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

 POLS_SINDV              Reviewed;        1245 AA.
P03316; C4T9C2; P11259; Q88870; Q88871; Q88872; Q88873; Q88874;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-APR-2018, entry version 159.
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;
Sindbis virus (SINV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus.
NCBI_TaxID=11034;
NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=53527; Culex.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
NCBI_TaxID=177155; Streptopelia turtur.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HRLP;
PubMed=6941270; DOI=10.1073/pnas.78.4.2062;
Rice C.M., Strauss J.H.;
"Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced
sequence of the encoded virus structural proteins.";
Proc. Natl. Acad. Sci. U.S.A. 78:2062-2066(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HRSP;
PubMed=6322438; DOI=10.1016/0042-6822(84)90428-8;
Strauss E.G., Rice C.M., Strauss J.H.;
"Complete nucleotide sequence of the genomic RNA of Sindbis virus.";
Virology 133:92-110(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=AR339;
PubMed=3462725; DOI=10.1073/pnas.83.18.6771;
Davis N.L., Fuller F.J., Dougherty W.G., Olmsted R.A., Johnston R.E.;
"A single nucleotide change in the E2 glycoprotein gene of Sindbis
virus affects penetration rate in cell culture and virulence in
neonatal mice.";
Proc. Natl. Acad. Sci. U.S.A. 83:6771-6775(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=ov-100;
Saito K., Shirasawa H., Yahata E., Yuan Q.;
"Sequence analysis of cDNA's derived from the RNA of Sindbis virus, a
potential oncolytic virus.";
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 329-394.
STRAIN=AR339;
PubMed=6087344; DOI=10.1073/pnas.81.15.4702;
Bell J.R., Kinney R.M., Trent D.W., Strauss E.G., Strauss J.H.;
"An evolutionary tree relating eight alphaviruses, based on amino-
terminal sequences of their glycoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 81:4702-4706(1984).
[6]
SUBCELLULAR LOCATION (PRECURSOR OF PROTEIN E3/E2), SUBCELLULAR
LOCATION (SPIKE GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION (SPIKE
GLYCOPROTEIN E1).
PubMed=875134;
Smith J.F., Brown D.T.;
"Envelopments of Sindbis virus: synthesis and organization of proteins
in cells infected with wild type and maturation-defective mutants.";
J. Virol. 22:662-678(1977).
[7]
FUNCTION (CAPSID PROTEIN).
PubMed=3656418;
Coombs K., Brown D.T.;
"Organization of the Sindbis virus nucleocapsid as revealed by
bifunctional cross-linking agents.";
J. Mol. Biol. 195:359-371(1987).
[8]
SUBCELLULAR LOCATION (CAPSID PROTEIN), SUBCELLULAR LOCATION (SPIKE
GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
PubMed=3829124;
Fuller S.D.;
"The T=4 envelope of Sindbis virus is organized by interactions with a
complementary T=3 capsid.";
Cell 48:923-934(1987).
[9]
SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
PubMed=2806407;
Migliaccio G., Pascale M.C., Leone A., Bonatti S.;
"Biosynthesis, membrane translocation, and surface expression of
Sindbis virus E1 glycoprotein.";
Exp. Cell Res. 185:203-216(1989).
[10]
AUTOCATALYTIC CLEAVAGE (CAPSID PROTEIN), AND MUTAGENESIS OF HIS-141;
ASP-147; ASP-163 AND SER-215.
PubMed=2335827;
Hahn C.S., Strauss J.H.;
"Site-directed mutagenesis of the proposed catalytic amino acids of
the Sindbis virus capsid protein autoprotease.";
J. Virol. 64:3069-3073(1990).
[11]
SUBCELLULAR LOCATION (6K PROTEIN).
PubMed=2408229;
Gaedigk-Nitschko K., Schlesinger M.J.;
"The Sindbis virus 6K protein can be detected in virions and is
acylated with fatty acids.";
Virology 175:274-281(1990).
[12]
PALMITOYLATION AT CYS-724, AND MUTAGENESIS OF CYS-724.
PubMed=1647069; DOI=10.1016/0042-6822(91)90133-V;
Gaedigk-Nitschko K., Schlesinger M.J.;
"Site-directed mutations in Sindbis virus E2 glycoprotein's
cytoplasmic domain and the 6K protein lead to similar defects in virus
assembly and budding.";
Virology 183:206-214(1991).
[13]
FUNCTION (CAPSID PROTEIN), CATALYTIC ACTIVITY (CAPSID PROTEIN), AND
ACTIVE SITE (CAPSID PROTEIN).
PubMed=1944569; DOI=10.1038/354037a0;
Choi H.K., Tong L., Minor W., Dumas P., Boege U., Rossmann M.G.,
Wengler G.;
"Structure of Sindbis virus core protein reveals a chymotrypsin-like
serine proteinase and the organization of the virion.";
Nature 354:37-43(1991).
[14]
TOPOLOGY.
PubMed=8432728; DOI=10.1083/jcb.120.4.877;
Liu N., Brown D.T.;
"Transient translocation of the cytoplasmic (endo) domain of a type I
membrane glycoprotein into cellular membranes.";
J. Cell Biol. 120:877-883(1993).
[15]
PALMITOYLATION AT CYS-744 AND CYS-745, AND MUTAGENESIS OF CYS-744 AND
CYS-745.
PubMed=8474160;
Ivanova L., Schlesinger M.J.;
"Site-directed mutations in the Sindbis virus E2 glycoprotein identify
palmitoylation sites and affect virus budding.";
J. Virol. 67:2546-2551(1993).
[16]
SUBUNIT (SPIKE GLYCOPROTEIN E1), SUBUNIT (SPIKE GLYCOPROTEIN E2), AND
SUBUNIT (PRECURSOR OF PROTEIN E3/E2).
PubMed=8623521; DOI=10.1006/viro.1996.0229;
Mulvey M., Brown D.T.;
"Assembly of the Sindbis virus spike protein complex.";
Virology 219:125-132(1996).
[17]
FUNCTION (6K PROTEIN), INTERACTION WITH 6K PROTEIN (SPIKE GLYCOPROTEIN
E1), INTERACTION WITH 6K PROTEIN (SPIKE GLYCOPROTEIN E2), INTERACTION
WITH SPIKE GLYCOPROTEIN 1 (6K PROTEIN), AND INTERACTION WITH SPIKE
GLYCOPROTEIN 2 (6K PROTEIN).
PubMed=8892914;
Yao J.S., Strauss E.G., Strauss J.H.;
"Interactions between PE2, E1, and 6K required for assembly of
alphaviruses studied with chimeric viruses.";
J. Virol. 70:7910-7920(1996).
[18]
FUNCTION (SPIKE GLYCOPROTEIN E2).
PubMed=8995682;
Carleton M., Lee H., Mulvey M., Brown D.T.;
"Role of glycoprotein PE2 in formation and maturation of the Sindbis
virus spike.";
J. Virol. 71:1558-1566(1997).
[19]
MUTAGENESIS OF TRP-264.
PubMed=9445057;
Paredes A.M., Heidner H., Thuman-Commike P., Prasad B.V.V.,
Johnston R.E., Chiu W.;
"Structural localization of the E3 glycoprotein in attenuated Sindbis
virus mutants.";
J. Virol. 72:1534-1541(1998).
[20]
FUNCTION (6K PROTEIN).
PubMed=9707418; DOI=10.1093/emboj/17.16.4585;
DeTulleo L., Kirchhausen T.;
"The clathrin endocytic pathway in viral infection.";
EMBO J. 17:4585-4593(1998).
[21]
FUNCTION (SPIKE GLYCOPROTEIN E1), AND FUNCTION (6K PROTEIN).
PubMed=10482600;
Smit J.M., Bittman R., Wilschut J.;
"Low-pH-dependent fusion of Sindbis virus with receptor-free
cholesterol-and sphingolipid-containing liposomes.";
J. Virol. 73:8476-8484(1999).
[22]
FUNCTION (6K PROTEIN).
PubMed=12424249; DOI=10.1074/jbc.M206611200;
Sanz M.A., Madan V., Carrasco L., Nieva J.L.;
"Interfacial domains in Sindbis virus 6K protein. Detection and
functional characterization.";
J. Biol. Chem. 278:2051-2057(2003).
[23]
FUNCTION (SPIKE GLYCOPROTEIN E1).
PubMed=12573591;
Sanz M.A., Rejas M.T., Carrasco L.;
"Individual expression of sindbis virus glycoproteins. E1 alone
promotes cell fusion.";
Virology 305:463-472(2003).
[24]
FUNCTION (6K PROTEIN).
PubMed=17483865; DOI=10.1007/s00232-007-9003-6;
Antoine A.F., Montpellier C., Cailliau K., Browaeys-Poly E.,
Vilain J.P., Dubuisson J.;
"The alphavirus 6K protein activates endogenous ionic conductances
when expressed in Xenopus oocytes.";
J. Membr. Biol. 215:37-48(2007).
[25]
FUNCTION (ASSEMBLY PROTEIN E3), AND DISULFIDE BOND (ASSEMBLY PROTEIN
E3).
PubMed=19109378; DOI=10.1128/JVI.02158-08;
Parrott M.M., Sitarski S.A., Arnold R.J., Picton L.K., Hill R.B.,
Mukhopadhyay S.;
"Role of conserved cysteines in the alphavirus E3 protein.";
J. Virol. 83:2584-2591(2009).
[26]
SUBCELLULAR LOCATION (CAPSID PROTEIN), AND SUBCELLULAR LOCATION (SPIKE
GLYCOPROTEIN E2).
PubMed=23785213; DOI=10.1128/JVI.01299-13;
Zheng Y., Kielian M.;
"Imaging of the alphavirus capsid protein during virus replication.";
J. Virol. 87:9579-9589(2013).
[27]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 107-264.
PubMed=8831786; DOI=10.1006/jmbi.1996.0505;
Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G.,
Rossmann M.G., Kuhn R.J.;
"Structural analysis of Sindbis virus capsid mutants involving
assembly and catalysis.";
J. Mol. Biol. 262:151-167(1996).
[28]
ERRATUM.
Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G.,
Rossmann M.G., Kuhn R.J.;
J. Mol. Biol. 266:633-634(1997).
-!- FUNCTION: Capsid protein: Forms an icosahedral capsid with a T=4
symmetry composed of 240 copies of the capsid protein surrounded
by a lipid membrane through which penetrate 80 spikes composed of
trimers of E1-E2 heterodimers. 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:0000269|PubMed:1944569, ECO:0000269|PubMed:3656418}.
-!- FUNCTION: Assembly protein E3: May be a disulfide isomerase that
catalyzes the proper folding and disulfide bond formation in
pE2/E2. E3 possesses labile disulfide bonds and is in close
proximity to E2 throughout the assembly pathway.
{ECO:0000269|PubMed:19109378}.
-!- FUNCTION: Spike glycoprotein E2: Plays an essential role in viral
attachment to target host cell, by binding to the cell receptor.
Synthesized as a pE2 precursor which is processed by furin at the
cell membrane just before virion budding, giving rise to E2-E1
heterodimer. The pE2-E1 heterodimer is stable, whereas E2-E1 is
unstable and dissociate at low pH. pE2 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,
ECO:0000269|PubMed:8995682}.
-!- FUNCTION: Protein 6K: Acts as a viroporin that participates in
virus glycoprotein processing, cell permeabilization and budding
of viral particles. Disrupts the calcium homeostasis of the cell,
probably at the endoplasmic reticulum level resulting in the
increased levels of cytoplasmic calcium. 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:0000269|PubMed:10482600,
ECO:0000269|PubMed:12424249, ECO:0000269|PubMed:17483865,
ECO:0000269|PubMed:8892914, ECO:0000269|PubMed:9707418}.
-!- 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. {ECO:0000269|PubMed:10482600,
ECO:0000269|PubMed:12573591}.
-!- CATALYTIC ACTIVITY: Autocatalytic release of the core protein from
the N-terminus of the togavirus structural polyprotein by
hydrolysis of a -Trp-|-Ser- bond. {ECO:0000269|PubMed:1944569}.
-!- SUBUNIT: Precursor of protein E3/E2: The precursor of protein
E3/E2 and E1 form a heterodimer shortly after synthesis
(PubMed:8623521). Spike glycoprotein E1: The precursor of protein
E3/E2 and E1 form a heterodimer shortly after synthesis
(PubMed:8623521). 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 (PubMed:8623521). 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 (PubMed:8623521). Spike glycoprotein E1: Spike at virion
surface are constituted of three E2-E1 heterodimers
(PubMed:8623521). Spike glycoprotein E2: Spike at virion surface
are constituted of three E2-E1 heterodimers (PubMed:8623521).
Spike glycoprotein E1: After target cell attachment and
endocytosis, E1 change conformation to form homotrimers (By
similarity). 6K protein: Interacts with spike glycoprotein E1
(PubMed:8892914). 6K protein: Interacts with spike glycoprotein E2
(PubMed:8892914). Spike glycoprotein E1: Interacts with 6K protein
(PubMed:8892914). Spike glycoprotein E2: Interacts with 6K protein
(PubMed:8892914). {ECO:0000250|UniProtKB:P03315,
ECO:0000269|PubMed:8623521, ECO:0000269|PubMed:8892914}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion
{ECO:0000269|PubMed:3829124}. Host cytoplasm
{ECO:0000269|PubMed:23785213}. Host cell membrane
{ECO:0000269|PubMed:23785213}.
-!- SUBCELLULAR LOCATION: Precursor of protein E3/E2: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000255}.
Host cell membrane {ECO:0000269|PubMed:875134}; Single-pass type I
membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000269|PubMed:3829124}; Single-pass type I membrane protein
{ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:23785213,
ECO:0000269|PubMed:875134}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: 6K protein: Host cell membrane
{ECO:0000269|PubMed:2408229}; Multi-pass membrane protein
{ECO:0000255}. Virion membrane {ECO:0000269|PubMed:2408229};
Multi-pass membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000269|PubMed:3829124}; Single-pass type I membrane protein
{ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:2806407,
ECO:0000269|PubMed:875134}; Single-pass type I membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Structural polyprotein;
IsoId=P03316-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Frameshifted structural polyprotein;
IsoId=P0DOK0-1; Sequence=External;
Note=Produced by ribosomal frameshifting.;
-!- 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 (By similarity). Capsid protein is auto-
cleaved during polyprotein translation, unmasking a signal peptide
at the N-terminus of the precursor of E3/E2 (PubMed:2335827). The
remaining polyprotein is then targeted to the host endoplasmic
reticulum, where host signal peptidase cleaves it into pE2, 6K and
E1 proteins (By similarity). pE2 is further processed to mature E3
and E2 by host furin in trans-Golgi vesicle (By similarity).
{ECO:0000250|UniProtKB:P03315, ECO:0000269|PubMed:2335827}.
-!- 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:0000269|PubMed:1647069, ECO:0000269|PubMed:8432728}.
-!- 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}.
-!- SIMILARITY: Belongs to the alphavirus structural polyprotein
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ld4";
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EMBL; V01403; CAA24684.1; -; Genomic_RNA.
EMBL; J02363; AAA96976.1; -; Genomic_RNA.
EMBL; M13818; AAA47485.1; -; Genomic_RNA.
EMBL; AB372876; BAH70330.1; -; Genomic_RNA.
PIR; A03916; VHWVB.
PIR; A25894; VHWVSB.
PIR; B03916; VHWVB2.
RefSeq; NP_062890.1; NC_001547.1. [P03316-1]
PDB; 1KXA; X-ray; 3.10 A; A=106-264.
PDB; 1KXB; X-ray; 2.90 A; A=106-264.
PDB; 1KXC; X-ray; 3.10 A; A=106-264.
PDB; 1KXD; X-ray; 3.00 A; A=106-264.
PDB; 1KXE; X-ray; 3.20 A; A=106-264.
PDB; 1KXF; X-ray; 2.38 A; A=106-264.
PDB; 1LD4; EM; 11.40 A; A/B/C/D=1-264, M/N/O/P=807-1245.
PDB; 1SVP; X-ray; 2.00 A; A/B=106-266.
PDB; 1Z8Y; EM; 9.00 A; A/C/E/G=807-1096, B/D/F/H=1101-1189, I/K/M/O=1215-1245, J/L/N/P=691-726, Q/R/S/T=114-264.
PDB; 2SNV; X-ray; 2.80 A; A=114-264.
PDB; 2SNW; X-ray; 2.70 A; A/B=107-264.
PDB; 3J0F; EM; -; A/B/C/D=1-264, E/F/G/H=807-1245, I/J/K/L=329-751.
PDB; 3MUU; X-ray; 3.29 A; A/B/C/D/E/F=329-672, A/B/C/D/E/F=807-1192.
PDB; 3MUW; EM; -; A/D/E/F=807-1190, U/X/Y/Z=329-672.
PDBsum; 1KXA; -.
PDBsum; 1KXB; -.
PDBsum; 1KXC; -.
PDBsum; 1KXD; -.
PDBsum; 1KXE; -.
PDBsum; 1KXF; -.
PDBsum; 1LD4; -.
PDBsum; 1SVP; -.
PDBsum; 1Z8Y; -.
PDBsum; 2SNV; -.
PDBsum; 2SNW; -.
PDBsum; 3J0F; -.
PDBsum; 3MUU; -.
PDBsum; 3MUW; -.
ProteinModelPortal; P03316; -.
SMR; P03316; -.
DIP; DIP-29032N; -.
MEROPS; S03.001; -.
SwissPalm; P03316; -.
GeneID; 1502155; -.
KEGG; vg:1502155; -.
KO; K19288; -.
OrthoDB; VOG0900007W; -.
EvolutionaryTrace; P03316; -.
PMAP-CutDB; P03316; -.
Proteomes; UP000006710; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
GO; GO:0098029; C:icosahedral viral capsid, spike; IDA:CACAO.
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:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL.
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:0061025; P:membrane fusion; IDA:CACAO.
GO; GO:0019062; P:virion attachment to host cell; IMP:CACAO.
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; Complete proteome;
Direct protein sequencing; 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; Reference proteome; Ribosomal frameshifting;
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 1 264 Capsid protein.
/FTId=PRO_0000041321.
CHAIN 265 751 Precursor of protein E3/E2.
{ECO:0000250}.
/FTId=PRO_0000226238.
CHAIN 265 328 Assembly protein E3.
/FTId=PRO_0000041322.
CHAIN 329 751 Spike glycoprotein E2.
/FTId=PRO_0000041323.
CHAIN 752 806 6K protein.
/FTId=PRO_0000041324.
CHAIN 807 1245 Spike glycoprotein E1.
/FTId=PRO_0000041325.
TRANSMEM 696 716 Helical. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TRANSMEM 1215 1235 Helical. {ECO:0000255}.
DOMAIN 114 264 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 93 101 Ribosome-binding. {ECO:0000250}.
REGION 265 279 Functions as an uncleaved signal peptide
for the precursor of protein E3/E2.
{ECO:0000250|UniProtKB:P03315}.
REGION 890 907 E1 fusion peptide loop.
{ECO:0000250|UniProtKB:Q8JUX5}.
ACT_SITE 141 141 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027,
ECO:0000269|PubMed:1944569}.
ACT_SITE 163 163 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027,
ECO:0000269|PubMed:1944569}.
ACT_SITE 215 215 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027,
ECO:0000269|PubMed:1944569}.
SITE 264 265 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03315}.
SITE 328 329 Cleavage; by host furin. {ECO:0000250}.
SITE 751 752 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 806 807 Cleavage; by host signal peptidase.
{ECO:0000250}.
LIPID 724 724 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:1647069}.
LIPID 744 744 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:8474160}.
LIPID 745 745 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:8474160}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1051 1051 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 283 289 {ECO:0000269|PubMed:19109378}.
DISULFID 855 920 {ECO:0000250}.
DISULFID 868 900 {ECO:0000250}.
DISULFID 869 902 {ECO:0000250}.
DISULFID 874 884 {ECO:0000250}.
DISULFID 1065 1077 {ECO:0000250}.
DISULFID 1107 1182 {ECO:0000250}.
DISULFID 1112 1186 {ECO:0000250}.
DISULFID 1134 1176 {ECO:0000250}.
VARIANT 329 331 SVI -> RVT (in strain: AR339).
VARIANT 333 333 D -> G (in strain: HRLP).
VARIANT 351 351 V -> E (in strain: AR339 and HRLP).
VARIANT 398 398 K -> E (in strain: AR339).
VARIANT 442 442 S -> R (causes attenuation of the virus).
VARIANT 447 447 N -> KNGSF (in strain: ov-100).
VARIANT 500 500 R -> G (in strain: AR339).
VARIANT 719 719 K -> L (in strain: TE12).
VARIANT 919 919 D -> V (in strain: HRLP).
MUTAGEN 141 141 H->A,P: Complete loss of autocatalytic
cleavage by capsid protein.
{ECO:0000269|PubMed:2335827}.
MUTAGEN 141 141 H->R: No loss of autocatalytic cleavage
by capsid protein. No infectious virus is
produced. {ECO:0000269|PubMed:2335827}.
MUTAGEN 147 147 D->H,Y: No loss of autocatalytic cleavage
by capsid protein. No infectious virus is
produced. {ECO:0000269|PubMed:2335827}.
MUTAGEN 163 163 D->H: No loss of autocatalytic cleavage
by capsid protein. No infectious virus is
produced. {ECO:0000269|PubMed:2335827}.
MUTAGEN 163 163 D->N: No loss of autocatalytic cleavage
by capsid protein. Infectious virus is
produced. {ECO:0000269|PubMed:2335827}.
MUTAGEN 215 215 S->A,I: Complete loss of autocatalytic
cleavage by capsid protein.
{ECO:0000269|PubMed:2335827}.
MUTAGEN 215 215 S->C: 40% reduction in autocatalytic
cleavage by capsid protein. No infectious
virus is produced.
{ECO:0000269|PubMed:2335827}.
MUTAGEN 215 215 S->T: 90% reduction in autocatalytic
cleavage by capsid protein. No infectious
virus is produced.
{ECO:0000269|PubMed:2335827}.
MUTAGEN 264 264 W->F: 73% loss of cleavage by capsid
protease. {ECO:0000269|PubMed:9445057}.
MUTAGEN 724 724 C->A: Loss of palmitoylation.
{ECO:0000269|PubMed:1647069}.
MUTAGEN 744 745 CC->AA: Complete loss of infectivity.
MUTAGEN 744 744 C->A: Loss of palmitoylation.
{ECO:0000269|PubMed:8474160}.
MUTAGEN 745 745 C->A: Loss of palmitoylation.
{ECO:0000269|PubMed:8474160}.
STRAND 114 119 {ECO:0000244|PDB:1SVP}.
TURN 121 123 {ECO:0000244|PDB:2SNV}.
STRAND 125 132 {ECO:0000244|PDB:1SVP}.
STRAND 135 139 {ECO:0000244|PDB:1SVP}.
STRAND 144 148 {ECO:0000244|PDB:1SVP}.
HELIX 151 153 {ECO:0000244|PDB:1SVP}.
STRAND 157 159 {ECO:0000244|PDB:1SVP}.
HELIX 160 162 {ECO:0000244|PDB:1SVP}.
STRAND 164 168 {ECO:0000244|PDB:1SVP}.
HELIX 171 173 {ECO:0000244|PDB:1SVP}.
STRAND 176 178 {ECO:0000244|PDB:2SNW}.
STRAND 186 191 {ECO:0000244|PDB:1SVP}.
STRAND 194 199 {ECO:0000244|PDB:1SVP}.
STRAND 202 206 {ECO:0000244|PDB:1SVP}.
STRAND 218 220 {ECO:0000244|PDB:1SVP}.
STRAND 222 224 {ECO:0000244|PDB:2SNV}.
STRAND 226 235 {ECO:0000244|PDB:1SVP}.
STRAND 237 247 {ECO:0000244|PDB:1SVP}.
STRAND 249 251 {ECO:0000244|PDB:2SNV}.
STRAND 253 256 {ECO:0000244|PDB:1SVP}.
STRAND 342 345 {ECO:0000244|PDB:3MUU}.
STRAND 347 351 {ECO:0000244|PDB:3MUU}.
STRAND 353 357 {ECO:0000244|PDB:3MUU}.
STRAND 361 363 {ECO:0000244|PDB:3MUU}.
STRAND 367 374 {ECO:0000244|PDB:3MUU}.
STRAND 376 380 {ECO:0000244|PDB:3MUU}.
STRAND 382 385 {ECO:0000244|PDB:3MUU}.
STRAND 391 393 {ECO:0000244|PDB:3MUU}.
STRAND 405 407 {ECO:0000244|PDB:3MUU}.
STRAND 410 425 {ECO:0000244|PDB:3MUU}.
STRAND 428 432 {ECO:0000244|PDB:3MUU}.
STRAND 439 447 {ECO:0000244|PDB:3MUU}.
STRAND 449 454 {ECO:0000244|PDB:3MUU}.
STRAND 464 466 {ECO:0000244|PDB:3MUU}.
STRAND 473 483 {ECO:0000244|PDB:3MUU}.
STRAND 589 596 {ECO:0000244|PDB:3MUU}.
STRAND 603 607 {ECO:0000244|PDB:3MUU}.
STRAND 610 630 {ECO:0000244|PDB:3MUU}.
STRAND 637 643 {ECO:0000244|PDB:3MUU}.
STRAND 654 661 {ECO:0000244|PDB:3MUU}.
STRAND 807 814 {ECO:0000244|PDB:3MUU}.
STRAND 821 825 {ECO:0000244|PDB:3MUU}.
STRAND 833 842 {ECO:0000244|PDB:3MUU}.
STRAND 845 854 {ECO:0000244|PDB:3MUU}.
STRAND 857 860 {ECO:0000244|PDB:3MUU}.
STRAND 883 889 {ECO:0000244|PDB:3MUU}.
TURN 894 899 {ECO:0000244|PDB:3MUU}.
STRAND 903 905 {ECO:0000244|PDB:3MUU}.
STRAND 907 916 {ECO:0000244|PDB:3MUU}.
TURN 918 922 {ECO:0000244|PDB:3MUU}.
STRAND 925 934 {ECO:0000244|PDB:3MUU}.
STRAND 937 943 {ECO:0000244|PDB:3MUU}.
STRAND 946 951 {ECO:0000244|PDB:3MUU}.
STRAND 954 957 {ECO:0000244|PDB:3MUU}.
STRAND 959 961 {ECO:0000244|PDB:3MUU}.
STRAND 966 969 {ECO:0000244|PDB:3MUU}.
STRAND 981 985 {ECO:0000244|PDB:3MUU}.
STRAND 990 992 {ECO:0000244|PDB:3MUU}.
STRAND 1003 1005 {ECO:0000244|PDB:3MUU}.
STRAND 1008 1013 {ECO:0000244|PDB:3MUU}.
TURN 1014 1016 {ECO:0000244|PDB:3MUU}.
HELIX 1045 1050 {ECO:0000244|PDB:3MUU}.
HELIX 1057 1059 {ECO:0000244|PDB:3MUU}.
STRAND 1066 1068 {ECO:0000244|PDB:3MUU}.
TURN 1069 1072 {ECO:0000244|PDB:3MUU}.
STRAND 1073 1075 {ECO:0000244|PDB:3MUU}.
STRAND 1080 1089 {ECO:0000244|PDB:3MUU}.
HELIX 1090 1092 {ECO:0000244|PDB:3MUU}.
STRAND 1102 1111 {ECO:0000244|PDB:3MUU}.
STRAND 1116 1118 {ECO:0000244|PDB:3MUU}.
STRAND 1120 1130 {ECO:0000244|PDB:3MUU}.
STRAND 1137 1140 {ECO:0000244|PDB:3MUU}.
STRAND 1144 1146 {ECO:0000244|PDB:3MUU}.
STRAND 1148 1150 {ECO:0000244|PDB:3MUU}.
STRAND 1157 1163 {ECO:0000244|PDB:3MUU}.
SEQUENCE 1245 AA; 136766 MW; B77C18131703F1E6 CRC64;
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP
QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP GKRQRMALKL EADRLFDVKN
EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY
TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT
ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT VPCFSPVKIE
QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD HTVKEGTMDD IKISTSGPCR
RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT SCTLARKIKP KFVGREKYDL PPVHGKKIPC
TVYDRLKETT AGYITMHRPR PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS
TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD RDGLEYIWGN
HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SATVAMMIGV TVAVLCACKA
RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY LWSNSQPFFW VQLCIPLAAF
IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM
SSEVLPSTNQ EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG
TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ATSLTSKDLI
ASTDIRLLKP SAKNVHVPYT QASSGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG
NIPISIDIPN AAFIRTSDAP LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS
STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR


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