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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_EEVV8              Reviewed;        1254 AA.
P05674;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
05-DEC-2018, entry version 123.
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;
Venezuelan equine encephalitis virus (strain TC-83) (VEEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11037;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9268; Didelphis marsupialis (Southern opossum).
NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53535; Melanoconion.
NCBI_TaxID=9272; Philander opossum (Gray four-eyed opossum).
NCBI_TaxID=10162; Proechimys.
NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3755750; DOI=10.1099/0022-1317-67-9-1951;
Johnson B.J.B., Kinney R.M., Kost C.L., Trent D.W.;
"Molecular determinants of alphavirus neurovirulence: nucleotide and
deduced protein sequence changes during attenuation of Venezuelan
equine encephalitis virus.";
J. Gen. Virol. 67:1951-1960(1986).
-!- 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; X04368; CAA27883.1; -; mRNA.
PIR; A27871; VHWVVE.
PDB; 1EP5; X-ray; 2.30 A; A/B/C=119-275.
PDB; 1EP6; X-ray; 2.45 A; A/B/C=119-275.
PDB; 3J0C; EM; -; A/D/G/J=813-1254, B/E/H/K=335-757, C/F/I/L=114-275.
PDB; 3J0G; EM; -; M/N/O/P=276-334.
PDBsum; 1EP5; -.
PDBsum; 1EP6; -.
PDBsum; 3J0C; -.
PDBsum; 3J0G; -.
ProteinModelPortal; P05674; -.
SMR; P05674; -.
MEROPS; S03.001; -.
PRIDE; P05674; -.
EvolutionaryTrace; P05674; -.
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:0019031; C:viral envelope; 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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
3D-structure; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
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 envelope protein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 275 Capsid protein.
/FTId=PRO_0000041256.
CHAIN 276 757 Precursor of protein E3/E2.
/FTId=PRO_0000234319.
CHAIN 276 334 Assembly protein E3.
/FTId=PRO_0000041257.
CHAIN 335 757 Spike glycoprotein E2.
/FTId=PRO_0000041258.
CHAIN 758 812 6K protein.
/FTId=PRO_0000041259.
CHAIN 813 1254 Spike glycoprotein E1.
/FTId=PRO_0000041260.
TOPO_DOM 276 701 Extracellular. {ECO:0000255}.
TRANSMEM 702 722 Helical. {ECO:0000255}.
TOPO_DOM 723 757 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 758 772 Extracellular. {ECO:0000255}.
TRANSMEM 773 793 Helical. {ECO:0000255}.
TOPO_DOM 794 795 Cytoplasmic. {ECO:0000255}.
TRANSMEM 796 816 Helical. {ECO:0000255}.
TOPO_DOM 817 1224 Extracellular. {ECO:0000255}.
TRANSMEM 1225 1245 Helical. {ECO:0000255}.
TOPO_DOM 1246 1254 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 275 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 91 113 Ribosome-binding. {ECO:0000250}.
REGION 276 287 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 896 913 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 152 152 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 174 174 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 226 226 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 275 276 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 757 758 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 812 813 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 730 730 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 750 750 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 751 751 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 946 946 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 861 926 {ECO:0000250}.
DISULFID 874 906 {ECO:0000250}.
DISULFID 875 908 {ECO:0000250}.
DISULFID 880 890 {ECO:0000250}.
DISULFID 1071 1083 {ECO:0000250}.
DISULFID 1113 1188 {ECO:0000250}.
DISULFID 1118 1192 {ECO:0000250}.
DISULFID 1140 1182 {ECO:0000250}.
STRAND 127 132 {ECO:0000244|PDB:1EP5}.
STRAND 135 143 {ECO:0000244|PDB:1EP5}.
STRAND 146 150 {ECO:0000244|PDB:1EP5}.
STRAND 155 159 {ECO:0000244|PDB:1EP5}.
HELIX 160 164 {ECO:0000244|PDB:1EP5}.
STRAND 168 170 {ECO:0000244|PDB:1EP5}.
TURN 171 174 {ECO:0000244|PDB:1EP5}.
STRAND 175 179 {ECO:0000244|PDB:1EP5}.
TURN 182 186 {ECO:0000244|PDB:1EP5}.
STRAND 187 189 {ECO:0000244|PDB:1EP5}.
STRAND 197 202 {ECO:0000244|PDB:1EP5}.
STRAND 205 210 {ECO:0000244|PDB:1EP5}.
STRAND 213 217 {ECO:0000244|PDB:1EP5}.
STRAND 229 231 {ECO:0000244|PDB:1EP5}.
STRAND 237 247 {ECO:0000244|PDB:1EP5}.
STRAND 250 258 {ECO:0000244|PDB:1EP5}.
STRAND 262 267 {ECO:0000244|PDB:1EP5}.
SEQUENCE 1254 AA; 138486 MW; 7615698519A529F6 CRC64;
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF KQRRDAPPEG
PSAKKPKKEA SQKQKGGGQG KKKKNQGKKK AKTGPPNPKA QNGNKKKTNK KPGKRQRMVM
KLESDKTFPI MLEGKINGYA CVVGGKLFRP MHVEGKIDND VLAALKTKKA SKYDLEYADV
PQNMRADTFK YTHEKPQGYY SWHHGAVQYE NGRFTVPKGV GAKGDSGRPI LDNQGRVVAI
VLGGVNEGSR TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAQPPICYDR
KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF NEYKLTRPYM ARCIRCAVGS
CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIKE IPLHQVSLYT
SRPCHIVDGH GYFLLARCPA GDSITMEFKK DSVRHSCSVP YEVKFNPVGR ELYTHPPEHG
VEQACQVYAH DAQNRGAYVE MHLPGSEVDS SLVSLSGSSV TVTPPDGTSA LVECECGGTK
ISETINKTKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLI TRQLADEPHY THELISEPAV RNFTVTEKGW
EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IATVSVAAST
WLFCRSRVAC LTPYRLTPNA RIPFCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
IPLAALIVVT RLLRCVCCVV PFLVMAGAAA PAYEHATTMP SQAGISYNTI VNRAGYAPLP
ISITPTKIKL IPTVNLEYVT CHYKTGMDSP AIKCCGSQEC TPTYRPDEQC KVFTGVYPFM
WGGAYCFCDT ENTQVSKAYV MKSDDCLADH AEAYKAHTAS VQAFLNITVG EHSIVTTVYV
NGETPVNFNG VKITAGPLST AWTPFDRKIV QYAGEIYNYD FPEYGAGQPG AFGDIQSRTV
SSSDLYANTN LVLQRPKAGA IHVPYTQAPS GFEQWKKDKA PSLKFTAPFG CEIYTNPIRA
ENCAVGSIPL AFDIPDALFT RVSETPTLSA AECTLNECVY SSDFGGIATV KYSASKSGKC
AVHVPSGTAT LKEAAVELTE QGSATIHFST ANIHPEFRLQ ICTSYVTCKG DCHPPKDHIV
THPQYHAQTF TAAVSKTAWT WLTSLLGGSA VIIIIGLVLA TIVAMYVLTN QKHN


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