POLS_AURAV
ID POLS_AURAV Reviewed; 1244 AA.
AC Q86925;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
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 Aura virus (AURAV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=44158;
OH NCBI_TaxID=7158; Aedes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7747434; DOI=10.1006/viro.1995.1193;
RA Rumenapf T., Strauss E.G., Strauss J.H.;
RT "Aura virus is a New World representative of Sindbis-like viruses.";
RL Virology 208:621-633(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Ruemenapf T.H.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:4UON}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 110-265, AND SUBUNIT (CAPSID
RP PROTEIN).
RX PubMed=25100849; DOI=10.1128/jvi.01692-14;
RA Aggarwal M., Dhindwal S., Kumar P., Kuhn R.J., Tomar S.;
RT "trans-Protease activity and structural insights into the active form of
RT the alphavirus capsid protease.";
RL J. Virol. 88:12242-12253(2014).
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 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:P03315};
CC -!- SUBUNIT: [Capsid protein]: Homodimer (PubMed:25100849). 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:Q8JUX5,
CC ECO:0000269|PubMed:25100849, 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: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: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: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: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.
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DR EMBL; AF126284; AAD13623.1; -; Genomic_RNA.
DR RefSeq; NP_632024.1; NC_003900.1.
DR PDB; 4AGJ; X-ray; 1.98 A; A=110-267.
DR PDB; 4AGK; X-ray; 1.81 A; A=110-267.
DR PDB; 4UON; X-ray; 1.81 A; A/B=110-265.
DR PDB; 5G4B; X-ray; 2.24 A; A=110-267.
DR PDBsum; 4AGJ; -.
DR PDBsum; 4AGK; -.
DR PDBsum; 4UON; -.
DR PDBsum; 5G4B; -.
DR SMR; Q86925; -.
DR MEROPS; S03.001; -.
DR GeneID; 944526; -.
DR KEGG; vg:944526; -.
DR Proteomes; UP000007442; 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: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; Disulfide bond;
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 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..267
FT /note="Capsid protein"
FT /id="PRO_0000238706"
FT CHAIN 268..751
FT /note="Precursor of protein E3/E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238707"
FT CHAIN 268..328
FT /note="Assembly protein E3"
FT /id="PRO_0000238708"
FT CHAIN 329..751
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000238709"
FT CHAIN 752..806
FT /note="6K protein"
FT /id="PRO_0000238710"
FT CHAIN 807..1244
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000238711"
FT TOPO_DOM 268..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..1218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1240..1244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 117..267
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..69
FT /note="Host transcription inhibition"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT REGION 85..118
FT /note="Binding to the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 103..117
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250|UniProtKB:P27284"
FT REGION 188..198
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 224..228
FT /note="Dimerization of the capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P0DOK1"
FT REGION 268..280
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 62..103
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT MOTIF 149..159
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P09592"
FT COMPBIAS 61..78
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 191
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000269|PubMed:25100849"
FT SITE 192
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000269|PubMed:25100849"
FT SITE 225
FT /note="Involved in dimerization of the capsid protein"
FT /evidence="ECO:0000269|PubMed:25100849"
FT SITE 267..268
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 752..753
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 725
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 LIPID 746
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
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 1106..1181
FT /evidence="ECO:0000250"
FT DISULFID 1111..1185
FT /evidence="ECO:0000250"
FT DISULFID 1133..1175
FT /evidence="ECO:0000250"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4AGK"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4AGK"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4AGK"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4AGK"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4UON"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:4AGK"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4AGK"
SQ SEQUENCE 1244 AA; 137116 MW; FB6B682234ED2F46 CRC64;
MNSVFYNPFG RGAYAQPPIA WRPRRRAAPA PRPSGLTTQI QQLTRAVRAL VLDNATRRQR
PAPRTRPRKP KTQKPKPKKQ NQKPPQQQKK GKNQPQQPKK PKPGKRQRTA LKFEADRTFV
GKNEDGKIMG YAVAMEGKVI KPLHVKGTID HPALAKLKFT KSSSYDMEFA KLPTEMKSDA
FGYTTEHPEV FYNWHHGAVQ FSGGRFTIPT GVGGPGDSGR PILDNSGKVV AIVLGGANEV
PGTALSVVTW NKKGAAIKTT HEDTVEWSRA ITAMCILQNV TFPCDRPPTC YNRNPDLTLT
MLETNVNHPS YDVLLDAALR CPTRRHVRST PTDDFTLTAP YLGLCHRCKT MEPCYSPIKI
EKVWDDADDG VLRIQVSAQL GYNRAGTAAS ARLRFMGGGV PPEIQEGAIA DFKVFTSKPC
LHLSHKGYFV IVKCPPGDSI TTSLKVHGSD QTCTIPMRVG YKFVGREKYT LPPMHGTQIP
CLTYERTREK SAGYVTMHRP GQQSITMLME ESGGEVYVQP TSGRNVTYEC KCGDFKTGTV
TARTKIDGCT ERKQCIAISA DHVKWVFNSP DLIRHTDHTA QGKLHIPFPL QQAQCTVPLA
HLPGVKHAYR SMSLTLHAEH PTLLTTRHLG ENPQPTAEWI VGSVTRNFSI TIQGFEYTWG
NQKPVRVYAQ ESAPGNPHGW PHEIVRHYYH LYPFYTVTVL SGMGLAICAG LVISILCCCK
ARRDCLTPYQ LAPNATVPFL VTLCCCFQRT SADEFTDTMG YLWQHSQTMF WIQLVIPLAA
VITLVRCCSC CLPFLLVASP PNKADAYEHT ITVPNAPLNS YKALVERPGY APLNLEVMVM
NTQIIPSVKR EYITCRYHTV VPSPQIKCCG TVECPKGEKA DYTCKVFTGV YPFLWGGAQC
FCDSENSQLS DKYVELSTDC ATDHAEAVRV HTASVKSQLR ITYGNSTAQV DVFVNGVTPA
RSKDMKLIAG PLSTTFSPFD NKVIIYHGKV YNYDFPEFGA GTPGAFGDVQ ASSTTGSDLL
ANTAIHLQRP EARNIHVPYT QAPSGFEFWK NNSGQPLSDT APFGCKVNVN PLRADKCAVG
SLPISVDIPD AAFTRVSEPL PSLLKCTVTS CTYSTDYGGV LVLTYESDRA GQCAVHSHSS
TAVLRDPSVY VEQKGETTLK FSTRSLQADF EVSMCGTRTT CHAQCQPPTE HVMNRPQKST
PDFSSAISKT SWNWITALMG GISSIAAIAA IVLVIALVFT AQHR
