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ACOT12 acyl-CoA thioesterase 12 [ Mesitornis unicolor (brown roatelo) ]

Gene ID: 104543030, updated on 3-Aug-2024

Summary

Gene symbol
ACOT12
Gene description
acyl-CoA thioesterase 12
Locus tag
N332_10926
Gene type
protein coding
RefSeq status
MODEL
Organism
Mesitornis unicolor
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Mesitornithiformes; Mesitornithidae; Mesitornis
Annotation information
Annotation category: partial on reference assembly
Orthologs
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Genomic context

See ACOT12 in Genome Data Viewer
Location:
chromosome: Un
Exon count:
9
Annotation release Status Assembly Chr Location
100 current ASM69576v1 (GCF_000695765.1) Unplaced Scaffold NW_010159711.1 (2934..19976)

NW_010159711.1Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Genomic Sequence:
NW_010159711.1 Unplaced Scaffold Reference ASM69576v1

General protein information

Preferred Names
acyl-coenzyme A thioesterase 12
Names
Acyl-coenzyme A thioesterase 12

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Mesitornis unicolor 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 ASM69576v1

Genomic

  1. NW_010159711.1 Reference ASM69576v1

    Range
    2934..19976
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_010187526.1XP_010185828.1  acyl-coenzyme A thioesterase 12

    UniProtKB/TrEMBL
    A0A091QKW5
    Conserved Domains (2) summary
    cd03442
    Location:123237
    BFIT_BACH; Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, ...
    cl00509
    Location:160
    hot_dog; The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated ...