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Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]

 POLS_EEEV               Reviewed;        1239 AA.
P08768;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
25-APR-2018, entry version 117.
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 (EEEV) (Eastern equine
encephalomyelitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11021;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9126; Passeriformes.
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=82V-2137;
PubMed=2886548; DOI=10.1099/0022-1317-68-8-2129;
Chang G.-J.J., Trent D.W.;
"Nucleotide sequence of the genome region encoding the 26S mRNA of
eastern equine encephalomyelitis virus and the deduced amino acid
sequence of the viral structural proteins.";
J. Gen. Virol. 68:2129-2142(1987).
-!- 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; X05816; CAA29261.1; -; mRNA.
PIR; A26816; VHWVEE.
ProteinModelPortal; P08768; -.
SMR; P08768; -.
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.
2: Evidence at transcript level;
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 1 259 Capsid protein.
/FTId=PRO_0000041241.
CHAIN 260 742 Precursor of protein E3/E2.
/FTId=PRO_0000234316.
CHAIN 260 322 Assembly protein E3.
/FTId=PRO_0000041242.
CHAIN 323 742 Spike glycoprotein E2.
/FTId=PRO_0000041243.
CHAIN 743 798 6K protein.
/FTId=PRO_0000041244.
CHAIN 799 1239 Spike glycoprotein E1.
/FTId=PRO_0000041245.
TOPO_DOM 260 681 Extracellular. {ECO:0000255}.
TRANSMEM 682 702 Helical. {ECO:0000255}.
TOPO_DOM 703 742 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 743 754 Extracellular. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TOPO_DOM 776 776 Cytoplasmic. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TOPO_DOM 798 1215 Extracellular. {ECO:0000255}.
TRANSMEM 1216 1236 Helical. {ECO:0000255}.
TOPO_DOM 1237 1239 Cytoplasmic. {ECO:0000255}.
DOMAIN 110 259 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 89 97 Ribosome-binding. {ECO:0000250}.
REGION 260 271 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 714 734 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 882 899 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 136 136 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 158 158 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 210 210 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 259 260 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 322 323 Cleavage; by host furin. {ECO:0000250}.
SITE 742 743 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 798 799 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 705 705 S-palmitoyl cysteine; by host.
{ECO:0000255}.
LIPID 715 715 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 735 735 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 736 736 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 932 932 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 847 912 {ECO:0000250}.
DISULFID 860 892 {ECO:0000250}.
DISULFID 861 894 {ECO:0000250}.
DISULFID 866 876 {ECO:0000250}.
DISULFID 1058 1070 {ECO:0000250}.
DISULFID 1100 1175 {ECO:0000250}.
DISULFID 1105 1179 {ECO:0000250}.
SEQUENCE 1239 AA; 137432 MW; 8C7664A405D2D41C CRC64;
MFPYPTLNYP PMAPINPMAY RDPNPPRQVA PFRPPLAAQI EDLRRSIANL TLKQRAPNPP
AGPPAKRKKP APSLSLETKK KRPPPPAKKQ KRKPKPGKRQ RMCMKLESDK TFPIMLNGQV
NGYACVVGGR VFKPLHVEGR IDNEQLAAIK LKKASIYDLE YGDVPQCMKS DTLQYTSDKP
PGFYNWHHGA VQYENNRFTV PRGVGGKGDS GRPILDNKGR VVAIVQGGVN EGSRTALSVV
TWNQKGVTVK DTPEGSEPWS LATVMCVLAN ITFPCDQPPC MPCCYEKNPH ETLTMLEQNY
DSRAYDQLLD AAVKCNARRT RRDLDTHFTQ YKLARPYIAD CPNCGHSRCD SPIAIEEVRG
DAHAGVIRIQ TSAMFGLKRH GVDLAYMSFM NGKTQKSIKI DNLHVRTSAP CSLVSHHGYY
ILAQCPPGDT VTVGFHDGPN RHTCRLAHKV EFRPVGREKY RHPPEHGVEL PCNRYTHKRA
DQGHYVEMHQ PGLVGDHSLL SIHSAKVKIT VPSGAQVKYY CKCPDVREGI TSSDHTTTCT
DVKQCRAYLI DNKKWVYNSG RLPRGEGDTF KGKLHVPFVP VKAKCIATLA PEPLVEHKHR
TLILHLHPDH PTLLTTRSLG SDANPTRQWI ERPTTVNFTV TGEGLEYTWG NHPPKRVWAQ
ESGEGNPHGW PHVVVVYYYN RYPLTTIIGL CTCVAIIMVS CDHPCGSFSG LRNLCITPYK
LAPNAQVPIL LALLCCIKPT RADDTLQVLN YLWNNNQNFF WMQTLIPLAA LIVCMRMLAA
LFCCGPAFLL VCGAWAAAYE HTAVMPNKVG IPYKALVERP GYAPVHLQIQ LVNTRIIPST
NLEYITCKYK TKVPSPVVKC CGATQCTSKP HPDYQCQVFT GVYPFMWGGA YCFCDTENTQ
MSEAYVERSE ECSIDHAKAY KVHTGTVQAM VNITYGSVTW RSADVYVNGE TPAKIGDAKL
IIGPLSSAWS PFDNKVVVYG HEVYNYDFPE YGTGKAGSFG DLQSRTSTSN DLYANTNLKL
QRPQAGIVHT PFTQAPSGFE RWKRDKGAPL NDVAPFGCSI ALEPLRPENC AVGSIPISID
IPDAAFTRIS ETPTVSDLEC KITECTYASD FGGIATLPTN PVKQETVQFI VHQVLQLLKR
MTSPLLRAGS FTFHFSTANI HPAFKLQVCT SGITCKGDCK PPKDHIVDYP AQHTESFTSA
ISATAWSWLK VLVGGTSAFI VLGLIATAVV ALVLFFHRH


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