POLG_BANV
ID POLG_BANV Reviewed; 3393 AA.
AC C8XPA8;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
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;
DE EC=3.6.4.13;
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 Banzi virus (BANV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=38837;
OH NCBI_TaxID=7157; Culicidae (mosquitos).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9989; Rodentia.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC STRAIN=SAH 336 {ECO:0000312|EMBL:ABI54472.1};
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. Interacts (via N-terminus) with
CC host EXOC1 (via C-terminus); this interaction results in EXOC1
CC degradation through the proteasome degradation pathway.
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi. Interacts with protein prM. Interacts with non-structural
CC protein 1. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted. Interacts with envelope protein E.
CC {ECO:0000250|UniProtKB:P03314}.
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. May form homooligomers.
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B.
CC Interacts with non-structural protein 2A (via N-terminus). Interacts
CC with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
CC NS5; this interaction stimulates RNA-directed RNA polymerase NS5
CC guanylyltransferase activity. NS3 interacts with host PDCD6IP; this
CC interaction contributes to virion release.
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer. Interacts with
CC host STAT2; this interaction prevents the establishment of cellular
CC antiviral state. Interacts with host TRIM23; this interaction leads to
CC NS5 ubiquitination. {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: [Peptide pr]: Secreted
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: [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; DQ859056; ABI54472.1; -; Genomic_RNA.
DR RefSeq; YP_009222007.1; NC_029054.1.
DR SMR; C8XPA8; -.
DR MEROPS; S07.001; -.
DR GeneID; 40524942; -.
DR KEGG; vg:40524942; -.
DR Proteomes; UP000140353; 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 Cleavage on pair of basic residues; Disulfide bond;
KW 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..3393
FT /note="Genome polyprotein"
FT /id="PRO_0000441439"
FT CHAIN 1..90
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441440"
FT PROPEP 91..108
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_0000441441"
FT CHAIN 109..272
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441442"
FT CHAIN 109..197
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441443"
FT CHAIN 198..272
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441444"
FT CHAIN 273..763
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441445"
FT CHAIN 764..1115
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441446"
FT CHAIN 1116..1340
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441447"
FT CHAIN 1116..1306
FT /note="Non-structural protein 2A-alpha"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000441448"
FT CHAIN 1341..1469
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441449"
FT CHAIN 1470..2089
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441450"
FT CHAIN 2090..2213
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441451"
FT PEPTIDE 2214..2236
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441452"
FT CHAIN 2237..2488
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441453"
FT CHAIN 2489..3393
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000441454"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..272
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 273..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..763
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 764..1112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1113..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1134..1186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1208..1283
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1284..1304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1305..1341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1363..1365
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1366..1386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1387..1438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1439..1459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1460..2137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2138..2158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2159..2168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2169..2184
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2186..2206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2207..2221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2222..2236
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2237..2275
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2276..2296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2297..2344
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2345..2365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2366..2408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2409..2429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2430..2457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2458..2478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2479..3393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1470..1649
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1653..1809
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1804..1984
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2489..2753
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3017..3169
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 28..60
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT REGION 370..383
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1393..1432
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1657..1660
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT MOTIF 1757..1760
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 2860..2893
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 1521
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1545
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1606
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2549
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2634
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2670
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2706
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1666..1673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2544
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2574
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2575
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2592
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2619
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2620
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2635
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2708
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2927
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2931
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
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 2939
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 90..91
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 108..109
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 197..198
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 272..273
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 763..764
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1115..1116
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1340..1341
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1469..1470
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1927
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1930
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2089..2090
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2213..2214
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2236..2237
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2488..2489
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2501
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2504
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2505
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2507
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2512
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2516
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2549
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2634
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2638
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2670
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2701
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2703
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2706
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 275..302
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 346..377
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 364..388
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 453..553
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 570..600
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 767..778
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 818..905
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 941..986
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1043..1092
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1054..1076
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1054..1075
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1075..1079
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1076..1079
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
SQ SEQUENCE 3393 AA; 375607 MW; 8904BB7A51011FC4 CRC64;
MVNPKGVNVM AARVKRAAQK TKKKAVQVSR GLRGFVLFVL TQLFMGRKLT PNVRRLWKSS
DKNSLIHVLT KIKKIVGNLL MGVSRRKKRR SATTSGTVFM AMLGLTLAAS VARHAHHTLI
NITKDDAHKL LTLRNGNCTV VATDIGNWCP DNVEYDCVTL QDNEDPDDVD CWCYRVNNVR
VTYGRCKDGN TPRRSKRAVV ITAHLDQGLT TKKETWLGSS HFETQVQKVE KWIIRNPTYA
IAAILMSWYI GNSLKQRVVL LLLTLALGPA YATHCVGIPK RDFVQGVQGT TWVNLVLEQG
GCVTIMAEGK PSVDVWMDNI KFTSPTLVRR ISHTATISDT KIATACPSNG EAKLDEEHIK
EYACKRLYSD RGWGNGCGLF GKGSLVACAK YESTGHMDVY EMDMTKVEYT VKTQVHSGAK
SGDLSGVKTV SFAPTSGSQP VEFSGYGNMG LQCMIQSNVD FSTHYLVVMG NDAWLVHKAW
VEDITLPWKH GEGGTWKDKQ YMVEFGEPHA TTVKVLALGP QEGALRNALA GAMIVTYESS
GKTFKLHGGH VTCKATVSGL ALKGTTYTNC RGGLSFVKTP TDTGHGTVVM QVKVAKSAPC
RLTAIAADDA SGHVNRGTLV TSNPIAASNN DEVMIEINPP YGTSYLIVGV GDDKLVYQWK
KSGSTIGSLF SETVKGAQRM AIVGSSSWDF SSTSGFFSSV GKAIHTVFGT AFHGIFGGLS
WMTRILIGVL LVWLGLNSRN GTATTLMMLT GFIILFLSLG VGAEVGCSVN WGQKELKCGD
GIFVYNDVDD WMHKYKYHPE DPKVMAGLIA KAWEKGACGL TSVSELEHVM WVKIASEINA
ILEENEIDLT VVVHENKSVY RRGSRRFPRV ETELTYGWES WGKNFITDGK VSNNTFHVDG
KEDQCASKNR VWNSLEIEEF GFGVFHTNVF LRQKADKTNS CDTTLMGAAV KGNVAAHADP
GFWMESQENN GTWEIQSIEF TAYRECEWPV SHTVHGTQVM ESDMFMPKGI GGPVSHLNRM
QGYKVQTNGA WAYGKTVVQR ELCPDTSVVV DSSCSDRGKS IRSTTTEGKV IKEWCCRSCT
LPPVSYWTSE GCWYAMEVRP MKTPEKHLVR SWVTAGDSYP AWSIGLVAMF LFVDIMARSR
PTRKMMIGGT MLLLAIMIMG ELSYLDLLRY IIVVGEHFIE RENGGDVAYM AIMAASHLRP
GLMAMVFAKS MWSPKQRVLL ALGCAILQPF LTAQASALVW EWADSIGLVL LIVQGMVRNK
EKNWALVLLA LCSPVSMPVI RKASMIIGTG GLLLSLWKGG GSSMRKGLPL FAASAARVLG
LTKAHLSVLF ILLITKNGKR TWPISECLAA VGIFGAAFGT MFSEDETLLG PLALVGVVLI
VYTMFTQSDG LELVKAADIS WSDEAVVSGE ARRFDVALND SGEFKLLDEP PVSWLNVSFL
VVAIVASSLH PIALVVTLVA WTYWRTEKRS GVLWDVPLAP KVEACEHLED GVFRIIQKGL
FGSSQVGIGV AKDGVFHTMW HVTRGAFLMH SGKQLTPTWG SVRKDLVCYG GTWKLDGAWN
GVDEVQLIAV PPGKPATNVQ TKPGTFVLPT GDEAGAVLLD FPSGTSGSPI IDRHGNILGL
YGNGIVLENG AYASAISQAQ PGSVAEVETP GLDKMLRKGE FTMLDYHPGA GKTRKHLPNI
LKECERKRLR TLVLAPTRVV LSEMKEALTS VQAKFHTQAF NSTTTGREII DVMCHATFVH
RMLEGLRSGN WEVIIMDEAH FLDPTSIAAR GWAHHKSKTK ESAVIFMTAT PPGTSNEFPE
SNAEIEDVKK EIPSEPWSKG HEWILEDRRP TVWFLPSIKA ANVMAACLRK AERSVVVLNR
STFENVYPTI KTKKPDFILA TDIAEMGANL PVERVIDCRT AYKPVLVDER VALKGPLRIA
AAAAAQRRGR VGRNPDRDGD TYVYSEDTCE QNDHLVCWTE GSMLLDNMQV KGGFVAPLYE
EEASKTTMTP GECRLRDDQR KVFRTLIRKH DMPVWLSWQV AKSGLAADDR KWCFDGEDDN
AILGDNGEVI KARSPGGQRK ELKPRWSDAR IASDNTSLMN FIAFAEGRRS LPLSILWSVP
NQLSEKLVQS IDTLTILLRS EEGSRAHKLA LQQAPEAVST LLLLGMMAIC TLGLVILLMK
PKATDKMSMA MVTMAITGYL LKLGGMTHAQ VGGILLVFFI MMVVIIPESG TQRSINDNKL
AYVIILVGLV IGGVACNELG WLEKTKADLF GNNMTHAQTV VLPTINWNWL DFRPGAAWSL
YVGMATFLTP VFVHWIKNEY GNASLTGITP TAGILGALNQ GVPFVKLNTS VGVLLLSVWN
NFTTSSMLAA MVMLACHCLF VLPGVRAQCL REAQIRVFHG VAKNPMVDGN PTVDLEKEND
MPDLYEKKLA LVALGMAAVL NAAMVRTALT TAEMVVLGSA AVGPLLEGNT SAFWNGPLAV
AVAGVMRGNH YALIGIVYNL WLLKTARRGG SSALTYGEVW KRQLNLLGKQ EFMNYKVSDI
LEVDRSHARE VLNSGNDAVG VAVSRGSSKL NWLIERGYLR PTGRVVDLGC GRGGWSYTCA
AERQVTSVKA YTLGKEGHEK PRLIQSLGWN IIKFKDKSDI TRMTPHASDT LLCDIGESSS
NPEVEKERTL RVIEAVEKWM SPTTVSFCFK VLAPYKPDVI EALERFQLKH GGGIIRNPYS
RNSTHEMYYV SGVRNNILHM VNSTSRMLMR RMSRPSGRST VVPDLIYPTG TRSVASEAGP
LDLEKVKARI NRLKEEQEST WFVDSDHPYR TWHYHGSYVA KQSGTAASMI NGVVKLLSGP
WDRIEEVTNM AMTDTTPFGQ QRVFKEKVDT RAPEPPQGTR EIMKVVNQWL FDYLGRTKQP
RICTKEEFIN KVRSHAALGG ILTEQEGWSS AAEAVADPRF WSLVDKERQA HLEGRCETCI
YNMMGKREKK PSEFGRAKGS RAIWYMWLGA RFLEFEALGF LNEDHWLGRE NSKAGVEGIG
LQYLGYVVEE VARKGNGLVY ADDTAGWDTR ITEADLEDEQ YIMKRMSAEH RQLAWAVMEL
TYRNKVVKVP RPGPGGKILM DVISRRDQRG SGQVVTYPLN TATNMKVQLI RMAEAENVIT
RNDVEKVSLI TLKELQLWLE VNGVNRLERM AVSGDDCIVA PVDESFAGAL HHLNAMSKTR
KDISEWENSR GWTDWESVPF CSHHFHTLYL KDGRTIIAPC RCQDELIGRA RISPGNGWMI
KETAGLSKAY TQMWTLMYFH RRDLRLMANA ICSAVPIDWV PTGRTTWSIH ATGEWMSSDD
MLEVWNKVWI QDNPHVKDKT PIFAWRDVPY IQKGQDRACG SLVGTSLRAS WAESIMTSVH
RVRMLIGNER YVNYMESMDR YATQRCSAYG ELL
