AMPD3

Protein identityUniProt · HPA

UniProt accession

Q01432

Gene

AMPD3

Ensembl

ENSG00000133805

Chromosome

11

Canonical length

767 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Nuclear membrane,Nucleoli

Quaternary structure

Homotetramer

OverviewNCBI Gene

This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

767 residues, UniProt reviewed canonical sequence.

>Q01432|AMPD3
     1  MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG QKEAKERELQ
    61  KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP AASPAMSPTT PVVTGATSLP
   121  TPAPYAMPEF QRVTISGDYC AGITLEDYEQ AAKSLAKALM IREKYARLAY HRFPRITSQY
   181  LGHPRADTAP PEEGLPDFHP PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH
   241  QEPHSLPYPD LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL
   301  KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG RKITLRQVFD
   361  GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE LRDLYLKTEN YLGGEYFARM
   421  VKEVARELEE SKYQYSEPRL SIYGRSPEEW PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF
   481  RSKKLLPNFG KMLENIFLPL FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK
   541  SPNPDVWTSE QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF
   601  LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE FLHKGLHVSL
   661  STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS VLQSGLSHQE KQKFLGQNYY
   721  KEGPEGNDIR KTNVAQIRMA FRYETLCNEL SFLSDAMKSE EITALTN

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against AMPD3 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.25

Highest tissue expression

61 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about AMPD3.

Disease | AllUniProt

Conditions AMPD3 is implicated in, by any mechanism.

• Adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE) MIM:612874

Disease | GeneticClinVar

4 pathogenic / likely-pathogenic of 234 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Erythrocyte AMP deaminase deficiency
• AMPD3-related disorder
• Thyroid cancer, nonmedullary, 1

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.91

gnomAD pLI

0

gnomAD missense Z

0.67

DepMap mean gene effect

-0.01

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• AMP catabolic process
• AMP metabolic process
• IMP biosynthetic process
• IMP salvage

Molecular functions

• AMP deaminase activity
• metal ion binding

Cellular components

• cytosol
• extracellular region
• ficolin-1-rich granule lumen
• secretory granule lumen

Protein domainsUniProt · Pfam · InterPro

• AMP deaminase
• Adenosine/AMP deaminase active site
• Metal-dependent hydrolase
• AMP deaminase

KeywordsUniProt

• Hydrolase
• Metal-binding
• Nucleotide metabolism
• Phosphoprotein
• Zinc