Q6YMS4 · POLG_DEN3S

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. 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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.

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. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

Small envelope protein M

May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.

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. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

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 (By similarity).

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. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.

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
Site773-774Cleavage; by host signal peptidase
Site1125-1126Cleavage; by host
Site1343-1344Cleavage; by viral protease NS3
Site1473-1474Cleavage; by autolysis
Active site1524Charge relay system; for serine protease NS3 activity
Active site1548Charge relay system; for serine protease NS3 activity
Active site1608Charge relay system; for serine protease NS3 activity
Binding site1667-1674ATP (UniProtKB | ChEBI)
Site1931Involved in NS3 ATPase and RTPase activities
Site1934Involved in NS3 ATPase and RTPase activities
Site2092-2093Cleavage; by autolysis
Site2219-2220Cleavage; by viral protease NS3
Site2242-2243Cleavage; by host signal peptidase
Site2490-2491Cleavage; by viral protease NS3
Site2504mRNA cap binding
Site2507mRNA cap binding; via carbonyl oxygen
Site2508mRNA cap binding
Site2510mRNA cap binding; via carbonyl oxygen
Site2515mRNA cap binding
Site2519mRNA cap binding
Binding site2546S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2551For 2'-O-MTase activity
Site2551Essential for 2'-O-methyltransferase activity
Binding site2576S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2577S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2594S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2595S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2621S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2622S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site2636For 2'-O-MTase activity
Site2636Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
Binding site2637S-adenosyl-L-methionine (UniProtKB | ChEBI)
Site2640mRNA cap binding
Active site2670For 2'-O-MTase activity
Site2670Essential for 2'-O-methyltransferase activity
Site2701mRNA cap binding
Site2703mRNA cap binding
Active site2706For 2'-O-MTase activity
Site2706Essential for 2'-O-methyltransferase activity
Binding site2708S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2927Zn2+ 1 (UniProtKB | ChEBI)
Binding site2931Zn2+ 1 (UniProtKB | ChEBI)
Binding site2936Zn2+ 1 (UniProtKB | ChEBI)
Binding site2939Zn2+ 1 (UniProtKB | ChEBI)
Binding site3202Zn2+ 2 (UniProtKB | ChEBI)
Binding site3218Zn2+ 2 (UniProtKB | ChEBI)
Binding site3337Zn2+ 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

Gene names

    • Name
      pol

Organism names

Accessions

  • Primary accession
    Q6YMS4
  • Secondary accessions
    • Q6DLV0

Proteomes

Subcellular Location

Capsid protein C

Virion
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 domain1-100Cytoplasmic
Transmembrane101-120Helical
Topological domain121-243Extracellular
Transmembrane244-264Helical
Topological domain265Cytoplasmic
Transmembrane266-280Helical
Topological domain281-723Extracellular
Transmembrane724-744Helical
Topological domain745-750Cytoplasmic
Transmembrane751-771Helical
Topological domain772-1193Extracellular
Transmembrane1194-1218Helical
Topological domain1219-1224Cytoplasmic
Transmembrane1225-1243Helical
Topological domain1244-1267Lumenal
Transmembrane1268-1288Helical
Topological domain1289Cytoplasmic
Transmembrane1290-1308Helical
Topological domain1309-1315Lumenal
Transmembrane1316-1336Helical
Topological domain1337-1344Cytoplasmic
Transmembrane1345-1365Helical
Topological domain1366-1368Lumenal
Transmembrane1369-1389Helical
Topological domain1390-1443Cytoplasmic
Intramembrane1444-1464Helical
Topological domain1465-2146Cytoplasmic
Transmembrane2147-2167Helical
Topological domain2168-2169Lumenal
Intramembrane2170-2190Helical
Topological domain2191Lumenal
Transmembrane2192-2212Helical
Topological domain2213-2227Cytoplasmic
Transmembrane2228-2248Helical; Note=Signal for NS4B
Topological domain2249-2273Lumenal
Intramembrane2274-2294Helical
Topological domain2295-2305Lumenal
Intramembrane2306-2326Helical
Topological domain2327-2346Lumenal
Transmembrane2347-2367Helical
Topological domain2368-2412Cytoplasmic
Transmembrane2413-2433Helical
Topological domain2434-2458Lumenal
Transmembrane2459-2479Helical
Topological domain2480-3390Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant97
Natural variant684
Natural variant867
Natural variant1006
Natural variant1148
Natural variant1252
Natural variant1400
Natural variant1585
Natural variant1871
Natural variant2063
Natural variant2128
Natural variant2239
Natural variant2399
Natural variant2402
Mutagenesis252890% loss of 2'-O-MTase activity.
Mutagenesis253225% loss of 2'-O-MTase activity.
Mutagenesis2547Complete loss of 2'-O-MTase activity.
Mutagenesis2551Complete loss of 2'-O-MTase activity.
Mutagenesis257440% loss of 2'-O-MTase activity.
Mutagenesis2601Complete loss of 2'-O-MTase activity. Decreased thermostability both in the presence and absence of the RNA ligand.
Mutagenesis2636Complete loss of 2'-O-MTase activity.
Mutagenesis2670Complete loss of 2'-O-MTase activity.
Mutagenesis270198% loss of 2'-O-MTase activity.
Mutagenesis2706Complete loss of 2'-O-MTase activity.
Natural variant2856
Natural variant2862
Natural variant2864
Natural variant2970
Natural variant3093

Variants

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

The viewer provides 19 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_00002680881-100Capsid protein C
ChainPRO_00004052251-3390Genome polyprotein
PropeptidePRO_0000268089101-114ER anchor for the capsid protein C, removed in mature form by serine protease NS3
ChainPRO_0000268091115-205Peptide pr
ChainPRO_0000268090115-280Protein prM
Glycosylation183N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000268092206-280Small envelope protein M
ChainPRO_0000268093281-773Envelope 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 bond463↔563
Disulfide bond580↔611
ChainPRO_0000268094774-1125Non-structural protein 1
Disulfide bond777↔788
Disulfide bond828↔916
Glycosylation903N-linked (GlcNAc...) asparagine; by host
Disulfide bond952↔996
Glycosylation980N-linked (GlcNAc...) asparagine; by host
Disulfide bond1053↔1102
Disulfide bond1064↔1086
Disulfide bond1085↔1089
ChainPRO_00002680951126-1343Non-structural protein 2A
Glycosylation1132N-linked (GlcNAc...) asparagine; by host
Glycosylation1188N-linked (GlcNAc...) asparagine; by host
ChainPRO_00002680971344-1473Serine protease subunit NS2B
ChainPRO_00002680981474-2092Serine protease NS3
Modified residue1862N6-acetyllysine; by host
ChainPRO_00002680992093-2219Non-structural protein 4A
PeptidePRO_00002681002220-2242Peptide 2k
ChainPRO_00002681012243-2490Non-structural protein 4B
Glycosylation2300N-linked (GlcNAc...) asparagine; by host
Glycosylation2304N-linked (GlcNAc...) asparagine; by host
Glycosylation2456N-linked (GlcNAc...) asparagine; by host
ChainPRO_00002681022491-3390RNA-directed RNA polymerase NS5
Modified residue2546Phosphoserine

Post-translational modification

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 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.

Envelope protein E

N-glycosylated.

Non-structural protein 1

N-glycosylated. 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

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

RNA-directed RNA polymerase NS5

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

Keywords

PTM databases

Interaction

Subunit

Capsid protein C

Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity).

Protein prM

Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity).

Envelope protein E

Homodimer; in the endoplasmic reticulum and Golgi (By similarity).
Interacts with protein prM. Interacts with non-structural protein 1 (By similarity).

Non-structural protein 1

Homodimer; Homohexamer when secreted (By similarity).
Interacts with envelope protein E (By similarity).

Non-structural protein 2A

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

Serine protease subunit NS2B

Forms a heterodimer with serine protease NS3 (By similarity).
May form homooligomers (By similarity).

Serine protease NS3

Forms a heterodimer with NS2B. Interacts with NS4B (By similarity).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity).
Interacts with host SHFL (By similarity).

Non-structural protein 4A

Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta (By similarity).
Interacts with host SHFL (By similarity).
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.

RNA-directed RNA polymerase NS5

Homodimer (PubMed:24025331).
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3

Chemistry

Structure

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
Region1396-1435Interacts with and activates NS3 protease
Domain1474-1651Peptidase S7
Domain1654-1810Helicase ATP-binding
Region1658-1661Important for RNA-binding
Motif1758-1761DEAH box
Domain1820-1986Helicase C-terminal
Domain2492-2753mRNA cap 0-1 NS5-type MT
Motif2567-2570SUMO-interacting motif
Domain3018-3168RdRp 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
    3,390
  • Mass (Da)
    377,923
  • Last updated
    2004-07-05 v1
  • Checksum
    14C0E2C0C9189CCB
MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSKGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKVLKGFKKEISNMLSIINQRKKTSLCLMMILPAALAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCDDTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETWALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPTLDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQCLEPIEGKVVQYENLKYTVIITVHTGDQHQVGNETQGVTAEITPQASTTEAILPEYGTLGLECSPRTGLDFNEMILLTMKNKAWMVHRQWFFDLPLPWASGATTETPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGHLKCRLKMDKLELKGMSYAMCTNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKEEPVNIEAEPPFGESNIVIGIGDNALKINWYKKGSSIGKMFEATERGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGSAYTALFSGVSWVMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHTWTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDTLGVLEQGKRTLTPQPMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAAVKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWTNGVLESDMIIPKSLAGPISQHNYRPGYHTQTAGPWHLGKLELDFNYCEGTTVVITESCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPISEKEENMVKSLVSAGSGKVDNFTMGVLCLAILFEEVLRGKFGKKHMIAGVFFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTYLALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGVALGLMALKLITQFETYQLWTALVSLTCSNTIFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSILASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAPDVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTVLLKTALLIVSGIFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFHTMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTTPGTFQTTTGEIGAIALDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPAIVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFAGKTVWFVPSIKAGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGPMPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLKGESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGQRNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLALKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEDGGRAYRHAVEELPETMETLLLLGLMILLTGGAMLFLISGKGIGKTSIGLICVIASSGMLWMAEVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAATIAANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGLDKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLITHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDSVIFDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEALTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSIMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGETTHHAVSRGSAKLQWFVERNMVVPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGESSPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSSVNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHNSTWHYDDENPYKTWAYHGSYEVKATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKAMEITAEWLWRTLGRNKRPRLCTREEFTKKVRTNAAMGAVFTEENQWDSAKAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEEKIIQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPTGTVMDIISRKDQRGSGQLGTYGLNTFTNMEAQLVRQMEGEGVLTKADLENPHLLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCSHHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPTSRTTWSIHAHHQWMTTEDMLTVWNRVWIEENPWMEDKTPVTTWENVPYLGKREDQWCGSLIGLTSRATWAQNIPTAIQQVRSLIGNEEFLDYMPSMKRFRKEEESEGAIW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY099336
EMBL· GenBank· DDBJ
AAM51537.1
EMBL· GenBank· DDBJ
Genomic RNA
AY662691
EMBL· GenBank· DDBJ
AAT75224.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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