POLSF_SINDV
ID POLSF_SINDV Reviewed; 821 AA.
AC P0DOK0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Frameshifted 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=Protein TF;
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=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 [2]
RP SUBCELLULAR LOCATION (PRECURSOR OF PROTEIN E3/E2), AND SUBCELLULAR LOCATION
RP (SPIKE GLYCOPROTEIN E2).
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION (CAPSID PROTEIN), CATALYTIC ACTIVITY (CAPSID PROTEIN), AND ACTIVE
RP SITE (CAPSID 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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP FUNCTION (SPIKE GLYCOPROTEIN E1).
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 [14]
RP FUNCTION (SPIKE GLYCOPROTEIN E1), AND SUBUNIT.
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 [15]
RP FUNCTION (ASSEMBLY PROTEIN E3), AND 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 [16]
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 [17]
RP FUNCTION (PROTEIN TF), AND SUBCELLULAR LOCATION (PROTEIN TF).
RX PubMed=23720714; DOI=10.1128/jvi.00449-13;
RA Snyder J.E., Kulcsar K.A., Schultz K.L., Riley C.P., Neary J.T., Marr S.,
RA Jose J., Griffin D.E., Kuhn R.J.;
RT "Functional characterization of the alphavirus TF protein.";
RL J. Virol. 87:8511-8523(2013).
RN [18]
RP FUNCTION (PROTEIN TF), PALMITOYLATION (PROTEIN TF), AND SUBCELLULAR
RP LOCATION (PROTEIN TF).
RX PubMed=27852864; DOI=10.1128/jvi.02000-16;
RA Ramsey J., Renzi E.C., Arnold R.J., Trinidad J.C., Mukhopadhyay S.;
RT "Palmitoylation of sindbis virus TF protein Regulates its plasma membrane
RT localization and subsequent incorporation into virions.";
RL J. Virol. 91:0-0(2017).
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: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 (By similarity). 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 (By
CC similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P27284,
CC ECO:0000269|PubMed:1944569, ECO:0000269|PubMed:3656418}.
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 TF]: Plays a role in viral assembly and release.
CC {ECO:0000269|PubMed:23720714}.
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 (By similarity). Interacts with host IRAK1; the interaction leads to
CC inhibition of IRAK1-dependent signaling (By similarity).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5}.
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:Q8JUX5}.
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).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5}.
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}; Multi-pass membrane protein {ECO:0000255}. Host cell
CC membrane {ECO:0000269|PubMed:875134}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000269|PubMed:875134}; Multi-pass membrane protein {ECO:0000255}.
CC Host cell membrane {ECO:0000269|PubMed:23785213,
CC ECO:0000269|PubMed:3829124}; Multi-pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Protein TF]: Host cell membrane
CC {ECO:0000269|PubMed:27852864}; Single-pass membrane protein
CC {ECO:0000255}. Virion {ECO:0000269|PubMed:23720714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Frameshifted structural polyprotein;
CC IsoId=P0DOK0-1; Sequence=Displayed;
CC Name=Structural polyprotein;
CC IsoId=P03316-1; Sequence=External;
CC -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been
CC autocleaved, an internal uncleaved signal peptide directs the remaining
CC polyprotein to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Frameshifted structural polyprotein]: Specific enzymatic
CC cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved
CC during polyprotein translation, unmasking a signal peptide at the N-
CC terminus of the precursor of E3/E2. The remaining polyprotein is then
CC targeted to the host endoplasmic reticulum, where host signal peptidase
CC cleaves it into pE2 and TF. pE2 is further processed to mature E3 and
CC E2 by host furin in trans-Golgi vesicle.
CC {ECO:0000250|UniProtKB:P03315}.
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:8432728}.
CC -!- PTM: [Protein TF]: Palmitoylated via thioester bonds.
CC {ECO:0000269|PubMed:1647069, ECO:0000269|PubMed:27852864,
CC ECO:0000269|PubMed:8474160}.
CC -!- MISCELLANEOUS: [Frameshifted structural polyprotein]: Translated from a
CC subgenomic RNA synthesized during togavirus replication. {ECO:0000305}.
CC -!- MISCELLANEOUS: The strain HRSP sequence is shown.
CC -!- MISCELLANEOUS: [Isoform Frameshifted structural polyprotein]: Produced
CC by ribosomal frameshifting.
CC -!- SIMILARITY: Belongs to the alphavirus frameshifted structural
CC polyprotein family. {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; J02363; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; YP_006491225.1; NC_001547.1. [P0DOK0-1]
DR SMR; P0DOK0; -.
DR SwissPalm; P0DOK0; -.
DR GeneID; 13165406; -.
DR KEGG; vg:13165406; -.
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; 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: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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.40.2400; -; 1.
DR Gene3D; 2.60.40.3200; -; 1.
DR Gene3D; 2.60.40.4310; -; 1.
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; 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 PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW 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; Serine protease;
KW T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW 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..821
FT /note="Frameshifted structural polyprotein"
FT /id="PRO_0000442833"
FT CHAIN 1..264
FT /note="Capsid protein"
FT /id="PRO_0000442834"
FT CHAIN 265..751
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000442835"
FT CHAIN 265..328
FT /note="Assembly protein E3"
FT /id="PRO_0000442836"
FT CHAIN 329..751
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000442837"
FT CHAIN 752..821
FT /note="Protein TF"
FT /id="PRO_0000442838"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
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 93..101
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250"
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 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 264..265
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:2335827"
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 DISULFID 283..289
FT /evidence="ECO:0000269|PubMed:19109378"
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"
SQ SEQUENCE 821 AA; 91215 MW; 1D8BEBC0886C2985 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 LPFLSGCRRL PGEGRRLRTC DHCSKCATDT V
