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DAGLB diacylglycerol lipase beta [ Calidris pugnax (ruff) ]

Gene ID: 106893450, updated on 13-Mar-2024

Summary

Gene symbol
DAGLB
Gene description
diacylglycerol lipase beta
See related
Ensembl:ENSCPUG00000015667
Gene type
protein coding
RefSeq status
MODEL
Organism
Calidris pugnax
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Charadriiformes; Scolopacidae; Calidris
Orthologs
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Genomic context

Location:
chromosome: Un
Exon count:
14
Annotation release Status Assembly Chr Location
100 current ASM143184v1 (GCF_001431845.1) Unplaced Scaffold NW_015090925.1 (1358819..1372447, complement)

NW_015090925.1Genomic Context describing neighboring genes Neighboring gene small integral membrane protein 10-like protein 2A Neighboring gene Rac family small GTPase 1 Neighboring gene KDEL endoplasmic reticulum protein retention receptor 2 Neighboring gene otoancorin

Genomic regions, transcripts, and products

Genomic Sequence:
NW_015090925.1 Unplaced Scaffold Reference ASM143184v1

General protein information

Preferred Names
sn1-specific diacylglycerol lipase beta

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Calidris pugnax Annotation Release 100 details...Open this link in a new tab

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

Reference ASM143184v1

Genomic

  1. NW_015090925.1 Reference ASM143184v1

    Range
    1358819..1372447 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_014951435.1XP_014806921.1  sn1-specific diacylglycerol lipase beta

    Related
    ENSCPUP00000023053.1, ENSCPUT00000027175.1
    Conserved Domains (1) summary
    cd00519
    Location:244477
    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 ...