ID   POLS_CHIKS              Reviewed;        1248 AA.
AC   Q8JUX5; Q80S29; Q8QR21;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 125.
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   Chikungunya virus (strain S27-African prototype) (CHIKV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus; Chikungunya virus.
OX   NCBI_TaxID=371094;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=299627; Aedes furcifer (Mosquito).
OH   NCBI_TaxID=188700; Aedes polynesiensis (Polynesian tiger mosquito).
OH   NCBI_TaxID=9533; Cercopithecus.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH   NCBI_TaxID=9554; Papio (baboons).
OH   NCBI_TaxID=9573; Presbytis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12466484; DOI=10.1099/0022-1317-83-12-3075;
RA   Khan A.H., Morita K., Parquet Md Mdel C., Hasebe F., Mathenge E.G.,
RA   Igarashi A.;
RT   "Complete nucleotide sequence of chikungunya virus and evidence for an
RT   internal polyadenylation site.";
RL   J. Gen. Virol. 83:3075-3084(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Kinney R.M., Pfeffer M.;
RT   "Nucleotide sequence analyses of the 26S mRNAs of viruses of the genus
RT   Alphavirus.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Ross;
RA   Logue C.H., Atkins G.J.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE REVISION TO 91-97; 576 AND 592.
RA   Logue C.H., Chamberlain J.F., Atkins G.J.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION
RP   (SPIKE GLYCOPROTEIN E1).
RX   PubMed=6726893; DOI=10.1128/jvi.51.1.254-258.1984;
RA   Simizu B., Yamamoto K., Hashimoto K., Ogata T.;
RT   "Structural proteins of Chikungunya virus.";
RL   J. Virol. 51:254-258(1984).
RN   [6]
RP   SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1), AND SUBCELLULAR LOCATION
RP   (SPIKE GLYCOPROTEIN E2).
RX   PubMed=21762510; DOI=10.1186/1743-422x-8-353;
RA   Metz S.W., Geertsema C., Martina B.E., Andrade P., Heldens J.G.,
RA   van Oers M.M., Goldbach R.W., Vlak J.M., Pijlman G.P.;
RT   "Functional processing and secretion of Chikungunya virus E1 and E2
RT   glycoproteins in insect cells.";
RL   Virol. J. 8:353-353(2011).
RN   [7]
RP   SUBCELLULAR LOCATION (CAPSID PROTEIN), NUCLEAR LOCALIZATION SIGNAL, NULEAR
RP   EXPORT SIGNAL, AND INTERACTION WITH HOST KPNA4 (CAPSID PROTEIN).
RX   PubMed=23984714; DOI=10.1186/1743-422x-10-269;
RA   Thomas S., Rai J., John L., Schaefer S., Puetzer B.M., Herchenroeder O.;
RT   "Chikungunya virus capsid protein contains nuclear import and export
RT   signals.";
RL   Virol. J. 10:269-269(2013).
RN   [8]
RP   NULEAR EXPORT SIGNAL, SUBCELLULAR LOCATION (CAPSID PROTEIN), AND
RP   MUTAGENESIS OF LEU-51 AND MET-53.
RX   PubMed=29053568; DOI=10.3390/v9100306;
RA   Jacobs S.C., Taylor A., Herrero L.J., Mahalingam S., Fazakerley J.K.;
RT   "Mutation of a conserved nuclear export sequence in Chikungunya virus
RT   capsid protein disrupts host cell nuclear import.";
RL   Viruses 9:0-0(2017).
RN   [9]
RP   FUNCTION (SPIKE GLYCOPROTEIN E2), AND INTERACTION WITH HOST MXRA8 (SPIKE
RP   GLYCOPROTEIN E2).
RX   PubMed=29769725; DOI=10.1038/s41586-018-0121-3;
RA   Zhang R., Kim A.S., Fox J.M., Nair S., Basore K., Klimstra W.B.,
RA   Rimkunas R., Fong R.H., Lin H., Poddar S., Crowe J.E. Jr., Doranz B.J.,
RA   Fremont D.H., Diamond M.S.;
RT   "Mxra8 is a receptor for multiple arthritogenic alphaviruses.";
RL   Nature 557:570-574(2018).
RN   [10]
RP   FUNCTION (CAPSID PROTEIN).
RX   PubMed=33057424; DOI=10.1371/journal.ppat.1008999;
RA   Webb L.G., Veloz J., Pintado-Silva J., Zhu T., Rangel M.V., Mutetwa T.,
RA   Zhang L., Bernal-Rubio D., Figueroa D., Carrau L., Fenutria R., Potla U.,
RA   Reid S.P., Yount J.S., Stapleford K.A., Aguirre S., Fernandez-Sesma A.;
RT   "Chikungunya virus antagonizes cGAS-STING mediated type-I interferon
RT   responses by degrading cGAS.";
RL   PLoS Pathog. 16:e1008999-e1008999(2020).
RN   [11]
RP   STRUCTURE BY NMR OF 893-910, AND FUNCTION (SPIKE GLYCOPROTEIN E1).
RX   PubMed=22978677; DOI=10.1021/bi300901f;
RA   Mohanram H., Nip A., Domadia P.N., Bhunia A., Bhattacharjya S.;
RT   "NMR structure, localization, and vesicle fusion of Chikungunya virus
RT   fusion peptide.";
RL   Biochemistry 51:7863-7872(2012).
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). Degrades
CC       host cyclic GMP-AMP synthase (CGAS) thereby inhibiting the cGAS-STING
CC       pathway (PubMed:33057424). {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P27284,
CC       ECO:0000269|PubMed:33057424}.
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 MXRA8
CC       (PubMed:29769725). Synthesized as a p62 precursor which is processed by
CC       furin at the cell membrane just before virion budding, giving rise to
CC       E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is
CC       unstable and dissociate at low pH. p62 is processed at the last step,
CC       presumably to avoid E1 fusion activation before its final export to
CC       cell surface. E2 C-terminus contains a transitory transmembrane that
CC       would be disrupted by palmitoylation, resulting in reorientation of the
CC       C-terminal tail from lumenal to cytoplasmic side. This step is critical
CC       since E2 C-terminus is involved in budding by interacting with capsid
CC       proteins. This release of E2 C-terminus in cytoplasm occurs lately in
CC       protein export, and precludes premature assembly of particles at the
CC       endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000269|PubMed:29769725}.
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 target cell and endocytosis,
CC       acidification of the endosome would induce dissociation of E1/E2
CC       heterodimer and concomitant trimerization of the E1 subunits. This E1
CC       trimer is fusion active, and promotes release of viral nucleocapsid in
CC       cytoplasm after endosome and viral membrane fusion. Efficient fusion
CC       requires the presence of cholesterol and sphingolipid in the target
CC       membrane. Fusion is optimal at levels of about 1 molecule of
CC       cholesterol per 2 molecules of phospholipids, and is specific for
CC       sterols containing a 3-beta-hydroxyl group.
CC       {ECO:0000250|UniProtKB:P03315, ECO:0000269|PubMed:22978677}.
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]: Homodimer (By similarity). Homomultimer
CC       (Probable). Interacts with host karyopherin KPNA4; this interaction
CC       allows the nuclear import of the viral capsid protein
CC       (PubMed:23984714). Interacts with spike glycoprotein E2 (By
CC       similarity). Interacts with host IRAK1; the interaction leads to
CC       inhibition of IRAK1-dependent signaling (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000269|PubMed:23984714,
CC       ECO:0000305}.
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       ECO:0000250|UniProtKB:P0DOK1}.
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 (By
CC       similarity). After target cell attachment and endocytosis, E1 change
CC       conformation to form homotrimers (By similarity). Interacts with 6K
CC       protein (By similarity). {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1}.
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       capsid protein (By similarity). Interacts with 6K protein (By
CC       similarity). Interacts with host MXRA8; this interaction mediates virus
CC       entry (PubMed:29769725). {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC       ECO:0000269|PubMed:29769725}.
CC   -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1. Interacts
CC       with spike glycoprotein E2 (By similarity).
CC       {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC       ECO:0000250|UniProtKB:P0DOK1}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC       {ECO:0000269|PubMed:29053568}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P03316}. Host nucleus
CC       {ECO:0000269|PubMed:29053568}. Note=Shuttles between the cytoplasm and
CC       the nucleus. {ECO:0000269|PubMed:23984714,
CC       ECO:0000269|PubMed:29053568}.
CC   -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC       {ECO:0000269|PubMed:6726893}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:21762510}.
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:0000269|PubMed:6726893}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316,
CC       ECO:0000269|PubMed:21762510}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Structural polyprotein;
CC         IsoId=Q8JUX5-1; Sequence=Displayed;
CC       Name=Frameshifted structural polyprotein;
CC         IsoId=P0DOK1-1; Sequence=External;
CC   -!- DOMAIN: [Capsid protein]: The N-terminus contains a nuclear
CC       localization signal and a CRM1-mediated nuclear export signal
CC       (PubMed:23984714). 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:23984714}.
CC   -!- DOMAIN: [Isoform Structural polyprotein]: As soon as the capsid protein
CC       has been autocleaved, an internal uncleaved signal peptide directs the
CC       remaining polyprotein to the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: [Isoform Structural polyprotein]: Specific enzymatic cleavages in
CC       vivo yield mature proteins. Capsid protein is auto-cleaved during
CC       polyprotein translation, unmasking a signal peptide at the N-terminus
CC       of the precursor of E3/E2 (By similarity). The remaining polyprotein is
CC       then targeted to the host endoplasmic reticulum, where host signal
CC       peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further
CC       processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By
CC       similarity). {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: [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: [Isoform Structural polyprotein]: Translated from a
CC       subgenomic RNA synthesized during togavirus replication.
CC       {ECO:0000250|UniProtKB:Q86925}.
CC   -!- MISCELLANEOUS: [Isoform Structural polyprotein]: Produced by
CC       conventional translation.
CC   -!- SIMILARITY: Belongs to the alphavirus structural polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AF369024; AAN05102.2; -; Genomic_RNA.
DR   EMBL; AF339485; AAO33341.1; -; Genomic_RNA.
DR   EMBL; AF490259; AAM10747.2; -; Genomic_RNA.
DR   RefSeq; NP_690589.2; NC_004162.2.
DR   PDB; 2RSW; NMR; -; A=893-910.
DR   PDB; 7CVY; EM; 5.20 A; A/F/K/P=810-1248, B/G/L/Q=330-748, C/H/M/R=111-261.
DR   PDB; 7CVZ; EM; 4.70 A; A/D/G/J=810-1248, B/E/H/K=330-748, C/F/I/L=111-261.
DR   PDB; 7CW0; EM; 5.90 A; A/D/G/J=810-1248, B/E/H/K=330-748, C/F/I/L=111-261.
DR   PDB; 7CW2; EM; 4.50 A; A/D/G/J/M/P/a/d/g/j/m/p/s/v/y=810-1248, B/E/H/K/N/Q/b/e/h/k/n/q/t/w/z=330-748, C/F/I/L/O/R/S/c/f/i/l/o/r/u/x=111-261.
DR   PDB; 7CW3; EM; 9.40 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i=810-1248, B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j=330-748, s/t=111-261.
DR   PDBsum; 2RSW; -.
DR   PDBsum; 7CVY; -.
DR   PDBsum; 7CVZ; -.
DR   PDBsum; 7CW0; -.
DR   PDBsum; 7CW2; -.
DR   PDBsum; 7CW3; -.
DR   BMRB; Q8JUX5; -.
DR   EMDB; EMD-30476; -.
DR   EMDB; EMD-30477; -.
DR   EMDB; EMD-30478; -.
DR   EMDB; EMD-30479; -.
DR   EMDB; EMD-30480; -.
DR   SMR; Q8JUX5; -.
DR   BindingDB; Q8JUX5; -.
DR   MEROPS; S03.001; -.
DR   ABCD; Q8JUX5; 18 sequenced antibodies.
DR   KEGG; vg:956308; -.
DR   SABIO-RK; Q8JUX5; -.
DR   Proteomes; UP000000569; Segment.
DR   Proteomes; UP000126290; 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:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039619; C:T=4 icosahedral viral capsid; 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: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:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.2230; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1.
DR   Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1.
DR   Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; SSF81296; E set domains; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR   PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Cleavage on pair of basic residues;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host cytoplasm; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Protease; Reference proteome; Ribosomal frameshifting; RNA-binding;
KW   Serine protease; T=4 icosahedral capsid protein; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..261
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226219"
FT   CHAIN           262..748
FT                   /note="Precursor of protein E3/E2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226220"
FT   CHAIN           262..325
FT                   /note="Assembly protein E3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226221"
FT   CHAIN           326..748
FT                   /note="Spike glycoprotein E2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226222"
FT   CHAIN           749..809
FT                   /note="6K protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226223"
FT   CHAIN           810..1248
FT                   /note="Spike glycoprotein E1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226224"
FT   TOPO_DOM        262..692
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        714..748
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        749..763
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        764..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        785..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..1248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          113..261
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..68
FT                   /note="Host transcription inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   REGION          84..114
FT                   /note="Binding to the viral RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P27284"
FT   REGION          99..113
FT                   /note="Ribosome-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P27284"
FT   REGION          183..193
FT                   /note="Dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT   REGION          219..223
FT                   /note="Dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT   REGION          262..274
FT                   /note="Functions as an uncleaved signal peptide for the
FT                   precursor of protein E3/E2"
FT                   /evidence="ECO:0000250|UniProtKB:P03315"
FT   REGION          721..741
FT                   /note="Transient transmembrane before p62-6K protein
FT                   processing"
FT                   /evidence="ECO:0000255"
FT   REGION          893..910
FT                   /note="E1 fusion peptide loop"
FT                   /evidence="ECO:0000269|PubMed:22978677"
FT   MOTIF           61..99
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   MOTIF           144..154
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   COMPBIAS        73..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   SITE            187
FT                   /note="Involved in dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q86925"
FT   SITE            220
FT                   /note="Involved in dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q86925"
FT   SITE            261..262
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03315"
FT   SITE            325..326
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   SITE            748..749
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   SITE            809..810
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   LIPID           721
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           741
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           742
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           1242
FT                   /note="S-stearoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        670
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        950
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        858..923
FT                   /evidence="ECO:0000250"
FT   DISULFID        871..903
FT                   /evidence="ECO:0000250"
FT   DISULFID        872..905
FT                   /evidence="ECO:0000250"
FT   DISULFID        877..887
FT                   /evidence="ECO:0000250"
FT   DISULFID        1068..1080
FT                   /evidence="ECO:0000250"
FT   DISULFID        1110..1185
FT                   /evidence="ECO:0000250"
FT   DISULFID        1115..1189
FT                   /evidence="ECO:0000250"
FT   DISULFID        1137..1179
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         51
FT                   /note="L->A: Complete loss of nuclear expot of the capsid
FT                   protein; when associated with A-53."
FT                   /evidence="ECO:0000269|PubMed:29053568"
FT   MUTAGEN         53
FT                   /note="M->A: Complete loss of nuclear expot of the capsid
FT                   protein; when associated with A-51."
FT                   /evidence="ECO:0000269|PubMed:29053568"
FT   CONFLICT        63
FT                   /note="R -> K (in Ref. 1; AAN05102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519..520
FT                   /note="GR -> SQ (in Ref. 1; AAN05102)"
FT                   /evidence="ECO:0000305"
FT   HELIX           895..899
FT                   /evidence="ECO:0007829|PDB:2RSW"
FT   TURN            904..907
FT                   /evidence="ECO:0007829|PDB:2RSW"
SQ   SEQUENCE   1248 AA;  138114 MW;  1A2CEB5671529482 CRC64;
     MEFIPTQTFY NRRYQPRPWT PRPTIQVIRP RPRPQRQAGQ LAQLISAVNK LTMRAVPQQK
     PRRNRKNKKQ KQKQQAPQNN TNQKKQPPKK KPAQKKKKPG RRERMCMKIE NDCIFEVKHE
     GKVTGYACLV GDKVMKPAHV KGTIDNADLA KLAFKRSSKY DLECAQIPVH MKSDASKFTH
     EKPEGYYNWH HGAVQYSGGR FTIPTGAGKP GDSGRPIFDN KGRVVAIVLG GANEGARTAL
     SVVTWNKDIV TKITPEGAEE WSLAIPVMCL LANTTFPCSQ PPCIPCCYEK EPEETLRMLE
     DNVMRPGYYQ LLQASLTCSP HRQRRSTKDN FNVYKATRPY LAHCPDCGEG HSCHSPVALE
     RIRNEATDGT LKIQVSLQIG IGTDDSHDWT KLRYMDNHIP ADAGRAGLFV RTSAPCTITG
     TMGHFILARC PKGETLTVGF TDSRKISHSC THPFHHDPPV IGREKFHSRP QHGKELPCST
     YVQSNAATAE EIEVHMPPDT PDRTLLSQQS GNVKITVNGR TVRYKCNCGG SNEGLITTDK
     VINNCKVDQC HAAVTNHKKW QYNSPLVPRN AELGDRKGKI HIPFPLANVT CMVPKARNPT
     VTYGKNQVIM LLYPDHPTLL SYRSMGEEPN YQEEWVTHKK EVVLTVPTEG LEVTWGNNEP
     YKYWPQLSAN GTAHGHPHEI ILYYYELYPT MTVVVVSVAS FILLSMVGMA VGMCMCARRR
     CITPYELTPG ATVPFLLSLI CCIRTAKAAT YQEAAVYLWN EQQPLFWLQA LIPLAALIVL
     CNCLRLLPCC CKTLAFLAVM SIGAHTVSAY EHVTVIPNTV GVPYKTLVNR PGYSPMVLEM
     ELLSVTLEPT LSLDYITCEY KTVIPSPYVK CCGTAECKDK NLPDYSCKVF TGVYPFMWGG
     AYCFCDAENT QLSEAHVEKS ESCKTEFASA YRAHTASASA KLRVLYQGNN ITVTAYANGD
     HAVTVKDAKF IVGPMSSAWT PFDNKIVVYK GDVYNMDYPP FGAGRPGQFG DIQSRTPESK
     DVYANTQLVL QRPAAGTVHV PYSQAPSGFK YWLKERGASL QHTAPFGCQI ATNPVRAMNC
     AVGNMPISID IPDAAFTRVV DAPSLTDMSC EVPACTHSSD FGGVAIIKYA VSKKGKCAVH
     SMTNAVTIRE AEIEVEGNSQ LQISFSTALA SAEFRVQVCS TQVHCAAECH PPKDHIVNYP
     ASHTTLGVQD ISATAMSWVQ KITGGVGLVV AVAALILIVV LCVSFSRH
//