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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_EEEV3              Reviewed;        1240 AA.
P27284;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
05-DEC-2018, entry version 113.
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 va33[ten broeck]) (EEEV)
(Eastern equine encephalomyelitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11022;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9126; Passeriformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2024496; DOI=10.1016/0042-6822(91)90618-L;
Weaver S.C., Scott T.W., Rico-Hesse R.;
"Molecular evolution of eastern equine encephalomyelitis virus in
North America.";
Virology 182:774-784(1991).
-!- 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:
Reaction=Autocatalytic release of the core protein from the N-
terminus of the togavirus structural polyprotein by hydrolysis
of a -Trp-|-Ser- bond.; EC=3.4.21.90;
Evidence={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; M69094; AAA42980.1; -; Genomic_RNA.
PIR; A39992; VHWVEV.
ProteinModelPortal; P27284; -.
SMR; P27284; -.
PRIDE; P27284; -.
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; 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 1 260 Capsid protein. {ECO:0000250}.
/FTId=PRO_0000041246.
CHAIN 261 743 Precursor of protein E3/E2.
{ECO:0000250}.
/FTId=PRO_0000234317.
CHAIN 261 323 Assembly protein E3. {ECO:0000250}.
/FTId=PRO_0000041247.
CHAIN 324 743 Spike glycoprotein E2. {ECO:0000250}.
/FTId=PRO_0000041248.
CHAIN 744 799 6K protein. {ECO:0000250}.
/FTId=PRO_0000041249.
CHAIN 800 1240 Spike glycoprotein E1. {ECO:0000250}.
/FTId=PRO_0000041250.
TOPO_DOM 261 682 Extracellular. {ECO:0000255}.
TRANSMEM 683 703 Helical. {ECO:0000255}.
TOPO_DOM 704 743 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 744 758 Extracellular. {ECO:0000255}.
TRANSMEM 759 779 Helical. {ECO:0000255}.
TOPO_DOM 780 780 Cytoplasmic. {ECO:0000255}.
TRANSMEM 781 801 Helical. {ECO:0000255}.
TOPO_DOM 802 1216 Extracellular. {ECO:0000255}.
TRANSMEM 1217 1237 Helical. {ECO:0000255}.
TOPO_DOM 1238 1240 Cytoplasmic. {ECO:0000255}.
DOMAIN 111 260 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 92 98 Ribosome-binding. {ECO:0000250}.
REGION 261 272 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 715 735 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 883 900 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 137 137 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 159 159 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 211 211 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 260 261 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 323 324 Cleavage; by host furin. {ECO:0000250}.
SITE 743 744 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 799 800 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 706 706 S-palmitoyl cysteine; by host.
{ECO:0000255}.
LIPID 716 716 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 736 736 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 737 737 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 638 638 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 834 834 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 933 933 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 848 913 {ECO:0000250}.
DISULFID 861 893 {ECO:0000250}.
DISULFID 862 895 {ECO:0000250}.
DISULFID 867 877 {ECO:0000250}.
DISULFID 1059 1071 {ECO:0000250}.
DISULFID 1101 1176 {ECO:0000250}.
DISULFID 1106 1180 {ECO:0000250}.
SEQUENCE 1240 AA; 137291 MW; AEBEB1599D083045 CRC64;
MFPYPTLNYP PMAPINPMAY RDPNPPRQVA PFRPPLAAQI EDLRRSIANL TLKQRAPNPP
AGPPAKRKKP APKPKPAQAK KKRPPPPAKK QKRKPKPGKR QRMCMKLESD KTFPIMLNGQ
VNGYACVVGG RVFKPLHVEG RIDNEQLAAI KLKKASIYDL EYGDVPQCMK SDTLQYTSDK
PPGFYNWHHG AVQYENNRFT VPRGVGGKGD SGRPILDNKG RVVAIVLGGV NEGSRTALSV
VTWNQKGVTV KDTPEGSEPW SLATVMCVLA NITFPCDQPP CMPCCYEKNP HETLTMLEQN
YDSRAYDQLL DAAVKCNARR TRRDLDTHFT QYKLARPYIA DCPNCGHSRC DSPIAIEEVR
GDAHAGVIRI QTSAMFGLKT DGVDLAYMSF MNGKTQKSIK IDNLHVRTSA PCSLVSHHGY
YILAQCPPGD TVTVGFHDGP NRHTCTVAHK VEFRPVGREK YRHPPEHGVE LPCNRYTHKR
ADQGHYVEMH QPGLVADHSL LSIHSAKVKI TVPSGAQVKY YCKCPDVREG ITSSDHTTTC
TDVKQCRAYL IGNKKWVYNS GRLPRGEGDT FKGKLHVPFV PVKAKCIATL APEPLVEHKH
RTLILHLHPD HPTLLTTRSL GSDANPTRQW IERPTTVNFT VTGEGLEYTW GNHPPKRVWA
QESGEGNPHG WPHEVVVYYY NRYPLTTIIG LCTCVAIIMV SCVHPCGSFA GLRNLCITPY
KLAPNAQVPI LLALLCCIKP TRADDTLQVL NYLWNNNQNF FWMQTLIPLA ALIVCMRIVR
CLFCCGPAFL LVCGAWAAAY EHTAVMPNKV GIPYKALVER PGYAPVHLQI QLVNTSIIPS
TNLEYITCKY KTKVPSPVVK CCGATQCTSK PHPDYQCQVF TGVYPFMWGG AYCFCDTENT
QMSEAYVERS EECSIDHAKA YKVHTGTVQA MVNITYGSVS WRSADVYVNG ETPAKIGDAK
LIIGPLSSAW SPFDNKVVVY GHEVYNYDFP EYGTGKAGSF GDLQSRTSTS NDLYANTNLK
LQRPQAGIVH TPFTQAPSGF ERWKRDKGAP LNDVAPFGCS IALEPLRAEN CAVGSIPISI
DIPDAAFTRI SETPTVSDLE CKITECTYAS DFGGIATLPT NPVKQETVQF ILHQVLQLLK
RMTSPLLRAG SFTFHFSTAN IHPAFKLQVC TSGVTCKGDC KPPKDHIVDY PAQHTESFTS
AISATAWSWL KVLVGGTSAF IVLGLIATAV VALVLFFHRH


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