POLG_EHV
ID POLG_EHV Reviewed; 3401 AA.
AC C8XPB2;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein C;
DE AltName: Full=Core protein;
DE Contains:
DE RecName: Full=Protein prM;
DE Contains:
DE RecName: Full=Peptide pr;
DE Contains:
DE RecName: Full=Small envelope protein M;
DE AltName: Full=Matrix protein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=NS1;
DE Contains:
DE RecName: Full=Non-structural protein 2A;
DE Short=NS2A;
DE Contains:
DE RecName: Full=Non-structural protein 2A-alpha;
DE Short=NS2A-alpha;
DE Contains:
DE RecName: Full=Serine protease subunit NS2B;
DE AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE AltName: Full=Non-structural protein 2B;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.91;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
DE AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE AltName: Full=Non-structural protein 3;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE Contains:
DE RecName: Full=Peptide 2k;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase NS5;
DE EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=Non-structural protein 5;
OS Edge Hill virus (EHV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=64296;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC STRAIN=YMP 48 {ECO:0000312|EMBL:ABI54476.1};
RX PubMed=19741066; DOI=10.1099/vir.0.014506-0;
RA Grard G., Moureau G., Charrel R.N., Holmes E.C., Gould E.A.,
RA de Lamballerie X.;
RT "Genomics and evolution of Aedes-borne flaviviruses.";
RL J. Gen. Virol. 91:87-94(2010).
CC -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC to the cell membrane and gathering the viral RNA into a nucleocapsid
CC that forms the core of a mature virus particle. During virus entry, may
CC induce genome penetration into the host cytoplasm after hemifusion
CC induced by the surface proteins. Can migrate to the cell nucleus where
CC it modulates host functions. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC After virion release in extracellular space, gets dissociated from E
CC dimers. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC during intracellular virion assembly by masking and inactivating
CC envelope protein E fusion peptide. prM is the only viral peptide
CC matured by host furin in the trans-Golgi network probably to avoid
CC catastrophic activation of the viral fusion activity in acidic Golgi
CC compartment prior to virion release. prM-E cleavage is inefficient, and
CC many virions are only partially matured. These uncleaved prM would play
CC a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC pathway through M ectodomain. May display a viroporin activity.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC pathogenesis and viral replication. Once cleaved off the polyprotein,
CC is targeted to three destinations: the viral replication cycle, the
CC plasma membrane and the extracellular compartment. Essential for viral
CC replication. Required for formation of the replication complex and
CC recruitment of other non-structural proteins to the ER-derived membrane
CC structures. Excreted as a hexameric lipoparticle that plays a role
CC against host immune response. Antagonizing the complement function.
CC Binds to the host macrophages and dendritic cells. Inhibits signal
CC transduction originating from Toll-like receptor 3 (TLR3).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host immune response. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC serine protease function of NS3. May have membrane-destabilizing
CC activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus
CC assembly (By similarity). {ECO:0000250|UniProtKB:P03314,
CC ECO:0000255|PROSITE-ProRule:PRU00860}.
CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC required for the interferon antagonism activity of the latter.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC derived membrane vesicles where the viral replication takes place.
CC Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC nuclear translocation, thereby preventing the establishment of cellular
CC antiviral state by blocking the IFN-alpha/beta pathway.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) RNA genome, and performs the capping of genomes in the
CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC positions (By similarity). Besides its role in RNA genome replication,
CC also prevents the establishment of cellular antiviral state by blocking
CC the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I
CC induces binding of NS5 to host IFN-activated transcription factor
CC STAT2, preventing its transcriptional activity. Host TRIM23 is the E3
CC ligase that interacts with and polyubiquitinates NS5 to promote its
CC binding to STAT2 and trigger IFN-I signaling inhibition.
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00924};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC in EXOC1 degradation through the proteasome degradation pathway (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with protein prM (By similarity).
CC Interacts with non-structural protein 1 (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted (By similarity). Interacts with envelope protein E (By
CC similarity). NS1 interacts with NS4B (By similarity). Interacts with
CC host complement protein CFH; this interaction leads to the degradation
CC of C3 (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (By similarity). May form homooligomers (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC similarity). Interacts with non-structural protein 2A (via N-terminus)
CC (By similarity). Interacts with NS4B (By similarity). Interacts with
CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC (By similarity). NS3 interacts with host PDCD6IP; this interaction
CC contributes to virion release (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer (By similarity).
CC Interacts with host STAT2; this interaction prevents the establishment
CC of cellular antiviral state (By similarity). Interacts with serine
CC protease NS3 (By similarity). Interacts with host TRIM23; this
CC interaction leads to NS5 ubiquitination (By similarity).
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC Peripheral membrane protein; Lumenal side
CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC reticulum membrane; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC endoplasmic reticulum membrane; Peripheral membrane protein;
CC Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
CC Note=Located in RE-associated vesicles hosting the replication complex.
CC NS5 protein is mainly localized in the nucleus rather than in ER
CC vesicles. {ECO:0000250|UniProtKB:P17763}.
CC -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC envelope protein E contain an endoplasmic reticulum retention signal.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. The nascent capsid protein C contains a C-terminal
CC hydrophobic domain that act as a signal sequence for translocation of
CC prM into the lumen of the ER. Mature capsid protein C is cleaved at a
CC site upstream of this hydrophobic domain by NS3. prM is cleaved in
CC post-Golgi vesicles by a host furin, releasing the mature small
CC envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a
CC C-terminally truncated form of non-structural protein 2A, results from
CC partial cleavage by NS3. Specific enzymatic cleavages in vivo yield
CC mature proteins peptide 2K acts as a signal sequence and is removed
CC from the N-terminus of NS4B by the host signal peptidase in the ER
CC lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-
CC mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.
CC -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC releasing the mature small envelope protein M, and peptide pr. This
CC cleavage is incomplete as up to 30% of viral particles still carry
CC uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC glycosylated and this is required for efficient secretion of the
CC protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: Polyubiquitinated; ubiquitination is probably mediated by host
CC TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not
CC ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.
CC -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC residues. This phosphorylation may trigger NS5 nuclear localization.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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DR EMBL; DQ859060; ABI54476.1; -; Genomic_RNA.
DR RefSeq; YP_009256192.1; NC_030289.1.
DR SMR; C8XPB2; -.
DR MEROPS; S07.001; -.
DR GeneID; 27964207; -.
DR KEGG; vg:27964207; -.
DR Proteomes; UP000136711; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; 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:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.10.8.970; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.260.50; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding; Capsid protein;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; GTP-binding;
KW Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW Host nucleus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW Membrane; Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW Secreted; Serine protease; Suppressor of RNA silencing; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Viral attachment to host cell; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus entry into host cell; Zinc.
FT CHAIN 1..3401
FT /note="Genome polyprotein"
FT /id="PRO_0000441470"
FT CHAIN 1..100
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441471"
FT PROPEP 101..117
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441472"
FT CHAIN 118..281
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441473"
FT CHAIN 118..206
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441474"
FT CHAIN 207..281
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441475"
FT CHAIN 282..774
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441476"
FT CHAIN 775..1126
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441477"
FT CHAIN 1127..1351
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441478"
FT CHAIN 1127..1317
FT /note="Non-structural protein 2A-alpha"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441479"
FT CHAIN 1352..1480
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441480"
FT CHAIN 1481..2102
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441481"
FT CHAIN 2103..2228
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441482"
FT PEPTIDE 2229..2251
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441483"
FT CHAIN 2252..2498
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441484"
FT CHAIN 2499..3401
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441485"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..281
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 282..725
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..1122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1123..1143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1144..1198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1199..1219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1220..1287
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1309..1352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1353..1373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1374..1376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1377..1397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1398..1447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1448..1468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1469..2154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2155..2175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2176..2181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2182..2200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2201
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2202..2222
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2223..2235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2236..2250
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2251..2285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 2286..2306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2307..2354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2355..2375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2376..2418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2419..2439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2440..2467
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2468..2488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2489..3401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1481..1661
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1665..1821
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1816..1995
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2499..2763
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3026..3178
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 379..392
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1404..1443
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1669..1672
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT MOTIF 1769..1772
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 2869..2902
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 1532
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1556
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1617
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2559
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2644
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2680
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2716
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1678..1685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2554
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2584
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2585
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2602
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2603
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2629
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2630
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2645
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2718
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2936
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2940
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2945
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 100..101
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 117..118
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 206..207
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 281..282
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 774..775
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 1126..1127
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 1351..1352
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 1480..1481
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 1940
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1943
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2102..2103
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2228..2229
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 2251..2252
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 2498..2499
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2511
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2514
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2515
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2517
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2522
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2526
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2559
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2644
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2648
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2680
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2711
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2713
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2716
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 284..311
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 355..386
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 373..397
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 462..564
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 581..611
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 778..789
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 829..916
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 952..997
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1054..1103
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1065..1087
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1086..1090
FT /evidence="ECO:0000250|UniProtKB:P17763"
SQ SEQUENCE 3401 AA; 377294 MW; 7CE3AD4F322122C2 CRC64;
MPVRPRNKPK GVNVMAAGKV AQKIKNKLKS KAKAIGNISK GLRGFILFIL AQIFWARKLT
PRVRTMWKKV DKAKATRVLK GIRNIATQLI TGLAGRKKRR SMTHGIILSL GVTMVIGASL
HHHGGRYLLN VTHADLGKTF TIGSGNCTAN IVEAGSWCSD SMEYECVTLA EAEEPDDIDC
WCRGVERVRV TYGRCKNGLD SRRSRRAAVI TAHIDKGLTT RQEKWLSTSM GERQIQRIER
WMMRNPFYAA ISLLLAWWVG SDIKQKVLIA FLVLAIGPAY STHCVGIPKR DFVQGVQGNT
WVNLVLDQGS CVTLSSDNKP SVDIWLDSIF ISSPVLVRRV SHTATISDTK VQTACPTNGE
AKLEEEASAE YECKKTYSDR GWGNGCGLFG KGSIVACAKY TSTGHMDVYE IDSTKIEYVT
KAQVHAGMKH DDTTMVKEVK FEPTTGSMDV EFTGYGTLGL ECHVQTMVDM ANYYLVVMGQ
EAWLVHKQWV EDITLPWKIG EGGFWRDKHY MVEFTEPHAT TMTVMVLGAQ EGALRTALAG
AMVVTYTDSS GTKKFSLKGG HVSCKARMNG LVLKGSTYTM CKGGFSFVKT PTDTGHGTAV
MQVKVSKGTP CRIPVQAVDS SNGGTNRATL ITANPIAATT EDEVMIELSP PYGESYIMIG
TGDDKLTYHW HKSGSTIGSL FTETYKGAQR MAIIGDDAWD FSSSSNFFNS IGKALHTVFG
NVFHSIFGGL SWITKIILGG MFLWLGVNSR NQTMCMVLMA VGGILLFMTL GVSGEVGCSL
DIKRRELKCG DGLFLFNDVN DWTHKYKFHP EDPKLLASLI KKSHQEGRCG LSSVNEVEHR
MWNSIKTEIN AMFEENGVDL SVVVKDSKLH YKMGSHAFPK VEEGLSLGWK NWGKSLVFEP
KQSNVSFIID GTSEDCPFTN RIWNAFVVEE FGIGMFTTNV FLTHKVDFTK QCDASLLGAG
VKGDVAVHGD PTLWMESRKE NGTWQLHTIQ MNGLRECFWP QTHTIHGSSV MESAMFLPKQ
YGGPVSHHNH YTGYAVQTAG PWNVQPLIVK RETCPGTQVR VDEQCRDRGN SVRSTTSEGK
IIPEWCCRSC TLPPVSFWGP DSCWYAMEIR PQNVHEEHLV RSWASAGTGM AESSLGLVAL
FLFTDIFARK RMTRKFMVIG CLGVLSVMIV GGFTALDLIR YIIVVGQHFA SMNHGGDVAY
LAIIAVGKLR PGLLMMYSFK AAWSPKERVM VALGLLVFQA VLGDFVHTGL WEWADAAGMC
ILIIQGMATR KEKTYIMPIL ALLTPLSMEI IRKTGIFACV GLLGLSLWRG GDTTMRKGMP
LLAGAATAAS GLTRASLSVV FILCATAASR RSWPIGEIMA IVGIVGTGFG MAVNDQASLA
GPMLVFGLIM IVYATLGRAD GLTLKRVGDI TWEEEAVHSG SSTRYDVTLN EAGEFKLVHE
EPVVWSHVVF LVVALIAASV HPIALVVVTI IWTYGKKHLR GGVLWDIPIA PPVEEAEPLE
DGVYAILQSG LMGKAQAGVG VAQEGVFHTM WHVTRGGFLM VGGKRLTPHW ASVKRDLICY
GGNWKLDGKW DGVEEVQLIA VAPGKAPTNV QTKPGVFRMA DGTEIGAVAL DYPSGTSGSP
IVNEKGQVIG LYGNGIVIGG SGYVSSIAQI AGGEGVTEEP LLDTATMLRK GKLTVLDYHP
GAGKTRIFLP YILKECVRRK LRTLVLAPTR VVLSEMREAL RDVAVKYHTQ AFQAAGTGRE
LVDAMCHATL SHRMLESSRS VNWEVIIMDE AHYMDPTSIA ARGWAAHKAN NHESAVIFMT
ATPPGSANEF PESNGEIEDL RRDIPTEPWN KGHEWILEDR RPTVWFLPSI RAANNIAACL
RRSERSVVVL NRQTFETVYP TIKTKKPDFI LATDIAEMGA NLGVERVIDC RTSYKPVLTT
DGRVVIKGPL RIPASAAAQR RGRVGRCKDR DTDSYVYSEE TSEDNGHYVC WTEASMLLDN
MEVKGGMVAP LYDVEAQKTE MVPGEARLRD DQRKVFRTLI KRYDLPVWVS WQVAKSGLML
EDRKWCFDGD DENTILNDNG EKILARSPGG QRKFLCPRWN DSRLYYDNAS LMSFLAFAEG
RRSYLGVWHA VQMAPLKLGE KLTESLDTMV MLMRSEEGTR AYKLASTNAP EAVTILLMTG
IVVACTLGVG LAFMWPKGVD KMSMGMITMS IAGYLMLQGG LTPVQVASVL LIFFIFMVVL
IPEAGTQRSI NDNKTLYVLL GVALLIGAIT ANEMGYLEKT KRDLLGERVQ NEWKLELPMF
DLRPGAAWSI YVGLATLVMP VLDHWIRTEY GSLSLTGIAQ QASILQAMDK GVPFFKLNMS
VIVLLVSVWN NFSMLSVLCG VGLLGVHCAF VLPGLRAQAA KQAQRRVYHG VAKNPVVDGQ
TTAEIETAPE MPPLYEKKLA LVLLGVVAIA NGVMVRSAFS MAETVVLLSA AVGPLLEGNT
SAIWNGPMAV AMAGIMRGNY YAGIGLAYNL WILQSPKRGR STTMTLGELW KRQLNLMGKR
EFELYKITDI HEVDRSQAQA VMKAGIDNVG ISVSRGTSKL KWMVDRNYVE PLGRVVDLGC
GRGGWSYLCA ASKRVSSVKA YTLGITGHEK PVNVQSLGWN IIKFKDKTDV FKMEPHACET
LLCDIGESSS NPLVEMERTL KVIDNVERWM SPTTESYCFK VLAPYRPEVI ERLERFQLKY
GGGIVRVPFS RNSTHEMYYV SGVKNNLTHM VSCVSRLLLR RMTHPDGRCK VEADVVFPTG
TRNVASDLGP MDLSKVKDRV NRLRSEQGTW FQDDSHPYRT WHYLGSYVAK QSGSAATMVN
GVVKMLSMPW DRIENVTQLA MTDTTPYGQQ RVFKEKVDTR APPPPPGTRA IMEVVNKWMF
DFLAREKAPR ICTKEEFINK VRSNAALGNM LEEQDGWKDA ATAVQDPRFW ALVDRERQVH
LEGRCETCIY NMMGKREKKP AEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFGREN
SLAGVEGVGL QYLGYVVKNV WEKSNGIMYA DDTAGWDTRV TEADLDDEQY LLSKMEGYHK
KLASAVMNMT YKYKVVKVPR PGPGGKVFMD VIARQDQRGS GQVVTYPLNT GTNMKVQLIR
MAEGEGVISR HDIERVTIKT LNALRVWLAE NGAERLSRMA VSGDDCVVAP LDERFGLALH
HLNAMSKIRK DIDDWTESIP WRSWESVPFC SHHFHQLFLK DGRSIVVPCR DQDELVGRAR
VSPGNGWKLK ETACLSKAYA QMWLLMYFHK RDLRLMGNAI CSSVPAHWVP TGRTTWSIHA
HNEWISSERM LDVWNKVWIV DNPHMPDKTC IDDWRDVPYL PKSQDRLCGS LIGITARASW
AENIRAVVNK IRGMIGNEVY SDHLSVMGRY TYSVQEVGTV L
