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Adal adenosine deaminase-like [ Mus musculus (house mouse) ]

Gene ID: 75894, updated on 12-May-2024

Summary

Official Symbol
Adalprovided by MGI
Official Full Name
adenosine deaminase-likeprovided by MGI
Primary source
MGI:MGI:1923144
See related
Ensembl:ENSMUSG00000027259 AllianceGenome:MGI:1923144
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Mus musculus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as
4930578F03Rik
Summary
Predicted to enable adenosine deaminase activity. Predicted to be involved in adenosine catabolic process and inosine biosynthetic process. Predicted to act upstream of or within nucleotide metabolic process. Orthologous to human ADAL (adenosine deaminase like). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Ubiquitous expression in adrenal adult (RPKM 7.4), CNS E14 (RPKM 5.6) and 28 other tissues See more
Orthologs
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Genomic context

See Adal in Genome Data Viewer
Location:
2 E5; 2 60.37 cM
Exon count:
14
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCm39 (GCF_000001635.27) 2 NC_000068.8 (120970525..120989921)
108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 2 NC_000068.7 (121140044..121159440)

Chromosome 2 - NC_000068.8Genomic Context describing neighboring genes Neighboring gene transglutaminase 7 Neighboring gene predicted gene, 23858 Neighboring gene leucine carboxyl methyltransferase 2 Neighboring gene zinc finger SCAN domains 29 Neighboring gene tubulin, gamma complex component 4 Neighboring gene transformation related protein 53 binding protein 1 Neighboring gene STARR-seq mESC enhancer starr_05522 Neighboring gene STARR-seq mESC enhancer starr_05523 Neighboring gene STARR-positive B cell enhancer ABC_E2640 Neighboring gene STARR-seq mESC enhancer starr_05524 Neighboring gene STARR-positive B cell enhancer ABC_E5972 Neighboring gene STARR-seq mESC enhancer starr_05525 Neighboring gene microtubule-associated protein 1 A Neighboring gene diphosphoinositol pentakisphosphate kinase 1

Genomic regions, transcripts, and products

Expression

  • Project title: Mouse ENCODE transcriptome data
  • Description: RNA profiling data sets generated by the Mouse ENCODE project.
  • BioProject: PRJNA66167
  • Publication: PMID 25409824
  • Analysis date: n/a

Variation

Alleles

Alleles of this type are documented at Mouse Genome Informatics  (MGI)
  • Endonuclease-mediated (1) 
  • Gene trapped (1) 
  • Targeted (1) 

Pathways from PubChem

General gene information

Markers

Clone Names

  • MGC62428, MGC63264

Gene Ontology Provided by MGI

Function Evidence Code Pubs
enables adenosine deaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables deaminase activity IEA
Inferred from Electronic Annotation
more info
 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
 
enables metal ion binding 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 inosine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
 
acts_upstream_of_or_within nucleotide metabolic process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
is_active_in cellular_component ND
No biological Data available
more info
 

General protein information

Preferred Names
adenosine deaminase-like protein
NP_001277740.1
NP_001277741.1
NP_001342677.1
NP_083751.1
XP_006500414.1
XP_006500415.1
XP_006500416.1
XP_006500422.1
XP_006500423.1
XP_011238139.1
XP_030108038.1
XP_030108039.1
XP_030108040.1
XP_030108041.1
XP_030108042.1
XP_030108043.1
XP_036018550.1
XP_036018551.1
XP_036018552.1
XP_036018553.1
XP_036018554.1

NCBI Reference Sequences (RefSeq)

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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_001290811.1NP_001277740.1  adenosine deaminase-like protein isoform b

    See identical proteins and their annotated locations for NP_001277740.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) contains alternate 5' exon structure, and it thus differs in its 5' UTR and initiates translation at a downstream in-frame start codon, compared to variant 1. The encoded isoform (b) is shorter at the N-terminus, compared to variant 1.
    Source sequence(s)
    AK016299, AK048809, AK049697
    Consensus CDS
    CCDS71121.1
    UniProtKB/Swiss-Prot
    Q80SY6
    Related
    ENSMUSP00000028702.4, ENSMUST00000028702.10
    Conserved Domains (1) summary
    cd00443
    Location:1277
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  2. NM_001290812.1NP_001277741.1  adenosine deaminase-like protein isoform c

    Status: VALIDATED

    Description
    Transcript Variant: This variant (3) contains alternate 5' exon structure, and it thus differs in its 5' UTR and initiates translation at a downstream in-frame start codon, and it also includes an additional in-frame exon in the 3' coding region, compared to variant 1. The encoded isoform (c) is shorter at the N-terminus, compared to variant 1.
    Source sequence(s)
    AK039677, AK048809, AK049697
    Consensus CDS
    CCDS79836.1
    UniProtKB/TrEMBL
    Z4YL50
    Related
    ENSMUSP00000106293.2, ENSMUST00000110665.8
    Conserved Domains (1) summary
    cl00281
    Location:3237
    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 ...
  3. NM_001355748.1NP_001342677.1  adenosine deaminase-like protein isoform 4

    Status: VALIDATED

    Description
    Transcript Variant: This variant (4) lacks two alternate exons compared to variant 1. The resulting isoform (4) is shorter at the N-terminus compared to isoform 1.
    Source sequence(s)
    AL845479
    Consensus CDS
    CCDS89543.1
    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  4. NM_029475.2NP_083751.1  adenosine deaminase-like protein isoform a

    See identical proteins and their annotated locations for NP_083751.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (a). The 5' UTR of this variant is incomplete due to lack of a complete transcript and splice pattern ambiguity in the upstream region.
    Source sequence(s)
    AK048809, AK049697, BC050879
    Consensus CDS
    CCDS16633.1
    UniProtKB/Swiss-Prot
    A2ARU3, A2ARU4, Q80SY6, Q8BLN3, Q8BX67, Q9D4Q6
    Related
    ENSMUSP00000067133.6, ENSMUST00000066155.6
    Conserved Domains (1) summary
    cd00443
    Location:17344
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000068.8 Reference GRCm39 C57BL/6J

    Range
    120970525..120989921
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_006500351.3XP_006500414.1  adenosine deaminase-like protein isoform X1

    See identical proteins and their annotated locations for XP_006500414.1

    UniProtKB/Swiss-Prot
    A2ARU3, A2ARU4, Q80SY6, Q8BLN3, Q8BX67, Q9D4Q6
    Conserved Domains (1) summary
    cd00443
    Location:17344
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  2. XM_030252181.1XP_030108041.1  adenosine deaminase-like protein isoform X3

    Conserved Domains (1) summary
    cd00443
    Location:1230
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  3. XM_006500352.4XP_006500415.1  adenosine deaminase-like protein isoform X1

    See identical proteins and their annotated locations for XP_006500415.1

    UniProtKB/Swiss-Prot
    A2ARU3, A2ARU4, Q80SY6, Q8BLN3, Q8BX67, Q9D4Q6
    Related
    ENSMUSP00000113052.2, ENSMUST00000119031.8
    Conserved Domains (1) summary
    cd00443
    Location:17344
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  4. XM_006500359.3XP_006500422.1  adenosine deaminase-like protein isoform X4

    See identical proteins and their annotated locations for XP_006500422.1

    UniProtKB/Swiss-Prot
    Q80SY6
    Related
    ENSMUSP00000106290.3, ENSMUST00000110662.9
    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  5. XM_030252183.1XP_030108043.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  6. XM_030252178.1XP_030108038.1  adenosine deaminase-like protein isoform X2

    Conserved Domains (1) summary
    cd00443
    Location:1277
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  7. XM_036162657.1XP_036018550.1  adenosine deaminase-like protein isoform X3

    Conserved Domains (1) summary
    cd00443
    Location:1230
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  8. XM_030252180.1XP_030108040.1  adenosine deaminase-like protein isoform X3

    Conserved Domains (1) summary
    cd00443
    Location:1230
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  9. XM_036162658.1XP_036018551.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  10. XM_030252179.1XP_030108039.1  adenosine deaminase-like protein isoform X3

    Conserved Domains (1) summary
    cd00443
    Location:1230
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  11. XM_011239837.2XP_011238139.1  adenosine deaminase-like protein isoform X5

    Conserved Domains (1) summary
    cd00443
    Location:17380
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  12. XM_030252182.1XP_030108042.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  13. XM_006500360.3XP_006500423.1  adenosine deaminase-like protein isoform X4

    See identical proteins and their annotated locations for XP_006500423.1

    UniProtKB/Swiss-Prot
    Q80SY6
    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  14. XM_006500353.5XP_006500416.1  adenosine deaminase-like protein isoform X1

    See identical proteins and their annotated locations for XP_006500416.1

    UniProtKB/Swiss-Prot
    A2ARU3, A2ARU4, Q80SY6, Q8BLN3, Q8BX67, Q9D4Q6
    Conserved Domains (1) summary
    cd00443
    Location:17344
    ADA_AMPD; Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase ...
  15. XM_036162661.1XP_036018554.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  16. XM_036162660.1XP_036018553.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...
  17. XM_036162659.1XP_036018552.1  adenosine deaminase-like protein isoform X4

    Conserved Domains (1) summary
    cl00281
    Location:3201
    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 ...