{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DTC1","uniProtkbId":"R1A_SARS2","entryAudit":{"firstPublicDate":"2020-04-22","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-04-22","entryVersion":31,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Severe acute respiratory syndrome coronavirus 2","commonName":"2019-nCoV","synonyms":["SARS-CoV-2"],"taxonId":2697049,"lineage":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus","Betacoronavirus pandemicum"]},"organismHosts":[{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606}],"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Replicase polyprotein 1a"},"shortNames":[{"value":"pp1a"}]},"alternativeNames":[{"fullName":{"value":"ORF1a polyprotein"}}],"contains":[{"recommendedName":{"fullName":{"value":"Host translation inhibitor nsp1"}},"alternativeNames":[{"fullName":{"value":"Leader protein"}},{"fullName":{"value":"Non-structural protein 1"},"shortNames":[{"value":"nsp1"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 2"},"shortNames":[{"value":"nsp2"}]},"alternativeNames":[{"fullName":{"value":"p65 homolog"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32726803"}],"value":"Papain-like protease nsp3"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37242344"}],"value":"3.2.2.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}],"value":"3.4.19.12"},{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 3"},"shortNames":[{"value":"nsp3"}]},{"fullName":{"value":"PL2-PRO"}},{"fullName":{"value":"Papain-like proteinase"},"shortNames":[{"value":"PL-PRO"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4"},"shortNames":[{"value":"nsp4"}]}},{"recommendedName":{"fullName":{"value":"3C-like proteinase nsp5"},"shortNames":[{"value":"3CL-PRO"},{"value":"3CLp"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39673710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40118151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41289387"}],"value":"3.4.22.69"}]},"alternativeNames":[{"fullName":{"value":"Main protease"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32272481"}],"value":"Mpro"}]},{"fullName":{"value":"Non-structural protein 5"},"shortNames":[{"value":"nsp5"}]},{"fullName":{"value":"SARS coronavirus main proteinase"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 6"},"shortNames":[{"value":"nsp6"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 7"},"shortNames":[{"value":"nsp7"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 8"},"shortNames":[{"value":"nsp8"}]}},{"recommendedName":{"fullName":{"value":"RNA-capping enzyme subunit nsp9"}},"alternativeNames":[{"fullName":{"value":"Non-structural protein 9"},"shortNames":[{"value":"nsp9"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"2.7.7.50"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 10"},"shortNames":[{"value":"nsp10"}]},"alternativeNames":[{"fullName":{"value":"Growth factor-like peptide"},"shortNames":[{"value":"GFL"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 11"},"shortNames":[{"value":"nsp11"}]}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein"}],"commentType":"FUNCTION","molecule":"Replicase polyprotein 1a"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32680882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33479166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36534661"}],"value":"Inhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:32680882, PubMed:32908316, PubMed:33080218, PubMed:33479166). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:32680882, PubMed:32908316, PubMed:33080218, PubMed:33479166). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:32680882, PubMed:32979938, PubMed:33080218). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). This inhibits the integrated stress response (ISR) in the infected cell by preventing EIF2S1/eIF2-alpha phosphorylation upstream of stress granule formation and depletes host G3BP1 (PubMed:36534661). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"Host translation inhibitor nsp1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35878012"}],"value":"Enhances mRNA repression of the 4EHP-GYF2 complex in the host, thereby inhibiting the antiviral response and facilitating SARS-CoV-2 replication. Possibly acts in cooperation with nsp1, which induces ribosome stalling on host mRNA, triggering mRNA repression by the host 4EHP-GYF2 complex which is enhanced by nsp2"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32578982"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32733001"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33727702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37242344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38652662"}],"value":"Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:35551511). Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (PubMed:35551511). Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (PubMed:35551511). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Also prevents host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803, PubMed:38652662). Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5) and STING1, but not RIGI (PubMed:33727702, PubMed:38652662). Contains an ADP-ribose hydrolase activity that binds ADP-ribose and catalyzes the removal of mono-ADP-ribose (de-MARylation), usually bound to a glutamate or aspartate (PubMed:32578982, PubMed:37242344). ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs) (PubMed:32578982)"}],"commentType":"FUNCTION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (PubMed:35551511)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35594856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37073102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38814682"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39673710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39773525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40118151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41289387"}],"value":"Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Cleaves and inactivates human TRMT1, preventing tRNA guanine(26)-dimethylation of tRNAs (PubMed:37073102, PubMed:38814682, PubMed:39773525). Inhibits host pyroptosis through the cleavage and inactivation of host gasdermin D/GSDMD (PubMed:39673710, PubMed:40118151). In contrast, it is able to activate GSDME-mediated pyroptosis in lung epithelial cells by mediating (1) the cleavage and inactivation of human GSDMD and catalyzing (2) cleavage and activation of human NLRP1, leading to concomitant initiation of GSDME-mediated pyroptosis, promoting the release of interleukins 1B, 6, 16 and 18 (PubMed:35594856). Also able to cleave and activate host gasdermins GSDMD and GSDME, thereby promoting unconventional secretion of the viral nucleocapsid through gasdermin pores into the host extracellular space (PubMed:39673710). In the host extracellular space, cleaves and inactivates IFNL1/IFN-lambda-1 (PubMed:39673710). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (PubMed:32198291, PubMed:32272481). Cleaves host STIM1 producing two functional fragments: STIM1 N-terminus, which inhibits MAVS-mediated IFNB signaling by disrupting signalosome formation, and STIM1 C-terminus, which suppresses p65-driven IFNB transcription (PubMed:41289387)"}],"commentType":"FUNCTION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (LDs) (PubMed:35551511). LDs are consumed during DMV formation (PubMed:35551511). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"}],"value":"Plays a role in viral RNA synthesis (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"}],"value":"Plays a role in viral RNA synthesis (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs (PubMed:35944563). The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate (PubMed:35944563). Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA (PubMed:35944563). The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures (PubMed:35944563). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"RNA-capping enzyme subunit nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease (By similarity) and nsp16 2'-O-methyltransferase activities (PubMed:35944563). Therefore plays an essential role in viral mRNAs cap methylation"}],"commentType":"FUNCTION","molecule":"Non-structural protein 10"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).","ecNumber":"3.4.19.12","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}]}},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = L-aspartyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54428"},{"database":"Rhea","id":"RHEA-COMP:9867"},{"database":"Rhea","id":"RHEA-COMP:13832"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29961"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:138102"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54429"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = L-glutamyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58248"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"Rhea","id":"RHEA-COMP:15089"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:142540"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58249"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"3C-like proteinase nsp5","reaction":{"name":"TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.","ecNumber":"3.4.22.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39673710"}]}},{"commentType":"CATALYTIC ACTIVITY","molecule":"RNA-capping enzyme subunit nsp9","reaction":{"name":"a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67012"},{"database":"Rhea","id":"RHEA-COMP:17165"},{"database":"Rhea","id":"RHEA-COMP:17166"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:167616"},{"database":"ChEBI","id":"CHEBI:167617"}],"ecNumber":"2.7.7.50","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:67014"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Inhibited ex vivo by K22. It may shift NSP6 zippering activity towards the nuclear envelope, thereby impairing formation of the NSP6-compartment necessary for viral transcription/replication"}],"commentType":"ACTIVITY REGULATION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}],"value":"Inhibited in vitro by GRL-0617"}],"commentType":"ACTIVITY REGULATION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"}],"value":"Inhibited by pyridone-containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2 replication in human lung cells (PubMed:32198291). Inhibited ex vivo by michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by compound 11a and 11b (PubMed:32321856)"}],"commentType":"ACTIVITY REGULATION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with host PHB and PHB2"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32763915"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35044811"}],"value":"May form homohexamers (PubMed:32763915). Interacts with N protein (PubMed:35044811)"}],"commentType":"SUBUNIT","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39223933"}],"value":"3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity (PubMed:32198291). Interacts with host FBXO22; this interaction promotes the proteasomal degradation of nsp5 (PubMed:39223933)"}],"commentType":"SUBUNIT","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with PL-PRO and nsp6"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Forms homodimers (PubMed:35551511). Interacts with host ZFYVE1 (DFCP1) (PubMed:35551511), which leads to ER and DMVs binding to lipid droplets. Interacts with host TBK1; this interaction decreases IRF3 phosphorylation by 57%, which leads to reduced IFN-beta production"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"value":"Interacts with nsp8 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33232691"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"value":"Interacts with nsp7, nsp13 and nsp12 (PubMed:33232691) to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"Is a dimer (By similarity). 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