A0A3Q9JZM3 · A0A3Q9JZM3_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.
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.
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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site1555Charge relay system; for serine protease NS3 activity
Active site1579Charge relay system; for serine protease NS3 activity
Active site1639Charge relay system; for serine protease NS3 activity
Binding site2583S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2613S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2614S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2631S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2632S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2658S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2659S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2747S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site2967Zn2+ 1 (UniProtKB | ChEBI)
Binding site2971Zn2+ 1 (UniProtKB | ChEBI)
Binding site2976Zn2+ 1 (UniProtKB | ChEBI)
Binding site2979Zn2+ 1 (UniProtKB | ChEBI)
Binding site3244Zn2+ 2 (UniProtKB | ChEBI)
Binding site3260Zn2+ 2 (UniProtKB | ChEBI)
Binding site3379Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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 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 STAT1 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

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

  • Taxonomic identifier
  • Strain
    • SH7
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus japonicum

Accessions

  • Primary accession
    A0A3Q9JZM3

Subcellular Location

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

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane111-130Helical
Transmembrane254-273Helical
Transmembrane280-301Helical
Transmembrane746-767Helical
Transmembrane774-794Helical
Transmembrane1182-1200Helical
Transmembrane1220-1239Helical
Transmembrane1251-1274Helical
Transmembrane1280-1304Helical
Transmembrane1342-1365Helical
Transmembrane1377-1395Helical
Transmembrane1477-1497Helical
Transmembrane2173-2193Helical
Transmembrane2200-2220Helical
Transmembrane2226-2244Helical
Transmembrane2256-2278Helical
Transmembrane2311-2328Helical
Transmembrane2366-2392Helical

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond297↔324
Disulfide bond354↔410
Disulfide bond368↔399
Disulfide bond386↔415
Disulfide bond484↔581
Disulfide bond598↔629

Keywords

Interaction

Subunit

Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.
Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway.
Homodimer; Homohexamer when secreted. Interacts with envelope protein E. NS1 interacts with NS4B. Interacts with host complement protein CFH; this interaction leads to the degradation of C3.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1374-1504Flavivirus NS2B
Domain1505-1682Peptidase S7
Domain1685-1841Helicase ATP-binding
Domain1852-2017Helicase C-terminal
Region1950-1972Disordered
Domain2528-2793MRNA cap 0-1 NS5-type MT
Domain3057-3209RdRp catalytic

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    3,432
  • Mass (Da)
    379,990
  • Last updated
    2019-04-10 v1
  • Checksum
    3DC0EED622530FF1
MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKHLTSFKRELGTLIDAVNKRGKKQNKRGGNESLIMWLASLAIVTACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVHTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAVALGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLEGDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCGLFGKGSIDTCAKFSCTSKAIGRMIQPENIKYAVGIFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEVTLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLSLPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQALAGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELTYSGSDGPCKIPIVSVASLNDMTPVGRLVTVNPFVATSSSNSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLAALGDTAWDFGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAIDITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHQEGVCGVRSVTRLEHQMWESVRDELNVLLKENAVDLSVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDERRAWNSMQIEDFGFGITSTRVWLKIREENTDGCDGAIIGTAVKGHVAVHSDLSYWIESRLNDTWKLERAVFGEVKSCTWPETHTLWGDGVEESELIIPHTIAGPRSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSIRTTTDSGKLITDWCCRSCSLPPLRFRTENGCWYGMEIRPVRHDETTLVRSQVDAFNGEMIDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYTDLARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSARWTNQENVVLVLGAAFFQLASVDLQIGVHGILNAAAIAWMIVRAITFPTTSTVAMPILALLTPGMRALYLDTYRIILLVIGICSLLQERRKTMAKKKGAVLLGLALTSTGWFSPTTIAAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLDRAADISWEMEAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWLLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCLKGDTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRISYGGPWRFDRKWNGTDDVQVIVVEPGKPAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVPDAYTPSMLKKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNEIVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDLQDEIPDRAWSSGYEWITDYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIMLDNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILEDNTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGGKAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLVALLLMVVLIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGRTQAPGLTGLPSMALDLRPATAWALYGGSTVVLTPLLKHLITSEYVTTSLASISSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLVTLHYGYMLPGWQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLTLWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSRDEFFKYRREAIIEVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVKGYTKGGAGHEEPMLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIEKMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVHSDQKKIRKRIQKLREEFATTWHKDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPAGVKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVGDPLFWEMVNEERENHLRGECHTCVYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSGVQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVKPLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNVKDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKTPITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAIIGKENYVDYMTSLRRYEDVLIQEDRVI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH753129
EMBL· GenBank· DDBJ
AZS59361.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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