<Entry>
<Accession>A8E5V9</Accession>
        <ProteinName>Stimulator</ProteinName>
        <GeneName>sting1</GeneName>
        <OS_id>8364</OS_id>
        <ReferenceProteome>None</ReferenceProteome>
        <SubcellularLocation>
<Location>SL-0198</Location>
<Comments>Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited (PubMed:30842662). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842662}.</Comments>
</SubcellularLocation>
<CrossReferences>
<CrossReference>
<Database>UNIPROT</Database>
<ID>A8E5V9</ID>
</CrossReference>
<CrossReference>
<Database>Pfam</Database>
<ID>PF15009</ID>
</CrossReference>
</CrossReferences>
<Function>Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Exhibits guanine base- specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling (PubMed:26300263). {ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:30842662}.</Function>
<OntologyTerms>
<Ontology>GO:0005776</Ontology>
<Ontology>GO:0000421</Ontology>
<Ontology>GO:0005737</Ontology>
<Ontology>GO:0031410</Ontology>
<Ontology>GO:0005789</Ontology>
<Ontology>GO:0033116</Ontology>
<Ontology>GO:0000139</Ontology>
<Ontology>GO:0016021</Ontology>
<Ontology>GO:0048471</Ontology>
<Ontology>GO:0061507</Ontology>
<Ontology>GO:0035438</Ontology>
<Ontology>GO:0042803</Ontology>
<Ontology>GO:0002218</Ontology>
<Ontology>GO:0000045</Ontology>
<Ontology>GO:0051607</Ontology>
<Ontology>GO:0045087</Ontology>
<Ontology>GO:0032728</Ontology>
<Ontology>GO:0016239</Ontology>
<Ontology>GO:0032481</Ontology>
<Ontology>GO:0061709</Ontology>
</OntologyTerms>
<Topology>
        <Type>Transmembrane</Type>
        <Source>UniProt</Source>
        <Annotation>Sequence Analysis {ECO:0000255}</Annotation>
        </Topology>
<Sequence>MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQQHSEEYSML</Sequence>
        <SequenceLength>329</SequenceLength>
        </Entry>