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Nudt7 nudix hydrolase 7 [ Urocitellus parryii (Arctic ground squirrel) ]

Gene ID: 113185765, updated on 15-Mar-2024

Summary

Gene symbol
Nudt7
Gene description
nudix hydrolase 7
See related
Ensembl:ENSUPAG00010009093
Gene type
protein coding
RefSeq status
MODEL
Organism
Urocitellus parryii
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae; Xerinae; Marmotini; Urocitellus
Orthologs
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Genomic context

See Nudt7 in Genome Data Viewer
Location:
chromosome: Un
Exon count:
4
Annotation release Status Assembly Chr Location
100 current ASM342692v1 (GCF_003426925.1) Unplaced Scaffold NW_020540001.1 (4068089..4082039, complement)

NW_020540001.1Genomic Context describing neighboring genes Neighboring gene C-type lectin domain family 3 member A Neighboring gene vesicle amine transport 1 like Neighboring gene ADAM metallopeptidase with thrombospondin type 1 motif 18 Neighboring gene MON1 homolog B, secretory trafficking associated

Genomic regions, transcripts, and products

Genomic Sequence:
NW_020540001 Unplaced Scaffold Reference ASM342692v1

General protein information

Preferred Names
peroxisomal coenzyme A diphosphatase NUDT7

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Urocitellus parryii 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 ASM342692v1

Genomic

  1. NW_020540001.1 Reference ASM342692v1

    Range
    4068089..4082039 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_026392992.1XP_026248777.1  peroxisomal coenzyme A diphosphatase NUDT7

    UniProtKB/TrEMBL
    A0A8D2HEQ9
    Related
    ENSUPAP00010011222.1, ENSUPAT00010012891.1
    Conserved Domains (1) summary
    cd03426
    Location:41193
    CoAse; Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative ...