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   24-JAN-2024, entry version 106.
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;
OC   Phlebovirus riftense.
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   EMDB; EMD-4197; -.
DR   EMDB; EMD-4198; -.
DR   EMDB; EMD-4199; -.
DR   EMDB; EMD-4200; -.
DR   SMR; P21401; -.
DR   GlyCosmos; P21401; 3 sites, No reported glycans.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0044193; C:host cell mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:perturbation by virus of host apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   DisProt; DP02493; -.
DR   Gene3D; 2.60.40.3770; -; 1.
DR   Gene3D; 2.60.98.50; -; 3.
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
//