Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
CPT2 Deficiency Modeled in Zebrafish: Abnormal Neural Development, Electrical Activity, Behavior, and Schizophrenia-Related Gene Expression.
-
CPT2 is an inner mitochondrial membrane protein of the carnitine shuttle acting in long-chain fatty acid beta-oxidation.
"Carnitine palmitoyltransferase 2 (CPT2) is an inner mitochondrial membrane protein of the carnitine shuttle and is involved in the beta-oxidation of long chain fatty acids"
-
CPT2 converts long-chain acylcarnitine to acyl-CoA at the inner mitochondrial membrane.
"carnitine palmitoyltransferase 2 (CPT2) that converts the long-chain acylcarnitine to acyl-CoA for oxidation in the inner mitochondrial membrane"
-
Knockdown in zebrafish disturbs lipid utilization and deposition, body size and brain development.
"CPT2 knockdown resulted in abnormal lipid utilization and deposition, reduction in body size, and abnormal brain development"
-
Neural and behavioral phenotypes follow CPT2 knockdown in zebrafish.
"Axonal projections, neurotransmitter synthesis, electrical hyperactivity, and swimming behavior were disrupted in CPT2 knockdown zebrafish"
-
Zebrafish Cpt2 protein is present in mitochondrial fractions isolated from larvae.
"A representative Western blot of CPT2 protein levels isolated from the mitochondrial fraction of 200 WT, CTRL-injected, TB-injected, and SB-injected zebrafish is shown"
Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling.
-
CPT2 is active with medium-chain (C8-C12) and long-chain (C14-C18) acyl-CoA esters but not with short-, very-long-chain or branched-chain substrates.
"We show that CPT2 is active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters, whereas virtually no activity was found with short- and very long-chain acyl-CoAs or with branched-chain amino acid oxidation intermediates"
-
Trans-2-enoyl-CoA intermediates are poor substrates.
"Trans-2-enoyl-CoA intermediates were also found to be poor substrates for CPT2."
UniProtKB entry Q5U3U3 for Danio rerio cpt2
-
Reconverts acylcarnitines to acyl-CoA esters for beta-oxidation.
"Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion"
-
Active with medium and long-chain acyl-CoA esters.
"Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters."
-
Peripheral protein on the matrix side of the mitochondrial inner membrane.
"SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side"
Falcon deep research report on Danio rerio cpt2 (Q5U3U3)
-
CPT2 has distinct CoA, acyl and carnitine binding sites, the structural basis for its substrate-specific acyltransferase chemistry.
"summarizes structural binding architecture (distinct CoA, acyl, and carnitine binding sites) and key residues implicated in catalysis and substrate binding"