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 04-NOV-2026, entry version 191. 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; Alphavirus sindbis. 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 E1 (6K PROTEIN), AND INTERACTION WITH SPIKE GLYCOPROTEIN E2 RP (6K 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 (CAPSID 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 FUNCTION (PROTEIN 6K), SUBCELLULAR LOCATION (PROTEIN 6K), AND ACTIVITY RP REGULATION (PROTEIN 6K). RX PubMed=36191050; DOI=10.1371/journal.ppat.1010892; RA Elmasri Z., Negi V., Kuhn R.J., Jose J.; RT "Requirement of a functional ion channel for Sindbis virus glycoprotein RT transport, CPV-II formation, and efficient virus budding."; RL PLoS Pathog. 18:e1010892-e1010892(2022). RN [31] RP FUNCTION (SPIKE GLYCOPROTEIN E1), INTERACTION WITH HOST VLDLR AND RP LRP8/APOER2 (SPIKE GLYCOPROTEIN E1), FUNCTION (SPIKE GLYCOPROTEIN E2), AND RP INTERACTION WITH HOST VLDLR AND LRP8/APOER2 (SPIKE GLYCOPROTEIN E2). RC STRAIN=DAK Ar Mg812; 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 [32] {ECO:0007744|PDB:2SNV} RP X-RAY CRYSTALLOGRAPHY, AND ACTIVE SITE. RX PubMed=8450538; DOI=10.1006/jmbi.1993.1139; RA Tong L., Wengler G., Rossmann M.G.; RT "Refined structure of Sindbis virus core protein and comparison with other RT chymotrypsin-like serine proteinase structures."; RL J. Mol. Biol. 230:228-247(1993). RN [33] {ECO:0007744|PDB:1KXA, ECO:0007744|PDB:1KXB, ECO:0007744|PDB:1KXC, ECO:0007744|PDB:1KXD, ECO:0007744|PDB:1KXE, ECO:0007744|PDB:1KXF, ECO:0007744|PDB:2SNW} RP X-RAY CRYSTALLOGRAPHY. 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 [34] 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). RN [35] {ECO:0007744|PDB:1SVP} RP X-RAY CRYSTALLOGRAPHY, MUTAGENESIS OF 108-LEU--LEU-110 AND RP 109-LYS--GLU-111, AND SUBUNIT (CAPSID PROTEIN). RX PubMed=8736552; DOI=10.1016/s0969-2126(96)00059-7; RA Lee S., Owen K.E., Choi H.K., Lee H., Lu G., Wengler G., Brown D.T., RA Rossmann M.G., Kuhn R.J.; RT "Identification of a protein binding site on the surface of the alphavirus RT nucleocapsid and its implication in virus assembly."; RL Structure 4:531-541(1996). RN [36] {ECO:0007744|PDB:1LD4} RP STRUCTURE BY ELECTRON MICROSCOPY AND 807-1245, DISULFIDE BONDS, COILED RP COILS, FUNCTION (CAPSID PROTEIN), GLYCOSYLATION AT ASN-524; ASN-646; RP ASN-945 AND ASN-1051, AND SUBUNIT (CAPSID PROTEIN). RX PubMed=12388725; DOI=10.1128/jvi.76.22.11645-11658.2002; RA Zhang W., Mukhopadhyay S., Pletnev S.V., Baker T.S., Kuhn R.J., RA Rossmann M.G.; RT "Placement of the structural proteins in Sindbis virus."; RL J. Virol. 76:11645-11658(2002). RN [37] {ECO:0007744|PDB:1Z8Y} RP STRUCTURE BY ELECTRON MICROSCOPY; 691-726; 807-1096; 1101-1189 AND RP 1215-1245, DISULFIDE BONDS, FUNCTION (CAPSID PROTEIN), INTERACTION WITH THE RP CAPSID PROTEIN (SPIKE GLYCOPROTEIN E2), INTERACTION WITH SPIKE GLYCOPROTEIN RP E2 (CAPSID PROTEIN), AND TOPOLOGY. RX PubMed=16407066; DOI=10.1016/j.str.2005.07.025; RA Mukhopadhyay S., Zhang W., Gabler S., Chipman P.R., Strauss E.G., RA Strauss J.H., Baker T.S., Kuhn R.J., Rossmann M.G.; RT "Mapping the structure and function of the E1 and E2 glycoproteins in RT alphaviruses."; RL Structure 14:63-73(2006). RN [38] {ECO:0007744|PDB:3MUU, ECO:0007744|PDB:3MUW} RP X-RAY CRYSTALLOGRAPHY AND 807-1192, DISULFIDE BONDS, AND FUNCTION (SPIKE RP GLYCOPROTEIN E2). RX PubMed=21124457; DOI=10.1038/nature09546; RA Li L., Jose J., Xiang Y., Kuhn R.J., Rossmann M.G.; RT "Structural changes of envelope proteins during alphavirus fusion."; RL Nature 468:705-708(2010). RN [39] {ECO:0007744|PDB:3J0F} RP STRUCTURE BY ELECTRON MICROSCOPY; 329-751 AND 807-1245, FUNCTION (CAPSID RP PROTEIN), INTERACTION WITH THE CAPSID PROTEIN (SPIKE GLYCOPROTEIN E2), AND RP INTERACTION WITH SPIKE GLYCOPROTEIN E2 (CAPSID PROTEIN). RX PubMed=22001018; DOI=10.1016/j.jmb.2011.09.045; RA Tang J., Jose J., Chipman P., Zhang W., Kuhn R.J., Baker T.S.; RT "Molecular links between the E2 envelope glycoprotein and nucleocapsid core RT in Sindbis virus."; RL J. Mol. Biol. 414:442-459(2011). 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:12388725, PubMed:16407066, PubMed:22001018, CC PubMed:8415660). The capsid protein binds to the viral RNA genome at a CC site adjacent to a ribosome binding site for viral genome translation CC following genome release (By similarity). Possesses a protease activity CC that results in its autocatalytic cleavage from the nascent structural CC protein (PubMed:1944569). Following its self-cleavage, the capsid CC protein transiently associates with ribosomes, and within several CC minutes the protein binds to viral RNA and rapidly assembles into CC icosahedric core particles (By similarity). The resulting nucleocapsid CC eventually associates with the cytoplasmic domain of the spike CC glycoprotein E2 at the cell membrane, leading to budding and formation CC of mature virions (PubMed:9143274). In case of infection, new virions CC attach to target cells and after clathrin-mediated endocytosis their CC membrane fuses with the host endosomal membrane (PubMed:9707418). This CC leads to the release of the nucleocapsid into the cytoplasm, followed CC by an uncoating event necessary for the genomic RNA to become CC accessible (By similarity). The uncoating might be triggered by the CC interaction of capsid proteins with ribosomes (PubMed:3656418). Binding CC of ribosomes would release the genomic RNA since the same region is CC genomic RNA-binding and ribosome-binding (By similarity). 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 (PubMed:33673546). {ECO:0000250|UniProtKB:P03315, CC ECO:0000250|UniProtKB:P27284, ECO:0000269|PubMed:12388725, CC ECO:0000269|PubMed:16407066, ECO:0000269|PubMed:1944569, CC ECO:0000269|PubMed:22001018, ECO:0000269|PubMed:33673546, CC ECO:0000269|PubMed:3656418, ECO:0000269|PubMed:8415660, CC ECO:0000269|PubMed:9143274, ECO:0000269|PubMed:9707418}. CC -!- FUNCTION: [Assembly protein E3]: Provides the signal sequence for the CC translocation of the precursor of protein E3/E2 to the host endoplasmic CC reticulum. Furin-cleaved E3 remains associated with spike glycoprotein CC E1 and mediates pH protection of the latter during the transport via CC the secretory pathway. After virion release from the host cell, the CC assembly protein E3 is gradually released in the extracellular space. CC {ECO:0000250|UniProtKB:P03315}. CC -!- FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to CC target host cell, by binding to the cell receptors VLDLR or LRP8/APOER2 CC (PubMed:34929721). Synthesized as a pE2 precursor which is processed by CC furin at the cell membrane just before virion budding, giving rise to CC E2-E1 heterodimer. The pE2-E1 heterodimer is stable, whereas E2-E1 is CC unstable and dissociate at low pH. pE2 is processed at the last step, CC presumably to avoid E1 fusion activation before its final export to CC cell surface. E2 C-terminus contains a transitory transmembrane that CC would be disrupted by palmitoylation, resulting in reorientation of the CC C-terminal tail from lumenal to cytoplasmic side. This step is critical CC since E2 C-terminus is involved in budding by interacting with capsid CC proteins. This release of E2 C-terminus in cytoplasm occurs lately in CC protein export, and precludes premature assembly of particles at the CC endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315, CC ECO:0000269|PubMed:8995682}. CC -!- FUNCTION: [6K protein]: Acts as a viroporin that participates in virus CC glycoprotein processing and transport to the plasma membrane, cell CC permeabilization and budding of viral particles (PubMed:12424249, CC PubMed:36191050, PubMed:8892914). Disrupts the calcium homeostasis of CC the cell, probably at the endoplasmic reticulum level resulting in the CC increased levels of cytoplasmic calcium (PubMed:17483865). Because of CC its lipophilic properties, the 6K protein is postulated to influence CC the selection of lipids that interact with the transmembrane domains of CC the glycoproteins, which, in turn, affects the deformability of the CC bilayer required for the extreme curvature that occurs as budding CC proceeds. Present in low amount in virions, about 3% compared to viral CC glycoproteins (By similarity). {ECO:0000250|UniProtKB:P03315, CC ECO:0000269|PubMed:12424249, ECO:0000269|PubMed:17483865, CC ECO:0000269|PubMed:36191050, ECO:0000269|PubMed:8892914}. 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 (PubMed:12573591, PubMed:21124457). After virus attachment to CC target cell via host VLDLR or LRP8/APOER2 and endocytosis, CC acidification of the endosome induces dissociation of E1/E2 heterodimer CC and concomitant trimerization of the E1 subunits (PubMed:21124457, CC PubMed:34929721). This E1 trimer is fusion active, and promotes release CC of viral nucleocapsid in cytoplasm after endosome and viral membrane CC fusion (PubMed:21124457). Efficient fusion requires the presence of CC cholesterol and sphingolipid in the target membrane (PubMed:10482600). CC {ECO:0000269|PubMed:10482600, ECO:0000269|PubMed:12573591, CC ECO:0000269|PubMed:21124457, 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:0000250|UniProtKB:P03315}; CC -!- ACTIVITY REGULATION: The channel activity is blocked by 5-N, N- CC Hexamethylene amiloride. {ECO:0000269|PubMed:36191050}. CC -!- SUBUNIT: [Capsid protein]: Homomultimer (PubMed:12388725, CC PubMed:8736552). Interacts with host karyopherin KPNA4; this CC interaction allows the nuclear import of the viral capsid protein (By CC similarity). Interacts with spike glycoprotein E2 (PubMed:22001018, CC PubMed:9143274). Interacts with host IRAK1; the interaction leads to CC inhibition of IRAK1-dependent signaling (PubMed:33673546). CC {ECO:0000250|UniProtKB:Q8JUX5, ECO:0000269|PubMed:12388725, CC ECO:0000269|PubMed:22001018, ECO:0000269|PubMed:33673546, CC ECO:0000269|PubMed:8736552, ECO:0000269|PubMed:9143274}. 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 a trimer of E2-E1 CC heterodimers (PubMed:8623521). After target cell attachment and CC endocytosis, E1 change conformation to form homotrimers (By CC similarity). E2-E1 heterodimers interact with host VLDLR or LRP8/APOER2 CC to mediate viral entry (PubMed:34929721). Interacts with 6K protein CC (PubMed:8892914). {ECO:0000250|UniProtKB:Q8JUX5, CC ECO:0000269|PubMed:34929721, ECO:0000269|PubMed:8623521, CC ECO:0000269|PubMed:8892914}. CC -!- SUBUNIT: [Spike glycoprotein E2]: Interacts with spike glycoprotein E1 CC (PubMed:8623521). Processing of the precursor of protein E3/E2 into E2 CC and E3 results in a heterodimer of the spike glycoproteins E2 and E1 CC (PubMed:8623521). Spike at virion surface are constituted of a trimer CC of E2-E1 heterodimers (PubMed:8623521). E2-E1 heterodimers interact CC with host VLDLR or LRP8/APOER2 to mediate viral entry CC (PubMed:34929721). Interacts with 6K protein (PubMed:8892914). CC Interacts with the capsid protein (PubMed:16407066, PubMed:22001018). CC {ECO:0000269|PubMed:16407066, ECO:0000269|PubMed:22001018, CC ECO:0000269|PubMed:34929721, ECO:0000269|PubMed:8623521, CC ECO:0000269|PubMed:8892914}. CC -!- SUBUNIT: [6K protein]: Oligomer (By similarity). Interacts with spike CC glycoprotein E1 (PubMed:8892914). Interacts with spike glycoprotein E2 CC (PubMed:8892914). {ECO:0000250|UniProtKB:Q5XXP3, CC 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}. Host Golgi apparatus CC {ECO:0000269|PubMed:36191050}. Host Golgi apparatus, host trans-Golgi CC network. Host endoplasmic reticulum {ECO:0000269|PubMed:36191050}. 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.org/Info_Page.php?VDB=1ld4"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P03316; -. DR MDposit; P03316; -. DR SMR; P03316; -. DR DIP; DIP-29032N; -. DR IntAct; P03316; 1. DR DrugBank; DB03316; 1,4-Dioxane. DR MEROPS; S03.001; -. DR GlyCosmos; P03316; 5 sites, No reported glycans. DR SwissPalm; P03316; -. DR ABCD; P03316; 1 sequenced antibody. DR GeneID; 1502155; -. DR KEGG; vg:1502155; -. DR EvolutionaryTrace; P03316; -. DR PRO; PR:P03316; -. DR Proteomes; UP000006710; Segment. DR GO; GO:0030430; C:host cell cytoplasm; EXP:UniProtKB. DR GO; GO:0044165; C:host cell endoplasmic reticulum; EXP:UniProtKB. DR GO; GO:0044177; C:host cell Golgi apparatus; EXP:UniProtKB. DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB. 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: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; EXP:UniProtKB. DR GO; GO:0015267; F:channel activity; IEA:UniProtKB-KW. 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:0098670; P:entry receptor-mediated virion attachment to 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:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039722; P:symbiont-mediated suppression of host toll-like receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IMP:CACAO. DR DisProt; DP03350; -. DR FunFam; 2.40.10.10:FF:000075; Structural polyprotein; 1. DR Gene3D; 1.10.287.2230; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1. DR Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1. DR Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1. DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. 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; 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; SSF81296; E set domains; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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; Coiled coil; 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 endoplasmic reticulum; KW Host Golgi apparatus; Host membrane; Host nucleus; Host-virus interaction; KW Hydrolase; Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate; KW Protease; Reference proteome; Ribosomal frameshifting; RNA-binding; KW Serine protease; T=4 icosahedral capsid protein; Transmembrane; KW Transmembrane helix; Transport; Viral attachment to host cell; KW Viral attachment to host entry receptor; Viral envelope protein; KW Viral ion channel; Viral penetration into host cytoplasm; Virion; KW Virus endocytosis by host; 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 TOPO_DOM 329..690 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 691..718 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:16407066" FT TOPO_DOM 719..751 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TOPO_DOM 752..763 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 764..784 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 785 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 786..806 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 807..1214 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1215..1239 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:16407066" FT TOPO_DOM 1240..1245 FT /note="Cytoplasmic" 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 157..162 FT /note="Interaction with spike glycoprotein E2" FT /evidence="ECO:0000269|PubMed:22001018" 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 249..253 FT /note="Interaction with spike glycoprotein E2" FT /evidence="ECO:0000269|PubMed:22001018" 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 719..723 FT /note="Interaction with the capsid protein" FT /evidence="ECO:0000269|PubMed:22001018" FT REGION 890..907 FT /note="E1 fusion peptide loop" FT /evidence="ECO:0000250|UniProtKB:Q8JUX5" FT COILED 682..730 FT /evidence="ECO:0000269|PubMed:12388725" FT COILED 1196..1245 FT /evidence="ECO:0000269|PubMed:12388725" 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 38..49 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 67..106 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, ECO:0000269|PubMed:8450538" FT ACT_SITE 163 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027, FT ECO:0000269|PubMed:1944569, ECO:0000269|PubMed:8450538" FT ACT_SITE 215 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027, FT ECO:0000269|PubMed:1944569, ECO:0000269|PubMed:8450538" 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|UniProtKB:P03315" FT SITE 751..752 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P03315" FT SITE 806..807 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P03315" 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:0000269|PubMed:12388725" FT CARBOHYD 646 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:12388725" FT CARBOHYD 945 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:12388725" FT CARBOHYD 1051 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:12388725" FT DISULFID 283..289 FT /evidence="ECO:0000269|PubMed:19109378" FT DISULFID 480..594 FT /evidence="ECO:0000250|UniProtKB:Q5XXP3" FT DISULFID 529..554 FT /evidence="ECO:0000250|UniProtKB:Q5XXP3" FT DISULFID 531..548 FT /evidence="ECO:0000250|UniProtKB:Q5XXP3" FT DISULFID 724..745 FT /evidence="ECO:0000250|UniProtKB:Q5XXP3" FT DISULFID 855..920 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 868..900 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 869..902 FT /evidence="ECO:0000269|PubMed:12388725, FT ECO:0000269|PubMed:16407066, ECO:0000269|PubMed:21124457, FT ECO:0007744|PDB:1LD4, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 874..884 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 1065..1077 FT /evidence="ECO:0000269|PubMed:12388725, FT ECO:0000269|PubMed:16407066, ECO:0000269|PubMed:21124457, FT ECO:0007744|PDB:1LD4, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 1107..1182 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 1112..1186 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" FT DISULFID 1134..1176 FT /evidence="ECO:0000269|PubMed:16407066, FT ECO:0000269|PubMed:21124457, ECO:0007744|PDB:1Z8Y, FT ECO:0007744|PDB:3MUU" 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 108..110 FT /note="LKL->DKK: 97% loss of replication and loss of FT nucleocapsid accumulation." FT /evidence="ECO:0000269|PubMed:8736552" FT MUTAGEN 108..110 FT /note="LKL->DKN: 95% loss of replication and loss of FT nucleocapsid accumulation." FT /evidence="ECO:0000269|PubMed:8736552" FT MUTAGEN 108..110 FT /note="LKL->NKD: 80% loss of replication and loss of FT nucleocapsid accumulation." FT /evidence="ECO:0000269|PubMed:8736552" FT MUTAGEN 108..110 FT /note="LKL->NKK: 80% loss of replication and loss of FT nucleocapsid accumulation." FT /evidence="ECO:0000269|PubMed:8736552" FT MUTAGEN 109..111 FT /note="KLE->ALA: No effect on replication and 40% loss of FT nucleocapsid accumulation." FT /evidence="ECO:0000269|PubMed:8736552" 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 865..867 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..1069 FT /evidence="ECO:0007829|PDB:3MUU" FT STRAND 1072..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 //