POLS_SINDV
ID POLS_SINDV Reviewed; 1245 AA.
AC P03316; C4T9C2; P11259; Q88870; Q88871; Q88872; Q88873; Q88874;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Structural polyprotein;
DE AltName: Full=p130;
DE Contains:
DE RecName: Full=Capsid protein;
DE EC=3.4.21.90 {ECO:0000250|UniProtKB:P03315};
DE AltName: Full=Coat protein;
DE Short=C;
DE Contains:
DE RecName: Full=Precursor of protein E3/E2;
DE AltName: Full=p62;
DE AltName: Full=pE2;
DE Contains:
DE RecName: Full=Assembly protein E3;
DE Contains:
DE RecName: Full=Spike glycoprotein E2;
DE AltName: Full=E2 envelope glycoprotein;
DE Contains:
DE RecName: Full=6K protein;
DE Contains:
DE RecName: Full=Spike glycoprotein E1;
DE AltName: Full=E1 envelope glycoprotein;
OS Sindbis virus (SINV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11034;
OH NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=53527; Culex.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
OH NCBI_TaxID=177155; Streptopelia turtur.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=HRLP;
RX PubMed=6941270; DOI=10.1073/pnas.78.4.2062;
RA Rice C.M., Strauss J.H.;
RT "Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence
RT of the encoded virus structural proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2062-2066(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=HRSP;
RX PubMed=6322438; DOI=10.1016/0042-6822(84)90428-8;
RA Strauss E.G., Rice C.M., Strauss J.H.;
RT "Complete nucleotide sequence of the genomic RNA of Sindbis virus.";
RL Virology 133:92-110(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AR339;
RX PubMed=3462725; DOI=10.1073/pnas.83.18.6771;
RA Davis N.L., Fuller F.J., Dougherty W.G., Olmsted R.A., Johnston R.E.;
RT "A single nucleotide change in the E2 glycoprotein gene of Sindbis virus
RT affects penetration rate in cell culture and virulence in neonatal mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6771-6775(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=ov-100;
RA Saito K., Shirasawa H., Yahata E., Yuan Q.;
RT "Sequence analysis of cDNA's derived from the RNA of Sindbis virus, a
RT potential oncolytic virus.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 329-394.
RC STRAIN=AR339;
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 [6]
RP SUBCELLULAR LOCATION (PRECURSOR OF PROTEIN E3/E2), SUBCELLULAR LOCATION
RP (SPIKE GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
RX PubMed=875134; DOI=10.1128/jvi.22.3.662-678.1977;
RA Smith J.F., Brown D.T.;
RT "Envelopments of Sindbis virus: synthesis and organization of proteins in
RT cells infected with wild type and maturation-defective mutants.";
RL J. Virol. 22:662-678(1977).
RN [7]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=3656418; DOI=10.1016/0022-2836(87)90657-7;
RA Coombs K., Brown D.T.;
RT "Organization of the Sindbis virus nucleocapsid as revealed by bifunctional
RT cross-linking agents.";
RL J. Mol. Biol. 195:359-371(1987).
RN [8]
RP SUBCELLULAR LOCATION (CAPSID PROTEIN), SUBCELLULAR LOCATION (SPIKE
RP GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
RX PubMed=3829124; DOI=10.1016/0092-8674(87)90701-x;
RA Fuller S.D.;
RT "The T=4 envelope of Sindbis virus is organized by interactions with a
RT complementary T=3 capsid.";
RL Cell 48:923-934(1987).
RN [9]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
RX PubMed=2806407; DOI=10.1016/0014-4827(89)90049-9;
RA Migliaccio G., Pascale M.C., Leone A., Bonatti S.;
RT "Biosynthesis, membrane translocation, and surface expression of Sindbis
RT virus E1 glycoprotein.";
RL Exp. Cell Res. 185:203-216(1989).
RN [10]
RP AUTOCATALYTIC CLEAVAGE (CAPSID PROTEIN), AND MUTAGENESIS OF HIS-141;
RP ASP-147; ASP-163 AND SER-215.
RX PubMed=2335827; DOI=10.1128/jvi.64.6.3069-3073.1990;
RA Hahn C.S., Strauss J.H.;
RT "Site-directed mutagenesis of the proposed catalytic amino acids of the
RT Sindbis virus capsid protein autoprotease.";
RL J. Virol. 64:3069-3073(1990).
RN [11]
RP SUBCELLULAR LOCATION (6K PROTEIN).
RX PubMed=2408229; DOI=10.1016/0042-6822(90)90209-a;
RA Gaedigk-Nitschko K., Schlesinger M.J.;
RT "The Sindbis virus 6K protein can be detected in virions and is acylated
RT with fatty acids.";
RL Virology 175:274-281(1990).
RN [12]
RP PALMITOYLATION AT CYS-724, AND MUTAGENESIS OF CYS-724.
RX PubMed=1647069; DOI=10.1016/0042-6822(91)90133-v;
RA Gaedigk-Nitschko K., Schlesinger M.J.;
RT "Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic
RT domain and the 6K protein lead to similar defects in virus assembly and
RT budding.";
RL Virology 183:206-214(1991).
RN [13]
RP FUNCTION (CAPSID PROTEIN), ACTIVE SITE (CAPSID PROTEIN), AND DOMAIN (CAPSID
RP PROTEIN).
RX PubMed=1944569; DOI=10.1038/354037a0;
RA Choi H.K., Tong L., Minor W., Dumas P., Boege U., Rossmann M.G.,
RA Wengler G.;
RT "Structure of Sindbis virus core protein reveals a chymotrypsin-like serine
RT proteinase and the organization of the virion.";
RL Nature 354:37-43(1991).
RN [14]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=8415660; DOI=10.1073/pnas.90.19.9095;
RA Paredes A.M., Brown D.T., Rothnagel R., Chiu W., Schoepp R.J.,
RA Johnston R.E., Prasad B.V.;
RT "Three-dimensional structure of a membrane-containing virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9095-9099(1993).
RN [15]
RP TOPOLOGY.
RX PubMed=8432728; DOI=10.1083/jcb.120.4.877;
RA Liu N., Brown D.T.;
RT "Transient translocation of the cytoplasmic (endo) domain of a type I
RT membrane glycoprotein into cellular membranes.";
RL J. Cell Biol. 120:877-883(1993).
RN [16]
RP PALMITOYLATION AT CYS-744 AND CYS-745, AND MUTAGENESIS OF CYS-744 AND
RP CYS-745.
RX PubMed=8474160; DOI=10.1128/jvi.67.5.2546-2551.1993;
RA Ivanova L., Schlesinger M.J.;
RT "Site-directed mutations in the Sindbis virus E2 glycoprotein identify
RT palmitoylation sites and affect virus budding.";
RL J. Virol. 67:2546-2551(1993).
RN [17]
RP SUBUNIT (SPIKE GLYCOPROTEIN E1), SUBUNIT (SPIKE GLYCOPROTEIN E2), AND
RP SUBUNIT (PRECURSOR OF PROTEIN E3/E2).
RX PubMed=8623521; DOI=10.1006/viro.1996.0229;
RA Mulvey M., Brown D.T.;
RT "Assembly of the Sindbis virus spike protein complex.";
RL Virology 219:125-132(1996).
RN [18]
RP FUNCTION (6K PROTEIN), INTERACTION WITH 6K PROTEIN (SPIKE GLYCOPROTEIN E1),
RP INTERACTION WITH 6K PROTEIN (SPIKE GLYCOPROTEIN E2), INTERACTION WITH SPIKE
RP GLYCOPROTEIN 1 (6K PROTEIN), AND INTERACTION WITH SPIKE GLYCOPROTEIN 2 (6K
RP PROTEIN).
RX PubMed=8892914; DOI=10.1128/jvi.70.11.7910-7920.1996;
RA Yao J.S., Strauss E.G., Strauss J.H.;
RT "Interactions between PE2, E1, and 6K required for assembly of alphaviruses
RT studied with chimeric viruses.";
RL J. Virol. 70:7910-7920(1996).
RN [19]
RP FUNCTION (CAPSID PROTEIN), INTERACTION WITH SPIKE GLYCOPROTEIN E2 (CAPSID
RP PROTEIN), AND INTERACTION WITH CAPSID PROTEIN (SPIKE GLYCOPROTEIN E2).
RX PubMed=9143274; DOI=10.1006/viro.1997.8480;
RA Owen K.E., Kuhn R.J.;
RT "Alphavirus budding is dependent on the interaction between the
RT nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the
RT E2 envelope glycoprotein.";
RL Virology 230:187-196(1997).
RN [20]
RP FUNCTION (SPIKE GLYCOPROTEIN E2).
RX PubMed=8995682; DOI=10.1128/jvi.71.2.1558-1566.1997;
RA Carleton M., Lee H., Mulvey M., Brown D.T.;
RT "Role of glycoprotein PE2 in formation and maturation of the Sindbis virus
RT spike.";
RL J. Virol. 71:1558-1566(1997).
RN [21]
RP MUTAGENESIS OF TRP-264.
RX PubMed=9445057; DOI=10.1128/jvi.72.2.1534-1541.1998;
RA Paredes A.M., Heidner H., Thuman-Commike P., Prasad B.V.V., Johnston R.E.,
RA Chiu W.;
RT "Structural localization of the E3 glycoprotein in attenuated Sindbis virus
RT mutants.";
RL J. Virol. 72:1534-1541(1998).
RN [22]
RP FUNCTION (6K PROTEIN).
RX PubMed=9707418; DOI=10.1093/emboj/17.16.4585;
RA DeTulleo L., Kirchhausen T.;
RT "The clathrin endocytic pathway in viral infection.";
RL EMBO J. 17:4585-4593(1998).
RN [23]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), AND FUNCTION (6K PROTEIN).
RX PubMed=10482600; DOI=10.1128/jvi.73.10.8476-8484.1999;
RA Smit J.M., Bittman R., Wilschut J.;
RT "Low-pH-dependent fusion of Sindbis virus with receptor-free
RT cholesterol- and sphingolipid-containing liposomes.";
RL J. Virol. 73:8476-8484(1999).
RN [24]
RP FUNCTION (6K PROTEIN).
RX PubMed=12424249; DOI=10.1074/jbc.m206611200;
RA Sanz M.A., Madan V., Carrasco L., Nieva J.L.;
RT "Interfacial domains in Sindbis virus 6K protein. Detection and functional
RT characterization.";
RL J. Biol. Chem. 278:2051-2057(2003).
RN [25]
RP FUNCTION (SPIKE GLYCOPROTEIN E1).
RX PubMed=12573591; DOI=10.1006/viro.2002.1771;
RA Sanz M.A., Rejas M.T., Carrasco L.;
RT "Individual expression of sindbis virus glycoproteins. E1 alone promotes
RT cell fusion.";
RL Virology 305:463-472(2003).
RN [26]
RP FUNCTION (6K PROTEIN).
RX PubMed=17483865; DOI=10.1007/s00232-007-9003-6;
RA Antoine A.F., Montpellier C., Cailliau K., Browaeys-Poly E., Vilain J.P.,
RA Dubuisson J.;
RT "The alphavirus 6K protein activates endogenous ionic conductances when
RT expressed in Xenopus oocytes.";
RL J. Membr. Biol. 215:37-48(2007).
RN [27]
RP DISULFIDE BOND (ASSEMBLY PROTEIN E3).
RX PubMed=19109378; DOI=10.1128/jvi.02158-08;
RA Parrott M.M., Sitarski S.A., Arnold R.J., Picton L.K., Hill R.B.,
RA Mukhopadhyay S.;
RT "Role of conserved cysteines in the alphavirus E3 protein.";
RL J. Virol. 83:2584-2591(2009).
RN [28]
RP SUBCELLULAR LOCATION (CAPSID PROTEIN), AND SUBCELLULAR LOCATION (SPIKE
RP GLYCOPROTEIN E2).
RX PubMed=23785213; DOI=10.1128/jvi.01299-13;
RA Zheng Y., Kielian M.;
RT "Imaging of the alphavirus capsid protein during virus replication.";
RL J. Virol. 87:9579-9589(2013).
RN [29]
RP FUNCTION (CAPSID PROTEIN), AND INTERACTION WITH HOST IRAK1 (CAPSID
RP PROTEIN).
RX PubMed=33673546; DOI=10.3390/v13030377;
RA Landers V.D., Wilkey D.W., Merchant M.L., Mitchell T.C., Sokoloski K.J.;
RT "The Alphaviral Capsid Protein Inhibits IRAK1-Dependent TLR Signaling.";
RL Viruses 13:0-0(2021).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 107-264.
RX PubMed=8831786; DOI=10.1006/jmbi.1996.0505;
RA Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G., Rossmann M.G.,
RA Kuhn R.J.;
RT "Structural analysis of Sindbis virus capsid mutants involving assembly and
RT catalysis.";
RL J. Mol. Biol. 262:151-167(1996).
RN [31]
RP ERRATUM OF PUBMED:8831786.
RA Choi H.-K., Lee S., Zhang Y.-P., McKinney B.R., Wengler G., Rossmann M.G.,
RA Kuhn R.J.;
RL J. Mol. Biol. 266:633-634(1997).
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 (PubMed:8415660). 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:1944569).
CC Following its self-cleavage, the capsid protein transiently associates
CC with ribosomes, and within several minutes the protein binds to viral
CC RNA and rapidly assembles into icosahedric core particles (By
CC similarity). The resulting nucleocapsid eventually associates with the
CC cytoplasmic domain of the spike glycoprotein E2 at the cell membrane,
CC leading to budding and formation of mature virions (PubMed:9143274). In
CC case of infection, new virions attach to target cells and after
CC clathrin-mediated endocytosis their membrane fuses with the host
CC endosomal membrane (By similarity). This leads to the release of the
CC nucleocapsid into the cytoplasm, followed by an uncoating event
CC necessary for the genomic RNA to become accessible (By similarity). The
CC uncoating might be triggered by the interaction of capsid proteins with
CC ribosomes (PubMed:3656418). Binding of ribosomes would release the
CC genomic RNA since the same region is genomic RNA-binding and ribosome-
CC binding (By similarity). Specifically inhibits interleukin-1 receptor-
CC associated kinase 1/IRAK1-dependent signaling during viral entry,
CC representing a means by which the alphaviruses may evade innate immune
CC detection and activation prior to viral gene expression
CC (PubMed:33673546). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P27284, ECO:0000269|PubMed:1944569,
CC ECO:0000269|PubMed:33673546, ECO:0000269|PubMed:3656418,
CC ECO:0000269|PubMed:8415660, ECO:0000269|PubMed:9143274}.
CC -!- FUNCTION: [Assembly protein E3]: Provides the signal sequence for the
CC translocation of the precursor of protein E3/E2 to the host endoplasmic
CC reticulum. Furin-cleaved E3 remains associated with spike glycoprotein
CC E1 and mediates pH protection of the latter during the transport via
CC the secretory pathway. After virion release from the host cell, the
CC assembly protein E3 is gradually released in the extracellular space.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Spike glycoprotein E2]: Plays an essential role in viral
CC attachment to target host cell, by binding to the cell receptor.
CC Synthesized as a pE2 precursor which is processed by furin at the cell
CC membrane just before virion budding, giving rise to E2-E1 heterodimer.
CC The pE2-E1 heterodimer is stable, whereas E2-E1 is unstable and
CC dissociate at low pH. pE2 is processed at the last step, presumably to
CC avoid E1 fusion activation before its final export to cell surface. E2
CC C-terminus contains a transitory transmembrane that would be disrupted
CC by palmitoylation, resulting in reorientation of the C-terminal tail
CC from lumenal to cytoplasmic side. This step is critical since E2 C-
CC terminus is involved in budding by interacting with capsid proteins.
CC This release of E2 C-terminus in cytoplasm occurs lately in protein
CC export, and precludes premature assembly of particles at the
CC endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315,
CC ECO:0000269|PubMed:8995682}.
CC -!- FUNCTION: Protein 6K: Acts as a viroporin that participates in virus
CC glycoprotein processing, cell permeabilization and budding of viral
CC particles. Disrupts the calcium homeostasis of the cell, probably at
CC the endoplasmic reticulum level resulting in the increased levels of
CC cytoplasmic calcium. Because of its lipophilic properties, the 6K
CC protein is postulated to influence the selection of lipids that
CC interact with the transmembrane domains of the glycoproteins, which, in
CC turn, affects the deformability of the bilayer required for the extreme
CC curvature that occurs as budding proceeds. Present in low amount in
CC virions, about 3% compared to viral glycoproteins.
CC {ECO:0000269|PubMed:10482600, ECO:0000269|PubMed:12424249,
CC ECO:0000269|PubMed:17483865, ECO:0000269|PubMed:8892914,
CC ECO:0000269|PubMed:9707418}.
CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein.
CC Fusion activity is inactive as long as E1 is bound to E2 in mature
CC virion. After virus attachment to target cell and endocytosis,
CC acidification of the endosome would induce dissociation of E1/E2
CC heterodimer and concomitant trimerization of the E1 subunits. This E1
CC trimer is fusion active, and promotes release of viral nucleocapsid in
CC cytoplasm after endosome and viral membrane fusion. Efficient fusion
CC requires the presence of cholesterol and sphingolipid in the target
CC membrane. {ECO:0000269|PubMed:10482600, ECO:0000269|PubMed:12573591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytic release of the core protein from the N-terminus
CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315};
CC -!- SUBUNIT: [Capsid protein]: Homomultimer (Probable). Interacts with host
CC karyopherin KPNA4; this interaction allows the nuclear import of the
CC viral capsid protein (By similarity). Interacts with spike glycoprotein
CC E2 (PubMed:9143274). Interacts with host IRAK1; the interaction leads
CC to inhibition of IRAK1-dependent signaling (PubMed:33673546).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:Q8JUX5,
CC ECO:0000269|PubMed:33673546, ECO:0000269|PubMed:9143274, ECO:0000305}.
CC -!- SUBUNIT: [Precursor of protein E3/E2]: The precursor of protein E3/E2
CC and E1 form a heterodimer shortly after synthesis (PubMed:8623521).
CC {ECO:0000269|PubMed:8623521}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: The precursor of protein E3/E2 and E1
CC form a heterodimer shortly after synthesis (PubMed:8623521). 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 (PubMed:8623521).
CC Spike at virion surface are constituted of three E2-E1 heterodimers
CC (PubMed:8623521). After target cell attachment and endocytosis, E1
CC change conformation to form homotrimers (By similarity). Interacts with
CC 6K protein (PubMed:8892914). {ECO:0000250, ECO:0000269|PubMed:8623521,
CC ECO:0000269|PubMed:8892914}.
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 (PubMed:8623521). Spike at virion surface are
CC constituted of three E2-E1 heterodimers (PubMed:8623521). Interacts
CC with 6K protein (PubMed:8892914). {ECO:0000269|PubMed:8623521,
CC ECO:0000269|PubMed:8892914}.
CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1
CC (PubMed:8892914). Interacts with spike glycoprotein E2
CC (PubMed:8892914). {ECO:0000269|PubMed:8892914}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000269|PubMed:3829124}. Host cytoplasm
CC {ECO:0000269|PubMed:23785213}. Host cell membrane
CC {ECO:0000269|PubMed:23785213}. Host nucleus
CC {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and
CC the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [Precursor of protein E3/E2]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000255}. Host
CC cell membrane {ECO:0000269|PubMed:875134}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000269|PubMed:3829124}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:23785213,
CC ECO:0000269|PubMed:875134}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane
CC {ECO:0000269|PubMed:2408229}; Multi-pass membrane protein
CC {ECO:0000255}. Virion membrane {ECO:0000269|PubMed:2408229}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000269|PubMed:3829124}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:2806407,
CC ECO:0000269|PubMed:875134}; 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=P03316-1; Sequence=Displayed;
CC Name=Frameshifted structural polyprotein;
CC IsoId=P0DOK0-1; Sequence=External;
CC -!- DOMAIN: [Capsid protein]: The very N-terminus also plays a role in the
CC particle assembly process (By similarity). The N-terminus also contains
CC a nuclear localization signal and a supra nuclear export signal
CC (supraNES), which is an unusually strong NES that mediates host CRM1
CC binding in the absence of RanGTP and thus can bind CRM1, not only in
CC the nucleus, but also in the cytoplasm (By similarity). The C-terminus
CC functions as a protease during translation to cleave itself from the
CC translating structural polyprotein (PubMed:1944569).
CC {ECO:0000250|UniProtKB:P09592, ECO:0000269|PubMed:1944569}.
CC -!- DOMAIN: [Isoform Structural polyprotein]: As soon as the capsid protein
CC has been autocleaved, an internal uncleaved signal peptide directs the
CC remaining polyprotein to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Isoform Structural polyprotein]: Specific enzymatic cleavages in
CC vivo yield mature proteins. Capsid protein is auto-cleaved during
CC polyprotein translation, unmasking a signal peptide at the N-terminus
CC of the precursor of E3/E2 (PubMed:2335827). 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 (By
CC similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000269|PubMed:2335827}.
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:1647069,
CC ECO:0000269|PubMed:8432728}.
CC -!- PTM: [Spike glycoprotein E1]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E2]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Assembly protein E3]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [6K protein]: Palmitoylated via thioester bonds.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- MISCELLANEOUS: [Isoform Structural polyprotein]: Translated from a
CC subgenomic RNA synthesized during togavirus replication.
CC {ECO:0000250|UniProtKB:Q86925}.
CC -!- MISCELLANEOUS: [Isoform Structural polyprotein]: Produced by
CC conventional translation.
CC -!- SIMILARITY: Belongs to the alphavirus structural polyprotein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ld4";
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DR EMBL; V01403; CAA24684.1; -; Genomic_RNA.
DR EMBL; J02363; AAA96976.1; -; Genomic_RNA.
DR EMBL; M13818; AAA47485.1; -; Genomic_RNA.
DR EMBL; AB372876; BAH70330.1; -; Genomic_RNA.
DR PIR; A03916; VHWVB.
DR PIR; A25894; VHWVSB.
DR PIR; B03916; VHWVB2.
DR RefSeq; NP_062890.1; NC_001547.1. [P03316-1]
DR PDB; 1KXA; X-ray; 3.10 A; A=106-264.
DR PDB; 1KXB; X-ray; 2.90 A; A=106-264.
DR PDB; 1KXC; X-ray; 3.10 A; A=106-264.
DR PDB; 1KXD; X-ray; 3.00 A; A=106-264.
DR PDB; 1KXE; X-ray; 3.20 A; A=106-264.
DR PDB; 1KXF; X-ray; 2.38 A; A=106-264.
DR PDB; 1LD4; EM; 11.40 A; A/B/C/D=1-264, M/N/O/P=807-1245.
DR PDB; 1SVP; X-ray; 2.00 A; A/B=106-266.
DR 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.
DR PDB; 2SNV; X-ray; 2.80 A; A=114-264.
DR PDB; 2SNW; X-ray; 2.70 A; A/B=107-264.
DR PDB; 3J0F; EM; -; A/B/C/D=1-264, E/F/G/H=807-1245, I/J/K/L=329-751.
DR PDB; 3MUU; X-ray; 3.29 A; A/B/C/D/E/F=329-672, A/B/C/D/E/F=807-1192.
DR PDB; 3MUW; EM; -; A/D/E/F=807-1190, U/X/Y/Z=329-672.
DR PDBsum; 1KXA; -.
DR PDBsum; 1KXB; -.
DR PDBsum; 1KXC; -.
DR PDBsum; 1KXD; -.
DR PDBsum; 1KXE; -.
DR PDBsum; 1KXF; -.
DR PDBsum; 1LD4; -.
DR PDBsum; 1SVP; -.
DR PDBsum; 1Z8Y; -.
DR PDBsum; 2SNV; -.
DR PDBsum; 2SNW; -.
DR PDBsum; 3J0F; -.
DR PDBsum; 3MUU; -.
DR PDBsum; 3MUW; -.
DR SMR; P03316; -.
DR DIP; DIP-29032N; -.
DR DrugBank; DB03316; 1,4-Dioxane.
DR MEROPS; S03.001; -.
DR SwissPalm; P03316; -.
DR ABCD; P03316; 1 sequenced antibody.
DR GeneID; 1502155; -.
DR KEGG; vg:1502155; -.
DR EvolutionaryTrace; P03316; -.
DR Proteomes; UP000006710; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
DR GO; GO:0098029; C:icosahedral viral capsid, spike; IDA:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IDA:UniProtKB.
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:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL.
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:0061025; P:membrane fusion; IDA:CACAO.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; IMP:CACAO.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.40.2400; -; 1.
DR Gene3D; 2.60.40.3200; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.40.4310; -; 1.
DR Gene3D; 2.60.98.10; -; 3.
DR InterPro; IPR002548; Alpha_E1_glycop.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR002533; Alpha_E3_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
DR Pfam; PF01589; Alpha_E1_glycop; 1.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
DR Pfam; PF01563; Alpha_E3_glycop; 1.
DR Pfam; PF00944; Peptidase_S3; 1.
DR PRINTS; PR00798; TOGAVIRIN.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein;
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..264
FT /note="Capsid protein"
FT /id="PRO_0000041321"
FT CHAIN 265..751
FT /note="Precursor of protein E3/E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000226238"
FT CHAIN 265..328
FT /note="Assembly protein E3"
FT /id="PRO_0000041322"
FT CHAIN 329..751
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041323"
FT CHAIN 752..806
FT /note="6K protein"
FT /id="PRO_0000041324"
FT CHAIN 807..1245
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041325"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..264
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..70
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 86..115
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 100..114
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 185..195
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 221..225
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 265..279
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 890..907
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 63..100
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 146..156
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 37..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027,
FT ECO:0000269|PubMed:1944569"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027,
FT ECO:0000269|PubMed:1944569"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027,
FT ECO:0000269|PubMed:1944569"
FT SITE 189
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 222
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 264..265
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 328..329
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 751..752
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 806..807
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT LIPID 724
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:1647069"
FT LIPID 744
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8474160"
FT LIPID 745
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8474160"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 283..289
FT /evidence="ECO:0000269|PubMed:19109378"
FT DISULFID 855..920
FT /evidence="ECO:0000250"
FT DISULFID 868..900
FT /evidence="ECO:0000250"
FT DISULFID 869..902
FT /evidence="ECO:0000250"
FT DISULFID 874..884
FT /evidence="ECO:0000250"
FT DISULFID 1065..1077
FT /evidence="ECO:0000250"
FT DISULFID 1107..1182
FT /evidence="ECO:0000250"
FT DISULFID 1112..1186
FT /evidence="ECO:0000250"
FT DISULFID 1134..1176
FT /evidence="ECO:0000250"
FT VARIANT 329..331
FT /note="SVI -> RVT (in strain: AR339)"
FT VARIANT 333
FT /note="D -> G (in strain: HRLP)"
FT VARIANT 351
FT /note="V -> E (in strain: AR339 and HRLP)"
FT VARIANT 398
FT /note="K -> E (in strain: AR339)"
FT VARIANT 442
FT /note="S -> R (causes attenuation of the virus)"
FT VARIANT 447
FT /note="N -> KNGSF (in strain: ov-100)"
FT VARIANT 500
FT /note="R -> G (in strain: AR339)"
FT VARIANT 719
FT /note="K -> L (in strain: TE12)"
FT VARIANT 919
FT /note="D -> V (in strain: HRLP)"
FT MUTAGEN 141
FT /note="H->A,P: Complete loss of autocatalytic cleavage by
FT capsid protein."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 141
FT /note="H->R: No loss of autocatalytic cleavage by capsid
FT protein. No infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 147
FT /note="D->H,Y: No loss of autocatalytic cleavage by capsid
FT protein. No infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 163
FT /note="D->H: No loss of autocatalytic cleavage by capsid
FT protein. No infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 163
FT /note="D->N: No loss of autocatalytic cleavage by capsid
FT protein. Infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 215
FT /note="S->A,I: Complete loss of autocatalytic cleavage by
FT capsid protein."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 215
FT /note="S->C: 40% reduction in autocatalytic cleavage by
FT capsid protein. No infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 215
FT /note="S->T: 90% reduction in autocatalytic cleavage by
FT capsid protein. No infectious virus is produced."
FT /evidence="ECO:0000269|PubMed:2335827"
FT MUTAGEN 264
FT /note="W->F: 73% loss of cleavage by capsid protease."
FT /evidence="ECO:0000269|PubMed:9445057"
FT MUTAGEN 724
FT /note="C->A: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:1647069"
FT MUTAGEN 744..745
FT /note="CC->AA: Complete loss of infectivity."
FT MUTAGEN 744
FT /note="C->A: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:8474160"
FT MUTAGEN 745
FT /note="C->A: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:8474160"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1SVP"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2SNV"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1SVP"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1SVP"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1SVP"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2SNW"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2SNV"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2SNV"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1SVP"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 410..425
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 473..483
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 589..596
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 610..630
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 654..661
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 807..814
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 833..842
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 845..854
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 883..889
FT /evidence="ECO:0007829|PDB:3MUU"
FT TURN 894..899
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 903..905
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 907..916
FT /evidence="ECO:0007829|PDB:3MUU"
FT TURN 918..922
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 925..934
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 937..943
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 946..951
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 954..957
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 966..969
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 981..985
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1003..1005
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1008..1013
FT /evidence="ECO:0007829|PDB:3MUU"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:3MUU"
FT HELIX 1045..1050
FT /evidence="ECO:0007829|PDB:3MUU"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1066..1068
FT /evidence="ECO:0007829|PDB:3MUU"
FT TURN 1069..1072
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1073..1075
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1080..1089
FT /evidence="ECO:0007829|PDB:3MUU"
FT HELIX 1090..1092
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1102..1111
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1116..1118
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1120..1130
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1137..1140
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1144..1146
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1148..1150
FT /evidence="ECO:0007829|PDB:3MUU"
FT STRAND 1157..1163
FT /evidence="ECO:0007829|PDB:3MUU"
SQ 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
