adah-1 adenosine deaminase [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: adah-1
Official Full Name: adenosine deaminase
Primary source: WormBase:WBGene00015551
Locus tag: CELE_C06G3.5
See related: AllianceGenome:WB:WBGene00015551
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable adenosine deaminase activity. Predicted to be involved in hypoxanthine salvage; negative regulation of adenosine receptor signaling pathway; and purine ribonucleoside metabolic process. Predicted to be active in cytosol and external side of plasma membrane. Is expressed in several structures, including head mesodermal cell; nervous system; pharynx; rectal gland cell; and reproductive system. Human ortholog(s) of this gene implicated in asthma; colon cancer; pleural tuberculosis; severe combined immunodeficiency (multiple); and uterine fibroid. Orthologous to human ADA (adenosine deaminase). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See adah-1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 6

Sequence:: Chromosome: IV; NC_003282.8 (7024211..7028147)

Chromosome IV - NC_003282.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003282.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

C06G3.5 (e-PCR)
- UniSTS:308974

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables adenosine deaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables adenosine deaminase activity	IEA Inferred from Electronic Annotation more info
enables deaminase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in adenosine catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in hypoxanthine salvage	IBA Inferred from Biological aspect of Ancestor more info
involved_in inosine biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of adenosine receptor signaling pathway	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in external side of plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: adenosine deaminase

NP_001368090.1

Confirmed by transcript evidence

NP_501087.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

NC_003282.8 Reference assembly

Range

7024211..7028147

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_068686.7 → NP_501087.1 adenosine deaminase [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_501087.1

Status: REVIEWED

UniProtKB/TrEMBL

H2KYI5

Conserved Domains (1) summary

cd01320
Location:48 → 383

ADA; Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in ...
NM_001380300.3 → NP_001368090.1 adenosine deaminase [Caenorhabditis elegans]

Status: REVIEWED

UniProtKB/TrEMBL

Q86NI2

Conserved Domains (1) summary

cl00281
Location:6 → 341

metallo-dependent_hydrolases; Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a ...