POLS_SFV
ID POLS_SFV Reviewed; 1253 AA.
AC P03315; B3TP01; Q809B6; Q8JMP5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Structural polyprotein;
DE AltName: Full=p130;
DE Contains:
DE RecName: Full=Capsid protein;
DE EC=3.4.21.90 {ECO:0000269|PubMed:3553612};
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 Semliki forest virus (SFV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11033;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9368; Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
OH NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
OH NCBI_TaxID=170865; Halcyon.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=158617; Quelea.
OH NCBI_TaxID=34630; Rhipicephalus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A7;
RX PubMed=9225028; DOI=10.1099/0022-1317-78-7-1551;
RA Tarbatt C.J., Glasgow G.M., Mooney D.A., Sheahan B.J., Atkins G.J.;
RT "Sequence analysis of the avirulent, demyelinating A7 strain of Semliki
RT Forest virus.";
RL J. Gen. Virol. 78:1551-1557(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MTV;
RX PubMed=18753222; DOI=10.1099/vir.0.2008/002121-0;
RA Tan le V., Ha do Q., Hien V.M., van der Hoek L., Farrar J., de Jong M.D.;
RT "Me Tri virus: a Semliki Forest virus strain from Vietnam?";
RL J. Gen. Virol. 89:2132-2135(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=L10;
RA Logue C., Mooney D., Shanley R., Atkins G.J.;
RT "Semliki Forest Virus - L10 Strain Complete Genome.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-305.
RX PubMed=6935652; DOI=10.1073/pnas.77.11.6376;
RA Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H.;
RT "The capsid protein of Semliki Forest virus has clusters of basic amino
RT acids and prolines in its amino-terminal region.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:6376-6380(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 266-1253.
RX PubMed=6985476; DOI=10.1038/288236a0;
RA Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H.;
RT "Nucleotide sequence of cDNA coding for Semliki Forest virus membrane
RT glycoproteins.";
RL Nature 288:236-241(1980).
RN [6]
RP PROTEIN SEQUENCE OF 334-402 AND 816-881.
RX PubMed=6087344; DOI=10.1073/pnas.81.15.4702;
RA Bell J.R., Kinney R.M., Trent D.W., Strauss E.G., Strauss J.H.;
RT "An evolutionary tree relating eight alphaviruses, based on amino-terminal
RT sequences of their glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4702-4706(1984).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7398872; DOI=10.1016/0014-5793(80)81158-6;
RA Kalkkinen N.;
RT "Carboxyl-terminal sequence analysis of the four structural proteins of
RT Semliki Forest virus.";
RL FEBS Lett. 115:163-166(1980).
RN [8]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=516447; DOI=10.1016/0042-6822(79)90006-0;
RA Ulmanen I., Soederlund H., Kaeaeriaeinen L.;
RT "Role of protein synthesis in the assembly of Semliki forest virus
RT nucleocapsid.";
RL Virology 99:265-276(1979).
RN [9]
RP FUNCTION (CAPSID PROTEIN), AUTOCATALYTIC CLEAVAGE BY CAPSID PROTEIN,
RP MUTAGENESIS OF 219-SER-GLY-220, CATALYTIC ACTIVITY (CAPSID PROTEIN), ACTIVE
RP SITE (CAPSID PROTEIN), AND PROTEOLYTIC CLEAVAGE (STRUCTURAL POLYPROTEIN).
RX PubMed=3553612; DOI=10.1128/jvi.61.5.1301-1309.1987;
RA Melancon P., Garoff H.;
RT "Processing of the Semliki Forest virus structural polyprotein: role of the
RT capsid protease.";
RL J. Virol. 61:1301-1309(1987).
RN [10]
RP STEAROYLATION AT CYS-1248, AND PALMITOYLATION.
RX PubMed=3143715; DOI=10.1016/s0021-9258(18)37332-0;
RA Schmidt M., Schmidt M.F., Rott R.;
RT "Chemical identification of cysteine as palmitoylation site in a
RT transmembrane protein (Semliki Forest virus E1).";
RL J. Biol. Chem. 263:18635-18639(1988).
RN [11]
RP FUNCTION (SPIKE GLYCOPROTEIN E2).
RX PubMed=1714373; DOI=10.1002/j.1460-2075.1991.tb07773.x;
RA Kail M., Hollinshead M., Ansorge W., Pepperkok R., Frank R., Griffiths G.,
RA Vaux D.;
RT "The cytoplasmic domain of alphavirus E2 glycoprotein contains a short
RT linear recognition signal required for viral budding.";
RL EMBO J. 10:2343-2351(1991).
RN [12]
RP MUTAGENESIS OF ARG-330 AND ARG-333, AND PROTEOLYTIC CLEAVAGE (PRECURSOR OF
RP PROTEIN E3/E2).
RX PubMed=2005112; DOI=10.1016/s0021-9258(19)67660-x;
RA Jain S.K., DeCandido S., Kielian M.;
RT "Processing of the p62 envelope precursor protein of Semliki Forest
RT virus.";
RL J. Biol. Chem. 266:5756-5761(1991).
RN [13]
RP MUTAGENESIS OF ASP-890; LYS-894; GLY-898; PRO-901; MET-903 AND GLY-906.
RX PubMed=2072453; DOI=10.1128/jvi.65.8.4292-4300.1991;
RA Levy-Mintz P., Kielian M.;
RT "Mutagenesis of the putative fusion domain of the Semliki Forest virus
RT spike protein.";
RL J. Virol. 65:4292-4300(1991).
RN [14]
RP CLEAVAGE BY SIGNAL PEPTIDASE, AND MUTAGENESIS OF ALA-755 AND ALA-815.
RX PubMed=1985194; DOI=10.1128/jvi.65.1.147-154.1991;
RA Liljestrom P., Garoff H.;
RT "Internally located cleavable signal sequences direct the formation of
RT Semliki Forest virus membrane proteins from a polyprotein precursor.";
RL J. Virol. 65:147-154(1991).
RN [15]
RP FUNCTION (PROTEIN 6K).
RX PubMed=1962454; DOI=10.1016/0042-6822(91)90556-q;
RA Lusa S., Garoff H., Liljestrom P.;
RT "Fate of the 6K membrane protein of Semliki Forest virus during virus
RT assembly.";
RL Virology 185:843-846(1991).
RN [16]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), AND SUBUNIT (SPIKE GLYCOPROTEIN E1).
RX PubMed=1433520; DOI=10.1128/jvi.66.12.7309-7318.1992;
RA Wahlberg J.M., Bron R., Wilschut J., Garoff H.;
RT "Membrane fusion of Semliki Forest virus involves homotrimers of the fusion
RT protein.";
RL J. Virol. 66:7309-7318(1992).
RN [17]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=1433506; DOI=10.1128/jvi.66.12.7049-7058.1992;
RA Singh I., Helenius A.;
RT "Role of ribosomes in Semliki Forest virus nucleocapsid uncoating.";
RL J. Virol. 66:7049-7058(1992).
RN [18]
RP FUNCTION (6K PROTEIN).
RX PubMed=7983743; DOI=10.1128/jvi.69.1.469-475.1995;
RA Loewy A., Smyth J., von Bonsdorff C.H., Liljestrom P., Schlesinger M.J.;
RT "The 6-kilodalton membrane protein of Semliki Forest virus is involved in
RT the budding process.";
RL J. Virol. 69:469-475(1995).
RN [19]
RP MUTAGENESIS OF GLY-898 AND GLY-906.
RX PubMed=9425157; DOI=10.1083/jcb.140.1.91;
RA Vashishtha M., Phalen T., Marquardt M.T., Ryu J.S., Ng A.C., Kielian M.;
RT "A single point mutation controls the cholesterol dependence of Semliki
RT Forest virus entry and exit.";
RL J. Cell Biol. 140:91-99(1998).
RN [20]
RP FUNCTION (CAPSID PROTEIN), AND AUTOCATALYTIC CLEAVAGE (CAPSID PROTEIN).
RX PubMed=9642067; DOI=10.1006/jmbi.1998.1817;
RA Skoging U., Liljestrom P.;
RT "Role of the C-terminal tryptophan residue for the structure-function of
RT the alphavirus capsid protein.";
RL J. Mol. Biol. 279:865-872(1998).
RN [21]
RP INTERACTION WITH HUMAN CHAPERONE P4HB/PDI, AND INTERACTION WITH HUMAN
RP CHAPERONE PDIA3/ERP57.
RX PubMed=10573423; DOI=10.1038/47062;
RA Molinari M., Helenius A.;
RT "Glycoproteins form mixed disulphides with oxidoreductases during folding
RT in living cells.";
RL Nature 402:90-93(1999).
RN [22]
RP MUTAGENESIS OF LEU-859 AND VAL-993.
RX PubMed=12438597; DOI=10.1128/jvi.76.24.12712-12722.2002;
RA Chatterjee P.K., Eng C.H., Kielian M.;
RT "Novel mutations that control the sphingolipid and cholesterol dependence
RT of the Semliki Forest virus fusion protein.";
RL J. Virol. 76:12712-12722(2002).
RN [23]
RP PROTEOLYTIC CLEAVAGE (STRUCTURAL POLYPROTEIN).
RX PubMed=12584323; DOI=10.1128/jvi.77.5.2981-2989.2003;
RA Zhang X., Fugere M., Day R., Kielian M.;
RT "Furin processing and proteolytic activation of Semliki Forest virus.";
RL J. Virol. 77:2981-2989(2003).
RN [24]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=15954801; DOI=10.1371/journal.pbio.0030233;
RA Vonderheit A., Helenius A.;
RT "Rab7 associates with early endosomes to mediate sorting and transport of
RT Semliki forest virus to late endosomes.";
RL PLoS Biol. 3:E233-E233(2005).
RN [25]
RP FUNCTION (ASSEMBLY PROTEIN E3).
RX PubMed=21430054; DOI=10.1128/jvi.00130-11;
RA Sjoeberg M., Lindqvist B., Garoff H.;
RT "Activation of the alphavirus spike protein is suppressed by bound E3.";
RL J. Virol. 85:5644-5650(2011).
RN [26]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), INTERACTION WITH HOST VLDLR AND LRP8
RP (SPIKE GLYCOPROTEIN E1), FUNCTION (SPIKE GLYCOPROTEIN E2), AND INTERACTION
RP WITH HOST VLDLR AND LRP8 (SPIKE GLYCOPROTEIN E2).
RX PubMed=34929721; DOI=10.1038/s41586-021-04326-0;
RA Clark L.E., Clark S.A., Lin C., Liu J., Coscia A., Nabel K.G., Yang P.,
RA Neel D.V., Lee H., Brusic V., Stryapunina I., Plante K.S., Ahmed A.A.,
RA Catteruccia F., Young-Pearse T.L., Chiu I.M., Llopis P.M., Weaver S.C.,
RA Abraham J.;
RT "VLDLR and ApoER2 are receptors for multiple alphaviruses.";
RL Nature 602:475-480(2022).
RN [27]
RP FUNCTION (ASSEMBLY PROTEIN E3).
RX PubMed=23864626; DOI=10.1128/jvi.01507-13;
RA Uchime O., Fields W., Kielian M.;
RT "The role of E3 in pH protection during alphavirus assembly and exit.";
RL J. Virol. 87:10255-10262(2013).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 119-267.
RX PubMed=9094737;
RX DOI=10.1002/(sici)1097-0134(199703)27:3<345::aid-prot3>3.0.co;2-c;
RA Choi H.-K., Lu G., Lee S., Wengler G., Rossmann M.G.;
RT "Structure of Semliki Forest virus core protein.";
RL Proteins 27:345-359(1997).
RN [29]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 119-267, AND DISULFIDE
RP BONDS.
RX PubMed=10882067; DOI=10.1016/s1097-2765(00)80421-9;
RA Mancini E.J., Clarke M., Gowen B.E., Rutten T., Fuller S.D.;
RT "Cryo-electron microscopy reveals the functional organization of an
RT enveloped virus, Semliki Forest virus.";
RL Mol. Cell 5:255-266(2000).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 816-1205.
RX PubMed=11301009; DOI=10.1016/s0092-8674(01)00303-8;
RA Lescar J., Roussel A., Wien M.W., Navaza J., Fuller S.D., Wengler G.,
RA Wengler G., Rey F.A.;
RT "The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral
RT assembly primed for fusogenic activation at endosomal pH.";
RL Cell 105:137-148(2001).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 816-1206, GLYCOSYLATION AT
RP ASN-956, DISULFIDE BONDS, AND SUBUNIT (SPIKE GLYCOPROTEIN E1).
RX PubMed=14737160; DOI=10.1038/nature02239;
RA Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., Lepault J.,
RA Kielian M., Rey F.A.;
RT "Conformational change and protein-protein interactions of the fusion
RT protein of Semliki Forest virus.";
RL Nature 427:320-325(2004).
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 (PubMed:3553612,
CC PubMed:9642067). Following its self-cleavage, the capsid protein
CC transiently associates with ribosomes, and within several minutes the
CC protein binds to viral RNA and rapidly assembles into icosahedric core
CC particles (PubMed:516447). The resulting nucleocapsid eventually
CC associates with the cytoplasmic domain of the spike glycoprotein E2 at
CC the cell membrane, leading to budding and formation of mature virions
CC (By similarity). In case of infection, new virions attach to target
CC cells and after clathrin-mediated endocytosis their membrane fuses with
CC the host endosomal membrane (PubMed:15954801). This leads to the
CC release of the nucleocapsid into the cytoplasm, followed by an
CC uncoating event necessary for the genomic RNA to become accessible
CC (PubMed:1433506). The uncoating might be triggered by the interaction
CC of capsid proteins with ribosomes (PubMed:1433506). Binding of
CC ribosomes would release the genomic RNA since the same region is
CC genomic RNA-binding and ribosome-binding (PubMed:1433506). Specifically
CC inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent
CC signaling during viral entry, representing a means by which the
CC alphaviruses may evade innate immune detection and activation prior to
CC viral gene expression (By similarity). {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P27284, ECO:0000269|PubMed:1433506,
CC ECO:0000269|PubMed:15954801, ECO:0000269|PubMed:3553612,
CC ECO:0000269|PubMed:516447, ECO:0000269|PubMed:9642067}.
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:0000269|PubMed:21430054, ECO:0000269|PubMed:23864626}.
CC -!- FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to
CC target host cell, by binding to the cell receptors VLDLR or LRP8
CC (PubMed:34929721). 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:0000269|PubMed:1714373}.
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:0000269|PubMed:1962454,
CC ECO:0000269|PubMed:7983743}.
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 via host VLDLR or LRP8
CC and endocytosis, acidification of the endosome would induce
CC dissociation of E1/E2 heterodimer and concomitant trimerization of the
CC E1 subunits (PubMed:34929721). This E1 trimer is fusion active, and
CC promotes release of viral nucleocapsid in cytoplasm after endosome and
CC viral membrane fusion. Efficient fusion requires the presence of
CC cholesterol and sphingolipid in the target membrane. Fusion is optimal
CC at levels of about 1 molecule of cholesterol per 2 molecules of
CC phospholipids, and is specific for sterols containing a 3-beta-hydroxyl
CC group. {ECO:0000269|PubMed:1433520, ECO:0000269|PubMed:34929721}.
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:0000269|PubMed:3553612};
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 (By similarity).
CC Interacts with spike glycoprotein E2 (By similarity). Interacts with
CC host IRAK1; the interaction leads to inhibition of IRAK1-dependent
CC signaling (By similarity). {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5,
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:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC ECO:0000250|UniProtKB:Q8JUX5}.
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). E2-E1 heterodimers interact with host VLDLR or LRP8 to
CC mediate viral entry (PubMed:34929721).After target cell attachment and
CC endocytosis, E1 change conformation to form homotrimers
CC (PubMed:1433520, PubMed:14737160). Interacts with 6K protein (By
CC similarity). {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5,
CC ECO:0000269|PubMed:34929721}.
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). E2-E1
CC heterodimers interact with host VLDLR or LRP8 to mediate viral entry
CC (PubMed:34929721). Interacts with 6K protein (By similarity).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1 (By
CC similarity). Interacts with spike glycoprotein E2 (By similarity).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}. Host nucleus
CC {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and
CC the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
CC {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Structural polyprotein;
CC IsoId=P03315-1; Sequence=Displayed;
CC Name=Frameshifted structural polyprotein;
CC IsoId=P0DJZ6-1; Sequence=External;
CC -!- DOMAIN: [Capsid protein]: The N-terminus contains a nuclear
CC localization signal and a CRM1-mediated nuclear export signal (By
CC similarity). The C-terminus functions as a protease during translation
CC to cleave itself from the translating structural polyprotein (By
CC similarity). {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:Q8JUX5}.
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 (PubMed:3553612). The remaining polyprotein
CC is 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
CC (PubMed:12584323). Protein processing process takes about 30 minutes at
CC physiologic temperatures. The folding of the p62/6K/E1 precursor
CC requires the formation of intrachain disulfide bonds and has been shown
CC to involve a transient covalent interaction between the nascent and
CC newly synthesized heterodimer and the host-cell chaperones, P4HB/PDI
CC and PDIA3/ERp57. The folding pathway also includes non covalent
CC interaction with human CANX/calnexin and CALR/calreticulin.
CC {ECO:0000269|PubMed:12584323, ECO:0000269|PubMed:1985194,
CC ECO:0000269|PubMed:2005112, ECO:0000269|PubMed:3553612,
CC ECO:0000269|PubMed:9642067}.
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:0000269|PubMed:3143715}.
CC -!- PTM: Envelope E1, E2 and E3 proteins are N-glycosylated.
CC {ECO:0000269|PubMed:14737160}.
CC -!- PTM: [Spike glycoprotein E1]: Stearoylated.
CC {ECO:0000269|PubMed:3143715}.
CC -!- PTM: [6K protein]: Palmitoylated via thioester bonds with about four
CC covalently bound fatty acids per molecule.
CC {ECO:0000269|PubMed:3143715}.
CC -!- MISCELLANEOUS: The mature virion nucleocapsid consists of 240 copies of
CC the capsid protein. 80 spike trimers of E1 and E2 are present at the
CC surface of mature virion. They project about 100 Angstroms from the
CC outer surface and are located at the local and strict three fold axis
CC of the icosahedral lattice. The glycoproteins splay out to form a
CC protein shell or skirt covering most of the outer surface of the
CC membrane bilayer.
CC -!- MISCELLANEOUS: [Isoform Structural polyprotein]: Translated from a
CC subgenomic RNA synthesized during togavirus replication.
CC -!- MISCELLANEOUS: [Isoform Structural polyprotein]: Produced by
CC conventional translation.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1dwn";
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DR EMBL; Z48163; CAD90834.1; -; Genomic_RNA.
DR EMBL; EU350586; ACB12688.1; -; Genomic_RNA.
DR EMBL; AY112987; AAM64227.1; -; Genomic_RNA.
DR EMBL; X04129; CAA27742.1; -; Genomic_RNA.
DR PIR; A93861; VHWV.
DR PIR; S42462; S42462.
DR RefSeq; NP_463458.1; NC_003215.1. [P03315-1]
DR PDB; 1DYL; EM; 9.00 A; A/B/C/D=119-267.
DR PDB; 1I9W; X-ray; 3.00 A; A=816-1205.
DR PDB; 1RER; X-ray; 3.20 A; A/B/C=816-1206.
DR PDB; 1VCP; X-ray; 3.00 A; A/B/C=119-267.
DR PDB; 1VCQ; X-ray; 3.10 A; A/B=119-267.
DR PDB; 2ALA; X-ray; 3.00 A; A=816-1206.
DR PDB; 2V33; X-ray; 1.55 A; A/B=1107-1197.
DR PDBsum; 1DYL; -.
DR PDBsum; 1I9W; -.
DR PDBsum; 1RER; -.
DR PDBsum; 1VCP; -.
DR PDBsum; 1VCQ; -.
DR PDBsum; 2ALA; -.
DR PDBsum; 2V33; -.
DR SMR; P03315; -.
DR MEROPS; C09.001; -.
DR MEROPS; S03.001; -.
DR TCDB; 1.G.4.1.1; the viral pore-forming membrane fusion protein-4 (vmfp4) family.
DR GlyConnect; 575; 2 N-Linked glycans.
DR GlyConnect; 576; 2 N-Linked glycans.
DR GlyConnect; 577; 1 N-Linked glycan.
DR iPTMnet; P03315; -.
DR SwissPalm; P03315; -.
DR GeneID; 922351; -.
DR KEGG; vg:922351; -.
DR EvolutionaryTrace; P03315; -.
DR Proteomes; UP000000570; Genome.
DR Proteomes; UP000108382; Genome.
DR Proteomes; UP000125835; Genome.
DR Proteomes; UP000174511; Genome.
DR GO; GO:0044174; C:host cell endosome; IDA:CACAO.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IMP:CACAO.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR DisProt; DP00999; -.
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; Autocatalytic cleavage; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Direct protein sequencing;
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; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..267
FT /note="Capsid protein"
FT /id="PRO_0000041311"
FT CHAIN 268..755
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000226237"
FT CHAIN 268..333
FT /note="Assembly protein E3"
FT /id="PRO_0000041312"
FT CHAIN 334..755
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041313"
FT CHAIN 756..815
FT /note="6K protein"
FT /id="PRO_0000041314"
FT CHAIN 816..1253
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041315"
FT TOPO_DOM 268..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..770
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..1230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1252..1253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 119..267
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 37..71
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 58..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..120
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 105..119
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 189..199
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 225..229
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 728..748
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 899..916
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 64..105
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 150..160
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 64..81
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027,
FT ECO:0000269|PubMed:3553612"
FT SITE 193
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 226
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 267..268
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:3553612"
FT SITE 333..334
FT /note="Cleavage; by host furin"
FT SITE 755..756
FT /note="Cleavage; by host signal peptidase"
FT SITE 815..816
FT /note="Cleavage; by host signal peptidase"
FT LIPID 718
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255"
FT LIPID 728
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 748
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 749
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 1248
FT /note="S-stearoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:3143715"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:14737160,
FT ECO:0000269|PubMed:6985476"
FT DISULFID 119..134
FT DISULFID 864..929
FT DISULFID 877..909
FT DISULFID 878..911
FT DISULFID 883..893
FT DISULFID 1074..1086
FT DISULFID 1116..1191
FT DISULFID 1121..1195
FT DISULFID 1143..1185
FT VARIANT 62
FT /note="A -> T (in strain: A7)"
FT VARIANT 63
FT /note="R -> G (in strain: L10)"
FT VARIANT 85
FT /note="N -> K (in strain: A7, L10 and MTV)"
FT VARIANT 279
FT /note="A -> T (in strain: A7)"
FT VARIANT 291
FT /note="V -> A (in strain: A7)"
FT VARIANT 370
FT /note="V -> I (in strain: A7, L10 and MTV)"
FT VARIANT 437
FT /note="K -> T (in strain: A7, L10 and MTV)"
FT VARIANT 545
FT /note="N -> S (in strain: A7)"
FT VARIANT 548
FT /note="M -> K (in strain: A7 and MTV)"
FT VARIANT 614
FT /note="E -> K (in strain: MTV)"
FT VARIANT 700
FT /note="V -> A (in strain: A7)"
FT VARIANT 704
FT /note="V -> A (in strain: A7)"
FT VARIANT 722
FT /note="V -> A (in strain: A7 and MTV)"
FT VARIANT 880
FT /note="A -> S (in strain: A7)"
FT VARIANT 930
FT /note="R -> K (in strain: A7)"
FT VARIANT 1043
FT /note="M -> T (in strain: A7 and MTV)"
FT VARIANT 1112
FT /note="I -> T (in strain: A7 and MTV)"
FT VARIANT 1134
FT /note="T -> K (in strain: A7)"
FT VARIANT 1138
FT /note="N -> D (in strain: A7, L10 and MTV)"
FT VARIANT 1165
FT /note="G -> R (in strain: MTV)"
FT VARIANT 1188
FT /note="R -> K (in strain: A7 and MTV)"
FT MUTAGEN 219..220
FT /note="SG->RST: Loss of autocatalytic cleavage by capsid
FT protein."
FT /evidence="ECO:0000269|PubMed:3553612"
FT MUTAGEN 267
FT /note="W->A,R: Complete loss of cleavage by capsid
FT protease."
FT MUTAGEN 330
FT /note="R->S: Complete loss of p62 precursor processing."
FT /evidence="ECO:0000269|PubMed:2005112"
FT MUTAGEN 333
FT /note="R->F: Complete loss of p62 precursor processing."
FT /evidence="ECO:0000269|PubMed:2005112"
FT MUTAGEN 755
FT /note="A->F: Complete loss of p62 precursor-6K cleavage."
FT /evidence="ECO:0000269|PubMed:1985194"
FT MUTAGEN 815
FT /note="A->F: Complete loss of 6K protein-E1 envelope
FT glycoprotein cleavage."
FT /evidence="ECO:0000269|PubMed:1985194"
FT MUTAGEN 859
FT /note="L->F: E1 fusion is less cholesterol and sphingolipid
FT dependent."
FT /evidence="ECO:0000269|PubMed:12438597"
FT MUTAGEN 890
FT /note="D->A: Shifts the pH threshold for fusion to a more
FT acidic range."
FT /evidence="ECO:0000269|PubMed:2072453"
FT MUTAGEN 894
FT /note="K->Q: No effect on E1 fusion activity."
FT /evidence="ECO:0000269|PubMed:2072453"
FT MUTAGEN 898
FT /note="G->A: Shifts the pH threshold for fusion to a more
FT acidic range."
FT /evidence="ECO:0000269|PubMed:2072453,
FT ECO:0000269|PubMed:9425157"
FT MUTAGEN 898
FT /note="G->D: No effect on E1 fusion activity."
FT /evidence="ECO:0000269|PubMed:2072453,
FT ECO:0000269|PubMed:9425157"
FT MUTAGEN 901
FT /note="P->D: Retention of E1 protein in endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:2072453"
FT MUTAGEN 903
FT /note="M->L: No effect on E1 fusion activity."
FT /evidence="ECO:0000269|PubMed:2072453"
FT MUTAGEN 906
FT /note="G->A: Shifts the pH threshold for fusion to a more
FT acidic range."
FT /evidence="ECO:0000269|PubMed:2072453,
FT ECO:0000269|PubMed:9425157"
FT MUTAGEN 906
FT /note="G->D: Complete loss of E1 fusion activity."
FT /evidence="ECO:0000269|PubMed:2072453,
FT ECO:0000269|PubMed:9425157"
FT MUTAGEN 906
FT /note="G->P: Retention of E1 protein in endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:2072453,
FT ECO:0000269|PubMed:9425157"
FT MUTAGEN 993
FT /note="V->A: E1 fusion is less cholesterol and sphingolipid
FT dependent."
FT /evidence="ECO:0000269|PubMed:12438597"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1VCP"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1VCP"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1VCP"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1VCP"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 830..832
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 844..863
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 866..869
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 892..898
FT /evidence="ECO:0007829|PDB:2ALA"
FT HELIX 903..907
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 916..925
FT /evidence="ECO:0007829|PDB:2ALA"
FT TURN 927..931
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 934..954
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 958..962
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 974..978
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 990..994
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 999..1001
FT /evidence="ECO:0007829|PDB:2ALA"
FT HELIX 1007..1009
FT /evidence="ECO:0007829|PDB:1RER"
FT STRAND 1017..1024
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:1RER"
FT HELIX 1054..1061
FT /evidence="ECO:0007829|PDB:2ALA"
FT HELIX 1066..1068
FT /evidence="ECO:0007829|PDB:2ALA"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 1075..1077
FT /evidence="ECO:0007829|PDB:2ALA"
FT TURN 1078..1081
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 1089..1096
FT /evidence="ECO:0007829|PDB:2ALA"
FT HELIX 1099..1101
FT /evidence="ECO:0007829|PDB:2ALA"
FT TURN 1105..1107
FT /evidence="ECO:0007829|PDB:2ALA"
FT STRAND 1111..1122
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1124..1139
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1141..1146
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1150..1161
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1166..1174
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1179..1184
FT /evidence="ECO:0007829|PDB:2V33"
FT STRAND 1187..1192
FT /evidence="ECO:0007829|PDB:2V33"
SQ 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
