P17763 · POLG_DEN1W

Function

function

Capsid protein C

Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (PubMed:11893341).
During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions (PubMed:18420804, PubMed:21909430).
Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008).

Capsid protein C

Inhibits RNA silencing by interfering with host Dicer.

Peptide pr

Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.

Protein prM

Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release (PubMed:9971841).
prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:21388812).

Small envelope protein M

May play a role in virus budding (PubMed:25326389).
Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain (PubMed:13679613).
May display a viroporin activity (PubMed:16007501).

Envelope protein E

Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (PubMed:18369148).
prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:11893341).

Non-structural protein 1

Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).

Non-structural protein 1

Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.

Non-structural protein 2A

Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.

Serine protease subunit NS2B

Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (PubMed:26728778).

Serine protease NS3

Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.

Non-structural protein 4A

Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity).

Peptide 2k

Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.

Non-structural protein 4B

Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity).
Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of a cellular antiviral state by blocking the IFN-alpha/beta pathway (PubMed:15956546).

RNA-directed RNA polymerase NS5

Replicates the viral + and - RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.

Catalytic activity

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site100-101Cleavage; by viral protease NS3
Site114-115Cleavage; by host signal peptidase
Site205-206Cleavage; by host furin
Site280-281Cleavage; by host signal peptidase
Site775-776Cleavage; by host signal peptidase
Site1127-1128Cleavage; by host
Site1345-1346Cleavage; by viral protease NS3
Site1475-1476Cleavage; by autolysis
Active site1526Charge relay system; for serine protease NS3 activity
Active site1550Charge relay system; for serine protease NS3 activity
Active site1610Charge relay system; for serine protease NS3 activity
Binding site1669-1676ATP (UniProtKB | ChEBI)
Site1933Involved in NS3 ATPase and RTPase activities
Site1936Involved in NS3 ATPase and RTPase activities
Site2094-2095Cleavage; by autolysis
Site2221-2222Cleavage; by viral protease NS3
Site2244-2245Cleavage; by host signal peptidase
Site2493-2494Cleavage; by viral protease NS3
Site2507mRNA cap binding
Site2510mRNA cap binding; via carbonyl oxygen
Site2511mRNA cap binding
Site2513mRNA cap binding; via carbonyl oxygen
Site2518mRNA cap binding
Site2522mRNA cap binding
Binding site2549S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2554For 2'-O-MTase activity
Site2554Essential for 2'-O-methyltransferase activity
Binding site2579S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2580S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2597S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2598S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2624S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2625S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2639For 2'-O-MTase activity
Site2639Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
Binding site2640S-adenosyl-L-methionine (UniProtKB | ChEBI)
Site2643mRNA cap binding
Active site2673For 2'-O-MTase activity
Site2673Essential for 2'-O-methyltransferase activity
Site2704mRNA cap binding
Site2706mRNA cap binding
Active site2709For 2'-O-MTase activity
Site2709Essential for 2'-O-methyltransferase activity
Binding site2711S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2930Zn2+ 1 (UniProtKB | ChEBI)
Binding site2934Zn2+ 1 (UniProtKB | ChEBI)
Binding site2939Zn2+ 1 (UniProtKB | ChEBI)
Binding site2942Zn2+ 1 (UniProtKB | ChEBI)
Binding site3204Zn2+ 2 (UniProtKB | ChEBI)
Binding site3220Zn2+ 2 (UniProtKB | ChEBI)
Binding site3339Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell mitochondrion
Cellular Componenthost cell nucleus
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Cellular Componentviral capsid
Cellular Componentviral envelope
Cellular Componentvirion membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionchannel activity
Molecular Functiondouble-stranded RNA binding
Molecular Functionmetal ion binding
Molecular FunctionmRNA (nucleoside-2'-O-)-methyltransferase activity
Molecular FunctionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
Molecular Functionprotein dimerization activity
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionserine-type endopeptidase activity
Molecular Functionstructural molecule activity
Biological Processclathrin-dependent endocytosis of virus by host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processinduction by virus of host autophagy
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity
Biological Processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell
Biological Processvirus-mediated perturbation of host defense response

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    P17763
  • Secondary accessions
    • P27910
    • P89313
    • P89314

Proteomes

Subcellular Location

Capsid protein C

Host nucleus
Host cytoplasm

Peptide pr

Secreted

Small envelope protein M

Virion membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Envelope protein E

Virion membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Non-structural protein 1

Secreted
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Located in RE-derived vesicles hosting the replication complex.

Non-structural protein 2A

Host endoplasmic reticulum membrane
; Multi-pass membrane protein

Serine protease subunit NS2B

Host endoplasmic reticulum membrane ; Multi-pass membrane protein

Serine protease NS3

Host endoplasmic reticulum membrane
; Peripheral membrane protein
Note: Remains non-covalently associated to serine protease subunit NS2B.

Non-structural protein 4A

Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Host mitochondrion
Note: Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes.

Non-structural protein 4B

Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Note: Located in RE-derived vesicles hosting the replication complex.

RNA-directed RNA polymerase NS5

Host endoplasmic reticulum membrane
; Peripheral membrane protein
Host nucleus
Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes.

Features

Showing features for topological domain, transmembrane, intramembrane.

TypeIDPosition(s)Description
Topological domain1-101Cytoplasmic
Transmembrane102-119Helical
Topological domain120-242Extracellular
Transmembrane243-260Helical
Topological domain261Cytoplasmic
Transmembrane262-280Helical
Topological domain281-725Extracellular
Transmembrane726-746Helical
Topological domain747-752Cytoplasmic
Transmembrane753-773Helical
Topological domain774-1195Extracellular
Transmembrane1196-1220Helical
Topological domain1221-1226Cytoplasmic
Transmembrane1227-1245Helical
Topological domain1246-1269Lumenal
Transmembrane1270-1290Helical
Topological domain1291Cytoplasmic
Transmembrane1292-1310Helical
Topological domain1311-1315Lumenal
Transmembrane1316-1336Helical
Topological domain1337-1351Cytoplasmic
Transmembrane1352-1370Helical
Topological domain1371Lumenal
Transmembrane1372-1391Helical
Topological domain1392-1447Cytoplasmic
Intramembrane1448-1468Helical
Topological domain1469-2148Cytoplasmic
Transmembrane2149-2169Helical
Topological domain2170-2171Lumenal
Intramembrane2172-2192Helical
Topological domain2193Lumenal
Transmembrane2194-2214Helical
Topological domain2215-2229Cytoplasmic
Transmembrane2230-2244Helical; Note=Signal for NS4B
Topological domain2245-2276Lumenal
Intramembrane2277-2297Helical
Topological domain2298-2349Lumenal
Transmembrane2350-2370Helical
Topological domain2371-2415Cytoplasmic
Transmembrane2416-2436Helical
Topological domain2437-2461Lumenal
Transmembrane2462-2482Helical
Topological domain2483-3392Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant125-126in strain: Isolate Philippines/836-1/1984
Natural variant142in strain: Isolate Philippines/836-1/1984
Natural variant171-173in strain: Isolate Philippines/836-1/1984
Natural variant186in strain: Isolate Philippines/836-1/1984
Natural variant210in strain: Isolate Philippines/836-1/1984
Natural variant251in strain: Isolate Philippines/836-1/1984
Natural variant441in strain: Isolate Philippines/836-1/1984
Natural variant475in strain: Isolate Philippines/836-1/1984
Natural variant482in strain: Isolate 45AZ5
Natural variant573in strain: Isolate 45AZ5
Natural variant677in strain: Isolate Philippines/836-1/1984
Natural variant786in strain: Isolate Philippines/836-1/1984
Mutagenesis1138Impaired virion assembly.
Mutagenesis1147Impaired virion assembly.
Mutagenesis1227Impaired virion assembly.
Mutagenesis1252Complete loss of viral RNA synthesis.
Mutagenesis1314Impaired virion assembly.
Mutagenesis1315Impaired virion assembly.
Mutagenesis1327Complete loss of viral RNA synthesis.
Natural variant1689-1692in strain: Isolate 45AZ5
Natural variant2242in strain: Isolate 45AZ5
Natural variant2357in strain: Isolate 45AZ5
Natural variant2543in strain: Isolate 45AZ5
Natural variant2779in strain: Isolate 45AZ5
Natural variant3337in strain: Isolate 45AZ5

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, propeptide, glycosylation, disulfide bond, modified residue, peptide.

TypeIDPosition(s)Description
ChainPRO_00002646581-100Capsid protein C
ChainPRO_00004052071-3392Genome polyprotein
PropeptidePRO_0000264659101-114ER anchor for the capsid protein C, removed in mature form by serine protease NS3
ChainPRO_0000264661115-205Peptide pr
ChainPRO_0000264660115-280Protein prM
Glycosylation183N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000264662206-280Small envelope protein M
ChainPRO_0000264663281-775Envelope protein E
Disulfide bond283↔310
Disulfide bond340↔401
Glycosylation347N-linked (GlcNAc...) asparagine; by host
Disulfide bond354↔385
Disulfide bond372↔396
Glycosylation433N-linked (GlcNAc...) asparagine; by host
Disulfide bond465↔565
Disulfide bond582↔613
ChainPRO_0000264664776-1127Non-structural protein 1
Disulfide bond779↔790
Disulfide bond830↔918
Glycosylation905N-linked (GlcNAc...) asparagine; by host
Disulfide bond954↔998
Glycosylation982N-linked (GlcNAc...) asparagine; by host
Disulfide bond1055↔1104
Disulfide bond1066↔1088
Disulfide bond1087↔1091
ChainPRO_00002646661128-1345Non-structural protein 2A
Glycosylation1190N-linked (GlcNAc...) asparagine; by host
ChainPRO_00002646671346-1475Serine protease subunit NS2B
ChainPRO_00002646681476-2094Serine protease NS3
Modified residue1864N6-acetyllysine; by host
ChainPRO_00002646692095-2221Non-structural protein 4A
PeptidePRO_00002646702222-2244Peptide 2k
ChainPRO_00002646712245-2493Non-structural protein 4B
Glycosylation2303N-linked (GlcNAc...) asparagine; by host
Glycosylation2307N-linked (GlcNAc...) asparagine; by host
Glycosylation2459N-linked (GlcNAc...) asparagine; by host
ChainPRO_00002646722494-3392RNA-directed RNA polymerase NS5
Modified residue2549Phosphoserine

Post-translational modification

RNA-directed RNA polymerase NS5

Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.

Genome polyprotein

Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by the Serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.

Protein prM

Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.

Non-structural protein 1

N-glycosylated (PubMed:10364366, PubMed:8176380).
The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells

Serine protease NS3

Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication.

RNA-directed RNA polymerase NS5

Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.

Envelope protein E

N-glycosylated.

Keywords

Interaction

Subunit

Capsid protein C

Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus) (PubMed:19889084, PubMed:23522008); this interaction results in EXOC1 degradation through the proteasome degradation pathway (PubMed:23522008).

Protein prM

Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (PubMed:9971841).

Envelope protein E

Homodimer; in the endoplasmic reticulum and Golgi (PubMed:11893341).
Interacts with protein prM (PubMed:9971841).
Interacts with non-structural protein 1 (PubMed:26562291).

Non-structural protein 1

Homodimer; Homohexamer when secreted (PubMed:10364366, PubMed:2827377).
Interacts with envelope protein E (PubMed:26562291).

Non-structural protein 2A

Interacts (via N-terminus) with serine protease NS3.

Serine protease subunit NS2B

Forms a heterodimer with serine protease NS3 (PubMed:20042502).
May form homooligomers (PubMed:26728778).

Serine protease NS3

Forms a heterodimer with NS2B (PubMed:20042502).
Interacts with NS4B (PubMed:16894199).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (PubMed:15917225, PubMed:19850911).
Interacts with host SHFL (PubMed:27974568).

Non-structural protein 4A

Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta (PubMed:27252539).
Interacts with host SHFL (PubMed:27974568).
Interacts with host AUP1; the interaction occurs in the presence of Dengue virus NS4B and induces lipophagy which facilitates production of virus progeny particles (By similarity).

Non-structural protein 4B

Interacts with serine protease NS3 (PubMed:16894199).

RNA-directed RNA polymerase NS5

Homodimer (PubMed:26895240).
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (PubMed:19279106).
Interacts with serine protease NS3 (PubMed:15917225, PubMed:19850911).

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region1-15Interaction with host EXOC1
Region37-72Hydrophobic; homodimerization of capsid protein C
Region378-391Fusion peptide
Region1398-1437Interacts with and activates NS3 protease
Domain1476-1653Peptidase S7
Domain1656-1812Helicase ATP-binding
Region1660-1663Important for RNA-binding
Motif1760-1763DEAH box
Domain1822-1988Helicase C-terminal
Domain2495-2756mRNA cap 0-1 NS5-type MT
Motif2570-2573SUMO-interacting motif
Domain3020-3169RdRp catalytic

Domain

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.

Sequence similarities

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    3,392
  • Mass (Da)
    378,702
  • Last updated
    2006-12-12 v2
  • Checksum
    3A7C57D3054D2972
MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKVLRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTTATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLTMEKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVTDKEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEVHTWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVSGILAQGKKMIRPQPMEHKYSWKSWGKAKIIGADVQNTTFIIDGPNTPECPDNQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQVCDHRLMSAAIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCIWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTAGPWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKTIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENLVKSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLTMGQLTWNDLIRLCIMVGANASDKMGMGTTYLALMATFRMRPMFAVGLLFRRLTSREVLLLTVGLSLVASVELPNSLEELGDGLAMGIMMLKLLTDFQSHQLWATLLSLTFVKTTFSLHYAWKTMAMILSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLITENKIWGRKSWPLNEGIMAVGIVSILLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTLTILLKATLLAISGVYPMSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRILQRGLLGRSQVGVGVFQEGVFHTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNAGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGAIALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYLPAIVREAIRRNVRTLVLAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYDWITDFPGKTVWFVPSIKSGNDIANCLRKNGKRVVQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILAGPMPVTVASAAQRRGRIGRNQNKEGDQYIYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLRGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEIWTKEGERKKLRPRWLDARTYSDPLALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGKAYRHAMEELPDTIETLMLLALIAVLTGGVTLFFLSGRGLGKTSIGLLCVIASSALLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMILTAAANEMGLLETTKKDLGIGHAAAENHHHAAMLDVDLHPASAWTLYAVATTIITPMMRHTIENTTANISLTAIANQAAILMGLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVFMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDLDPVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSLMKSLGGGRRGTGAQGETLGEKWKRQLNQLSKSEFNTYKRSGIIEVDRSEAKEGLKRGEPTKHAVSRGTAKLRWFVERNLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDIGESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNIVSAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKNGHKSTWHYDEDNPYKTWAYHGSYEVKPSGSASSMVNGVVRLLTKPWDVIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRNKKPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQNEAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGIFSPSELETPNLAERVLDWLKKHGTERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPFCSHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWVPTSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDRWCGSLIGLTARATWATNIQVAINQVRRLIGNENYLDFMTSMKRFKNESDPEGALW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U88535
EMBL· GenBank· DDBJ
AAB70694.1
EMBL· GenBank· DDBJ
Genomic RNA
U88536
EMBL· GenBank· DDBJ
AAB70695.1
EMBL· GenBank· DDBJ
Genomic RNA
M23027
EMBL· GenBank· DDBJ
AAA42940.1
EMBL· GenBank· DDBJ
Genomic RNA
D00503
EMBL· GenBank· DDBJ
BAA00395.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

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