| IED ID | IndEnz0002000013 |
| Enzyme Type ID | protease000013 |
| Protein Name |
Genome polyprotein Cleaved into: Capsid protein C Capsid protein Core protein ; Protein prM Precursor membrane protein ; Peptide pr Peptide precursor ; Small envelope protein M Matrix protein ; Envelope protein E; Non-structural protein 1 NS1 ; Non-structural protein 2A NS2A ; Serine protease subunit NS2B Flavivirin protease NS2B regulatory subunit Non-structural protein 2B ; Serine protease NS3 EC 3.4.21.91 EC 3.6.1.15 EC 3.6.4.13 Flavivirin protease NS3 catalytic subunit Non-structural protein 3 ; Non-structural protein 4A NS4A ; Peptide 2k; Non-structural protein 4B NS4B ; RNA-directed RNA polymerase NS5 EC 2.1.1.56 EC 2.1.1.57 EC 2.7.7.48 NS5 |
| Gene Name | |
| Organism | Zika virus (isolate ZIKV/Human/Cambodia/FSS13025/2010) (ZIKV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Flasuviricetes Amarillovirales Flaviviridae Flavivirus (arboviruses group B) Zika virus (ZIKV) Zika virus (isolate ZIKV/Human/Cambodia/FSS13025/2010) (ZIKV) |
| Enzyme Sequence | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGTDTSVGIVGLLLTTAMAVEVTRRGNAYYMYLDRSDAGEAISFPTTMGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAAKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVPINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMMRRIIGDEEKYVDYLSTQVRYLGEEGSTPGVL |
| Enzyme Length | 3423 |
| Uniprot Accession Number | A0A142I5B9 |
| Absorption | |
| Active Site | ACT_SITE 1553; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 1577; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 1637; /note=Charge relay system; for serine protease NS3 activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00860; ACT_SITE 2581; /note=For 2'-O-MTase activity; /evidence=ECO:0000250|UniProtKB:Q6YMS4; ACT_SITE 2666; /note=For 2'-O-MTase activity; /evidence=ECO:0000250|UniProtKB:Q6YMS4; ACT_SITE 2702; /note=For 2'-O-MTase activity; /evidence=ECO:0000250|UniProtKB:Q6YMS4; ACT_SITE 2738; /note=For 2'-O-MTase activity; /evidence=ECO:0000250|UniProtKB:Q6YMS4 |
| Activity Regulation | |
| Binding Site | BINDING 2576; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2606; /note=S-adenosyl-L-methionine; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2607; /note=S-adenosyl-L-methionine; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2624; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2625; /note=S-adenosyl-L-methionine; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2630; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:A0A024B7W1; BINDING 2631; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:A0A024B7W1; BINDING 2651; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2652; /note=S-adenosyl-L-methionine; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2666; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:A0A024B7W1; BINDING 2667; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924; BINDING 2740; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00924 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q9Q6P4}; |
| DNA Binding | |
| EC Number | 3.4.21.91; 3.6.1.15; 3.6.4.13; 2.1.1.56; 2.1.1.57; 2.7.7.48 |
| Enzyme 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 the 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. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. 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. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [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. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (PubMed:32641828). In addition, host NCAM1 can also be used as entry receptor (PubMed:32753727). Interaction with host HSPA5 plays an important role in the early stages of infection as well (PubMed:33432092). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32753727, ECO:0000269|PubMed:33432092}.; FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (PubMed:31662457). Antagonizes also the host alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:31662457}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [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 (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Plays also a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (By similarity). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 1696..1703; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541; NP_BIND 2533..2539; /note=GTP; /evidence=ECO:0000250|UniProtKB:A0A024B7W1; NP_BIND 2669..2675; /note=GTP; /evidence=ECO:0000250|UniProtKB:A0A024B7W1; NP_BIND 2733..2735; /note=GTP; /evidence=ECO:0000250|UniProtKB:A0A024B7W1 |
| Features | Active site (7); Beta strand (10); Binding site (12); Chain (13); Cross-link (2); Disulfide bond (10); Domain (5); Glycosylation (4); Intramembrane (4); Metal binding (7); Modified residue (1); Motif (2); Mutagenesis (4); Nucleotide binding (4); Peptide (1); Propeptide (1); Region (7); Site (27); Topological domain (22); Transmembrane (17) |
| Keywords | 3D-structure;ATP-binding;Activation of host autophagy by virus;Capsid protein;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;GTP-binding;Glycoprotein;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Host nucleus;Host-virus interaction;Hydrolase;Inhibition of host STAT2 by virus;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Isopeptide bond;Membrane;Metal-binding;Methyltransferase;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-binding;RNA-directed RNA polymerase;S-adenosyl-L-methionine;Secreted;Serine protease;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation;Viral RNA replication;Viral attachment to host cell;Viral immunoevasion;Viral penetration into host cytoplasm;Virion;Virus entry into host cell;Zinc;mRNA capping;mRNA processing |
| Interact With | Q8N111; Q99653; Q9NWW5; Q4G0J3; Q9NX58; Q8NEJ9; O43251-6; O00767; Q16637; Q5BJD5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000269|PubMed:33432092}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}. |
| Modified Residue | MOD_RES 2576; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03314 |
| Post Translational Modification | PTM: [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. {ECO:0000250|UniProtKB:P17763}.; PTM: [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. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylation plays a role in virulence in mammalian and mosquito hosts, but may have no effect on neurovirulence. {ECO:0000250|UniProtKB:A0A024B7W1}.; PTM: [Envelope protein E]: Ubiquitination by host TRIM7 promotes virus attachment and fusion of the virus and the host endosome membrane. {ECO:0000269|PubMed:32641828}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated, which is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.; PTM: [RNA-directed RNA polymerase NS5]: Sumoylated, required for regulating IFN induced interferon stimulated genes/ISGs. {ECO:0000250|UniProtKB:A0A024B7W1}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 6UTA; 7BPK; 7BQ5; |
| Mapped Pubmed ID | 32321830; 34267374; |
| Motif | MOTIF 1787..1790; /note=DEAH box; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541; MOTIF 2908..2914; /note=Nuclear localization signal (NLS); /evidence=ECO:0000250|UniProtKB:Q32ZE1 |
| Gene Encoded By | |
| Mass | 379,109 |
| Kinetics | |
| Metal Binding | METAL 2959; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 2963; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 2968; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 2971; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 3234; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 3250; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q32ZE1; METAL 3369; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P14335 |
| Rhea ID | RHEA:67008; RHEA:67020; RHEA:21248; RHEA:23680; RHEA:13065 |
| Cross Reference Brenda |