ID   POLS_SINDO              Reviewed;        1245 AA.
AC   P27285; Q00349;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   08-NOV-2023, entry version 146.
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   Sindbis virus subtype Ockelbo (strain Edsbyn 82-5) (OCKV) (Ockelbo virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus; Sindbis virus.
OX   NCBI_TaxID=31699;
OH   NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=53527; Culex.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
OH   NCBI_TaxID=177155; Streptopelia turtur.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1673813; DOI=10.1016/0042-6822(91)90616-j;
RA   Shirako Y., Niklasson B., Dalrymple J.M., Strauss E.G., Strauss J.H.;
RT   "Structure of the Ockelbo virus genome and its relationship to other
RT   Sindbis viruses.";
RL   Virology 182:753-764(1991).
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).
CC       {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316,
CC       ECO:0000250|UniProtKB:P27284}.
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:P03315};
CC   -!- SUBUNIT: [Capsid protein]: Homodimer (By similarity). Homomultimer
CC       (Probable). Interacts with host karyopherin KPNA4; this interaction
CC       allows the nuclear import of the viral capsid protein (By similarity).
CC       Interacts with spike glycoprotein E2 (By similarity). Interacts with
CC       host IRAK1; the interaction leads to inhibition of IRAK1-dependent
CC       signaling (By similarity). {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC       ECO:0000250|UniProtKB:Q8JUX5, ECO:0000305}.
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:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5}.
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:P0DOK1,
CC       ECO:0000250|UniProtKB:Q8JUX5}.
CC   -!- SUBUNIT: [Spike glycoprotein E2]: Processing of the precursor of
CC       protein E3/E2 into E2 and E3 results in a heterodimer of the spike
CC       glycoproteins E2 and E1 (By similarity). Spike at virion surface are
CC       constituted of three E2-E1 heterodimers (By similarity). Interacts with
CC       6K protein (By similarity). Interacts with host MXRA8; this interaction
CC       mediates virus entry (By similarity). {ECO:0000250|UniProtKB:P03315,
CC       ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1,
CC       ECO:0000250|UniProtKB:Q8JUX5}.
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:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P03316}. Host nucleus
CC       {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and
CC       the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.
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: [Capsid protein]: The very N-terminus also plays a role in the
CC       particle assembly process (By similarity). The N-terminus also contains
CC       a nuclear localization signal and a supra nuclear export signal
CC       (supraNES), which is an unusually strong NES that mediates host CRM1
CC       binding in the absence of RanGTP and thus can bind CRM1, not only in
CC       the nucleus, but also in the cytoplasm (By similarity). The C-terminus
CC       functions as a protease during translation to cleave itself from the
CC       translating structural polyprotein (By similarity).
CC       {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592}.
CC   -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been
CC       autocleaved, an internal uncleaved signal peptide directs the remaining
CC       polyprotein to the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: 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 (By similarity). The remaining polyprotein is then
CC       targeted to the host endoplasmic reticulum, where host signal peptidase
CC       cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to
CC       mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: [Spike glycoprotein E2]: Palmitoylated via thioester bonds. These
CC       palmitoylations may induce disruption of the C-terminus transmembrane.
CC       This would result in the reorientation of E2 C-terminus from lumenal to
CC       cytoplasmic side. {ECO: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; M69205; AAA96973.1; -; Genomic_RNA.
DR   EMBL; M69207; AAA73066.1; -; Genomic_RNA.
DR   PIR; B39991; VHWV82.
DR   PDB; 1WYK; X-ray; 2.00 A; A/B/C/D=114-264.
DR   PDBsum; 1WYK; -.
DR   SMR; P27285; -.
DR   MEROPS; S03.001; -.
DR   EvolutionaryTrace; P27285; -.
DR   Proteomes; UP000006561; 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:0016020; C: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: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; 1.10.287.2230; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1.
DR   Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1.
DR   Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; SSF81296; E set domains; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host cytoplasm; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Protease; RNA-binding; Serine protease; T=4 icosahedral capsid protein;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..264
FT                   /note="Capsid protein"
FT                   /id="PRO_0000041316"
FT   CHAIN           265..751
FT                   /note="Precursor of protein E3/E2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000226240"
FT   CHAIN           265..328
FT                   /note="Assembly protein E3"
FT                   /id="PRO_0000041317"
FT   CHAIN           329..751
FT                   /note="Spike glycoprotein E2"
FT                   /id="PRO_0000041318"
FT   CHAIN           752..806
FT                   /note="6K protein"
FT                   /id="PRO_0000041319"
FT   CHAIN           807..1245
FT                   /note="Spike glycoprotein E1"
FT                   /id="PRO_0000041320"
FT   TRANSMEM        696..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        728..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        768..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        786..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1216..1234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..264
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..70
FT                   /note="Host transcription inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   REGION          86..115
FT                   /note="Binding to the viral RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P27284"
FT   REGION          100..114
FT                   /note="Ribosome-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P27284"
FT   REGION          185..195
FT                   /note="Dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT   REGION          221..225
FT                   /note="Dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT   REGION          265..279
FT                   /note="Functions as an uncleaved signal peptide for the
FT                   precursor of protein E3/E2"
FT                   /evidence="ECO:0000250|UniProtKB:P03315"
FT   REGION          890..907
FT                   /note="E1 fusion peptide loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT   MOTIF           63..100
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   MOTIF           146..156
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09592"
FT   COMPBIAS        37..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..103
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT   SITE            189
FT                   /note="Involved in dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q86925"
FT   SITE            222
FT                   /note="Involved in dimerization of the capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q86925"
FT   SITE            264..265
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03315"
FT   SITE            328..329
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   SITE            751..752
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   SITE            806..807
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   LIPID           724
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           744
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           745
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        945
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1051
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        855..920
FT                   /evidence="ECO:0000250"
FT   DISULFID        868..900
FT                   /evidence="ECO:0000250"
FT   DISULFID        869..902
FT                   /evidence="ECO:0000250"
FT   DISULFID        874..884
FT                   /evidence="ECO:0000250"
FT   DISULFID        1065..1077
FT                   /evidence="ECO:0000250"
FT   DISULFID        1107..1182
FT                   /evidence="ECO:0000250"
FT   DISULFID        1112..1186
FT                   /evidence="ECO:0000250"
FT   DISULFID        1134..1176
FT                   /evidence="ECO:0000250"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          125..132
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   TURN            171..176
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          226..236
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:1WYK"
FT   STRAND          253..256
FT                   /evidence="ECO:0007829|PDB:1WYK"
SQ   SEQUENCE   1245 AA;  136650 MW;  967EF00E675F84EF CRC64;
     MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP
     QNPRPRPPPR QKKQAPKQPP KPKKPKPQEK KKKQPAKTKP GKRQRMALKL EADRLFDVKN
     EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY
     TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT
     ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCNRPPTCY TREPSRALDI
     LEENVNHEAY DTLLNAILRC GSSGRSKRSV TDDFTLTSPY LGTCSYCHHT EPCFSPIKIE
     QVWDEADDNT IRIQTSAQFG YDKSGAASTN KYRYMSFEQD HTVKEGTMDD IKISTSGPCR
     RLSYKGYFLL AKCPPGDSVT VSIASSNSAT SCTMARKIKP KFVGREKYDL PPVHGKKIPC
     TVYDRLKETT AGYITMHRPG PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVT
     TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHADHTAQ GKLHLPFKLI PSTCMVPVAH
     APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWII GKTVRNFTVD RDGLEYIWGN
     HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SAAVAMMIGV TVAALCACKA
     RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY FWSNSQPFFW VQLCIPLAAV
     IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM
     SSEVLPSTNQ EYITCKFTTV VPSPKVKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
     FCDSENSQMS EAYVELSADC ATDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG
     TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGVFGDIQ ATSLTSKDLI
     ASTDIRLLKP SAKNVHVPYT QAASGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG
     NIPISIDIPN AAFIRTSDAP LVSTVKCDVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS
     STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
     DQEFQAAISK TSWSWLFALF GGASSLLIIG LTIFACSMML TSTRR
//