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Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); p62 (E3/E2); Protein E3 (Spike glycoprotein E3); Envelope glycoprotein E2 (Spike glycoprotein E2); Protein 6K; Envelope glycoprotein E1 (Spike glycoprotein E1)]

 POLS_SFV                Reviewed;        1253 AA.
P03315; B3TP01; Q809B6; Q8JMP5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 152.
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=p62;
AltName: Full=E3/E2;
Contains:
RecName: Full=Protein E3;
AltName: Full=Spike glycoprotein E3;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=Spike glycoprotein E2;
Contains:
RecName: Full=Protein 6K;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=Spike glycoprotein E1;
Semliki forest virus (SFV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus; SFV complex.
NCBI_TaxID=11033;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9368; Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
NCBI_TaxID=170865; Halcyon.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=158617; Quelea.
NCBI_TaxID=34630; Rhipicephalus.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A7;
PubMed=9225028; DOI=10.1099/0022-1317-78-7-1551;
Tarbatt C.J., Glasgow G.M., Mooney D.A., Sheahan B.J., Atkins G.J.;
"Sequence analysis of the avirulent, demyelinating A7 strain of
Semliki Forest virus.";
J. Gen. Virol. 78:1551-1557(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=MTV;
PubMed=18753222; DOI=10.1099/vir.0.2008/002121-0;
Tan le V., Ha do Q., Hien V.M., van der Hoek L., Farrar J.,
de Jong M.D.;
"Me Tri virus: a Semliki Forest virus strain from Vietnam?";
J. Gen. Virol. 89:2132-2135(2008).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=L10;
Logue C., Mooney D., Shanley R., Atkins G.J.;
"Semliki Forest Virus - L10 Strain Complete Genome.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-305.
PubMed=6935652; DOI=10.1073/pnas.77.11.6376;
Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H.;
"The capsid protein of Semliki Forest virus has clusters of basic
amino acids and prolines in its amino-terminal region.";
Proc. Natl. Acad. Sci. U.S.A. 77:6376-6380(1980).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 266-1253.
PubMed=6985476; DOI=10.1038/288236a0;
Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H.;
"Nucleotide sequence of cDNA coding for Semliki Forest virus membrane
glycoproteins.";
Nature 288:236-241(1980).
[6]
PROTEIN SEQUENCE OF 334-402 AND 816-881.
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).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=7398872; DOI=10.1016/0014-5793(80)81158-6;
Kalkkinen N.;
"Carboxyl-terminal sequence analysis of the four structural proteins
of Semliki Forest virus.";
FEBS Lett. 115:163-166(1980).
[8]
FUNCTION (CAPSID PROTEIN), AUTOCATALYTIC CLEAVAGE BY CAPSID PROTEIN,
AND MUTAGENESIS OF 219-SER-GLY-220.
PubMed=3553612;
Melancon P., Garoff H.;
"Processing of the Semliki Forest virus structural polyprotein: role
of the capsid protease.";
J. Virol. 61:1301-1309(1987).
[9]
STEAROYLATION AT CYS-1248, AND PALMITOYLATION.
PubMed=3143715;
Schmidt M., Schmidt M.F., Rott R.;
"Chemical identification of cysteine as palmitoylation site in a
transmembrane protein (Semliki Forest virus E1).";
J. Biol. Chem. 263:18635-18639(1988).
[10]
FUNCTION (ENVELOPE GLYCOPROTEIN E2).
PubMed=1714373;
Kail M., Hollinshead M., Ansorge W., Pepperkok R., Frank R.,
Griffiths G., Vaux D.;
"The cytoplasmic domain of alphavirus E2 glycoprotein contains a short
linear recognition signal required for viral budding.";
EMBO J. 10:2343-2351(1991).
[11]
CLEAVAGE SITE OF P62, AND MUTAGENESIS OF ARG-330 AND ARG-333.
PubMed=2005112;
Jain S.K., DeCandido S., Kielian M.;
"Processing of the p62 envelope precursor protein of Semliki Forest
virus.";
J. Biol. Chem. 266:5756-5761(1991).
[12]
MUTAGENESIS OF ASP-890; LYS-894; GLY-898; PRO-901; MET-903 AND
GLY-906.
PubMed=2072453;
Levy-Mintz P., Kielian M.;
"Mutagenesis of the putative fusion domain of the Semliki Forest virus
spike protein.";
J. Virol. 65:4292-4300(1991).
[13]
CLEAVAGE BY SIGNAL PEPTIDASE, AND MUTAGENESIS OF ALA-755 AND ALA-815.
PubMed=1985194;
Liljestrom P., Garoff H.;
"Internally located cleavable signal sequences direct the formation of
Semliki Forest virus membrane proteins from a polyprotein precursor.";
J. Virol. 65:147-154(1991).
[14]
FUNCTION (PROTEIN 6K).
PubMed=1962454; DOI=10.1016/0042-6822(91)90556-Q;
Lusa S., Garoff H., Liljestrom P.;
"Fate of the 6K membrane protein of Semliki Forest virus during virus
assembly.";
Virology 185:843-846(1991).
[15]
FUNCTION (ENVELOPE GLYCOPROTEIN E1).
PubMed=1433520;
Wahlberg J.M., Bron R., Wilschut J., Garoff H.;
"Membrane fusion of Semliki Forest virus involves homotrimers of the
fusion protein.";
J. Virol. 66:7309-7318(1992).
[16]
FUNCTION (PROTEIN 6K).
PubMed=7983743;
Loewy A., Smyth J., von Bonsdorff C.H., Liljestrom P.,
Schlesinger M.J.;
"The 6-kilodalton membrane protein of Semliki Forest virus is involved
in the budding process.";
J. Virol. 69:469-475(1995).
[17]
MUTAGENESIS OF GLY-898 AND GLY-906.
PubMed=9425157; DOI=10.1083/jcb.140.1.91;
Vashishtha M., Phalen T., Marquardt M.T., Ryu J.S., Ng A.C.,
Kielian M.;
"A single point mutation controls the cholesterol dependence of
Semliki Forest virus entry and exit.";
J. Cell Biol. 140:91-99(1998).
[18]
FUNCTION (CAPSID PROTEIN), AND AUTOCATALYTIC CLEAVAGE BY CAPSID
PROTEIN.
PubMed=9642067; DOI=10.1006/jmbi.1998.1817;
Skoging U., Liljestrom P.;
"Role of the C-terminal tryptophan residue for the structure-function
of the alphavirus capsid protein.";
J. Mol. Biol. 279:865-872(1998).
[19]
INTERACTION WITH HUMAN CHAPERONES P4HB/PDI AND PDIA3/ERP57.
PubMed=10573423; DOI=10.1038/47062;
Molinari M., Helenius A.;
"Glycoproteins form mixed disulphides with oxidoreductases during
folding in living cells.";
Nature 402:90-93(1999).
[20]
MUTAGENESIS OF LEU-859 AND VAL-993.
PubMed=12438597; DOI=10.1128/JVI.76.24.12712-12722.2002;
Chatterjee P.K., Eng C.H., Kielian M.;
"Novel mutations that control the sphingolipid and cholesterol
dependence of the Semliki Forest virus fusion protein.";
J. Virol. 76:12712-12722(2002).
[21]
PROTEOLYTIC PROCESSING OF P62 BY HOST FURIN.
PubMed=12584323; DOI=10.1128/JVI.77.5.2981-2989.2003;
Zhang X., Fugere M., Day R., Kielian M.;
"Furin processing and proteolytic activation of Semliki Forest
virus.";
J. Virol. 77:2981-2989(2003).
[22]
FUNCTION.
PubMed=15954801; DOI=10.1371/journal.pbio.0030233;
Vonderheit A., Helenius A.;
"Rab7 associates with early endosomes to mediate sorting and transport
of Semliki forest virus to late endosomes.";
PLoS Biol. 3:E233-E233(2005).
[23]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 119-267.
PubMed=9094737;
DOI=10.1002/(SICI)1097-0134(199703)27:3<345::AID-PROT3>3.0.CO;2-C;
Choi H.-K., Lu G., Lee S., Wengler G., Rossmann M.G.;
"Structure of Semliki Forest virus core protein.";
Proteins 27:345-359(1997).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 119-267, AND
DISULFIDE BONDS.
PubMed=10882067; DOI=10.1016/S1097-2765(00)80421-9;
Mancini E.J., Clarke M., Gowen B.E., Rutten T., Fuller S.D.;
"Cryo-electron microscopy reveals the functional organization of an
enveloped virus, Semliki Forest virus.";
Mol. Cell 5:255-266(2000).
[25]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 816-1205.
PubMed=11301009; DOI=10.1016/S0092-8674(01)00303-8;
Lescar J., Roussel A., Wien M.W., Navaza J., Fuller S.D., Wengler G.,
Wengler G., Rey F.A.;
"The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral
assembly primed for fusogenic activation at endosomal pH.";
Cell 105:137-148(2001).
[26]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 816-1206, GLYCOSYLATION AT
ASN-956, AND DISULFIDE BONDS.
PubMed=14737160; DOI=10.1038/nature02239;
Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B.,
Lepault J., Kielian M., Rey F.A.;
"Conformational change and protein-protein interactions of the fusion
protein of Semliki Forest virus.";
Nature 427:320-325(2004).
[27]
FUNCTION (PROTEIN E3).
PubMed=23864626; DOI=10.1128/JVI.01507-13;
Uchime O., Fields W., Kielian M.;
"The role of E3 in pH protection during alphavirus assembly and
exit.";
J. Virol. 87:10255-10262(2013).
-!- FUNCTION: Capsid protein: Possesses a protease activity that
results in its autocatalytic cleavage from the nascent structural
protein. Following its self-cleavage, the capsid protein
transiently associates with ribosomes, and within several minutes
the protein binds to viral RNA and rapidly assembles into
icosahedric core particles. The resulting nucleocapsid eventually
associates with the cytoplasmic domain of E2 at the cell membrane,
leading to budding and formation of mature virions. 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:3553612,
ECO:0000269|PubMed:9642067}.
-!- FUNCTION: Protein E3: Provides the signal sequence for p62 (E3/E2)
translocation to the host endoplasmic reticulum. Mediates pH
protection of E1 during secretory pathway trans- port.
{ECO:0000269|PubMed:23864626}.
-!- FUNCTION: Envelope glycoprotein E2: Plays a role in viral
attachment to target host cell, by binding to the cell receptor.
Synthesized as a p62 precursor which is processed by furin at the
cell membrane just before virion budding, giving rise to E2-E1
heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is
unstable and dissociate at low pH. p62 is processed at the last
step, presumably to avoid E1 fusion activation before its final
export to cell surface. E2 C-terminus contains a transitory
transmembrane that would be disrupted by palmitoylation, resulting
in reorientation of the C-terminal tail from lumenal to
cytoplasmic side. This step is critical since E2 C-terminus is
involved in budding by interacting with capsid proteins. This
release of E2 C-terminus in cytoplasm occurs lately in protein
export, and precludes premature assembly of particles at the
endoplasmic reticulum membrane. {ECO:0000269|PubMed:1714373}.
-!- FUNCTION: Protein 6K: Constitutive membrane protein involved in
virus glycoprotein processing, cell permeabilization, and the
budding of viral particles. Disrupts the calcium homeostasis of
the cell, probably at the endoplasmic reticulum level. This leads
to cytoplasmic calcium elevation. Because of its lipophilic
properties, the 6K protein is postulated to influence the
selection of lipids that interact with the transmembrane domains
of the glycoproteins, which, in turn, affects the deformability of
the bilayer required for the extreme curvature that occurs as
budding proceeds. Present in low amount in virions, about 3%
compared to viral glycoproteins. {ECO:0000269|PubMed:1962454,
ECO:0000269|PubMed:7983743}.
-!- FUNCTION: Envelope glycoprotein E1: Class II viral fusion protein.
Fusion activity is inactive as long as E1 is bound to E2 in mature
virion. After virus attachment to target cell and endocytosis,
acidification of the endosome would induce dissociation of E1/E2
heterodimer and concomitant trimerization of the E1 subunits. This
E1 trimer is fusion active, and promotes release of viral
nucleocapsid in cytoplasm after endosome and viral membrane
fusion. Efficient fusion requires the presence of cholesterol and
sphingolipid in the target membrane. Fusion is optimal at levels
of about 1 molecule of cholesterol per 2 molecules of
phospholipids, and is specific for sterols containing a 3-beta-
hydroxyl group. {ECO:0000269|PubMed:1433520}.
-!- CATALYTIC ACTIVITY: Autocatalytic release of the core protein from
the N-terminus of the togavirus structural polyprotein by
hydrolysis of a -Trp-|-Ser- bond.
-!- SUBUNIT: p62 and E1 form a heterodimer shortly after synthesis.
Processing of p62 into E2 and E3 results in a heterodimer of E2
and E1. Spike at virion surface are constituted of three E2-E1
heterodimers. After target cell attachment and endocytosis, E1
change conformation to form homotrimers.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: p62: Virion membrane {ECO:0000250}; Single-
pass type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 6K: Host cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Virion
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Structural polyprotein;
IsoId=P03315-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Frameshifted structural polyprotein;
IsoId=P0DJZ6-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting in Protein 6K ORF.;
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Capsid protein is auto-cleaved during polyprotein translation,
unmasking p62 signal peptide. The remaining polyprotein is then
targeted to the endoplasmic reticulum, where host signal peptidase
cleaves it into p62, 6K and E1 proteins. p62 is further processed
to mature E3 and E2 by host furin in trans-Golgi vesicle. Protein
processing process takes about 30 minutes at physiologic
temperatures. The folding of the p62/6K/E1 precursor requires the
formation of intrachain disulfide bonds and has been shown to
involve a transient covalent interaction between the nascent and
newly synthesized heterodimer and the host-cell chaperones,
P4HB/PDI and PDIA3/ERp57. The folding pathway also includes non
covalent interaction with human CANX/calnexin and
CALR/calreticulin. {ECO:0000269|PubMed:12584323,
ECO:0000269|PubMed:1985194, ECO:0000269|PubMed:2005112}.
-!- PTM: Envelope E1, E2 and E3 proteins are N-glycosylated.
{ECO:0000269|PubMed:14737160}.
-!- PTM: E2 is 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. 6K protein is also
palmitoylated with about four covalently bound fatty acids per
molecule. E1 is stearoylated. {ECO:0000269|PubMed:3143715}.
-!- MISCELLANEOUS: The mature virion nucleocapsid consists of 240
copies of the capsid protein. 80 spike trimers of E1 and E2 are
present at the surface of mature virion. They project about 100
Angstroms from the outer surface and are located at the local and
strict three fold axis of the icosahedral lattice. The
glycoproteins splay out to form a protein shell or skirt covering
most of the outer surface of the membrane bilayer.
-!- MISCELLANEOUS: Structural polyprotein is translated from a
subgenomic RNA synthesized during togavirus replication.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1dwn";
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EMBL; Z48163; CAD90834.1; -; Genomic_RNA.
EMBL; EU350586; ACB12688.1; -; Genomic_RNA.
EMBL; AY112987; AAM64227.1; -; Genomic_RNA.
EMBL; X04129; CAA27742.1; -; Genomic_RNA.
PIR; A93861; VHWV.
PIR; S42462; S42462.
RefSeq; NP_463458.1; NC_003215.1. [P03315-1]
PDB; 1DYL; EM; 9.00 A; A/B/C/D=119-267.
PDB; 1I9W; X-ray; 3.00 A; A=816-1205.
PDB; 1RER; X-ray; 3.20 A; A/B/C=816-1206.
PDB; 1VCP; X-ray; 3.00 A; A/B/C=119-267.
PDB; 1VCQ; X-ray; 3.10 A; A/B=119-267.
PDB; 2ALA; X-ray; 3.00 A; A=816-1206.
PDB; 2V33; X-ray; 1.55 A; A/B=1107-1197.
PDBsum; 1DYL; -.
PDBsum; 1I9W; -.
PDBsum; 1RER; -.
PDBsum; 1VCP; -.
PDBsum; 1VCQ; -.
PDBsum; 2ALA; -.
PDBsum; 2V33; -.
DisProt; DP00999; -.
ProteinModelPortal; P03315; -.
SMR; P03315; -.
MEROPS; S03.001; -.
TCDB; 1.G.4.1.1; the viral pore-forming membrane fusion protein-4 (vmfp4) family.
iPTMnet; P03315; -.
SwissPalm; P03315; -.
UniCarbKB; P03315; -.
GeneID; 922351; -.
KEGG; vg:922351; -.
KO; K19288; -.
OrthoDB; VOG0900007W; -.
EvolutionaryTrace; P03315; -.
Proteomes; UP000000570; Genome.
Proteomes; UP000108382; Genome.
Proteomes; UP000125835; Genome.
Proteomes; UP000174511; Genome.
GO; GO:0044174; C:host cell endosome; IDA:CACAO.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; IMP:CACAO.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 2.60.40.350; -; 1.
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; 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; Autocatalytic cleavage; 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 1 267 Capsid protein.
/FTId=PRO_0000041311.
CHAIN 268 755 p62.
/FTId=PRO_0000226237.
CHAIN 268 333 Protein E3.
/FTId=PRO_0000041312.
CHAIN 334 755 Envelope glycoprotein E2.
/FTId=PRO_0000041313.
CHAIN 756 815 Protein 6K.
/FTId=PRO_0000041314.
CHAIN 816 1253 Envelope glycoprotein E1.
/FTId=PRO_0000041315.
TOPO_DOM 268 701 Extracellular. {ECO:0000255}.
TRANSMEM 702 722 Helical. {ECO:0000255}.
TOPO_DOM 723 755 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 756 770 Extracellular. {ECO:0000255}.
TRANSMEM 771 791 Helical. {ECO:0000255}.
TOPO_DOM 792 792 Cytoplasmic. {ECO:0000255}.
TRANSMEM 793 813 Helical. {ECO:0000255}.
TOPO_DOM 814 1230 Extracellular. {ECO:0000255}.
TRANSMEM 1231 1251 Helical. {ECO:0000255}.
TOPO_DOM 1252 1253 Cytoplasmic. {ECO:0000255}.
DOMAIN 119 267 Peptidase S3. {ECO:0000255|PROSITE-
ProRule:PRU01027}.
REGION 1 113 Intrinsically disordered, in contact with
genomic RNA in nucleocapsid.
{ECO:0000255}.
REGION 94 106 Ribosome-binding.
REGION 728 748 Transient transmembrane before p62-6K
protein processing. {ECO:0000255}.
REGION 899 916 E1 fusion peptide loop.
ACT_SITE 145 145 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 151 151 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
ACT_SITE 219 219 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU01027}.
SITE 267 268 Cleavage; by capsid protein.
SITE 333 334 Cleavage; by host furin.
SITE 755 756 Cleavage; by host signal peptidase.
SITE 815 816 Cleavage; by host signal peptidase.
LIPID 718 718 S-palmitoyl cysteine; by host.
{ECO:0000255}.
LIPID 728 728 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 748 748 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 749 749 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 1248 1248 S-stearoyl cysteine; by host.
{ECO:0000269|PubMed:3143715}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 595 595 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 956 956 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:14737160,
ECO:0000269|PubMed:6985476}.
DISULFID 119 134
DISULFID 864 929
DISULFID 877 909
DISULFID 878 911
DISULFID 883 893
DISULFID 1074 1086
DISULFID 1116 1191
DISULFID 1121 1195
DISULFID 1143 1185
VARIANT 62 62 A -> T (in strain: A7).
VARIANT 63 63 R -> G (in strain: L10).
VARIANT 85 85 N -> K (in strain: A7, L10 and MTV).
VARIANT 279 279 A -> T (in strain: A7).
VARIANT 291 291 V -> A (in strain: A7).
VARIANT 370 370 V -> I (in strain: A7, L10 and MTV).
VARIANT 437 437 K -> T (in strain: A7, L10 and MTV).
VARIANT 545 545 N -> S (in strain: A7).
VARIANT 548 548 M -> K (in strain: A7 and MTV).
VARIANT 614 614 E -> K (in strain: MTV).
VARIANT 700 700 V -> A (in strain: A7).
VARIANT 704 704 V -> A (in strain: A7).
VARIANT 722 722 V -> A (in strain: A7 and MTV).
VARIANT 880 880 A -> S (in strain: A7).
VARIANT 930 930 R -> K (in strain: A7).
VARIANT 1043 1043 M -> T (in strain: A7 and MTV).
VARIANT 1112 1112 I -> T (in strain: A7 and MTV).
VARIANT 1134 1134 T -> K (in strain: A7).
VARIANT 1138 1138 N -> D (in strain: A7, L10 and MTV).
VARIANT 1165 1165 G -> R (in strain: MTV).
VARIANT 1188 1188 R -> K (in strain: A7 and MTV).
MUTAGEN 219 220 SG->RST: Loss of autocatalytic cleavage
by capsid protein.
{ECO:0000269|PubMed:3553612}.
MUTAGEN 267 267 W->A,R: Complete loss of cleavage by
capsid protease.
MUTAGEN 330 330 R->S: Complete loss of p62 precursor
processing. {ECO:0000269|PubMed:2005112}.
MUTAGEN 333 333 R->F: Complete loss of p62 precursor
processing. {ECO:0000269|PubMed:2005112}.
MUTAGEN 755 755 A->F: Complete loss of p62 precursor-6K
cleavage. {ECO:0000269|PubMed:1985194}.
MUTAGEN 815 815 A->F: Complete loss of 6K protein-E1
envelope glycoprotein cleavage.
{ECO:0000269|PubMed:1985194}.
MUTAGEN 859 859 L->F: E1 fusion is less cholesterol and
sphingolipid dependent.
{ECO:0000269|PubMed:12438597}.
MUTAGEN 890 890 D->A: Shifts the pH threshold for fusion
to a more acidic range.
{ECO:0000269|PubMed:2072453}.
MUTAGEN 894 894 K->Q: No effect on E1 fusion activity.
{ECO:0000269|PubMed:2072453}.
MUTAGEN 898 898 G->A: Shifts the pH threshold for fusion
to a more acidic range.
{ECO:0000269|PubMed:2072453,
ECO:0000269|PubMed:9425157}.
MUTAGEN 898 898 G->D: No effect on E1 fusion activity.
{ECO:0000269|PubMed:2072453,
ECO:0000269|PubMed:9425157}.
MUTAGEN 901 901 P->D: Retention of E1 protein in
endoplasmic reticulum.
{ECO:0000269|PubMed:2072453}.
MUTAGEN 903 903 M->L: No effect on E1 fusion activity.
{ECO:0000269|PubMed:2072453}.
MUTAGEN 906 906 G->A: Shifts the pH threshold for fusion
to a more acidic range.
{ECO:0000269|PubMed:2072453,
ECO:0000269|PubMed:9425157}.
MUTAGEN 906 906 G->D: Complete loss of E1 fusion
activity. {ECO:0000269|PubMed:2072453,
ECO:0000269|PubMed:9425157}.
MUTAGEN 906 906 G->P: Retention of E1 protein in
endoplasmic reticulum.
{ECO:0000269|PubMed:2072453,
ECO:0000269|PubMed:9425157}.
MUTAGEN 993 993 V->A: E1 fusion is less cholesterol and
sphingolipid dependent.
{ECO:0000269|PubMed:12438597}.
STRAND 120 125 {ECO:0000244|PDB:1VCP}.
STRAND 128 134 {ECO:0000244|PDB:1VCP}.
STRAND 139 141 {ECO:0000244|PDB:1VCP}.
STRAND 148 152 {ECO:0000244|PDB:1VCP}.
HELIX 153 156 {ECO:0000244|PDB:1VCP}.
STRAND 161 163 {ECO:0000244|PDB:1VCP}.
TURN 164 167 {ECO:0000244|PDB:1VCP}.
STRAND 168 172 {ECO:0000244|PDB:1VCP}.
HELIX 175 180 {ECO:0000244|PDB:1VCP}.
STRAND 190 195 {ECO:0000244|PDB:1VCP}.
STRAND 198 203 {ECO:0000244|PDB:1VCP}.
STRAND 206 210 {ECO:0000244|PDB:1VCP}.
STRAND 222 224 {ECO:0000244|PDB:1VCP}.
STRAND 230 239 {ECO:0000244|PDB:1VCP}.
STRAND 241 251 {ECO:0000244|PDB:1VCP}.
STRAND 253 259 {ECO:0000244|PDB:1VCP}.
STRAND 821 823 {ECO:0000244|PDB:2ALA}.
STRAND 830 832 {ECO:0000244|PDB:2ALA}.
STRAND 837 839 {ECO:0000244|PDB:2ALA}.
STRAND 844 863 {ECO:0000244|PDB:2ALA}.
STRAND 866 869 {ECO:0000244|PDB:2ALA}.
STRAND 874 876 {ECO:0000244|PDB:2ALA}.
STRAND 892 898 {ECO:0000244|PDB:2ALA}.
HELIX 903 907 {ECO:0000244|PDB:2ALA}.
STRAND 910 913 {ECO:0000244|PDB:2ALA}.
STRAND 916 925 {ECO:0000244|PDB:2ALA}.
TURN 927 931 {ECO:0000244|PDB:2ALA}.
STRAND 934 954 {ECO:0000244|PDB:2ALA}.
STRAND 958 962 {ECO:0000244|PDB:2ALA}.
STRAND 964 966 {ECO:0000244|PDB:2ALA}.
STRAND 969 971 {ECO:0000244|PDB:2ALA}.
STRAND 974 978 {ECO:0000244|PDB:2ALA}.
STRAND 990 994 {ECO:0000244|PDB:2ALA}.
STRAND 999 1001 {ECO:0000244|PDB:2ALA}.
HELIX 1007 1009 {ECO:0000244|PDB:1RER}.
STRAND 1017 1024 {ECO:0000244|PDB:2ALA}.
STRAND 1041 1043 {ECO:0000244|PDB:1RER}.
HELIX 1054 1061 {ECO:0000244|PDB:2ALA}.
HELIX 1066 1068 {ECO:0000244|PDB:2ALA}.
HELIX 1071 1073 {ECO:0000244|PDB:2ALA}.
STRAND 1075 1077 {ECO:0000244|PDB:2ALA}.
TURN 1078 1081 {ECO:0000244|PDB:2ALA}.
STRAND 1082 1084 {ECO:0000244|PDB:2ALA}.
STRAND 1089 1096 {ECO:0000244|PDB:2ALA}.
HELIX 1099 1101 {ECO:0000244|PDB:2ALA}.
TURN 1105 1107 {ECO:0000244|PDB:2ALA}.
STRAND 1111 1122 {ECO:0000244|PDB:2V33}.
STRAND 1124 1139 {ECO:0000244|PDB:2V33}.
STRAND 1141 1146 {ECO:0000244|PDB:2V33}.
STRAND 1150 1161 {ECO:0000244|PDB:2V33}.
STRAND 1166 1174 {ECO:0000244|PDB:2V33}.
STRAND 1179 1184 {ECO:0000244|PDB:2V33}.
STRAND 1187 1192 {ECO:0000244|PDB:2V33}.
SEQUENCE 1253 AA; 138017 MW; 2A73228D08B82AC5 CRC64;
MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN ALTMRQNAIA
PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK KKKKPGKRER MCMKIENDCI
FEVKHEGKVT GYACLVGDKV MKPAHVKGVI DNADLAKLAF KKSSKYDLEC AQIPVHMRSD
ASKYTHEKPE GHYNWHHGAV QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE
GSRTALSVVT WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE
ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA YCADCGAGHS
CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI RYADGHAIEN AVRSSLKVAT
SGDCFVHGTM GHFILAKCPP GEFLQVSIQD TRNAVRACRI QYHHDPQPVG REKFTIRPHY
GKEIPCTTYQ QTTAETVEEI DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN
VGTTNSDMTI NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV
PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT IPVPVDGMEY
HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV SAVVGMSLLA LISIFASCYM
LVAARSKCLT PYALTPGAAV PWTLGILCCA PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP
VACILIITYC LRNVLCCCKS LSFLVLLSLG ATARAYEHST VMPNVVGFPY KAHIERPGYS
PLTLQMQVVE TSLEPTLNLE YITCEYKTVV PSPYVKCCGA SECSTKEKPD YQCKVYTGVY
PFMWGGAYCF CDSENTQLSE AYVDRSDVCR HDHASAYKAH TASLKAKVRV MYGNVNQTVD
VYVNGDHAVT IGGTQFIFGP LSSAWTPFDN KIVVYKDEVF NQDFPPYGSG QPGRFGDIQS
RTVESNDLYA NTALKLARPS PGMVHVPYTQ TPSGFKYWLK EKGTALNTKA PFGCQIKTNP
VRAMNCAVGN IPVSMNLPDS AFTRIVEAPT IIDLTCTVAT CTHSSDFGGV LTLTYKTNKN
GDCSVHSHSN VATLQEATAK VKTAGKVTLH FSTASASPSF VVSLCSARAT CSASCEPPKD
HIVPYAASHS NVVFPDMSGT ALSWVQKISG GLGAFAIGAI LVLVVVTCIG LRR


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