A0A2S0T062 · A0A2S0T062_9FLAV

Function

function

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.
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.
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
Inhibits RNA silencing by interfering with host Dicer.
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).
May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.
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.
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.
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.
Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins.

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site1537Charge relay system; for serine protease NS3 activity
Active site1561Charge relay system; for serine protease NS3 activity
Active site1622Charge relay system; for serine protease NS3 activity
Binding site2945Zn2+ 1 (UniProtKB | ChEBI)
Binding site2949Zn2+ 1 (UniProtKB | ChEBI)
Binding site2954Zn2+ 1 (UniProtKB | ChEBI)
Binding site2957Zn2+ 1 (UniProtKB | ChEBI)
Binding site3222Zn2+ 2 (UniProtKB | ChEBI)
Binding site3238Zn2+ 2 (UniProtKB | ChEBI)
Binding site3357Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell nucleus
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Cellular Componentviral capsid
Cellular Componentvirion membrane
Molecular FunctionATP binding
Molecular Functiondouble-stranded RNA binding
Molecular FunctionGTP 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 Functionribonucleoside triphosphate phosphatase activity
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionserine-type endopeptidase activity
Molecular Functionstructural molecule activity
Biological Processfusion of virus membrane with host endosome membrane
Biological Processproteolysis
Biological Processsymbiont entry into host cell
Biological Processsymbiont-mediated suppression of host innate immune response
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

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 1122
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus flavi

Accessions

  • Primary accession
    A0A2S0T062

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein
Endoplasmic reticulum membrane
; Peripheral membrane protein
Endoplasmic reticulum membrane
; Peripheral membrane protein
Host endoplasmic reticulum membrane
; Multi-pass membrane protein
Host endoplasmic reticulum membrane
; Peripheral membrane protein
Host endoplasmic reticulum membrane
; Peripheral membrane protein
Host nucleus
Membrane
; Multi-pass membrane protein
Membrane
; Peripheral membrane protein
Secreted
Virion membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane105-125Helical
Transmembrane730-751Helical
Transmembrane758-778Helical
Transmembrane1133-1151Helical
Transmembrane1160-1182Helical
Transmembrane1202-1220Helical
Transmembrane1232-1249Helical
Transmembrane1293-1310Helical
Transmembrane1358-1376Helical
Transmembrane1382-1400Helical
Transmembrane1451-1477Helical
Transmembrane2157-2180Helical
Transmembrane2187-2204Helical
Transmembrane2210-2227Helical
Transmembrane2239-2256Helical
Transmembrane2293-2314Helical

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond288↔315
Disulfide bond345↔401
Disulfide bond359↔390
Disulfide bond377↔406
Disulfide bond467↔568
Disulfide bond585↔615

Keywords

Interaction

Subunit

Forms a heterodimer with serine protease NS3 (By similarity).
May form homooligomers
Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.
Homodimer; in the endoplasmic reticulum and Golgi (By similarity).
Interacts with protein prM (By similarity).
Interacts with non-structural protein 1
Interacts with serine protease NS3.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1355-1484Flavivirus NS2B
Domain1485-1665Peptidase S7
Domain1669-1825Helicase ATP-binding
Region1805-1826Disordered
Domain1820-1997Helicase C-terminal
Region1942-1963Disordered
Domain2507-2771MRNA cap 0-1 NS5-type MT
Domain3035-3187RdRp catalytic

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    3,411
  • Mass (Da)
    378,815
  • Last updated
    2018-07-18 v1
  • Checksum
    997742F15204A956
MSGRKAQGKTLGVNMVRRGVRSLSSKIKQKTKQIGSRPGPSRGVQGFVFFFLFNVLTGKKITAHLKKLWRMLDPRQGLVVLRKVKRVVASLMRGLSSRKRRSQDVLTIQFLILGMLLMVGGVTLVRRNRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKYWCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQKIERWLVRNPFFAATALAIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMAPDKPSLDISLETVAIDGPAEARKVCYSAVLTNVKINDKCPSTGEAHLEEENEGDNACKRTYSDRGWGNGCGLFGKGSIVACAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGRATLECQVQTAVDFSNSYIAEMEKESWIVDKQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIKVLALGNQEGSLKTALTGAMRVTKDTNNSKLYKLHGGHVACRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTAVMQVKVPKGAPCRIPVMVADDLTAAVNKGILVTVNPIASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFGSAGGFFTSVGKGIHTVFGSAFQGLFGGLSWITKVIMGVVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFVFRDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDSKNIYQRGTHPFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTMDCDGSILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKVQTNGPWMQVPLEVKREACPGTSVVVDGGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPKKTHDSHLVRSWVTAGEIHAIPFGLVSMMIAMEVVLRKRQGPKQILVGGMVLLGAXLVGQVTILDLLKLTVAVGLHFHEMNNGGDAMYMALIAAFSIRPGLLIGFGLRTLWSPRERLVLTLGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNVILPLMALLTPVTMAEVRLATMLFCTVVIIGVLHQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFMATRIFGRRSIPVNEALAAAGLVGVLAGLAFQEMENFLGPVAVGGILMMLVSVAGRVDGLELRKLGEVSWEEEAEISGSSARYDVTLSEQGEFKLLSEEKVPWDQVVMTSLALVGAAIHPFALLLVLAGWLFHVKGARRSGDVLWDIPTPKIIEECEYLEDGIYGIFQSTFLGASQRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLVPSWASVKEDLVAYGGSWKLDGRWDGEEEVQLIAAAPGKNVVNVQTKPSLFKVKNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTILDFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLEPTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWILADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEKEYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKPVLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIEGTKTPVSPGEMRLRDDQRRVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPLRPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVVLSELPDFLAKKGGEAVDTISVLLHSEEGSRAYRNALSMMPEAMTTVMLFVLAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGVKPTHISYIMLIFFVLMVVVVPEPGQQRTIQDNQVAYLIIGILTLISVVAANELGMLEKTKEDLFGKKNLIPSSAAPWSWPDFDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGNLSLSGIAQSASVLSFMDKGIPFMKMNISVIILLVSGWNSITVMPLLCGIGCAMLHWTLILPGIKAQQSKLAQRRVFHGVAKNPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSMTGVMRGNYYAFVGVMYNLWKMKTGRRGRANGKTLGEVWKRELNLLDKQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVAVSRGTAKLRWFHERGYVKLEGRVTDLGCGRGGWCYYAAAQREVSGVRGFTLGKEGHEKPMNVQSLGWNIITFKDKTDVHRLEPIKCDTLLCDIGESSPSSVTEGERTMRVLDTVEKWLSCGVESFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRNSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDRAAIEERVERIKSEYTATWFHDSDNPYRTWHYCGSYVTRTSGSAASMINGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKIMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAFLEEQEQWKTANEAVQDPKFWELVDEERRLHQQGRCRTCVYNMMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAALEGGGFYADDTAGWDTRITEADLDDEQEILNYMSPHHRKLALAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTITNLKVQLIRMAEAEMVIHHQHVQDCDDTALTKLEAWLAEHGCDRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKDISEWQPSKGWDDWESVPFCSHHFHELQLKDGRRIVVPCRDQDELVGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKRDMRLLSLAVSSAVPTSWVPQGRTTWSVHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTTVKEWRDIPYLTKRQDKLCGSLIGMTNRATWASHIHLVIHRIRTLIGKERYTDYLTVMDRYSVDADLQPGELI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MF170977
EMBL· GenBank· DDBJ
AWB14999.1
EMBL· GenBank· DDBJ
Genomic RNA

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