POLS_EEVV8
ID POLS_EEVV8 Reviewed; 1254 AA.
AC P05674;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Venezuelan equine encephalitis virus (strain TC-83) (VEEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11037;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9268; Didelphis marsupialis (Southern opossum).
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=53535; Melanoconion.
OH NCBI_TaxID=9272; Philander opossum (Gray four-eyed opossum).
OH NCBI_TaxID=10162; Proechimys.
OH NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3755750; DOI=10.1099/0022-1317-67-9-1951;
RA Johnson B.J.B., Kinney R.M., Kost C.L., Trent D.W.;
RT "Molecular determinants of alphavirus neurovirulence: nucleotide and
RT deduced protein sequence changes during attenuation of Venezuelan equine
RT encephalitis virus.";
RL J. Gen. Virol. 67:1951-1960(1986).
RN [2] {ECO:0007744|PDB:3J0C, ECO:0007744|PDB:3J0G}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF 276-334.
RX PubMed=21829169; DOI=10.1038/emboj.2011.261;
RA Zhang R., Hryc C.F., Cong Y., Liu X., Jakana J., Gorchakov R., Baker M.L.,
RA Weaver S.C., Chiu W.;
RT "4.4 A cryo-EM structure of an enveloped alphavirus Venezuelan equine
RT encephalitis virus.";
RL EMBO J. 30:3854-3863(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 (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 (By similarity). Following
CC its self-cleavage, the capsid protein transiently associates with
CC ribosomes, and within several minutes the protein binds to viral RNA
CC and rapidly assembles into icosahedric core particles (By similarity).
CC The resulting nucleocapsid eventually associates with the cytoplasmic
CC domain of the spike glycoprotein E2 at the cell membrane, leading to
CC budding and formation of mature virions (By similarity). In case of
CC infection, new virions attach to target cells and after clathrin-
CC mediated endocytosis their membrane fuses with the host endosomal
CC membrane (By similarity). This leads to the release of the nucleocapsid
CC into the cytoplasm, followed by an uncoating event necessary for the
CC genomic RNA to become accessible (By similarity). The uncoating might
CC be triggered by the interaction of capsid proteins with ribosomes (By
CC similarity). Binding of ribosomes would release the genomic RNA since
CC the same region is genomic RNA-binding and ribosome-binding (By
CC similarity). Specifically inhibits interleukin-1 receptor-associated
CC kinase 1/IRAK1-dependent signaling during viral entry, representing a
CC means by which the alphaviruses may evade innate immune detection and
CC activation prior to viral gene expression (By similarity). Inhibits
CC host transcription (By similarity). Forms a tetrameric complex with
CC XPO1/CRM1 and the nuclear import receptor importin (By similarity).
CC This complex blocks the central channel of host nuclear pores thereby
CC inhibiting the receptor-mediated nuclear transport and thus the host
CC mRNA and rRNA transcription (By similarity). The inhibition of
CC transcription is linked to a cytopathic effect on the host cell (By
CC similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592,
CC ECO:0000250|UniProtKB:P27284, ECO:0000250|UniProtKB:P36329}.
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 receptor LDLRAD3. Synthesized
CC as a p62 precursor which is processed by furin at the cell membrane
CC just before virion budding, giving rise to E2-E1 heterodimer. The p62-
CC E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at
CC low pH. p62 is processed at the last step, presumably to avoid E1
CC fusion activation before its final export to cell surface. E2 C-
CC terminus contains a transitory transmembrane that would be disrupted by
CC palmitoylation, resulting in reorientation of the C-terminal tail from
CC lumenal to cytoplasmic side. This step is critical since E2 C-terminus
CC is involved in budding by interacting with capsid proteins. This
CC release of E2 C-terminus in cytoplasm occurs lately in protein export,
CC and precludes premature assembly of particles at the endoplasmic
CC reticulum membrane. {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [6K protein]: Constitutive membrane protein involved in virus
CC glycoprotein processing, cell permeabilization, and the budding of
CC viral particles. Disrupts the calcium homeostasis of the cell, probably
CC at the endoplasmic reticulum level. This leads to cytoplasmic calcium
CC elevation. Because of its lipophilic properties, the 6K protein is
CC postulated to influence the selection of lipids that interact with the
CC transmembrane domains of the glycoproteins, which, in turn, affects the
CC deformability of the bilayer required for the extreme curvature that
CC occurs as budding proceeds. Present in low amount in virions, about 3%
CC compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.
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 cell receptor LDLRAD3 and
CC endocytosis, acidification of the endosome would induce dissociation of
CC E1/E2 heterodimer and concomitant trimerization of the E1 subunits.
CC This E1 trimer is fusion active, and promotes release of viral
CC nucleocapsid in cytoplasm after endosome and viral membrane fusion.
CC Efficient fusion requires the presence of cholesterol and sphingolipid
CC in the target membrane. Fusion is optimal at levels of about 1 molecule
CC of cholesterol per 2 molecules of phospholipids, and is specific for
CC sterols containing a 3-beta-hydroxyl group.
CC {ECO:0000250|UniProtKB:P03315}.
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:P03316};
CC -!- SUBUNIT: [Capsid protein]: Part of a tetrameric complex composed of
CC host CRM1, host importin alpha/beta dimer and the viral capsid; this
CC complex blocks the receptor-mediated transport through the nuclear pore
CC (By similarity). Interacts with host phosphatase PPP1CA; this
CC interaction dephosphorylates the capsid protein, which increases its
CC ability to bind to the viral genome (By similarity). Interacts with
CC host karyopherin KPNA4; this interaction allows the nuclear import of
CC the viral capsid protein (By similarity). Interacts with spike
CC glycoprotein E2 (By similarity). Interacts with host IRAK1; the
CC interaction leads to inhibition of IRAK1-dependent signaling (By
CC similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592,
CC 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:P03315, ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P09592}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: The precursor of protein E3/E2 and E1
CC form a heterodimer shortly after synthesis (By similarity). Processing
CC of the precursor of protein E3/E2 into E2 and E3 results in a
CC heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike
CC at virion surface are constituted of three E2-E1 heterodimers (By
CC similarity). After target cell attachment and endocytosis, E1 change
CC conformation to form homotrimers (By similarity). Interacts with 6K
CC protein (By similarity). Interacts with host LDLRAD3; this interaction
CC mediates viral entry to the host cell (By similarity).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P09592}.
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). Interacts with
CC 6K protein (By similarity). Interacts with host LDLRAD3; this
CC interaction mediates viral entry to the host cell (By similarity).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P09592}.
CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1 (By
CC similarity). Interacts with spike glycoprotein E2 (By similarity).
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:P09592}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P09592}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}. Host nucleus
CC {ECO:0000250|UniProtKB:P09592}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
CC {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- 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 -!- DOMAIN: [Capsid protein]: The very N-terminus plays a role in the
CC particle assembly process (By similarity). The N-terminus also contains
CC a nuclear localization signal and a supraphysiological nuclear export
CC signal (supraNES), which is an unusually strong NES that mediates host
CC CRM1 binding in the absence of RanGTP and thus can bind CRM1, not only
CC in the nucleus, but also in the cytoplasm (By similarity). The C-
CC terminus functions as a protease during translation to cleave itself
CC from the translating structural polyprotein (By similarity).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592}.
CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC mature proteins. Capsid protein is auto-cleaved during polyprotein
CC translation, unmasking a signal peptide at the N-terminus of the
CC precursor of E3/E2. The remaining polyprotein is then targeted to the
CC host endoplasmic reticulum, where host signal peptidase cleaves it into
CC pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2
CC by host furin in trans-Golgi vesicle. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Capsid protein]: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:P09592}.
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:0000250|UniProtKB:P03315}.
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: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togavirus replication.
CC {ECO:0000250|UniProtKB:Q86925}.
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DR EMBL; X04368; CAA27883.1; -; mRNA.
DR PIR; A27871; VHWVVE.
DR PDB; 1EP5; X-ray; 2.30 A; A/B/C=119-275.
DR PDB; 1EP6; X-ray; 2.45 A; A/B/C=119-275.
DR PDB; 3J0C; EM; -; A/D/G/J=813-1254, B/E/H/K=335-757, C/F/I/L=114-275.
DR PDB; 3J0G; EM; -; M/N/O/P=276-334.
DR PDB; 7SFU; EM; 4.20 A; A/D/G/J=813-1254, B/E/H/K=335-757, C/F/I/L=114-275.
DR PDB; 7SFV; EM; 4.00 A; A/D/G/J=813-1252, B/E/H/K=335-752, C/F/I/L=117-275.
DR PDB; 7SFW; EM; 3.20 A; A/D/G/J=813-1254, B/E/H/K=335-757, C/F/I/L=1-275.
DR PDBsum; 1EP5; -.
DR PDBsum; 1EP6; -.
DR PDBsum; 3J0C; -.
DR PDBsum; 3J0G; -.
DR PDBsum; 7SFU; -.
DR PDBsum; 7SFV; -.
DR PDBsum; 7SFW; -.
DR SMR; P05674; -.
DR MEROPS; S03.001; -.
DR ABCD; P05674; 10 sequenced antibodies.
DR EvolutionaryTrace; P05674; -.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; 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; 2.60.40.350; -; 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; Disulfide bond;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
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 gene expression shutoff by virus;
KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Protease; 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..275
FT /note="Capsid protein"
FT /id="PRO_0000041256"
FT CHAIN 276..757
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000234319"
FT CHAIN 276..334
FT /note="Assembly protein E3"
FT /id="PRO_0000041257"
FT CHAIN 335..757
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041258"
FT CHAIN 758..812
FT /note="6K protein"
FT /id="PRO_0000041259"
FT CHAIN 813..1254
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041260"
FT TOPO_DOM 276..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..772
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 817..1224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..275
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..33
FT /note="Necessary for nucleocapsid assembly and virus
FT assembly"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 33..68
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 45..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..127
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 112..126
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 276..287
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 896..913
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 41..48
FT /note="Supraphysiological nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 64..68
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 57..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 200
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 233
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 275..276
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 757..758
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 812..813
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT LIPID 730
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 750
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 751
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 861..926
FT /evidence="ECO:0000250"
FT DISULFID 874..906
FT /evidence="ECO:0000250"
FT DISULFID 875..908
FT /evidence="ECO:0000250"
FT DISULFID 880..890
FT /evidence="ECO:0000250"
FT DISULFID 1071..1083
FT /evidence="ECO:0000250"
FT DISULFID 1113..1188
FT /evidence="ECO:0000250"
FT DISULFID 1118..1192
FT /evidence="ECO:0000250"
FT DISULFID 1140..1182
FT /evidence="ECO:0000250"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1EP5"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1EP5"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1EP5"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:1EP5"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1EP5"
SQ SEQUENCE 1254 AA; 138486 MW; 7615698519A529F6 CRC64;
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF KQRRDAPPEG
PSAKKPKKEA SQKQKGGGQG KKKKNQGKKK AKTGPPNPKA QNGNKKKTNK KPGKRQRMVM
KLESDKTFPI MLEGKINGYA CVVGGKLFRP MHVEGKIDND VLAALKTKKA SKYDLEYADV
PQNMRADTFK YTHEKPQGYY SWHHGAVQYE NGRFTVPKGV GAKGDSGRPI LDNQGRVVAI
VLGGVNEGSR TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAQPPICYDR
KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF NEYKLTRPYM ARCIRCAVGS
CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIKE IPLHQVSLYT
SRPCHIVDGH GYFLLARCPA GDSITMEFKK DSVRHSCSVP YEVKFNPVGR ELYTHPPEHG
VEQACQVYAH DAQNRGAYVE MHLPGSEVDS SLVSLSGSSV TVTPPDGTSA LVECECGGTK
ISETINKTKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLI TRQLADEPHY THELISEPAV RNFTVTEKGW
EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IATVSVAAST
WLFCRSRVAC LTPYRLTPNA RIPFCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
IPLAALIVVT RLLRCVCCVV PFLVMAGAAA PAYEHATTMP SQAGISYNTI VNRAGYAPLP
ISITPTKIKL IPTVNLEYVT CHYKTGMDSP AIKCCGSQEC TPTYRPDEQC KVFTGVYPFM
WGGAYCFCDT ENTQVSKAYV MKSDDCLADH AEAYKAHTAS VQAFLNITVG EHSIVTTVYV
NGETPVNFNG VKITAGPLST AWTPFDRKIV QYAGEIYNYD FPEYGAGQPG AFGDIQSRTV
SSSDLYANTN LVLQRPKAGA IHVPYTQAPS GFEQWKKDKA PSLKFTAPFG CEIYTNPIRA
ENCAVGSIPL AFDIPDALFT RVSETPTLSA AECTLNECVY SSDFGGIATV KYSASKSGKC
AVHVPSGTAT LKEAAVELTE QGSATIHFST ANIHPEFRLQ ICTSYVTCKG DCHPPKDHIV
THPQYHAQTF TAAVSKTAWT WLTSLLGGSA VIIIIGLVLA TIVAMYVLTN QKHN
