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cpt-3 Choline/carnitine acyltransferase domain-containing protein [ Caenorhabditis elegans ]

Gene ID: 190055, updated on 2-Nov-2024

Summary

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Official Symbol
cpt-3
Official Full Name
Choline/carnitine acyltransferase domain-containing protein
Primary source
WormBase:WBGene00021703
Locus tag
CELE_Y48G9A.10
See related
AllianceGenome:WB:WBGene00021703
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable carnitine O-palmitoyltransferase activity. Predicted to be involved in carnitine metabolic process and fatty acid metabolic process. Predicted to be located in membrane. Predicted to be active in mitochondrion. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See cpt-3 in Genome Data Viewer
Location:
chromosome: III
Exon count:
7
Sequence:
Chromosome: III; NC_003281.10 (2082819..2088314)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene Uncharacterized protein Neighboring gene Tyrosine-protein phosphatase domain-containing protein Neighboring gene pseudo Neighboring gene Protein-tyrosine phosphatase Neighboring gene PIPK domain-containing protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A Mediator subunit, MDT-15, integrates regulation of fatty acid metabolism by NHR-49-dependent and -independent pathways in C. elegans. Taubert S, et al. Genes Dev, 2006 May 1. PMID 16651656, Free PMC Article
  2. IRE-1 and HSP-4 contribute to energy homeostasis via fasting-induced lipases in C. elegans. Jo H, et al. Cell Metab, 2009 May. PMID 19416714
  3. Intracellular lipid surveillance by small G protein geranylgeranylation. Watterson A, et al. Nature, 2022 May. PMID 35585236, Free PMC Article
  4. Evolutionary analysis of the carnitine- and choline acyltransferases suggests distinct evolution of CPT2 versus CPT1 and related variants. van der Hoek MD, et al. Biochim Biophys Acta Mol Cell Biol Lipids, 2018 Aug. PMID 29730527
  5. Fatty acid desaturation and the regulation of adiposity in Caenorhabditis elegans. Brock TJ, et al. Genetics, 2007 Jun. PMID 17435249, Free PMC Article

See all (9) citations in PubMed

GeneRIFs: Gene References Into Functions

General gene information

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Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables acyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables carnitine O-palmitoyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
involved_in carnitine metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in fatty acid metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
  

General protein information

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Preferred Names
Choline/carnitine acyltransferase domain-containing protein
NP_497498.2
  • Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003281.10 Reference assembly

    Range
    2082819..2088314
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_065097.5 → NP_497498.2  Choline/carnitine acyltransferase domain-containing protein [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_497498.2

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q9N3N3
    Conserved Domains (1) summary
    pfam00755
    Location:128 → 716
    Carn_acyltransf; Choline/Carnitine o-acyltransferase
Nucleotide Protein
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