GenomeNet

Database: UniProt
Entry: P07720
LinkDB: P07720
Original site: P07720 
ID   POLG_TBEVS              Reviewed;        3412 AA.
AC   P07720; P07721; Q88475; Q88476; Q88477; Q88478; Q88479; Q88877;
AC   Q88878; Q88879;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 3.
DT   18-SEP-2019, entry version 177.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Peptide 2k;
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=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=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   Tick-borne encephalitis virus Far Eastern subtype (strain Sofjin)
OS   (SOFV) (Sofjin virus).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=11087;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=34615; Ixodes persulcatus (Taiga tick).
OH   NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2136778; DOI=10.1016/0042-6822(90)90073-z;
RA   Pletnev A.G., Yamshchikov V.F., Blinov V.M.;
RT   "Nucleotide sequence of the genome and complete amino acid sequence of
RT   the polyprotein of tick-borne encephalitis virus.";
RL   Virology 174:250-263(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1190.
RX   PubMed=2970626; DOI=10.1093/nar/16.15.7750;
RA   Yamshchikov V.F., Pletnev A.G.;
RT   "Nucleotide sequence of the genome region encoding the structural
RT   proteins and the NS1 protein of the tick borne encephalitis virus.";
RL   Nucleic Acids Res. 16:7750-7750(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-683 AND 777-1002.
RX   PubMed=3709796; DOI=10.1016/0014-5793(86)81160-7;
RA   Pletnev A.G., Yamshchikov V.F., Blinov V.M.;
RT   "Tick-borne encephalitis virus genome. The nucleotide sequence coding
RT   for virion structural proteins.";
RL   FEBS Lett. 200:317-321(1986).
RN   [4]
RP   GLYCOSYLATION (ENVELOPE PROTEIN E).
RX   PubMed=2441520; DOI=10.1016/0042-6822(87)90460-0;
RA   Winkler G., Heinz F.X., Kunz C.;
RT   "Studies on the glycosylation of flavivirus E proteins and the role of
RT   carbohydrate in antigenic structure.";
RL   Virology 159:237-243(1987).
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (24.0 ANGSTROMS) OF 281-675.
RX   PubMed=11893341; DOI=10.1016/s0092-8674(02)00660-8;
RA   Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J.,
RA   Lenches E., Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G.,
RA   Baker T.S., Strauss J.H.;
RT   "Structure of dengue virus: implications for flavivirus organization,
RT   maturation, and fusion.";
RL   Cell 108:717-725(2002).
CC   -!- FUNCTION: Capsid protein C: Plays a role in virus budding by
CC       binding to the cell membrane and gathering the viral RNA into a
CC       nucleocapsid that forms the core of a mature virus particle.
CC       During virus entry, may induce genome penetration into the host
CC       cytoplasm after hemifusion induced by the surface proteins. Can
CC       migrate to the cell nucleus where it modulates host functions.
CC       {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
CC       envelope proteins in trans-Golgi by binding to envelope protein E
CC       at pH6.0. After virion release in extracellular space, gets
CC       dissociated from E 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
CC       Golgi compartment prior to virion release. 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: Small envelope protein M: May play a role in virus
CC       budding. Exerts cytotoxic effects by activating a mitochondrial
CC       apoptotic pathway through M ectodomain. May display a viroporin
CC       activity. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
CC       and mediates fusion between viral and cellular membranes. Envelope
CC       protein is synthesized in the endoplasmic reticulum in the form of
CC       heterodimer with protein prM. They play a role in virion budding
CC       in the ER, and the newly formed immature particle is covered with
CC       60 spikes composed of heterodimer between precursor prM and
CC       envelope protein E. The virion is transported to the Golgi
CC       apparatus where the low pH causes dissociation of PrM-E
CC       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
CC       polyprotein, is targeted to three destinations: the viral
CC       replication cycle, the plasma membrane and the extracellular
CC       compartment. Essential for viral replication. Required for
CC       formation of the replication complex and recruitment of other non-
CC       structural proteins to the ER-derived membrane structures.
CC       Excreted as a hexameric lipoparticle that plays a role against
CC       host immune response. Antagonizing the complement function. Binds
CC       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
CC       antagonizes the host immune response.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Non-structural protein 2B: Required cofactor for the
CC       serine protease function of NS3 (By similarity). May have
CC       membrane-destabilizing activity and form viroporins (By
CC       similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00859}.
CC   -!- FUNCTION: Serine protease NS3: Displays three enzymatic
CC       activities: serine protease, NTPase and RNA helicase. NS3 serine
CC       protease, in association with NS2B, performs its autocleavage and
CC       cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
CC       NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
CC       helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC   -!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
CC       of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
CC       energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
CC       is 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
CC       cellular antiviral state by blocking the IFN-alpha/beta pathway.
CC       Inhibits STAT2 translocation in the nucleus after IFN-alpha
CC       treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
CC       (+) and (-) genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC       2'-O positions. Besides its role in RNA genome replication, also
CC       prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
CC       Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
CC       activation of JAK-STAT signaling pathway.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which
CC         each of the Xaa can be either Arg or Lys and Yaa can be either
CC         Ser or Ala.; 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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-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)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681,
CC         Rhea:RHEA-COMP:15683, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143971, ChEBI:CHEBI:143975; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680,
CC         Rhea:RHEA-COMP:15682, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143973, ChEBI:CHEBI:143974; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-
CC         COMP:15683, Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143975,
CC         ChEBI:CHEBI:143977; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-
CC         COMP:15682, Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143974,
CC         ChEBI:CHEBI:143976; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
CC       with host EXOC1 (via C-terminus); this interaction results in
CC       EXOC1 degradation through the proteasome degradation pathway.
CC       Protein prM: Forms heterodimers with envelope protein E in the
CC       endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
CC       the endoplasmic reticulum and Golgi. Interacts with protein prM.
CC       Interacts with non-structural protein 1. Non-structural protein 1:
CC       Homodimer; Homohexamer when secreted. Interacts with envelope
CC       protein E. Non-structural protein 2A: Interacts (via N-terminus)
CC       with serine protease NS3. Non-structural protein 2B: Forms a
CC       heterodimer with serine protease NS3. May form homooligomers.
CC       Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
CC       NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
CC       NS5; this interaction stimulates RNA-directed RNA polymerase NS5
CC       guanylyltransferase activity. Non-structural protein 4B: Interacts
CC       with serine protease NS3. RNA-directed RNA polymerase NS5:
CC       Homodimer. Interacts with host STAT2; this interaction inhibits
CC       the phosphorylation of the latter, and, when all viral proteins
CC       are present (polyprotein), targets STAT2 for degradation.
CC       Interacts with serine protease NS3. Interacts with host SCRIB;
CC       this interaction targets NS5 to the cell membrane periphery and
CC       nucleus, thereby allowing efficient host nuclear STAT1 inhibition.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Capsid protein C: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
CC       region {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
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the 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
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
CC       membrane; Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC       Peripheral membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}. Note=Remains non-covalently associated to
CC       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:P14335}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-associated 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
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-derived 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:P06935}.
CC       Note=Located in RE-associated vesicles hosting the replication
CC       complex. NS5 protein is mainly localized in the nucleus rather
CC       than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M
CC       and envelope protein E contain an endoplasmic reticulum retention
CC       signal. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
CC       yield mature proteins. Cleavages in the lumen of endoplasmic
CC       reticulum are performed by host signal peptidase, whereas
CC       cleavages in the cytoplasmic side are performed by serine protease
CC       NS3. Signal cleavage at the 2K-4B site requires a prior NS3
CC       protease-mediated cleavage at the 4A-2K site.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr.
CC       This cleavage is incomplete as up to 30% of viral particles still
CC       carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Envelope protein E: N-glycosylated.
CC       {ECO:0000269|PubMed:2441520}.
CC   -!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
CC       is glycosylated and this is required for efficient secretion of
CC       the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like
CC       SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
CC       capsid structure;
CC       URL="http://viperdb.scripps.edu/info_page.php?VDB=1k4r";
DR   EMBL; X07755; CAA30581.1; -; Genomic_RNA.
DR   EMBL; X03870; CAA27500.1; -; Genomic_RNA.
DR   EMBL; X03870; CAA27501.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; X03870; CAA27502.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; X03870; CAA27503.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; X03871; CAA27505.1; -; Genomic_RNA.
DR   PIR; A33776; GNWVTB.
DR   PDB; 1K4R; EM; 24.00 A; A/B/C=281-675.
DR   PDBsum; 1K4R; -.
DR   SMR; P07720; -.
DR   PRIDE; P07720; -.
DR   EvolutionaryTrace; P07720; -.
DR   Proteomes; UP000007401; 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:0019031; C:viral envelope; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host 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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 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   InterPro; IPR011492; DEAD_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; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 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; 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   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   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;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW   Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN         1   3412       Genome polyprotein.
FT                                /FTId=PRO_0000405171.
FT   CHAIN         1     96       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037804.
FT   PROPEP       97    117       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000405172.
FT   CHAIN       118    280       Protein prM.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000405173.
FT   CHAIN       118    205       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037805.
FT   CHAIN       206    280       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037806.
FT   CHAIN       281    776       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037807.
FT   CHAIN       777   1128       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037808.
FT   CHAIN      1129   1358       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037809.
FT   CHAIN      1359   1489       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037810.
FT   CHAIN      1490   2110       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037811.
FT   CHAIN      2111   2236       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037812.
FT   PEPTIDE    2237   2259       Peptide 2k.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000405174.
FT   CHAIN      2260   2510       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037813.
FT   CHAIN      2511   3412       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037814.
FT   TOPO_DOM      1     98       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     99    119       Helical. {ECO:0000255}.
FT   TOPO_DOM    120    242       Extracellular. {ECO:0000255}.
FT   TRANSMEM    243    260       Helical. {ECO:0000255}.
FT   TOPO_DOM    261    261       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    262    280       Helical. {ECO:0000255}.
FT   TOPO_DOM    281    727       Extracellular. {ECO:0000255}.
FT   TRANSMEM    728    748       Helical. {ECO:0000255}.
FT   TOPO_DOM    749    755       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    756    776       Helical. {ECO:0000305}.
FT   TOPO_DOM    777   1187       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1188   1208       Helical. {ECO:0000255}.
FT   TOPO_DOM   1209   1236       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1237   1257       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1258   1293       Lumenal. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1294   1314       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1315   1327       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1328   1348       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1349   1359       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1360   1378       Helical. {ECO:0000255}.
FT   TOPO_DOM   1379   1382       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1383   1403       Helical. {ECO:0000255}.
FT   TOPO_DOM   1404   1454       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1455   1475       Helical. {ECO:0000255}.
FT   TOPO_DOM   1476   2160       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2161   2181       Helical. {ECO:0000255}.
FT   TOPO_DOM   2182   2189       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2190   2210       Helical. {ECO:0000255}.
FT   TOPO_DOM   2211   2211       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2212   2232       Helical. {ECO:0000255}.
FT   TOPO_DOM   2233   2244       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2245   2265       Helical; Note=Signal for NS4B.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2266   2299       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2300   2320       Helical. {ECO:0000255}.
FT   TOPO_DOM   2321   2343       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2344   2364       Helical. {ECO:0000255}.
FT   TOPO_DOM   2365   2368       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2369   2389       Helical. {ECO:0000255}.
FT   TOPO_DOM   2390   2430       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2431   2451       Helical. {ECO:0000255}.
FT   TOPO_DOM   2452   2476       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2477   2497       Helical. {ECO:0000255}.
FT   TOPO_DOM   2498   3412       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1490   1669       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1675   1831       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1841   2000       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2511   2775       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3038   3187       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1688   1695       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      378    391       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1410   1449       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   REGION     2729   2733       Interaction with host SCRIB.
FT                                {ECO:0000250|UniProtKB:Q01299}.
FT   MOTIF      1779   1782       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS    266    271       Poly-Val.
FT   COMPBIAS   1970   1973       Poly-Asp.
FT   ACT_SITE   1543   1543       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1567   1567       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1627   1627       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   2571   2571       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2656   2656       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2693   2693       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2729   2729       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   METAL      2948   2948       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2952   2952       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2957   2957       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2960   2960       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3222   3222       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3238   3238       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3357   3357       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   BINDING    2566   2566       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2596   2596       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2597   2597       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2615   2615       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2641   2641       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2642   2642       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2657   2657       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2731   2731       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE         96     97       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        117    118       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        205    206       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        280    281       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        776    777       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1128   1129       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1358   1359       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1489   1490       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1949   1949       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       1952   1952       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       2110   2111       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2236   2237       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2259   2260       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2510   2511       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2523   2523       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2526   2526       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2527   2527       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2529   2529       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2534   2534       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2538   2538       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2571   2571       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2656   2656       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2660   2660       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2693   2693       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2724   2724       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2726   2726       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2729   2729       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   MOD_RES    2566   2566       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    434    434       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:P14336,
FT                                ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    861    861       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    983    983       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    999    999       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    283    310       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    340    401       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    340    396       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    354    385       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    372    401       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    372    396       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    466    570       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    587    618       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    780    791       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    831    920       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    955   1000       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1057   1106       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1068   1090       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1089   1093       {ECO:0000250|UniProtKB:P17763}.
FT   CONFLICT    381    381       W -> S (in Ref. 3; CAA27500).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3412 AA;  377981 MW;  0F61CE6DCCDC5965 CRC64;
     MAGKAILKGK GGGPPRRVSK ETAKKTRQSR VQMPNGLVLM RMMGILWHAV AGTARSPVLK
     SFWKSVPLKQ ATAALRKIKK AVSTLMVGLQ RRGKRRSAVD WTGWLLVVVL LGVTLAATVR
     KERDGTTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLTYECVTID QGEEPVDVDC
     SCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGDLTGR GHKWLEGDSL RTHLTRVEGW
     VWKNKVLTLA VIAVVWLTVE SVVTRVAVVV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
     VTLVLELGGC VTITAEGKPS MDVWLDSIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
     TLAEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKAS CEAKKKATGH VYDANKIVYT
     VKVEPHTGDY VAANETHSGR KTASFTVSSE RTILTMGDYG DVSLLCRVAS GVDLAQTVIL
     ELDKTSEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ
     TGVLLKSLAG VPVAHIDGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRIPTD
     SGHDTVVMEV AFSGTKPCRI PVRAVAHGSP DVNVAMLMTP NPTIENNGGG FIEMQLPPGD
     NIIYVGELSH QWFQKGSSIG RVFQKTRKGI ERLTVIGEHA WDFGSTGGFL TSVGKALHTV
     LGGAFNSLFG GVGFLPKILV GVVLAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
     AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETLGALAS AIKETFEEGT CGIVPQNRLE
     MAMWRSSATE LNLALVEGDA NLTVVVDKLD PTDYRGGIPS LLKKGKDIKV SWKSWGHSMI
     WSVPEAPRLF MVGTEGSSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE STHECDTGVM
     GAAVKNGMAV HTDQSLWMKS VRNDTGTYIV ELLVTDLRNC SWPASHTIDN AEVVDSELFL
     PASLAGPRSW YNRIPGYSEQ VKGPWKYSPI RVTREECPGT RVTINADCDK RGASVRSTTE
     SGKVIPEWCC RTCTLPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGIP
     GIVALFVVLE YVIRRRPATG TTAMWGGIVV LALLVTGLVK IESLVRYVVA VGITFHLELG
     PEIVALTLLQ AVFELRVGLL SAFALRSNLT VREMVTIYFL LLVLELGLPS EGLGALWKWG
     DALAMGALIF RACTAEEKTG VGLLLMALMT QQDLATVHYG LMLFLGVASC CSIWKLIRGH
     REQKGLTWIV PLAGLLGGEG SGVRLVAFWE LTVHGRRRSF SEPLTVVGVM LTLASGMIRH
     TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELMNEGGEVS LRVRQDSMGN
     FHLTELEKEE RVMAFWLLAG LAASAFHWSG ILGVMGLWTL SEMLRTARRS GLVFSGQGGR
     ERGDRPFEVK DGVYRIFSPG LLWGQRQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
     WADVKEDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELLLD TGRRIGAVPI
     DLAKGTSGSP ILNSQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPP AVTGTGWTAK
     GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
     AVGDQQVGGS IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
     ENKCALVLMT ATPPGKSEPF PESNGAISSE EKQIPDGEWR DGFDWITEYE GRTAWFVPSS
     AKGGIIARTL IQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
     RTNIKPEEVD GRVELTGTRR VTTASAAQRR GRVGRQEGRT DEYIYSGQCD DDDSGLVQWK
     EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
     VAANVSSVTS RNWTWEGPEE NTVDEANGDL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
     EFVAYASGRR SFGDVLSGMS GVPELLRHRC VSAMDVFYTL MHEEPGSRAM KMAERDAPEA
     FLTVVEMMVL GLATLGVVWC FVVRTSISRM MLGTLVLLAS LALLWAGGVS YGNMAGVALI
     FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTVLWSEH
     EELRSWEEWT NIDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ATGAQAMRDL
     GGGAPFFGVA GHVMALGVVS LVGATPTSLV VGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
     SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLAIVLC LMSVVMNRTV PSTPRLLLWD
     WRQRDNCSNQ RRTPFGRCQA CGLSGVVRGS LWGFCPLGHR LWLRASGSRR GGSEGDTLGD
     LWKRKLNGCT KEEFFAYRRT GILETERDKA RELLKRGETN MGLAVSRGTA KLAWLEERGY
     ATLKGEVVDL GCGRGGWSYY AASRPAVMSV KACAIAGKGH ETPKMVTSLG WNLIKFRAGM
     DVFSMQPHRA DTIMCDIGES NPDAVVEGER TRKVILLMEQ WKNRNPTATC VFKALAPYRP
     EVTEALHRFQ LQWGGGLVRT PFSRNSTHEM YYSTAITGNI VNSVNIQSRK LLARFGDQRG
     PTRVPELDLG VGTRCVVLAE DKVKEKDVQE RISALREQYG ETWHMDREHP YRTWQYWAAT
     ACANRVGGAL INGVVKLLSW PWNAREDVVR MAMTDTTAFG QQRVFKEKVD TKAQEPQPGT
     KVIMRAVNDW ILERLARKSK PRMCSREEFI AKVKSNAALG AWSDEQNRWS SAKEAVEDPA
     FWQLVDEERE RHLAGRCAHC VYNMMGKREK KLGEFGVAKG SRAIWYMWLG SRFLEFEALG
     FLNEDHWASR GSSGSGVEGI SLNYLGWHLK GLSTLEGGLF YADDTAGWDT KVTNADLEDE
     EQLLRYMEGE HKQLAATIMQ KAYHAKVVKV ARPSRDGGCI MDVITRRDQR GSGQVVTYAL
     NTLTNIKVQL IRMMEGEGVI EASDAHNPRL LRVERWLRDH GEERLGRMLV SGDDCVVRPV
     DDRFSGALYF LNDMAKTRKD IGEWDHSVGF SNWEEVPFCS HHFHELVMKD GRTLIVPCRD
     QDELVGRARV SPGCGRSVRE TACLSKAYGQ MWLLSYFHRR DLRTLGLAIC SAVPVDWVPA
     GRTTWSIHAS GAWMTTEDML DVWNRVWILD NPFMHSKEKI AEWRDVPYLP KSHDMLCSSL
     VGRKERAEWA KNIWGAVEKV RKMIGQEKFK DYLSCMDRHD LHWESKLESS II
//
DBGET integrated database retrieval system