AMP deaminase 3 (AMPD3)
The protein contains 767 amino acids for an estimated molecular weight of 88812 Da.
AMP deaminase plays a critical role in energy metabolism. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No binding partner found
Biological Process
ADP metabolic process
AMP catabolic process
AMP metabolic process
ATP metabolic process
Energy homeostasis
Erythrocyte homeostasis
GTP metabolic process
IMP biosynthetic process
IMP salvage
Neutrophil degranulation
Nucleobase-containing small molecule metabolic process
Purine nucleobase metabolic process
Purine-containing compound salvage
Small molecule metabolic process
Cellular Component
Cytosol
Extracellular region
Ficolin-1-rich granule lumen
Secretory granule lumen
The reference OMIM entry for this protein is 102772
Adenosine monophosphate deaminase 3; ampd3
DESCRIPTION
Adenosine monophosphate deaminase-3 (EC 3.5.4.6) catalyzes the deamination of AMP to IMP in red cells and plays an important role in the purine nucleotide cycle. The AMPD3 gene encodes 2 erythrocyte isoforms, E1 and E2. An inherited defect in AMPD3 results in combined deficiency of these isoforms. Also see AMPD1 (102770) and AMPD2 (102771), which encode the L (liver) and M (muscle) isoforms of AMP deaminase, respectively.CLONING
Mahnke-Zizelman and Sabina (1992) isolated several AMPD3 cDNAs from different human nonskeletal muscle cDNA libraries. The cDNAs differed in their 5-prime terminal sequences. Yamada et al. (1992) also cloned a human AMPD3 cDNA. The 3.7-kb cDNA contains an open reading frame of 2,301 bp that encodes a deduced 767-amino acid protein with a predicted molecular mass of 89 kD. Mahnke-Zizelman et al. (1996) reported that the AMPD3 gene is widely expressed in human tissues and cells and that its expression is subject to transcriptional control by 3 tandem promoters. The AMPD3 transcripts encode the E isoforms of AMP deaminase. Mahnke-Zizelman et al. (1997) demonstrated that rat isoform C and human isoform E are homologous cross-species AMPD3 proteins.GENE STRUCTURE
Mahnke-Zizelman et al. (1996) demonstrated that the AMPD3 gene contains 17 exons spanning approximately 60 kb. They identified multiple promoters in proximal flanking sequence 5-prime to exons 1a, 1b, and 1c that regulate the production of alternative AMPD3 transcripts. Alternative splicing occurs in exon 1c.MAPPING
Whereas both the AMPD1 and AMPD2 genes are situated in the 1p21-p13 region of chromosome 1, Eddy et al. (1993) demonstrated that the AMPD3 gene is located on chromosome 11 in the region pter-p13. Sermsuvitayawong et al. (1997) demonstrated that the Ampd3 gene is located on mouse chromosome 7 in a region of conserved linkage homology with human 11p. The mouse homolog, however, has a different gene structure in the 5-prime region, the gene products are reported to be immunologically distinct, and Sermsuvitayawong et al. (1997) referred to the Ampd3 gene as the heart-type AMPD.MOLECULAR GENETICS
In 2 of the Japanese individuals with erythrocyte AMP deficiency (612874) reported by Ogasawara et al. (1987), Yamada et al. (1994) identified a mutation in the AMPD3 gene (102772.0001). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 102772 was added.