POLS_CHIKS
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 03-AUG-2022, entry version 120.
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.
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 SMR; Q8JUX5; -.
DR BindingDB; Q8JUX5; -.
DR MEROPS; S03.001; -.
DR ABCD; Q8JUX5; 18 sequenced antibodies.
DR GeneID; 956308; -.
DR KEGG; vg:956308; -.
DR SABIO-RK; Q8JUX5; -.
DR Proteomes; UP000000569; Genome.
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: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: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; 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; 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
