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    DAGLA diacylglycerol lipase alpha [ Bos taurus (domestic cattle) ]

    Gene ID: 523665, updated on 4-Oct-2024

    Summary

    Official Symbol
    DAGLAprovided by VGNC
    Official Full Name
    diacylglycerol lipase alphaprovided by VGNC
    Primary source
    VGNC:VGNC:27872
    See related
    BGD:BT14494; Ensembl:ENSBTAG00000013942
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Bos taurus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
    Orthologs
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    Genomic context

    See DAGLA in Genome Data Viewer
    Location:
    chromosome: 29
    Exon count:
    21
    Annotation release Status Assembly Chr Location
    RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 29 NC_037356.1 (40124700..40191155)

    Chromosome 29 - NC_037356.1Genomic Context describing neighboring genes Neighboring gene synaptotagmin 7 Neighboring gene microRNA mir-2885 Neighboring gene uncharacterized LOC112444860 Neighboring gene myelin regulatory factor Neighboring gene transmembrane protein 258 Neighboring gene flap structure-specific endonuclease 1

    Genomic regions, transcripts, and products

    Genomic Sequence:
    NC_037356.1 Chromosome 29 Reference ARS-UCD2.0 Primary Assembly

    General protein information

    Preferred Names
    diacylglycerol lipase-alpha
    NP_001179512.1
    XP_005226987.1
    XP_005226988.1

    NCBI Reference Sequences (RefSeq)

    NEW Try the new Transcript table

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001192583.3NP_001179512.1  diacylglycerol lipase-alpha

      See identical proteins and their annotated locations for NP_001179512.1

      Status: PROVISIONAL

      Source sequence(s)
      NKLS02000029
      UniProtKB/TrEMBL
      E1BBV2
      Conserved Domains (1) summary
      cd00519
      Location:288529
      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 ...

    RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

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

    Reference ARS-UCD2.0 Primary Assembly

    Genomic

    1. NC_037356.1 Reference ARS-UCD2.0 Primary Assembly

      Range
      40124700..40191155
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_005226931.5XP_005226988.1  diacylglycerol lipase-alpha isoform X1

      See identical proteins and their annotated locations for XP_005226988.1

      UniProtKB/TrEMBL
      E1BBV2
      Conserved Domains (1) summary
      cd00519
      Location:288529
      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 ...
    2. XM_005226930.5XP_005226987.1  diacylglycerol lipase-alpha isoform X1

      See identical proteins and their annotated locations for XP_005226987.1

      UniProtKB/TrEMBL
      E1BBV2
      Related
      ENSBTAP00000018523.4, ENSBTAT00000018523.6
      Conserved Domains (1) summary
      cd00519
      Location:288529
      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 ...