367607). They are able to attach the virion to the host cell
CC receptor CD209/DC-SIGN and to promote fusion of membranes with the late
CC endosome after endocytosis of the virion (PubMed:21767814). Plays a
CC role in the packaging of ribonucleoproteins and polymerase during virus
CC assembly (PubMed:21445316). {ECO:0000269|PubMed:18715915,
CC ECO:0000269|PubMed:21445316, ECO:0000269|PubMed:21767814,
CC ECO:0000269|PubMed:29367607}.
CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that
CC interacts with glycoprotein N (PubMed:18715915). Acts as a class II
CC fusion protein that is activated upon acidification and subsequent
CC repositioning of the glycoprotein N (PubMed:29367607). The glycoprotein
CC protrusions are arranged on an icosahedral lattice, with T=12
CC triangulation (PubMed:18715915, PubMed:29367607). They are able to
CC attach the virion to the host cell receptor CD209/DC-SIGN and to
CC promote fusion of membranes with the late endosome after endocytosis of
CC the virion (PubMed:21767814). {ECO:0000269|PubMed:18715915,
CC ECO:0000269|PubMed:21767814, ECO:0000269|PubMed:29367607}.
CC -!- FUNCTION: [Isoform NSm protein]: Plays a role in the inhibition of
CC virus-induced apoptosis. Plays a role for virus dissemination in
CC vertebrates. {ECO:0000269|PubMed:23097454,
CC ECO:0000269|PubMed:26038497}.
CC -!- FUNCTION: [NSm-Gn protein]: Plays a role for virus dissemination in
CC mosquitoes. May act as a structural virion protein in insects.
CC {ECO:0000269|PubMed:24489907, ECO:0000269|PubMed:26038497}.
CC -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C (By
CC similarity). Homotrimer (postfusion) (By similarity). Interacts with
CC nucleocapsid protein N and with the polymerase L in order to package
CC them into virus particles (PubMed:21445316). Interacts with host E3
CC ubiquitin-protein ligase UBR4; this interaction is important for viral
CC RNA production (PubMed:35032865). Interacts with host LRP1; this
CC interaction facilitates virus entry into the host cell
CC (PubMed:34559985). {ECO:0000250|UniProtKB:P03518,
CC ECO:0000250|UniProtKB:P09613, ECO:0000269|PubMed:21445316,
CC ECO:0000269|PubMed:34559985, ECO:0000269|PubMed:35032865}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein C.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:12414959, ECO:0000269|PubMed:21445316}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host
CC endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09613}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P09613}.
CC Note=Interaction between Glycoprotein N and Glycoprotein C is essential
CC for proper targeting of Glycoprotein C to the Golgi complex, where
CC virion budding occurs. {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:12414959}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Isoform NSm protein]: Host mitochondrion outer
CC membrane {ECO:0000269|PubMed:23097454}; Single-pass type II membrane
CC protein {ECO:0000303|PubMed:26038497}.
CC -!- SUBCELLULAR LOCATION: [NSm-Gn protein]: Host Golgi apparatus
CC {ECO:0000269|PubMed:3046119}. Virion {ECO:0000269|PubMed:24489907}.
CC Note=Localizes in virions maturing in cells of insect origin but not in
CC cells of mammalian origin. {ECO:0000269|PubMed:24489907}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=Envelopment polyprotein;
CC IsoId=P21401-1; Sequence=Displayed;
CC Name=NSm protein {ECO:0000303|PubMed:22710362}; Synonyms=P14;
CC IsoId=P21401-3; Sequence=VSP_057989, VSP_057990;
CC Name=NSm' protein {ECO:0000303|PubMed:22710362}; Synonyms=P13;
CC IsoId=P21401-5; Sequence=VSP_057988, VSP_057990;
CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-
CC terminus (By similarity). The cytoplasmic tail specifically interacts
CC with the ribonucleoproteins and is critical for genome packaging (By
CC similarity). {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins including NSm protein, Glycoprotein C, and
CC Glycoprotein N. {ECO:0000269|PubMed:16963099}.
CC -!- PTM: [Glycoprotein N]: Glycosylated (PubMed:2728348). The glycans can
CC attach to host CD209/DC-SIGN, and may play a role in virus entry into
CC dendritic cells (PubMed:21767814). {ECO:0000269|PubMed:21767814,
CC ECO:0000269|PubMed:2728348}.
CC -!- PTM: [Glycoprotein C]: Glycosylated (PubMed:2728348). The glycans can
CC attach to host CD209/DC-SIGN, and may play a role in virus entry into
CC dendritic cells (PubMed:21767814). {ECO:0000269|PubMed:21767814,
CC ECO:0000269|PubMed:2728348}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M25276; AAA47449.1; -; Genomic_RNA.
DR EMBL; DQ380206; ABD38819.1; -; Genomic_RNA.
DR PIR; A30183; VGVURF.
DR RefSeq; YP_003848705.1; NC_014396.1.
DR PDB; 6F8P; X-ray; 1.60 A; A=154-469.
DR PDB; 6F9B; EM; 13.30 A; A/C/E/G/I/K/M/O/Q/S/U/X=154-469, B/D/F/H/J/L/N/P/R/T/V/Y=691-1118.
DR PDB; 6F9C; EM; 8.00 A; A/C/E/G/I/K=154-469, B/D/F/H/J/L=691-1118.
DR PDB; 6F9D; EM; 13.30 A; A/C/E/G/I/K=154-469, B/D/F/H/J/L=691-1118.
DR PDB; 6F9E; EM; 13.30 A; A/C/E/G/I/K=154-469, B/D/F/H/J/L=691-1118.
DR PDB; 6F9F; EM; 13.30 A; A/C/E/G/I=154-469, B/D/F/H/J=691-1118.
DR PDB; 6I9I; X-ray; 1.98 A; C/D=154-469.
DR PDBsum; 6F8P; -.
DR PDBsum; 6F9B; -.
DR PDBsum; 6F9C; -.
DR PDBsum; 6F9D; -.
DR PDBsum; 6F9E; -.
DR PDBsum; 6F9F; -.
DR PDBsum; 6I9I; -.
DR SMR; P21401; -.
DR ABCD; P21401; 3 sequenced antibodies.
DR GeneID; 9538296; -.
DR KEGG; vg:9538296; -.
DR Proteomes; UP000002477; Genome.
DR Proteomes; UP000202138; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IDA:UniProtKB.
DR GO; GO:0044193; C:host cell mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044423; C:virion component; IDA:UniProtKB.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IDA:UniProtKB.
DR DisProt; DP02493; -.
DR InterPro; IPR016404; M_polyprot_prcur_phlebovir.
DR InterPro; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR InterPro; IPR009879; Phlebovirus_NSM.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
DR Pfam; PF07246; Phlebovirus_NSM; 2.
DR PIRSF; PIRSF003961; M_poly_PhleboV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Disulfide bond;
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 mitochondrion; Host mitochondrion outer membrane;
KW Host-virus interaction; Membrane;
KW Modulation of host cell apoptosis by virus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1197
FT /note="Envelopment polyprotein"
FT /id="PRO_0000247010"
FT CHAIN 17..690
FT /note="NSm-Gn protein"
FT /id="PRO_0000434914"
FT CHAIN 154..690
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036851"
FT CHAIN 691..1197
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036852"
FT TOPO_DOM 17..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:16963099"
FT TOPO_DOM 154..582
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TOPO_DOM 691..1159
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1181..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 131..153
FT /note="Internal signal sequence for glycoprotein N"
FT /evidence="ECO:0000303|PubMed:16963099"
FT REGION 608..650
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 646..650
FT /note="Important for correct targeting of the glycoproteins
FT to the Golgi complex but not for heterodimerization"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 675..690
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 777..783
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 819..830
FT /note="Fusion loop"
FT /evidence="ECO:0000269|PubMed:29367607"
FT SITE 153..154
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000269|PubMed:16963099"
FT SITE 690..691
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000269|PubMed:16963099"
FT SITE 1194
FT /note="Important for glycoprotein C and glycoprotein N
FT subcellular location"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 179..188
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 229..239
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 250..281
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 271..284
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 304..456
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 322..332
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 374..434
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 402..413
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 420..425
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 479..482
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 486..556
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 506..511
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 691..731
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 704..713
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 756..852
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 771..965
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 777..825
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 783..832
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 788..814
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 818..823
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 934..947
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 1029..1101
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 1039..1042
FT /evidence="ECO:0000269|PubMed:29367607"
FT DISULFID 1049..1083
FT /evidence="ECO:0000269|PubMed:29367607"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform NSm' protein)"
FT /id="VSP_057988"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform NSm protein)"
FT /id="VSP_057989"
FT VAR_SEQ 154..1197
FT /note="Missing (in isoform NSm protein and isoform NSm'
FT protein)"
FT /id="VSP_057990"
FT CONFLICT 9
FT /note="T -> I (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="I -> V (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="K -> E (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="H -> Y (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="L -> I (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="G -> R (in Ref. 2; ABD38819)"
FT /evidence="ECO:0000305"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6F8P"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6F8P"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:6F8P"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 334..347
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:6F8P"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6F8P"
FT STRAND 455..469
FT /evidence="ECO:0007829|PDB:6F8P"
SQ SEQUENCE 1197 AA; 130805 MW; 860B822CD968767F CRC64;
MYVLLTILTS VLVCEAIIRV SLSSTREETC FGDSTNPEMI EGAWDSLREE EMPEELSCSI
SGIREVKTSS QELYRALKAI IAADGLNNIT CHGKDPEDKI SLIKGPPHKK RVGIVRCERR
RDAKQIGRKT MAGIAMTVLP ALAVFALAPV VFAEDPHLRN RPGKGHNYID GMTQEDATCK
PVTYAGACSS FDVLLEKGKF PLFQSYAHHR TLLEAVHDTI IAKADPPSCD LLSAHGNPCM
KEKLVMKTHC PNDYQSAHHL NNDGKMASVK CPPKYELTED CNFCRQMTGA SLKKGSYPLQ
DLFCQSSEDD GSKLKTKMKG VCEVGVQALK KCDGQLSTAH EVVPFAVFKN SKKVYLDKLD
LKTEENLLPD SFVCFEHKGQ YKGTMDSGQT KRELKSFDIS QCPKIGGHGS KKCTGDAAFC
SAYECTAQYA NAYCSHANGS GIVQIQVSGV WKKPLCVGYE RVVVKRELSA KPIQRVEPCT
TCITKCEPHG LVVRSTGFKI SSAVACASGV CVTGSQSPST EITLKYPGIS QSSGGDIGVH
MAHDDQSVSS KIVAHCPPQD PCLVHDCIVC AHGLINYQCH TALSAFVVVF VFSSIAIICL
AILYRVLKCL KIAPRKVLNP LMWITAFIRW IYKKMVARVA DNINQVNREI GWMEGGQLVL
GNPAPIPRHA PIPRYSTYLM LLLIVSYASA CSELIQASSR ITTCSTEGVN TKCRLSGTAL
IRAGSVGAEA CLMLKGVKED QTKFLKLKTV SSELSCREGQ SYWTGSFSPK CLSSRRCHLV
GECHVNRCLS WRDNETSAEF SFVGESTTMR ENKCFEQCGG WGCGCFNVNP SCLFVHTYLQ
SVRKEALRVF NCIDWVHKLT LEITDFDGSV STIDLGASSS RFTNWGSVSL SLDAEGISGS
NSFSFIESPG KGYAIVDEPF SEIPRQGFLG EIRCNSESSV LSAHESCLRA PNLISYKPMI
DQLECTTNLI DPFVVFERGS LPQTRNDKTF AASKGNRGVQ AFSKGSVQAD LTLMFDNFEV
DFVGAAVSCD AAFLNLTGCY SCNAGARVCL SITSTGTGSL SAHNKDGSLH IVLPSENGTK
DQCQILHFTV PEVEEEFMYS CDGDERPLLV KGTLIAIDPF DDRREAGGES TVVNPKSGSW
NFFDWFSGLM SWFGGPLKTI LLICLYVALS IGLFFLLIYL GGTGLSKMWL AATKKAS
