POLS_EEVVT
ID POLS_EEVVT Reviewed; 1254 AA.
AC P09592; Q66593; Q66595; Q88691; Q88692; Q88693; Q88694; Q88695;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Structural polyprotein;
DE AltName: Full=p130;
DE Contains:
DE RecName: Full=Capsid protein;
DE EC=3.4.21.90 {ECO:0000250|UniProtKB:P03315};
DE AltName: Full=Coat protein;
DE Short=C;
DE Contains:
DE RecName: Full=Precursor of protein E3/E2;
DE AltName: Full=p62;
DE AltName: Full=pE2;
DE Contains:
DE RecName: Full=Assembly protein E3;
DE Contains:
DE RecName: Full=Spike glycoprotein E2;
DE AltName: Full=E2 envelope glycoprotein;
DE Contains:
DE RecName: Full=6K protein;
DE Contains:
DE RecName: Full=Spike glycoprotein E1;
DE AltName: Full=E1 envelope glycoprotein;
OS Venezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11038;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9268; Didelphis marsupialis (Southern opossum).
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=53535; Melanoconion.
OH NCBI_TaxID=9272; Philander opossum (Gray four-eyed opossum).
OH NCBI_TaxID=10162; Proechimys.
OH NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3088830; DOI=10.1016/0042-6822(86)90142-x;
RA Kinney R.M., Johnson B.J.B., Brown V.L., Trent D.W.;
RT "Nucleotide sequence of the 26 S mRNA of the virulent Trinidad donkey
RT strain of Venezuelan equine encephalitis virus and deduced sequence of the
RT encoded structural proteins.";
RL Virology 152:400-413(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2524126; DOI=10.1016/0042-6822(89)90347-4;
RA Kinney R.M., Johnson B.J.B., Welch J.B., Tsuchiya K.R., Trent D.W.;
RT "The full-length nucleotide sequences of the virulent Trinidad donkey
RT strain of Venezuelan equine encephalitis virus and its attenuated vaccine
RT derivative, strain TC-83.";
RL Virology 170:19-30(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TC-83;
RX PubMed=3755750; DOI=10.1099/0022-1317-67-9-1951;
RA Johnson B.J.B., Kinney R.M., Kost C.L., Trent D.W.;
RT "Molecular determinants of alphavirus neurovirulence: nucleotide and
RT deduced protein sequence changes during attenuation of Venezuelan equine
RT encephalitis virus.";
RL J. Gen. Virol. 67:1951-1960(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CoAn5384;
RX PubMed=9261393; DOI=10.1128/jvi.71.9.6697-6705.1997;
RA Powers A.M., Oberste M.S., Brault A.C., Rico-Hesse R., Schmura S.M.,
RA Smith J.F., Kang W., Sweeney W.P., Weaver S.C.;
RT "Repeated emergence of epidemic/epizootic Venezuelan equine encephalitis
RT from a single genotype of enzootic subtype ID virus.";
RL J. Virol. 71:6697-6705(1997).
RN [5]
RP FUNCTION (CAPSID PROTEIN), AND SUBCELLULAR LOCATION (CAPSID PROTEIN).
RX PubMed=17108023; DOI=10.1128/jvi.02073-06;
RA Garmashova N., Gorchakov R., Volkova E., Paessler S., Frolova E.,
RA Frolov I.;
RT "The Old World and New World alphaviruses use different virus-specific
RT proteins for induction of transcriptional shutoff.";
RL J. Virol. 81:2472-2484(2007).
RN [6]
RP FUNCTION (CAPSID PROTEIN), AND MUTAGENESIS OF LYS-51 AND GLN-52.
RX PubMed=17913819; DOI=10.1128/jvi.01576-07;
RA Garmashova N., Atasheva S., Kang W., Weaver S.C., Frolova E., Frolov I.;
RT "Analysis of Venezuelan equine encephalitis virus capsid protein function
RT in the inhibition of cellular transcription.";
RL J. Virol. 81:13552-13565(2007).
RN [7]
RP FUNCTION (CAPSID PROTEIN), IDENTIFICATION IN COMPLEX WITH HOST CRM1 AND
RP IMPORTIN ALPHA/BETA (CAPSID PROTEIN), NUCLEAR LOCALIZATION SIGNAL,
RP SUPRAPHYSIOLOGICAL NULEAR EXPORT SIGNAL, MUTAGENESIS OF LEU-48; PHE-50;
RP LYS-65 AND LYS-67, SUBCELLULAR LOCATION (CAPSID PROTEIN), AND DOMAIN
RP (CAPSID PROTEIN).
RX PubMed=20147401; DOI=10.1128/jvi.02554-09;
RA Atasheva S., Fish A., Fornerod M., Frolova E.I.;
RT "Venezuelan equine encephalitis virus capsid protein forms a tetrameric
RT complex with CRM1 and importin alpha/beta that obstructs nuclear pore
RT complex function.";
RL J. Virol. 84:4158-4171(2010).
RN [8]
RP DOMAIN (CAPSID PROTEIN).
RX PubMed=26656680; DOI=10.1128/jvi.02680-15;
RA Reynaud J.M., Lulla V., Kim D.Y., Frolova E.I., Frolov I.;
RT "The SD1 Subdomain of Venezuelan Equine Encephalitis Virus Capsid Protein
RT Plays a Critical Role in Nucleocapsid and Particle Assembly.";
RL J. Virol. 90:2008-2020(2016).
RN [9]
RP REVIEW (CAPSID PROTEIN).
RX PubMed=28961161; DOI=10.3390/v9100279;
RA Lundberg L., Carey B., Kehn-Hall K.;
RT "Venezuelan Equine Encephalitis Virus Capsid-The Clever Caper.";
RL Viruses 9:0-0(2017).
RN [10]
RP INTERACTION WITH HOST PPP1CA (CAPSID PROTEIN), PHOSPHORYLATION AT THR-93;
RP THR-108; SER-124 AND THR-127 (CAPSID PROTEIN), AND SUBCELLULAR LOCATION
RP (CAPSID PROTEIN).
RC STRAIN=TC-83, and Trinidad donkey;
RX PubMed=29769351; DOI=10.1128/jvi.02068-17;
RA Carey B.D., Ammosova T., Pinkham C., Lin X., Zhou W., Liotta L.A.,
RA Nekhai S., Kehn-Hall K.;
RT "Protein phosphatase 1alpha interacts with Venezuelan equine encephalitis
RT virus capsid protein and regulates viral replication through modulation of
RT capsid phosphorylation.";
RL J. Virol. 92:0-0(2018).
RN [11]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), FUNCTION (SPIKE GLYCOPROTEIN E2),
RP INTERACTION WITH HOST LDLRAD3 (SPIKE GLYCOPROTEIN E1), AND INTERACTION WITH
RP HOST LDLRAD3 (SPIKE GLYCOPROTEIN E2).
RX PubMed=34646020; DOI=10.1038/s41586-021-03963-9;
RA Basore K., Ma H., Kafai N.M., Mackin S., Kim A.S., Nelson C.A.,
RA Diamond M.S., Fremont D.H.;
RT "Structure of Venezuelan equine encephalitis virus in complex with the
RT LDLRAD3 receptor.";
RL Nature 598:672-676(2021).
RN [12]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), FUNCTION (SPIKE GLYCOPROTEIN E2),
RP INTERACTION WITH HOST LDLRAD3 (SPIKE GLYCOPROTEIN E1), AND INTERACTION WITH
RP HOST LDLRAD3 (SPIKE GLYCOPROTEIN E2).
RX PubMed=34646021; DOI=10.1038/s41586-021-03909-1;
RA Ma B., Huang C., Ma J., Xiang Y., Zhang X.;
RT "Structure of Venezuelan equine encephalitis virus with its receptor
RT LDLRAD3.";
RL Nature 598:677-681(2021).
CC -!- FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4
CC symmetry composed of 240 copies of the capsid protein surrounded by a
CC lipid membrane through which penetrate 80 spikes composed of trimers of
CC E1-E2 heterodimers (By similarity). The capsid protein binds to the
CC viral RNA genome at a site adjacent to a ribosome binding site for
CC viral genome translation following genome release (By similarity).
CC Possesses a protease activity that results in its autocatalytic
CC cleavage from the nascent structural protein (By similarity). Following
CC its self-cleavage, the capsid protein transiently associates with
CC ribosomes, and within several minutes the protein binds to viral RNA
CC and rapidly assembles into icosahedric core particles (By similarity).
CC The resulting nucleocapsid eventually associates with the cytoplasmic
CC domain of the spike glycoprotein E2 at the cell membrane, leading to
CC budding and formation of mature virions (By similarity). In case of
CC infection, new virions attach to target cells and after clathrin-
CC mediated endocytosis their membrane fuses with the host endosomal
CC membrane (By similarity). This leads to the release of the nucleocapsid
CC into the cytoplasm, followed by an uncoating event necessary for the
CC genomic RNA to become accessible (By similarity). The uncoating might
CC be triggered by the interaction of capsid proteins with ribosomes (By
CC similarity). Binding of ribosomes would release the genomic RNA since
CC the same region is genomic RNA-binding and ribosome-binding (By
CC similarity). Specifically inhibits interleukin-1 receptor-associated
CC kinase 1/IRAK1-dependent signaling during viral entry, representing a
CC means by which the alphaviruses may evade innate immune detection and
CC activation prior to viral gene expression (By similarity). Inhibits
CC host transcription (PubMed:17108023, PubMed:17913819). Forms a
CC tetrameric complex with XPO1/CRM1 and the nuclear import receptor
CC importin (PubMed:29769351, PubMed:20147401). This complex blocks the
CC central channel of host nuclear pores thereby inhibiting the receptor-
CC mediated nuclear transport and thus the host mRNA and rRNA
CC transcription (PubMed:29769351, PubMed:20147401). The inhibition of
CC transcription is linked to a cytopathic effect on the host cell
CC (PubMed:17913819). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P27284,
CC ECO:0000269|PubMed:17108023, ECO:0000269|PubMed:17913819,
CC ECO:0000269|PubMed:20147401, ECO:0000269|PubMed:29769351}.
CC -!- FUNCTION: [Assembly protein E3]: Provides the signal sequence for the
CC translocation of the precursor of protein E3/E2 to the host endoplasmic
CC reticulum. Furin-cleaved E3 remains associated with spike glycoprotein
CC E1 and mediates pH protection of the latter during the transport via
CC the secretory pathway. After virion release from the host cell, the
CC assembly protein E3 is gradually released in the extracellular space.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to
CC target host cell, by binding to the cell receptor LDLRAD3
CC (PubMed:34646020, PubMed:34646021). Synthesized as a p62 precursor
CC which is processed by furin at the cell membrane just before virion
CC budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is
CC stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is
CC processed at the last step, presumably to avoid E1 fusion activation
CC before its final export to cell surface. E2 C-terminus contains a
CC transitory transmembrane that would be disrupted by palmitoylation,
CC resulting in reorientation of the C-terminal tail from lumenal to
CC cytoplasmic side. This step is critical since E2 C-terminus is involved
CC in budding by interacting with capsid proteins. This release of E2 C-
CC terminus in cytoplasm occurs lately in protein export, and precludes
CC premature assembly of particles at the endoplasmic reticulum membrane
CC (By similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}.
CC -!- FUNCTION: [6K protein]: Constitutive membrane protein involved in virus
CC glycoprotein processing, cell permeabilization, and the budding of
CC viral particles. Disrupts the calcium homeostasis of the cell, probably
CC at the endoplasmic reticulum level. This leads to cytoplasmic calcium
CC elevation. Because of its lipophilic properties, the 6K protein is
CC postulated to influence the selection of lipids that interact with the
CC transmembrane domains of the glycoproteins, which, in turn, affects the
CC deformability of the bilayer required for the extreme curvature that
CC occurs as budding proceeds. Present in low amount in virions, about 3%
CC compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein.
CC Fusion activity is inactive as long as E1 is bound to E2 in mature
CC virion. After virus attachment to cell receptor LDLRAD3 and
CC endocytosis, acidification of the endosome would induce dissociation of
CC E1/E2 heterodimer and concomitant trimerization of the E1 subunits
CC (PubMed:34646020, PubMed:34646021). This E1 trimer is fusion active,
CC and promotes release of viral nucleocapsid in cytoplasm after endosome
CC and viral membrane fusion. Efficient fusion requires the presence of
CC cholesterol and sphingolipid in the target membrane. Fusion is optimal
CC at levels of about 1 molecule of cholesterol per 2 molecules of
CC phospholipids, and is specific for sterols containing a 3-beta-hydroxyl
CC group (By similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytic release of the core protein from the N-terminus
CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316};
CC -!- SUBUNIT: [Capsid protein]: Part of a tetrameric complex composed of
CC host CRM1, host importin alpha/beta dimer and the viral capsid; this
CC complex blocks the receptor-mediated transport through the nuclear pore
CC (PubMed:20147401). Interacts with host phosphatase PPP1CA; this
CC interaction dephosphorylates the capsid protein, which increases its
CC ability to bind to the viral genome (PubMed:29769351).
CC {ECO:0000269|PubMed:20147401, ECO:0000269|PubMed:29769351}.
CC -!- SUBUNIT: [Precursor of protein E3/E2]: The precursor of protein E3/E2
CC and E1 form a heterodimer shortly after synthesis (By similarity).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: The precursor of protein E3/E2 and E1
CC form a heterodimer shortly after synthesis (By similarity). Processing
CC of the precursor of protein E3/E2 into E2 and E3 results in a
CC heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike
CC at virion surface are constituted of three E2-E1 heterodimers. After
CC target cell attachment and endocytosis, E1 change conformation to form
CC homotrimers (By similarity). Interacts with 6K protein (By similarity).
CC Interacts with host LDLRAD3; this interaction mediates viral entry to
CC the host cell (PubMed:34646020, PubMed:34646021).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC ECO:0000269|PubMed:34646020, ECO:0000269|PubMed:34646021}.
CC -!- SUBUNIT: [Spike glycoprotein E2]: Processing of the precursor of
CC protein E3/E2 into E2 and E3 results in a heterodimer of the spike
CC glycoproteins E2 and E1 (By similarity). Spike at virion surface are
CC constituted of three E2-E1 heterodimers (By similarity). Interacts with
CC 6K protein (By similarity). Interacts with host LDLRAD3; this
CC interaction mediates viral entry to the host cell (PubMed:34646020,
CC PubMed:34646021). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000269|PubMed:34646020,
CC ECO:0000269|PubMed:34646021}.
CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1 (By
CC similarity). Interacts with spike glycoprotein E2 (By similarity).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC {ECO:0000269|PubMed:17108023, ECO:0000269|PubMed:29769351}. Host cell
CC membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus
CC {ECO:0000269|PubMed:17108023, ECO:0000269|PubMed:20147401}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
CC {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been
CC autocleaved, an internal uncleaved signal peptide directs the remaining
CC polyprotein to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- DOMAIN: [Capsid protein]: The very N-terminus plays a role in the
CC particle assembly process (PubMed:26656680). The N-terminus also
CC contains a nuclear localization signal and a supraphysiological nuclear
CC export signal (supraNES), which is an unusually strong NES that
CC mediates host CRM1 binding in the absence of RanGTP and thus can bind
CC CRM1, not only in the nucleus, but also in the cytoplasm
CC (PubMed:20147401). The C-terminus functions as a protease during
CC translation to cleave itself from the translating structural
CC polyprotein (By similarity). {ECO:0000250|UniProtKB:P03316,
CC ECO:0000269|PubMed:20147401, ECO:0000269|PubMed:26656680}.
CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC mature proteins. Capsid protein is auto-cleaved during polyprotein
CC translation, unmasking a signal peptide at the N-terminus of the
CC precursor of E3/E2. The remaining polyprotein is then targeted to the
CC host endoplasmic reticulum, where host signal peptidase cleaves it into
CC pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2
CC by host furin in trans-Golgi vesicle. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E2]: Palmitoylated via thioester bonds. These
CC palmitoylations may induce disruption of the C-terminus transmembrane.
CC This would result in the reorientation of E2 C-terminus from lumenal to
CC cytoplasmic side. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Capsid protein]: Phosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:29769351}.
CC -!- PTM: [Spike glycoprotein E1]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E2]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Assembly protein E3]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [6K protein]: Palmitoylated via thioester bonds.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togavirus replication.
CC {ECO:0000250|UniProtKB:Q86925}.
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DR EMBL; M14937; AAA42997.1; -; Genomic_RNA.
DR EMBL; J04332; AAB02519.1; -; Genomic_RNA.
DR EMBL; L01443; AAB02517.1; -; Genomic_RNA.
DR EMBL; L01442; AAC19322.1; -; Genomic_RNA.
DR EMBL; AF004466; AAC36382.1; -; Genomic_RNA.
DR PIR; B31467; VHWVVT.
DR PDB; 3VE6; X-ray; 2.83 A; B=59-70.
DR PDBsum; 3VE6; -.
DR SMR; P09592; -.
DR MEROPS; S03.001; -.
DR iPTMnet; P09592; -.
DR Proteomes; UP000008659; Genome.
DR Proteomes; UP000127220; Genome.
DR Proteomes; UP000146452; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0039653; P:suppression by virus of host transcription; IDA:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.40.2400; -; 1.
DR Gene3D; 2.60.40.3200; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.40.4310; -; 1.
DR Gene3D; 2.60.98.10; -; 3.
DR InterPro; IPR002548; Alpha_E1_glycop.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR002533; Alpha_E3_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
DR Pfam; PF01589; Alpha_E1_glycop; 1.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
DR Pfam; PF01563; Alpha_E3_glycop; 1.
DR Pfam; PF00944; Peptidase_S3; 1.
DR PRINTS; PR00798; TOGAVIRIN.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host cytoplasm; Host gene expression shutoff by virus;
KW Host membrane; Host mRNA suppression by virus; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host mRNA nuclear export by virus; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Protease; RNA-binding; Serine protease;
KW T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..275
FT /note="Capsid protein"
FT /id="PRO_0000041276"
FT CHAIN 276..757
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000234323"
FT CHAIN 276..334
FT /note="Assembly protein E3"
FT /id="PRO_0000041277"
FT CHAIN 335..757
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041278"
FT CHAIN 758..812
FT /note="6K protein"
FT /id="PRO_0000041279"
FT CHAIN 813..1254
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041280"
FT TOPO_DOM 276..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..772
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 817..1224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..275
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..33
FT /note="Necessary for nucleocapsid assembly and virus
FT assembly"
FT /evidence="ECO:0000269|PubMed:26656680"
FT REGION 33..68
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000269|PubMed:17913819"
FT REGION 45..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..127
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 112..126
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 276..287
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 730..750
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 896..913
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 41..48
FT /note="Supraphysiological nuclear export signal"
FT /evidence="ECO:0000269|PubMed:20147401"
FT MOTIF 64..68
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:20147401"
FT COMPBIAS 57..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 200
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 233
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 275..276
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 334..335
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 757..758
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 812..813
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29769351"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29769351"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29769351"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29769351"
FT LIPID 730
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 750
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 751
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 861..926
FT /evidence="ECO:0000250"
FT DISULFID 874..906
FT /evidence="ECO:0000250"
FT DISULFID 875..908
FT /evidence="ECO:0000250"
FT DISULFID 880..890
FT /evidence="ECO:0000250"
FT DISULFID 1071..1083
FT /evidence="ECO:0000250"
FT DISULFID 1113..1188
FT /evidence="ECO:0000250"
FT DISULFID 1118..1192
FT /evidence="ECO:0000250"
FT DISULFID 1140..1182
FT /evidence="ECO:0000250"
FT VARIANT 341
FT /note="K -> N (in strain: Isolate TC-83)"
FT VARIANT 419
FT /note="H -> Y (in strain: Isolate TC-83)"
FT VARIANT 454
FT /note="T -> R (in strain: Isolate TC-83)"
FT VARIANT 526
FT /note="V -> D (in strain: Isolate TC-83)"
FT VARIANT 630
FT /note="T -> I (in strain: Isolate TC-83)"
FT VARIANT 810
FT /note="A -> GA (in strain: Isolate CoAn5384 and Isolate TC-
FT 83)"
FT VARIANT 811
FT /note="G -> P"
FT VARIANT 973
FT /note="L -> I (in strain: Isolate TC-83)"
FT MUTAGEN 48
FT /note="L->A: Complete loss of capsid protein nuclear
FT export; when associated with A-50."
FT /evidence="ECO:0000269|PubMed:20147401"
FT MUTAGEN 50
FT /note="F->A: Complete loss of capsid protein nuclear
FT export; when associated with A-48."
FT /evidence="ECO:0000269|PubMed:20147401"
FT MUTAGEN 51
FT /note="K->E: Non-cytopathic, incapable of inhibiting host
FT transcription."
FT /evidence="ECO:0000269|PubMed:17913819"
FT MUTAGEN 52
FT /note="Q->P: Non-cytopathic, incapable of inhibiting host
FT transcription."
FT /evidence="ECO:0000269|PubMed:17913819"
FT MUTAGEN 65
FT /note="K->A: Complete loss of capsid protein nuclear
FT localization; when associated with A-67."
FT /evidence="ECO:0000269|PubMed:20147401"
FT MUTAGEN 67
FT /note="K->A: Complete loss of capsid protein nuclear
FT localization; when associated with A-65."
FT /evidence="ECO:0000269|PubMed:20147401"
SQ SEQUENCE 1254 AA; 138351 MW; 8B5398709A1B4020 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 KEYKLTRPYM ARCIRCAVGS
CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIKE IPLHQVSLHT
SRPCHIVDGH GYFLLARCPA GDSITMEFKK DSVTHSCSVP YEVKFNPVGR ELYTHPPEHG
VEQACQVYAH DAQNRGAYVE MHLPGSEVDS SLVSLSGSSV TVTPPVGTSA LVECECGGTK
ISETINKTKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLT TRQLADEPHY THELISEPAV RNFTVTEKGW
EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IATVSVAAST
WLFCRSRVAC LTPYRLTPNA RIPFCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
IPLAALIVVT RLLRCVCCVV PFLVMAGAAA GAYEHATTMP SQAGISYNTI VNRAGYAPLP
ISITPTKIKL IPTVNLEYVT CHYKTGMDSP AIKCCGSQEC TPTYRPDEQC KVFTGVYPFM
WGGAYCFCDT ENTQVSKAYV MKSDDCLADH AEAYKAHTAS VQAFLNITVG EHSIVTTVYV
NGETPVNFNG VKLTAGPLST 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
