POLS_EEEV3
ID POLS_EEEV3 Reviewed; 1240 AA.
AC P27284;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Eastern equine encephalitis virus (strain va33[ten broeck]) (EEEV) (Eastern
OS equine encephalomyelitis virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11022;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9126; Passeriformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2024496; DOI=10.1016/0042-6822(91)90618-l;
RA Weaver S.C., Scott T.W., Rico-Hesse R.;
RT "Molecular evolution of eastern equine encephalomyelitis virus in North
RT America.";
RL Virology 182:774-784(1991).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.4 ANGSTROMS) OF 1-260, RNA-BINDING
RP (CAPSID PROTEIN), AND FUNCTION (CAPSID PROTEIN).
RX PubMed=30540945; DOI=10.1016/j.celrep.2018.11.067;
RA Hasan S.S., Sun C., Kim A.S., Watanabe Y., Chen C.L., Klose T., Buda G.,
RA Crispin M., Diamond M.S., Klimstra W.B., Rossmann M.G.;
RT "Cryo-EM structures of eastern equine encephalitis virus reveal mechanisms
RT of virus disassembly and antibody neutralization.";
RL Cell Rep. 25:3136-3147.e5(2018).
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 (PubMed:30540945).
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:0000269|PubMed:30540945}.
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. Synthesized as a p62
CC precursor which is processed by furin at the cell membrane just before
CC virion budding, giving rise to E2-E1 heterodimer. The p62-E1
CC heterodimer is stable, whereas E2-E1 is unstable and dissociate at low
CC pH. p62 is processed at the last step, presumably to avoid E1 fusion
CC activation before its final export to cell surface. E2 C-terminus
CC 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 target cell and endocytosis,
CC acidification of the endosome would induce dissociation of E1/E2
CC heterodimer and concomitant trimerization of the E1 subunits. This E1
CC trimer is fusion active, and promotes release of viral nucleocapsid in
CC cytoplasm after endosome and viral membrane fusion. Efficient fusion
CC requires the presence of cholesterol and sphingolipid in the target
CC membrane. Fusion is optimal at levels of about 1 molecule of
CC 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.
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). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, 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). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, 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; M69094; AAA42980.1; -; Genomic_RNA.
DR PIR; A39992; VHWVEV.
DR PDB; 6MX4; EM; 4.40 A; C/F/I/L=1-260.
DR PDB; 6MX7; EM; 4.80 A; C/F/I/L=1-260.
DR PDBsum; 6MX4; -.
DR PDBsum; 6MX7; -.
DR SMR; P27284; -.
DR MEROPS; S03.001; -.
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: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: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; Cleavage on pair of basic residues;
KW Disulfide bond; 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;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN 1..260
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041246"
FT CHAIN 261..743
FT /note="Precursor of protein E3/E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000234317"
FT CHAIN 261..323
FT /note="Assembly protein E3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041247"
FT CHAIN 324..743
FT /note="Spike glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041248"
FT CHAIN 744..799
FT /note="6K protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041249"
FT CHAIN 800..1240
FT /note="Spike glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041250"
FT TOPO_DOM 261..682
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..758
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 802..1216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1238..1240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 111..260
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..35
FT /note="Necessary for nucleocapsid assembly and virus
FT assembly"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 36..69
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 82..112
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000269|PubMed:30540945"
FT REGION 97..111
FT /note="Ribosome-binding"
FT /evidence="ECO:0000269|PubMed:30540945"
FT REGION 261..272
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 715..735
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 883..900
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 43..50
FT /note="Supraphysiological nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 66..70
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..100
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 185
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 218
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 260..261
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 323..324
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 743..744
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 799..800
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT LIPID 706
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255"
FT LIPID 716
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 736
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 737
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 848..913
FT /evidence="ECO:0000250"
FT DISULFID 861..893
FT /evidence="ECO:0000250"
FT DISULFID 862..895
FT /evidence="ECO:0000250"
FT DISULFID 867..877
FT /evidence="ECO:0000250"
FT DISULFID 1059..1071
FT /evidence="ECO:0000250"
FT DISULFID 1101..1176
FT /evidence="ECO:0000250"
FT DISULFID 1106..1180
FT /evidence="ECO:0000250"
SQ SEQUENCE 1240 AA; 137291 MW; AEBEB1599D083045 CRC64;
MFPYPTLNYP PMAPINPMAY RDPNPPRQVA PFRPPLAAQI EDLRRSIANL TLKQRAPNPP
AGPPAKRKKP APKPKPAQAK KKRPPPPAKK QKRKPKPGKR QRMCMKLESD KTFPIMLNGQ
VNGYACVVGG RVFKPLHVEG RIDNEQLAAI KLKKASIYDL EYGDVPQCMK SDTLQYTSDK
PPGFYNWHHG AVQYENNRFT VPRGVGGKGD SGRPILDNKG RVVAIVLGGV NEGSRTALSV
VTWNQKGVTV KDTPEGSEPW SLATVMCVLA NITFPCDQPP CMPCCYEKNP HETLTMLEQN
YDSRAYDQLL DAAVKCNARR TRRDLDTHFT QYKLARPYIA DCPNCGHSRC DSPIAIEEVR
GDAHAGVIRI QTSAMFGLKT DGVDLAYMSF MNGKTQKSIK IDNLHVRTSA PCSLVSHHGY
YILAQCPPGD TVTVGFHDGP NRHTCTVAHK VEFRPVGREK YRHPPEHGVE LPCNRYTHKR
ADQGHYVEMH QPGLVADHSL LSIHSAKVKI TVPSGAQVKY YCKCPDVREG ITSSDHTTTC
TDVKQCRAYL IGNKKWVYNS GRLPRGEGDT FKGKLHVPFV PVKAKCIATL APEPLVEHKH
RTLILHLHPD HPTLLTTRSL GSDANPTRQW IERPTTVNFT VTGEGLEYTW GNHPPKRVWA
QESGEGNPHG WPHEVVVYYY NRYPLTTIIG LCTCVAIIMV SCVHPCGSFA GLRNLCITPY
KLAPNAQVPI LLALLCCIKP TRADDTLQVL NYLWNNNQNF FWMQTLIPLA ALIVCMRIVR
CLFCCGPAFL LVCGAWAAAY EHTAVMPNKV GIPYKALVER PGYAPVHLQI QLVNTSIIPS
TNLEYITCKY KTKVPSPVVK CCGATQCTSK PHPDYQCQVF TGVYPFMWGG AYCFCDTENT
QMSEAYVERS EECSIDHAKA YKVHTGTVQA MVNITYGSVS WRSADVYVNG ETPAKIGDAK
LIIGPLSSAW SPFDNKVVVY GHEVYNYDFP EYGTGKAGSF GDLQSRTSTS NDLYANTNLK
LQRPQAGIVH TPFTQAPSGF ERWKRDKGAP LNDVAPFGCS IALEPLRAEN CAVGSIPISI
DIPDAAFTRI SETPTVSDLE CKITECTYAS DFGGIATLPT NPVKQETVQF ILHQVLQLLK
RMTSPLLRAG SFTFHFSTAN IHPAFKLQVC TSGVTCKGDC KPPKDHIVDY PAQHTESFTS
AISATAWSWL KVLVGGTSAF IVLGLIATAV VALVLFFHRH
