{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"F6Z587","uniProtkbId":"F6Z587_HORSE","entryAudit":{"firstPublicDate":"1111-11-10","lastAnnotationUpdateDate":"1111-11-10","lastSequenceUpdateDate":"1111-11-10","entryVersion":1,"sequenceVersion":1},"annotationScore":0.0,"proteinExistence":"5: Uncertain","proteinDescription":{"recommendedName":{"fullName":{"value":"Uncharacterized protein"}}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0008006","source":"Google","id":"ProtNLM2","properties":[{"key":"model_score","value":"0.46"},{"key":"phmmer_accession","value":"Q4R6F8"},{"key":"phmmer_score","value":"60.6"}]}],"value":"Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0008006","source":"Google","id":"ProtNLM2","properties":[{"key":"model_score","value":"0.95"},{"key":"phmmer_accession","value":"P10809"},{"key":"phmmer_score","value":"1099.6"}]}],"value":"Mitochondrion matrix","id":"SL-0170"}}]}],"references":[{"referenceNumber":1,"citation":{"id":"CI-FC84BSHK1H4IL","citationType":"unpublished observations"},"referencePositions":["required field"]}],"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1}}}