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Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); p62 (E3/E2); E3 protein (Spike glycoprotein E3); E2 envelope glycoprotein (Spike glycoprotein E2); 6K protein; E1 envelope glycoprotein (Spike glycoprotein E1)]

 POLS_EEEVF              Reviewed;        1242 AA.
Q4QXJ7;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
23-MAY-2018, entry version 76.
RecName: Full=Structural polyprotein;
AltName: Full=p130;
Contains:
RecName: Full=Capsid protein;
EC=3.4.21.90;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=Precursor of protein E3/E2;
AltName: Full=p62;
AltName: Full=pE2;
Contains:
RecName: Full=Assembly protein E3;
Contains:
RecName: Full=Spike glycoprotein E2;
AltName: Full=E2 envelope glycoprotein;
Contains:
RecName: Full=6K protein;
Contains:
RecName: Full=Spike glycoprotein E1;
AltName: Full=E1 envelope glycoprotein;
Eastern equine encephalitis virus (strain Florida 91-469) (EEEV)
(Eastern equine encephalomyelitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=374598;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9126; Passeriformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16147892; DOI=10.1080/10425170500136889;
Platteborze P.L., Kondig J.P., Schoepp R.J., Wasieloski L.P.;
"Comparative sequence analysis of the eastern equine encephalitis
virus pathogenic strains FL91-4679 and GA97 to other North American
strains.";
DNA Seq. 16:308-320(2005).
-!- FUNCTION: Capsid protein: Possesses a protease activity that
results in its autocatalytic cleavage from the nascent structural
protein. Following its self-cleavage, the capsid protein
transiently associates with ribosomes, and within several minutes
the protein binds to viral RNA and rapidly assembles into
icosahedric core particles. The resulting nucleocapsid eventually
associates with the cytoplasmic domain of the spike glycoprotein
E2 at the cell membrane, leading to budding and formation of
mature virions. In case of infection, new virions attach to target
cells and after clathrin-mediated endocytosis their membrane fuses
with the host endosomal membrane. This leads to the release of the
nucleocapsid into the cytoplasm, followed by an uncoating event
necessary for the genomic RNA to become accessible. The uncoating
might be triggered by the interaction of capsid proteins with
ribosomes. Binding of ribosomes would release the genomic RNA
since the same region is genomic RNA-binding and ribosome-binding.
{ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: Assembly protein E3: Provides the signal sequence for
the translocation of the precursor of protein E3/E2 to the host
endoplasmic reticulum. Mediates pH protection of spike
glycoprotein E1 during the transport via the secretory pathway.
{ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: Spike glycoprotein E2: Plays a role in viral attachment
to target host cell, by binding to the cell receptor. Synthesized
as a p62 precursor which is processed by furin at the cell
membrane just before virion budding, giving rise to E2-E1
heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is
unstable and dissociate at low pH. p62 is processed at the last
step, presumably to avoid E1 fusion activation before its final
export to cell surface. E2 C-terminus contains a transitory
transmembrane that would be disrupted by palmitoylation, resulting
in reorientation of the C-terminal tail from lumenal to
cytoplasmic side. This step is critical since E2 C-terminus is
involved in budding by interacting with capsid proteins. This
release of E2 C-terminus in cytoplasm occurs lately in protein
export, and precludes premature assembly of particles at the
endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: 6K protein: Constitutive membrane protein involved in
virus glycoprotein processing, cell permeabilization, and the
budding of viral particles. Disrupts the calcium homeostasis of
the cell, probably at the endoplasmic reticulum level. This leads
to cytoplasmic calcium elevation. Because of its lipophilic
properties, the 6K protein is postulated to influence the
selection of lipids that interact with the transmembrane domains
of the glycoproteins, which, in turn, affects the deformability of
the bilayer required for the extreme curvature that occurs as
budding proceeds. Present in low amount in virions, about 3%
compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.
-!- FUNCTION: Spike glycoprotein E1: Class II viral fusion protein.
Fusion activity is inactive as long as E1 is bound to E2 in mature
virion. After virus attachment to target cell and endocytosis,
acidification of the endosome would induce dissociation of E1/E2
heterodimer and concomitant trimerization of the E1 subunits. This
E1 trimer is fusion active, and promotes release of viral
nucleocapsid in cytoplasm after endosome and viral membrane
fusion. Efficient fusion requires the presence of cholesterol and
sphingolipid in the target membrane. Fusion is optimal at levels
of about 1 molecule of cholesterol per 2 molecules of
phospholipids, and is specific for sterols containing a 3-beta-
hydroxyl group. {ECO:0000250|UniProtKB:P03315}.
-!- CATALYTIC ACTIVITY: Autocatalytic release of the core protein from
the N-terminus of the togavirus structural polyprotein by
hydrolysis of a -Trp-|-Ser- bond. {ECO:0000250|UniProtKB:P03316}.
-!- SUBUNIT: Precursor of protein E3/E2: The precursor of protein
E3/E2 and E1 form a heterodimer shortly after synthesis. Spike
glycoprotein E1: The precursor of protein E3/E2 and E1 form a
heterodimer shortly after synthesis. Spike glycoprotein E1:
Processing of the precursor of protein E3/E2 into E2 and E3
results in a heterodimer of the spike glycoproteins E2 and E1.
Spike glycoprotein E2: Processing of the precursor of protein
E3/E2 into E2 and E3 results in a heterodimer of the spike
glycoproteins E2 and E1. Spike glycoprotein E1: Spike at virion
surface are constituted of three E2-E1 heterodimers. Spike
glycoprotein E2: Spike at virion surface are constituted of three
E2-E1 heterodimers. Spike glycoprotein E1: After target cell
attachment and endocytosis, E1 change conformation to form
homotrimers. 6K protein: Interacts with spike glycoprotein E1. 6K
protein: Interacts with spike glycoprotein E2. Spike glycoprotein
E1: Interacts with 6K protein. Spike glycoprotein E2: Interacts
with 6K protein. {ECO:0000250|UniProtKB:P03315,
ECO:0000250|UniProtKB:P03316}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion
{ECO:0000250|UniProtKB:P03316}. Host cytoplasm
{ECO:0000250|UniProtKB:P03316}. Host cell membrane
{ECO:0000250|UniProtKB:P03316}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:P03316}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q8JUX5}.
-!- SUBCELLULAR LOCATION: 6K protein: Host cell membrane
{ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
{ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316};
Multi-pass membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5};
Single-pass type I membrane protein {ECO:0000255}.
-!- DOMAIN: Structural polyprotein: As soon as the capsid protein has
been autocleaved, an internal uncleaved signal peptide directs the
remaining polyprotein to the endoplasmic reticulum.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Capsid protein is auto-cleaved during
polyprotein translation, unmasking a signal peptide at the N-
terminus of the precursor of E3/E2. The remaining polyprotein is
then targeted to the host endoplasmic reticulum, where host signal
peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further
processed to mature E3 and E2 by host furin in trans-Golgi
vesicle. {ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E2: Palmitoylated via thioester bonds.
These palmitoylations may induce disruption of the C-terminus
transmembrane. This would result in the reorientation of E2 C-
terminus from lumenal to cytoplasmic side.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E1: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Spike glycoprotein E2: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: Assembly protein E3: N-glycosylated.
{ECO:0000250|UniProtKB:P03315}.
-!- PTM: 6K protein: Palmitoylated via thioester bonds.
{ECO:0000250|UniProtKB:P03315}.
-!- MISCELLANEOUS: Structural polyprotein: Translated from a
subgenomic RNA synthesized during togavirus replication.
{ECO:0000250|UniProtKB:Q86925}.
-----------------------------------------------------------------------
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EMBL; AY705241; AAT96380.1; -; Genomic_RNA.
ProteinModelPortal; Q4QXJ7; -.
SMR; Q4QXJ7; -.
MEROPS; S03.001; -.
PRIDE; Q4QXJ7; -.
OrthoDB; VOG090000ST; -.
Proteomes; UP000008298; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
InterPro; IPR002548; Alpha_E1_glycop.
InterPro; IPR000936; Alpha_E2_glycop.
InterPro; IPR002533; Alpha_E3_glycop.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000930; Peptidase_S3.
Pfam; PF01589; Alpha_E1_glycop; 1.
Pfam; PF00943; Alpha_E2_glycop; 1.
Pfam; PF01563; Alpha_E3_glycop; 1.
Pfam; PF00944; Peptidase_S3; 1.
PRINTS; PR00798; TOGAVIRIN.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS51690; ALPHAVIRUS_CP; 1.
3: Inferred from homology;
Capsid protein; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Palmitate;
Protease; Serine protease; T=4 icosahedral capsid protein;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
CHAIN 1 261 Capsid protein. {ECO:0000250}.
/FTId=PRO_0000238730.
CHAIN 262 744 Precursor of protein E3/E2.
/FTId=PRO_0000238731.
CHAIN 262 324 Assembly protein E3.
/FTId=PRO_0000238732.
CHAIN 325 744 Spike glycoprotein E2.
/FTId=PRO_0000238733.
CHAIN 745 801 6K protein.
/FTId=PRO_0000238734.
CHAIN 802 1242 Spike glycoprotein E1.
/FTId=PRO_0000238735.
TOPO_DOM 325 688 Extracellular. {ECO:0000255}.
TRANSMEM 689 709 Helical. {ECO:0000255}.
TOPO_DOM 710 744 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 745 759 Extracellular. {ECO:0000255}.
TRANSMEM 760 780 Helical. {ECO:0000255}.
TRANSMEM 781 801 Helical. {ECO:0000255}.
TOPO_DOM 802 1218 Extracellular. {ECO:0000255}.
TRANSMEM 1219 1239 Helical. {ECO:0000255}.
TOPO_DOM 1240 1242 Cytoplasmic. {ECO:0000255}.
DOMAIN 112 261 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 7 106 Intrinsically disordered, in contact with
genomic RNA in nucleocapsid.
{ECO:0000255}.
REGION 87 99 Ribosome-binding. {ECO:0000250}.
REGION 262 273 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 717 737 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 885 902 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 138 138 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 160 160 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 212 212 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 261 262 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 324 325 Cleavage; by host furin. {ECO:0000250}.
SITE 744 745 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 801 802 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 717 717 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 737 737 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 738 738 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 850 915 {ECO:0000250}.
DISULFID 863 895 {ECO:0000250}.
DISULFID 864 897 {ECO:0000250}.
DISULFID 869 879 {ECO:0000250}.
DISULFID 1061 1073 {ECO:0000250}.
DISULFID 1103 1178 {ECO:0000250}.
DISULFID 1108 1182 {ECO:0000250}.
DISULFID 1130 1172 {ECO:0000250}.
SEQUENCE 1242 AA; 137554 MW; 4EA1AECB02FFA752 CRC64;
MFPYPTLNYP PMAPINPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIAN LTLKQRAPNP
PAGPPAKRKK PAPKPKPAQA KKKRPPPPAK KQKRKPKPGK RQRMCMKLES DKTFPIMLNG
QVNGYACVVG GRVFKPLHVE GRIDNEQLAA IKLKKASIYD LEYGDVPQCM KSDTLQYTSD
KPPGFYNWHH GAVQYENNRF TVPRGVGGKG DSGRPILDNK GRVVAIVLGG VNEGSRTALS
VVTWNQKGVT VKDTPEGSEP WSLATVMCVL ANITFPCDQP PCMPCCYEKN PHETLTMLEQ
NYDSRAYDQL LDAAVKCNAR RTRRDLDTHF TQYKLARPYI ADCPNCGHSR CDSPIAIEEV
RGDAHAGVIR IQTSAMFGLK TDGVDLAYMS FMNGKTQKSI KIDNLHVRTS APCSLVSHHG
YYILAQCPPG DTVTVGFHDG PNRHTCTVAH KVEFRPVGRE KYRHPPEHGV ELPCNRYTHK
RADQGHYVEM HQPGLVADHS LLSIHSAKVK ITVPSGAQVK YYCKCPDVRE GITSSDHTTT
CTDVKQCRAY LIDNKKWVYN SGRLPRGEGD TFKGKLHVPF VPVKAKCIAT LAPEPLVEHK
HRTLILHLHP DHPTLLTTRS LGSDANPTRQ WIERPTTVNF TVTGEGLEYT WGNHPPKRVW
AQESGEGNPH GWPHEVVVYY YNRYPLTTII GLCTCVAIIM VSCVTSVWLL CRTRNLCITP
YKLAPNAQVP ILLALLCCIK PTRADDTLQV LNYLWNNNQN FFWMQTLIPL AALIVCMRML
RCLFCCGPAF LLVCGALGAA AYEHTAVMPN KVGIPYKALV ERPGYAPVHL QIQLVNTRII
PSTNLEYITC KYKTKVPSPV VKCCGATQCT SKPHPDYQCQ VFTGVYPFMW GGAYCFCDTE
NTQMSEAYVE RSEECSIDHA KAYKVHTGTV QAMVNITYGS VSWRSADVYV NGETPAKIGD
AKLIIGPLSS AWSPFDNKVV VYGHEVYNYD FPEYGTGKAG SFGDLQSRTS TSNDLYANTN
LKLQRPQAGI VHTPFTQAPS GFERWKRDKG APLNDVAPFG CSIALEPLRA ENCAVGSIPI
SIDIPDAAFT RISETPTVSD LECKITECTY ASDFGGIATV AYKSSKAGNC PIHSPSGVAV
IKENDVTLAE SGSFTFHFST ANIHPAFKLQ VCTSAVTCKG DCKPPKDHIV DYPAQHTESF
TSAISATAWS WLKVLVGGTS AFIVLGLIAT AVVALVLFFH RH


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