O08739 · AMPD3_MOUSE

  • Protein
    AMP deaminase 3
  • Gene
    Ampd3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

AMP deaminase plays a critical role in energy metabolism.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.

Features

Showing features for binding site, active site.

1766100200300400500600700
TypeIDPosition(s)Description
Binding site316Zn2+ (UniProtKB | ChEBI); catalytic
Binding site318substrate
Binding site318Zn2+ (UniProtKB | ChEBI); catalytic
Binding site387-392substrate
Binding site585Zn2+ (UniProtKB | ChEBI); catalytic
Binding site588substrate
Active site607Proton acceptor
Binding site662Zn2+ (UniProtKB | ChEBI); catalytic
Binding site663-666substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionAMP deaminase activity
Molecular Functionmetal ion binding
Biological ProcessADP catabolic process
Biological ProcessADP metabolic process
Biological ProcessAMP catabolic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process
Biological Processenergy homeostasis
Biological Processerythrocyte homeostasis
Biological ProcessGTP metabolic process
Biological ProcessIMP biosynthetic process
Biological ProcessIMP salvage

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AMP deaminase 3
  • EC number
  • Alternative names
    • AMP deaminase H-type
    • AMP deaminase isoform E
    • Heart-type AMPD

Gene names

    • Name
      Ampd3

Organism names

  • Taxonomic identifier
  • Strains
    • 129/Sv
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O08739
  • Secondary accessions
    • O88692
    • Q8CFR4

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001944111-766AMP deaminase 3
Modified residue85Phosphoserine
Modified residue107Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Found in heart, lung brain, spleen, kidney and to a lesser extent in liver.

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region89-119Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    766
  • Mass (Da)
    88,652
  • Last updated
    2011-07-27 v2
  • Checksum
    94991133B18B8AA5
MPRQFPKLNMSDLDEHVRLLAEKVFAKVLREEDSKDVMSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPTQQDWKGPPTASPAMSPATPLVPGATSKPGPAPYAMPEYQRVTISGDYCAGITVEDYEQAAKSLAKALMIREKYARLAYHRFPRTTAQYLAHQGESVPLEEGLPDFHPPPLPQEDPYCLDDAPPNLGYLVRMHGGVLFVYDNQTMLERQEPHSLPYPDLETYIVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKLGRKITLRQVFDSLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEDSKYQYSEPRLSIYGRSPKEWSSLARWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPSPDLWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTK

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6XQD0F6XQD0_MOUSEAmpd3137
D3YU73D3YU73_MOUSEAmpd3111
D3Z4N3D3Z4N3_MOUSEAmpd3184
A0A1L1SRX2A0A1L1SRX2_MOUSEAmpd3775

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict251in Ref. 1; BAA19933
Sequence conflict645in Ref. 1; BAA19933

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D85596
EMBL· GenBank· DDBJ
BAA19933.1
EMBL· GenBank· DDBJ
mRNA
D88994
EMBL· GenBank· DDBJ
BAA32548.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AK133465
EMBL· GenBank· DDBJ
BAE21671.1
EMBL· GenBank· DDBJ
mRNA
CH466531
EMBL· GenBank· DDBJ
EDL16988.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466531
EMBL· GenBank· DDBJ
EDL16989.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466531
EMBL· GenBank· DDBJ
EDL16990.1
EMBL· GenBank· DDBJ
Genomic DNA
BC040366
EMBL· GenBank· DDBJ
AAH40366.1
EMBL· GenBank· DDBJ
mRNA
BC056380
EMBL· GenBank· DDBJ
AAH56380.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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