POLS_EEVV3
ID POLS_EEVV3 Reviewed; 1255 AA.
AC P36329;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 3880) (VEEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=36382;
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 [GENOMIC RNA].
RX PubMed=1448915; DOI=10.1016/0042-6822(92)90232-e;
RA Kinney R.M., Tsuchiya K.R., Sneider J.M., Trent D.W.;
RT "Genetic evidence that epizootic Venezuelan equine encephalitis (VEE)
RT viruses may have evolved from enzootic VEE subtype I-D virus.";
RL Virology 191:569-580(1992).
RN [2]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=16427678; DOI=10.1016/j.virol.2005.11.051;
RA Kolokoltsov A.A., Fleming E.H., Davey R.A.;
RT "Venezuelan equine encephalitis virus entry mechanism requires late
RT endosome formation and resists cell membrane cholesterol depletion.";
RL Virology 347:333-342(2006).
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 (PubMed:16427678). 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 (By similarity). 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). Inhibits host transcription (By similarity). Forms a
CC tetrameric complex with XPO1/CRM1 and the nuclear import receptor
CC importin (By similarity). This complex blocks the central channel of
CC host nuclear pores thereby inhibiting the receptor-mediated nuclear
CC transport and thus the host mRNA and rRNA transcription (By
CC similarity). The inhibition of transcription is linked to a cytopathic
CC effect on the host cell (By similarity). {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592,
CC ECO:0000250|UniProtKB:P27284, ECO:0000269|PubMed:16427678}.
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. Spike at virion
CC surface are constituted of three E2-E1 heterodimers (By similarity).
CC After target cell attachment and endocytosis, E1 change conformation to
CC form homotrimers (By similarity). Interacts with 6K protein (By
CC similarity). Interacts with host LDLRAD3; this interaction mediates
CC 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; L00930; AAC19325.1; -; Genomic_RNA.
DR PIR; D44213; D44213.
DR SMR; P36329; -.
DR MEROPS; S03.001; -.
DR Proteomes; UP000008299; 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: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 3: Inferred from homology;
KW Capsid protein; 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_0000041251"
FT CHAIN 276..757
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000234318"
FT CHAIN 276..334
FT /note="Assembly protein E3"
FT /id="PRO_0000041252"
FT CHAIN 335..757
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041253"
FT CHAIN 758..813
FT /note="6K protein"
FT /id="PRO_0000041254"
FT CHAIN 814..1255
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041255"
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
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 816..1225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1226..1246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1247..1255
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 44..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 730..750
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 897..914
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 334..335
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 757..758
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 813..814
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 47
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
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 947
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 862..927
FT /evidence="ECO:0000250"
FT DISULFID 875..907
FT /evidence="ECO:0000250"
FT DISULFID 876..909
FT /evidence="ECO:0000250"
FT DISULFID 881..891
FT /evidence="ECO:0000250"
FT DISULFID 1072..1084
FT /evidence="ECO:0000250"
FT DISULFID 1114..1189
FT /evidence="ECO:0000250"
FT DISULFID 1119..1193
FT /evidence="ECO:0000250"
FT DISULFID 1141..1183
FT /evidence="ECO:0000250"
SQ SEQUENCE 1255 AA; 138298 MW; 7D730E17CAECA310 CRC64;
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF KQRREAPPEG
PPAKKPKREA PQKQKGGGQG 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 KEYKLTRPYM ARCIRCAVGS
CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIEE IPLHQVSLHT
SRPCHIVDGH GYFLLARCPA GDSITMEFKK DAVTHSCSVP YEVKFNPVGR ELYTHPPEHG
AEQACQVYAH DAQNRGAYVE MHLPGSEVDS SLVSLSGSSV TVTPPAGTSA LVECECGGTK
ISETINTAKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLT TRQLADEPHY THELISEPVV RNFSVTEKGW
EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IVTVSIAAST
WLLCKSRVSC LTPYRLTPNA RMPLCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
IPLAALIVVT RLLRCVCCVV PFLVVAGAAG AGAYEHATTM PSQAGIPYNT IVNRAGYAPL
PISITPTKIK LIPTVNLEYV TCHYKTGMDS PAIKCCGSQE CTPTYRPDEQ CKVFTGVYPF
MWGGAYCFCD TENTQVSKAY VMKSDDCLAD HAEAYKAHTA SVQAFLNITV GEHSIVTTVY
VNGETPVNFN GVKLTAGPLS TAWTPFDRKI VQYAGEIYNY DFPEYGAGQP GAFGDIQSRT
VSSSDLYANT NLVLQRPKAG AIHVPYTQAP SGFEQWKKDK APSLKFTAPF GCEIYTNPIR
AENCAVGSIP LAFDIPDALF TRVSETPTLS AAECTLNECV YSSDFGGIAT VKYSASKSGK
CAVHVPSGTA TLKEAAIELA EQGSATIHFS TANIHPEFRL QICTSYVTCK GDCHPPKDHI
VTHPQYHAQT FTAAVSKTAW TWLTSLLGGS AVIIIIGLVL ATIVAMYVLT NQKHN
