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Envelopment polyprotein (M polyprotein) [Cleaved into: NSm-Gn protein (p78 protein); Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]

 GP_RVFVZ                Reviewed;        1197 AA.
P21401;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
07-JUN-2017, entry version 85.
RecName: Full=Envelopment polyprotein;
AltName: Full=M polyprotein;
Contains:
RecName: Full=NSm-Gn protein {ECO:0000303|PubMed:22710362};
AltName: Full=p78 protein;
Contains:
RecName: Full=Glycoprotein N {ECO:0000303|PubMed:22710362};
Short=Gn;
AltName: Full=Glycoprotein G1;
Contains:
RecName: Full=Glycoprotein C {ECO:0000303|PubMed:22710362};
Short=Gc;
AltName: Full=Glycoprotein G2;
Flags: Precursor;
Name=GP;
Rift valley fever virus (strain ZH-548 M12) (RVFV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses; Bunyavirales;
Phenuiviridae; Phlebovirus.
NCBI_TaxID=11589;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=297284; Bos taurus x Bison bison (beefalo).
NCBI_TaxID=9837; Camelus bactrianus (Bactrian camel).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2705307; DOI=10.1016/0042-6822(89)90171-2;
Takehara K., Min M.K., Battles J.K., Sugiyama K., Emery V.C.,
Dalrymple J.M., Bishop D.H.L.;
"Identification of mutations in the M RNA of a candidate vaccine
strain of Rift Valley fever virus.";
Virology 169:452-457(1989).
[2]
SUBCELLULAR LOCATION (NSM-GN PROTEIN).
PubMed=3046119; DOI=10.1016/0042-6822(88)90174-2;
Wasmoen T.L., Kakach L.T., Collett M.S.;
"Rift Valley fever virus M segment: cellular localization of M
segment-encoded proteins.";
Virology 166:275-280(1988).
[3]
GLYCOSYLATION (GLYCOPROTEIN N), AND GLYCOSYLATION (GLYCOPROTEIN D).
PubMed=2728348; DOI=10.1016/0042-6822(89)90442-X;
Kakach L.T., Suzich J.A., Collett M.S.;
"Rift Valley fever virus M segment: phlebovirus expression strategy
and protein glycosylation.";
Virology 170:505-510(1989).
[4]
SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
(GLYCOPROTEIN C).
PubMed=12414959; DOI=10.1128/JVI.76.23.12200-12210.2002;
Gerrard S.R., Nichol S.T.;
"Characterization of the Golgi retention motif of Rift Valley fever
virus G(N) glycoprotein.";
J. Virol. 76:12200-12210(2002).
[5]
PROTEIN CLEAVAGE (ENVELOPMENT POLYPROTEIN).
PubMed=16963099; DOI=10.1016/j.virol.2006.08.002;
Gerrard S.R., Nichol S.T.;
"Synthesis, proteolytic processing and complex formation of N-
terminally nested precursor proteins of the Rift Valley fever virus
glycoproteins.";
Virology 357:124-133(2007).
[6]
FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
PubMed=18715915; DOI=10.1128/JVI.01191-08;
Freiberg A.N., Sherman M.B., Morais M.C., Holbrook M.R.,
Watowich S.J.;
"Three-dimensional organization of Rift Valley fever virus revealed by
cryoelectron tomography.";
J. Virol. 82:10341-10348(2008).
[7]
INTERACTION OF GLYCOPROTEIN N WITH PROTEIN N AND POLYMERASE L,
FUNCTION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION (GLYCOPROTEIN N).
PubMed=21445316; DOI=10.1371/journal.pone.0018070;
Piper M.E., Sorenson D.R., Gerrard S.R.;
"Efficient cellular release of Rift Valley fever virus requires
genomic RNA.";
PLoS ONE 6:E18070-E18070(2011).
[8]
GLYCOSYLATION (GLYCOPROTEIN N), AND GLYCOSYLATION (GLYCOPROTEIN C).
PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
Helenius A.;
"DC-SIGN as a receptor for phleboviruses.";
Cell Host Microbe 10:75-88(2011).
[9]
REVIEW.
PubMed=22710362; DOI=10.1016/j.antiviral.2012.06.001;
Ikegami T.;
"Molecular biology and genetic diversity of Rift Valley fever virus.";
Antiviral Res. 95:293-310(2012).
[10]
FUNCTION (ISOFORM NSM PROTEIN), AND SUBCELLULAR LOCATION (ISOFORM NSM
PROTEIN).
PubMed=23097454; DOI=10.1128/JVI.02192-12;
Terasaki K., Won S., Makino S.;
"The C-terminal region of Rift Valley fever virus NSm protein targets
the protein to the mitochondrial outer membrane and exerts
antiapoptotic function.";
J. Virol. 87:676-682(2013).
[11]
FUNCTION (ISOFORM NSM PROTEIN), AND FUNCTION (NSM-GN PROTEIN).
PubMed=26038497; DOI=10.1038/emi.2014.71;
Kreher F., Tamietti C., Gommet C., Guillemot L., Ermonval M.,
Failloux A.B., Panthier J.J., Bouloy M., Flamand M.;
"The Rift Valley fever accessory proteins NSm and P78/NSm-GN are
distinct determinants of virus propagation in vertebrate and
invertebrate hosts.";
Emerg. Microbes Infect. 3:E71-E71(2014).
[12]
FUNCTION (NSM-GN PROTEIN), AND SUBCELLULAR LOCATION (NSM-GN PROTEIN).
STRAIN=ZH-501;
PubMed=24489907; DOI=10.1371/journal.pone.0087385;
Weingartl H.M., Zhang S., Marszal P., McGreevy A., Burton L.,
Wilson W.C.;
"Rift Valley fever virus incorporates the 78 kDa glycoprotein into
virions matured in mosquito C6/36 cells.";
PLoS ONE 9:E87385-E87385(2014).
-!- FUNCTION: Glycoprotein N: Structural component of the virion that
interacts with glycoprotein N. About 720 Gn and 720 Gc proteins
form 12 pentameric and 110 hexameric capsomeres. Theses capsomeres
are arranged on the virus envelop surface in an icosahedral
lattice with a T=12 quasisymmetry. Attaches the virion to a cell
receptor and thereby promotes fusion after endocytosis of the
virion. Contains a Golgi retention signal on its C-terminal region
and brings Gc to the host Golgi apparatus where assembly occurs.
{ECO:0000269|PubMed:18715915, ECO:0000269|PubMed:21445316}.
-!- FUNCTION: Glycoprotein C: Structural component of the virion that
interacts with glycoprotein C. About 720 Gn and 720 Gc proteins
form 12 pentameric and 110 hexameric capsomeres. Theses capsomeres
are arranged on the virus envelop surface in an icosahedral
lattice with a T=12 quasisymmetry. Attaches the virion to a cell
receptor and thereby promotes fusion after endocytosis of the
virion. {ECO:0000269|PubMed:18715915}.
-!- FUNCTION: Isoform NSm protein: Plays a role in the inhibition of
virus-induced apoptosis. Plays a role for virus dissemination in
vertebrates. {ECO:0000269|PubMed:23097454,
ECO:0000269|PubMed:26038497}.
-!- FUNCTION: NSm-Gn protein: Plays a role for virus dissemination in
mosquitoes. May act as a strucutral virion protein in insects.
{ECO:0000269|PubMed:24489907, ECO:0000269|PubMed:26038497}.
-!- SUBUNIT: Glycoprotein C and Glycoprotein N interact with each
other. Glycoprotein Gn interacts with nucleocapsid protein N and
with the polymerase L in order to package them into virus
particles. {ECO:0000269|PubMed:21445316}.
-!- SUBCELLULAR LOCATION: Glycoprotein N: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host Golgi apparatus membrane {ECO:0000269|PubMed:12414959,
ECO:0000269|PubMed:21445316}; Single-pass type I membrane protein
{ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Glycoprotein C: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host Golgi apparatus membrane {ECO:0000269|PubMed:12414959};
Single-pass type I membrane protein {ECO:0000305}.
Note=Interaction between Gn and Gc is essential for proper
targeting of GC to the Golgi complex, where virion budding occurs.
{ECO:0000269|PubMed:12414959}.
-!- SUBCELLULAR LOCATION: Isoform NSm protein: Host mitochondrion
outer membrane {ECO:0000269|PubMed:23097454}.
-!- SUBCELLULAR LOCATION: NSm-Gn protein: Host Golgi apparatus
{ECO:0000269|PubMed:3046119}. Virion
{ECO:0000269|PubMed:24489907}. Note=Localizes in virions maturing
in cells of insect origin but not in cells of mammalian origin.
{ECO:0000269|PubMed:24489907}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=Envelopment polyprotein;
IsoId=P21401-1; Sequence=Displayed;
Name=NSm protein {ECO:0000303|PubMed:22710362}; Synonyms=P14;
IsoId=P21401-3; Sequence=VSP_057989, VSP_057990;
Name=NSm' protein {ECO:0000303|PubMed:22710362}; Synonyms=P13;
IsoId=P21401-5; Sequence=VSP_057988, VSP_057990;
-!- PTM: Envelopment polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins including NSm protein, Glycoprotein C, and
Glycoprotein N. {ECO:0000269|PubMed:16963099}.
-!- PTM: Glycoprotein C: Glycosylated by host (PubMed:2728348). The
glycans can attach to host CD209/DC-SIGN, and may play a role in
virus entry into dendritic cells (PubMed:21767814).
{ECO:0000269|PubMed:21767814, ECO:0000269|PubMed:2728348}.
-!- PTM: Glycoprotein N: Glycosylated by host (PubMed:2728348). The
glycans can attach to host CD209/DC-SIGN, and may play a role in
virus entry into dendritic cells (PubMed:21767814).
{ECO:0000269|PubMed:21767814, ECO:0000269|PubMed:2728348}.
-!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M25276; AAA47449.1; -; Genomic_RNA.
PIR; A30183; VGVURF.
SMR; P21401; -.
PRIDE; P21401; -.
OrthoDB; VOG090002Z2; -.
Proteomes; UP000002477; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IDA:UniProtKB.
GO; GO:0044193; C:host cell mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019012; C:virion; IDA:UniProtKB.
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:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
GO; GO:0019068; P:virion assembly; IDA:UniProtKB.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR016404; M_polyprot_prcur_phlebovir.
InterPro; IPR010826; Phlebovirus_G1.
InterPro; IPR009878; Phlebovirus_G2.
InterPro; IPR009879; Phlebovirus_NSM.
Pfam; PF07243; Phlebovirus_G1; 1.
Pfam; PF07245; Phlebovirus_G2; 1.
Pfam; PF07246; Phlebovirus_NSM; 2.
PIRSF; PIRSF003961; M_poly_PhleboV; 1.
1: Evidence at protein level;
Alternative initiation; 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 mitochondrion; Host mitochondrion outer membrane;
Host-virus interaction; Membrane;
Modulation of host cell apoptosis by virus; Reference proteome;
Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral penetration into host cytoplasm;
Virion; Virus entry into host cell.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 1197 Envelopment polyprotein.
/FTId=PRO_0000247010.
CHAIN 17 690 NSm-Gn protein.
/FTId=PRO_0000434914.
CHAIN 154 690 Glycoprotein N. {ECO:0000255}.
/FTId=PRO_0000036851.
CHAIN 691 1197 Glycoprotein C. {ECO:0000255}.
/FTId=PRO_0000036852.
TOPO_DOM 17 582 Lumenal. {ECO:0000255}.
TRANSMEM 583 603 Helical. {ECO:0000255}.
TOPO_DOM 604 690 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 691 1159 Lumenal. {ECO:0000255}.
TRANSMEM 1160 1180 Helical. {ECO:0000255}.
TOPO_DOM 1181 1197 Cytoplasmic. {ECO:0000255}.
SITE 690 691 Cleavage; by host signal peptidase.
{ECO:0000250}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 794 794 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1035 1035 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VAR_SEQ 1 51 Missing (in isoform NSm' protein).
/FTId=VSP_057988.
VAR_SEQ 1 38 Missing (in isoform NSm protein).
/FTId=VSP_057989.
VAR_SEQ 154 1197 Missing (in isoform NSm protein and
isoform NSm' protein).
/FTId=VSP_057990.
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


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