A0A3Q9JZM3 · A0A3Q9JZM3_9FLAV
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3432 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
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
- ATP + H2O = ADP + phosphate + H+
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1555 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: H | ||||||
Active site | 1579 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: D | ||||||
Active site | 1639 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: S | ||||||
Binding site | 2583 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2613 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2614 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 2631 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 2632 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2658 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2659 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 2747 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 2967 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2971 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2976 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2979 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3244 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3260 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3379 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus japonicum
Accessions
- Primary accessionA0A3Q9JZM3
Subcellular Location
UniProt Annotation
GO Annotation
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Virion membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 111-130 | Helical | ||||
Sequence: LIMWLASLAIVTACAGAMKL | ||||||
Transmembrane | 254-273 | Helical | ||||
Sequence: WIIRNPGYAFLAVALGWMLG | ||||||
Transmembrane | 280-301 | Helical | ||||
Sequence: VVFTILLLLVAPAYSFNCLGMG | ||||||
Transmembrane | 746-767 | Helical | ||||
Sequence: LFGGMSWITQGLMGALLLWMGV | ||||||
Transmembrane | 774-794 | Helical | ||||
Sequence: IALAFLATGGVLVFLATNVHA | ||||||
Transmembrane | 1182-1200 | Helical | ||||
Sequence: AVLGALLVLMLGGITYTDL | ||||||
Transmembrane | 1220-1239 | Helical | ||||
Sequence: VLHLALIAVFKIQPAFLVMN | ||||||
Transmembrane | 1251-1274 | Helical | ||||
Sequence: VVLVLGAAFFQLASVDLQIGVHGI | ||||||
Transmembrane | 1280-1304 | Helical | ||||
Sequence: IAWMIVRAITFPTTSTVAMPILALL | ||||||
Transmembrane | 1342-1365 | Helical | ||||
Sequence: AVLLGLALTSTGWFSPTTIAAGLM | ||||||
Transmembrane | 1377-1395 | Helical | ||||
Sequence: ATEFLSAVGLMFAIVGGLA | ||||||
Transmembrane | 1477-1497 | Helical | ||||
Sequence: CIGLAALTPWAIVPAAFGYWL | ||||||
Transmembrane | 2173-2193 | Helical | ||||
Sequence: ALETITLIVAITVMTGGFFLL | ||||||
Transmembrane | 2200-2220 | Helical | ||||
Sequence: IGKMGLGALVLTLATFFLWAA | ||||||
Transmembrane | 2226-2244 | Helical | ||||
Sequence: KIAGTLLVALLLMVVLIPE | ||||||
Transmembrane | 2256-2278 | Helical | ||||
Sequence: LAVFLICVLTVVGVVAANEYGML | ||||||
Transmembrane | 2311-2328 | Helical | ||||
Sequence: ATAWALYGGSTVVLTPLL | ||||||
Transmembrane | 2366-2392 | Helical | ||||
Sequence: TVGLVFLGCWGQITLTTFLTAMVLVTL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 297↔324 | |||||
Sequence: CLGMGNRDFIEGASGATWVDLVLEGDSC | ||||||
Disulfide bond | 354↔410 | |||||
Sequence: CYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCGLFGKGSIDTC | ||||||
Disulfide bond | 368↔399 | |||||
Sequence: CPTTGEAHNEKRADSSYVCKQGFTDRGWGNGC | ||||||
Disulfide bond | 386↔415 | |||||
Sequence: CKQGFTDRGWGNGCGLFGKGSIDTCAKFSC | ||||||
Disulfide bond | 484↔581 | |||||
Sequence: CEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLSLPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQALAGAIVVEYSSSVKLTSGHLKC | ||||||
Disulfide bond | 598↔629 | |||||
Sequence: CTEKFSFAKNPADTGHGTVVIELTYSGSDGPC |
Keywords
- PTM
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.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1374-1504 | Flavivirus NS2B | ||||
Sequence: GWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLDRAADISWEMEAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWLLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKR | ||||||
Domain | 1505-1682 | Peptidase S7 | ||||
Sequence: GGVFWDTPSPKPCLKGDTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRISYGGPWRFDRKWNGTDDVQVIVVEPGKPAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVPDA | ||||||
Domain | 1685-1841 | Helicase ATP-binding | ||||
Sequence: PSMLKKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNEIVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDLQ | ||||||
Domain | 1852-2017 | Helicase C-terminal | ||||
Sequence: GYEWITDYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIMLDNIHMPNGLVAQLYGPE | ||||||
Region | 1950-1972 | Disordered | ||||
Sequence: NPSPITSASAAQRRGRVGRNPNQ | ||||||
Domain | 2528-2793 | MRNA cap 0-1 NS5-type MT | ||||
Sequence: GRPGGRTLGEQWKEKLNAMSRDEFFKYRREAIIEVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVKGYTKGGAGHEEPMLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIEKMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRA | ||||||
Domain | 3057-3209 | RdRp catalytic | ||||
Sequence: GKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVKPLDDRFATA |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,432
- Mass (Da)379,990
- Last updated2019-04-10 v1
- Checksum3DC0EED622530FF1