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THEM5 thioesterase superfamily member 5 [ Felis catus (domestic cat) ]

Gene ID: 101082506, updated on 17-Aug-2024

Summary

Official Symbol
THEM5
Official Full Name
thioesterase superfamily member 5
Primary source
VGNC:VGNC:66160
See related
EnsemblRapid:ENSFCTG00005021632
Gene type
protein coding
RefSeq status
MODEL
Organism
Felis catus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis
Orthologs
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Genomic context

See THEM5 in Genome Data Viewer
Location:
chromosome: C1
Exon count:
6
Annotation release Status Assembly Chr Location
105 current F.catus_Fca126_mat1.0 (GCF_018350175.1) C1 NC_058375.1 (106365265..106373654, complement)
104 previous assembly Felis_catus_9.0 (GCF_000181335.3) C1 NC_018730.3 (106870612..106879006, complement)

Chromosome C1 - NC_058375.1Genomic Context describing neighboring genes Neighboring gene RAR related orphan receptor C Neighboring gene C2 calcium dependent domain containing 4D Neighboring gene golgin subfamily A member 7-like Neighboring gene thioesterase superfamily member 4

Genomic regions, transcripts, and products

General protein information

Preferred Names
acyl-coenzyme A thioesterase THEM5

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Felis catus Annotation Release 105 details...Open this link in a new tab

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

Reference F.catus_Fca126_mat1.0 Primary Assembly

Genomic

  1. NC_058375.1 Reference F.catus_Fca126_mat1.0 Primary Assembly

    Range
    106365265..106373654 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_003990639.5XP_003990688.1  acyl-coenzyme A thioesterase THEM5

    See identical proteins and their annotated locations for XP_003990688.1

    UniProtKB/TrEMBL
    M3WEA3
    Related
    ENSFCTP00005045353.1, ENSFCTT00005062015.1
    Conserved Domains (1) summary
    cl00509
    Location:141237
    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 ...