Low molecular weight phosphotyrosine protein phosphatase (ACP1)
The protein contains 158 amino acids for an estimated molecular weight of 18042 Da.
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity. (updated: April 1, 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs11691572 | |
| allele ACP1*A | |
| dbSNP:rs35569198 |
Biological Process
Cellular Component
Cytoplasm
Cytoplasmic side of plasma membrane
Cytosol
Extracellular exosome
Sarcolemma
The reference OMIM entry for this protein is 171500
Acid phosphatase 1, soluble; acp1
Phosphatase, acid, of erythrocyte
CLONING
Wo et al. (1992) cloned genes encoding 2 low molecular weight phosphotyrosyl protein phosphatases from a human placenta cDNA library. They were found to have identical nucleotide sequences, with the exception of a 108-bp segment in the middle of the open reading frame. From further studies they concluded that the 2 represent the fast and slow electrophoretic forms of red cell acid phosphatase and that this enzyme is not unique to the red cell but instead is expressed in all human tissues.GENE FUNCTION
Sensabaugh and Golden (1978) showed that ACP1 is inhibited by folic acid and various folates, and that the inhibition is phenotype dependent: ACP1(C) more than ACP1(A) more than ACP1(B). This explains elevation of ACP levels in red cells of patients with megaloblastic anemia and also variation in incidence and severity of favism (134700) in persons with G6PD deficiency (300908). Swallow et al. (1973) showed that 'red cell' acid phosphatase is not limited to erythrocytes but can be demonstrated in other tissues, including cultured fibroblasts and lymphoblastoid cells where there is no possibility of contamination by blood.MAPPING
Weitkamp et al. (1969) presented data suggesting that the acid phosphatase locus may be on chromosome 2. Renwick (1971) presented an analysis of the Weitkamp data supporting assignment to chromosome 2. Ferguson-Smith et al. (1973) presented deletion mapping evidence that the acid phosphatase locus is on the distal end of the short arm of chromosome 2, somewhere between 2p23 and 2pter. A child lacking this segment was of phenotype B whereas the father and mother were homozygous phenotype B and A, respectively. Hulten et al. (1966) described a family in which studies of a reciprocal translocation involving chromosome 2 suggested that the Kidd locus may be on one of the involved chromosomes. Cell hybrid studies confirmed the localization of acid phosphatase-1 on chromosome 2 (Povey et al., 1974). Chu et al. (1975) presented cell-hybrid evidence for synteny of gal-1-PT, acid phosphatase, MDH1 (154200), and gal-plus-activator (GLAT; 137030) and for assignment to chromosome 2. Junien et al. (1979) assigned the ACP1 locus to 2p25. Larson et al. (1982) studied 4 patients who had inherited an unbalanced form of a familial reciprocal translocation, t(2;10)(p24;q26), giving them partial duplication of 2p. Increased levels of acid phosphatase indicated that ACP1 is located in the 2p24-2pter region and that MDH is not. The previous inconsistency of the SRO (smallest region of overlap) was now resolved; ACP1 is at 2p25. By deletion mapping, Beemer et al. (1983) concluded that ACP1 is located at 2p25 whereas MDH is closer to the centromere, i.e., in 2p25-p23. They pointed to the report of Larson et al. (1982) as confirming their findings. Wakita et al. (1985) presented evidence in support of location of ACP1 at 2p25. In a patient with duplication of 2p25.3-p25.1, ACP activity was 1.4 times the mean value for normal persons. Lothe et al. (1986) found that ACP1 is very closely linked (theta = 0.01) to a RFLP called D2S1 that maps to 2pter-p23. Siciliano et al. (1987) and Thompson et al. (1987) resolved earlier ambiguity of the ACP1 assignment (2p23 or 2p25) by demonstrating in hybrid cells with rearranged chromosomes that ACP1 is located at band 2p23, proximal to MDH1 (154200). ACP1 is seemingly remote from APOB (107730); linkage studies demonstrate no close linkage (Berg, 1987). There may ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 171500 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed