{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0C6U8","secondaryAccessions":["P59641"],"uniProtkbId":"R1A_SARS","entryAudit":{"firstPublicDate":"2008-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-06-10","entryVersion":129,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Severe acute respiratory syndrome coronavirus","commonName":"SARS-CoV","taxonId":694009,"lineage":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus","Betacoronavirus pandemicum"]},"organismHosts":[{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606},{"scientificName":"Paguma larvata","commonName":"Masked palm civet","taxonId":9675}],"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":{"value":"Papain-like protease nsp3"},"shortNames":[{"value":"PL-PRO"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}],"value":"3.2.2.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17692280"}],"value":"3.4.19.12"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16306590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17692280"}],"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 3"},"shortNames":[{"value":"nsp3"}]},{"fullName":{"value":"PL2-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":"12917450"}],"value":"3.4.22.69"}]},"alternativeNames":[{"fullName":{"value":"Main protease"},"shortNames":[{"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":[{"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"}]}}]},"genes":[{"orfNames":[{"value":"1a"}]}],"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:0000269","source":"PubMed","id":"23035226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30943371"}],"value":"Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371)"}],"commentType":"FUNCTION","molecule":"Host translation inhibitor nsp1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19640993"}],"value":"May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16271890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17692280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19369340"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24622840"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24410069"},{"evidenceCode":"ECO:0000305"}],"value":"Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:17692280). 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 (By similarity). ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs) (Probable). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Also prevents host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)"}],"commentType":"FUNCTION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24410069"}],"value":"Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00772"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16226257"}],"value":"Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH"}],"commentType":"FUNCTION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24991833"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24410069"}],"value":"Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Plays a role in the initial induction of autophagosomes from host endoplasmic reticulum. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22039154"}],"value":"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"}],"commentType":"FUNCTION","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22039154"}],"value":"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"}],"commentType":"FUNCTION","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19153232"}],"value":"Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures"}],"commentType":"FUNCTION","molecule":"RNA-capping enzyme subunit nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22635272"}],"value":"Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation"}],"commentType":"FUNCTION","molecule":"Non-structural protein 10"},{"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":"12917450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"}]}},{"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":"12917450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17692280"}]}},{"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:0000250","source":"UniProtKB","id":"P0DTC1"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54429"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}]}]},{"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:0000250","source":"UniProtKB","id":"P0DTC1"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58249"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}]}]},{"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:0000250","source":"UniProtKB","id":"P0DTC1"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:67014"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}]}]},{"commentType":"COFACTOR","molecule":"Papain-like protease nsp3","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16306590"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.15,"unit":"mM","substrate":"peptide TSAVLQSGFRK-NH(2)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"}]},{"constant":0.58,"unit":"mM","substrate":"peptide SGVTFQGKFKK","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"}]},{"constant":1.44,"unit":"mM","substrate":"peptide ATVRLQAGNAT","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"}]}],"note":{"texts":[{"value":"The kinetic parameters are studied for the 3C-like proteinase domain."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"}],"value":"Optimum pH is 7.0 for 3C-like proteinase activity."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19640993"}],"value":"Interacts with host PHB and PHB2"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21345958"}],"value":"Interacts with papain-like protease and non-structural protein 6"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14561748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15507456"}],"value":"Exists as monomer and homodimer. Only the homodimer shows catalytic activity"}],"commentType":"SUBUNIT","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16228002"}],"value":"Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16228002"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17532020"}],"value":"Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (PubMed:16228002). Interacts with ORF6 protein (PubMed:17532020)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19153232"}],"value":"Homodimer"}],"commentType":"SUBUNIT","molecule":"RNA-capping enzyme subunit nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16873247"}],"value":"Homododecamer"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 10"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0C6U8","intActId":"EBI-15810860"},"interactantTwo":{"uniProtKBAccession":"P0C6U8","geneName":"1a","intActId":"EBI-15810860"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C6U8","intActId":"EBI-15810860"},"interactantTwo":{"uniProtKBAccession":"P0C6U8","geneName":"1a","chainId":"PRO_0000338259","intActId":"EBI-25496008"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000338257","intActId":"EBI-25635190"},"interactantTwo":{"uniProtKBAccession":"P05161","geneName":"ISG15","intActId":"EBI-746466"},"numberOfExperiments":5,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000338257","intActId":"EBI-25635190"},"interactantTwo":{"uniProtKBAccession":"Q64339","geneName":"Isg15","intActId":"EBI-8345781"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000338257","intActId":"EBI-25635190"},"interactantTwo":{"uniProtKBAccession":"L5LC70","geneName":"MDA_GLEAN10007532","intActId":"EBI-25760965"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000338257","intActId":"EBI-25635190"},"interactantTwo":{"uniProtKBAccession":"Q9H074-2","geneName":"PAIP1","intActId":"EBI-12101100"},"numberOfExperiments":7,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000338257","intActId":"EBI-25635190"},"interactantTwo":{"uniProtKBAccession":"P62992","geneName":"RPS27A","chainId":"PRO_0000396474","intActId":"EBI-25820711"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000338263","intActId":"EBI-25610723"},"interactantTwo":{"uniProtKBAccession":"P0C6U8","geneName":"1a","chainId":"PRO_0000338263","intActId":"EBI-25610723"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000338265","intActId":"EBI-25492625"},"interactantTwo":{"uniProtKBAccession":"P0C6X7","geneName":"rep","chainId":"PRO_0000037310","intActId":"EBI-25474098"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 2","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host endosome","id":"SL-0393"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Papain-like protease nsp3","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Host membrane","id":"SL-0380"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 4","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21345958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"}],"value":"Localizes in virally-induced cytoplasmic double-membrane vesicles"}]},"subcellularLocations":[{"location":{"value":"Host membrane","id":"SL-0380"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23943763"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"3C-like proteinase nsp5","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host Golgi apparatus","id":"SL-0395"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 6","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 7","note":{"texts":[{"value":"nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Host cytoplasm, host perinuclear region","id":"SL-0382"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host endoplasmic reticulum","id":"SL-0388"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 8","note":{"texts":[{"value":"nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17532020"}],"value":"Host cytoplasm, host perinuclear region","id":"SL-0382"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host endoplasmic reticulum","id":"SL-0388"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"RNA-capping enzyme subunit nsp9","note":{"texts":[{"value":"nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Host cytoplasm, host perinuclear region","id":"SL-0382"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Host endoplasmic reticulum","id":"SL-0388"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 10","note":{"texts":[{"value":"nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. 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