POLS_WEEV
ID POLS_WEEV Reviewed; 1236 AA.
AC P13897; Q88696; Q88697; Q88698; Q88699; Q88700;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Western equine encephalitis virus (WEEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11039;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=7164; Anopheles.
OH NCBI_TaxID=7177; Culex tarsalis (Encephalitis mosquito).
OH NCBI_TaxID=30427; Haemorhous mexicanus (House finch) (Carpodacus mexicanus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH NCBI_TaxID=48849; Passer domesticus (House sparrow) (Fringilla domestica).
OH NCBI_TaxID=34999; Thamnophis.
OH NCBI_TaxID=37591; Urocitellus richardsonii (Richardson's ground squirrel) (Spermophilus richardsonii).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=BFS1703;
RX PubMed=3413072; DOI=10.1073/pnas.85.16.5997;
RA Hahn C.S., Lustig S., Strauss E.G., Strauss J.H.;
RT "Western equine encephalitis virus is a recombinant virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5997-6001(1988).
RN [2]
RP PROTEIN SEQUENCE OF 320-385 AND 798-862.
RX PubMed=6087344; DOI=10.1073/pnas.81.15.4702;
RA Bell J.R., Kinney R.M., Trent D.W., Strauss E.G., Strauss J.H.;
RT "An evolutionary tree relating eight alphaviruses, based on amino-terminal
RT sequences of their glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4702-4706(1984).
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 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:P03316}.
CC -!- FUNCTION: Protein 6K: Acts as a viroporin that participates in virus
CC glycoprotein processing, cell permeabilization and budding of viral
CC particles. Disrupts the calcium homeostasis of the cell, probably at
CC the endoplasmic reticulum level resulting in the increased levels of
CC cytoplasmic calcium. Because of its lipophilic properties, the 6K
CC protein is postulated to influence the selection of lipids that
CC interact with the transmembrane domains of the glycoproteins, which, in
CC turn, affects the deformability of the bilayer required for the extreme
CC curvature that occurs as budding proceeds. Present in low amount in
CC virions, about 3% compared to viral glycoproteins.
CC {ECO:0000250|UniProtKB:P03316}.
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. {ECO:0000250|UniProtKB:P03316}.
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). {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; J03854; AAA42999.1; -; Genomic_RNA.
DR PIR; A35587; VHWVWE.
DR SMR; P13897; -.
DR MEROPS; S03.001; -.
DR ABCD; P13897; 7 sequenced antibodies.
DR Proteomes; UP000007630; 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: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 Capsid protein; Cleavage on pair of basic residues;
KW Direct protein sequencing; 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;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN 1..259
FT /note="Capsid protein"
FT /id="PRO_0000041327"
FT CHAIN 260..742
FT /note="Precursor of protein E3/E2"
FT /id="PRO_0000234326"
FT CHAIN 260..319
FT /note="Assembly protein E3"
FT /id="PRO_0000041328"
FT CHAIN 320..742
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041329"
FT CHAIN 743..797
FT /note="6K protein"
FT /id="PRO_0000041330"
FT CHAIN 798..1236
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000041331"
FT TOPO_DOM 260..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..1205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1206..1226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1227..1236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 110..259
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..36
FT /note="Necessary for nucleocapsid assembly and virus
FT assembly"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 37..70
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 44..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..111
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 96..110
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 260..271
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 717..737
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 881..898
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT MOTIF 44..51
FT /note="Supraphysiological nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 67..70
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 69..99
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 184
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 217
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:Q86925"
FT SITE 259..260
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 319..320
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 742..743
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 797..798
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT LIPID 715
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 735
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 CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 846..911
FT /evidence="ECO:0000250"
FT DISULFID 859..891
FT /evidence="ECO:0000250"
FT DISULFID 860..893
FT /evidence="ECO:0000250"
FT DISULFID 865..875
FT /evidence="ECO:0000250"
FT DISULFID 1056..1068
FT /evidence="ECO:0000250"
FT DISULFID 1098..1173
FT /evidence="ECO:0000250"
FT DISULFID 1103..1177
FT /evidence="ECO:0000250"
FT DISULFID 1125..1167
FT /evidence="ECO:0000250"
FT CONFLICT 361
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="H -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1236 AA; 136082 MW; 0756DB0B0A1CCA96 CRC64;
MFPYPQLNFP PVYPTNPMAY RDPNPPRCRW RPFRPPLAAQ IEDLRRSIAN LTFKQRSPNP
PPGPPPKKKK SAPKPKPTQP KKKKQQAKKT KRKPKPGKRQ RMCMKLESDK TFPIMLNGQV
NGYACVVGGR LMKPLHVEGK IDNEQLAAVK LKKASMYDLE YGDVPQNMKS DTLQYTSDKP
PGFYNWHHGA VQYENGRFTV PRGVGGKGDS GRPILDNRGR VVAIVLGGAN EGTRTALSVV
TWNQKGVTIK DTPEGSEPWS LVTALCVLSN VTFPCDKPPV CYSLAPERTL DVLEENVDNP
NYDTLLENVL KCPSRRPKRS ITDDFTLTSP YLGFCPYCRH SAPCFSPIKI ENVWDESDDG
SIRIQVSAQF GYNQAGTADV TKFRYMSFDH DHDIKEDSMD KIAISTSGPC RRLGHKGYFL
LAQCPPGDSV TVSITSGASE NSCTVEKKIR RKFVGREEYL FPPVHGKLVK CHVYDHLKET
SAGYITMHRP GPHAYKSYLE EASGEVYIKP PSGKNVTYEC KCGDYSTGIV STRTKMNGCT
KAKQCIAYKS DQTKWVFNSP DLIRHTDHSV QGKLHIPFRL TPTVCPVPLA HTPTVTKWFK
GITLHLTATR PTLLTTRKLG LRADATAEWI TGTTSRNFSV GREGLEYVWG NHEPVRVWAQ
ESAPGDPHGW PHEIIIHYYH RHPVYTVIVL CGVALAILVG TASSAACIAK ARRDCLTPYA
LAPNATVPTA LAVLCCIRPT NAETFGETLN HLWFNNQPFL WAQLCIPLAA LVILFRCFSC
CMPFLLVAGV CLGKVDAFEH ATTVPNVPGI PYKALVERAG YAPLNLEITV VSSELTPSTN
KEYVTCRFHT VIPSPQVKCC GSLECKASSK ADYTCRVFGG VYPFMWGGAQ CFCDSENTQL
SEAYVEFAPD CTIDHAVALK VHTAALKVGL RIVYGNTTAH LDTFVNGVTP GSSRDLKVIA
GPISAAFSPF DHKVVIRKGL VYNYDFPEYG AMKPGAFGDI QASSLDATDI VARTDIRLLK
PSVKNIHVPY TQAVSGYEMW KNNSGRPLQE TAPFGCKIEV EPLRASNCAY GHIPISIDIP
DAAFVRSSES PTILEVSCTV ADCIYSADFG GSLTLQYKAD REGHCPVHSH STTAVLKEAT
THVTAVGSIT LHFSTSSPQA NFIVSLCGKK TTCNAECKPP ADHIIGEPHK VDQEFQAAVS
KTSWNWLLAL FGGASSLIVV GLIVLVCSSM LINTRR
