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K11E4.1 Fungal lipase-like domain-containing protein [ Caenorhabditis elegans ]

Gene ID: 187295, updated on 2-Nov-2024

Summary

Official Symbol
K11E4.1
Official Full Name
Fungal lipase-like domain-containing protein
Primary source
WormBase:WBGene00010773
Locus tag
CELE_K11E4.1
See related
AllianceGenome:WB:WBGene00010773
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 be involved in lipid metabolic process. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

See K11E4.1 in Genome Data Viewer
Location:
chromosome: X
Exon count:
9
Sequence:
Chromosome: X; NC_003284.9 (13714157..13716327)

Chromosome X - NC_003284.9Genomic Context describing neighboring genes Neighboring gene START domain-containing protein Neighboring gene tRNA Neighboring gene ncRNA Neighboring gene tRNA-Lys Neighboring gene tRNA-Lys Neighboring gene tRNA-Lys

General protein information

Preferred Names
Fungal lipase-like domain-containing protein
NP_510294.3
  • 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_003284.9 Reference assembly

    Range
    13714157..13716327
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_077893.5NP_510294.3  Fungal lipase-like domain-containing protein [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_510294.3

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q21428
    Conserved Domains (1) summary
    cd00519
    Location:32250
    Lipase_3; Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of ...