3'(2'),5'-bisphosphate nucleotidase 1 (BPNT1)
The protein contains 308 amino acids for an estimated molecular weight of 33392 Da.
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. (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.
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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Biological Process
3'-phosphoadenosine 5'-phosphosulfate metabolic process
Dephosphorylation
Inositol phosphate dephosphorylation
Nervous system development
Nucleobase-containing compound metabolic process
Phosphatidylinositol phosphate biosynthetic process
Small molecule metabolic process
Xenobiotic metabolic process
The reference OMIM entry for this protein is 604053
3-prime(2-prime),5-prime-@bisphosphate nucleotidase 1; bpnt1
Bisphosphate 3-prime-nucleotidase
CLONING
At subtherapeutic concentrations, lithium, a major drug used to treat manic depression, inhibits members of a magnesium-dependent phosphomonoesterase family. Fructose 1,6-bisphosphatase (611570), inositol monophosphatase (602064), and inositol polyphosphate 1-phosphatase (INPP1; 147263), members of this family, contain a conserved motif involved in metal/lithium binding and catalysis. By searching EST databases for sequences related to the conserved motif in INPP1, Spiegelberg et al. (1999) identified mouse and human cDNAs encoding a novel magnesium-dependent phosphomonoesterase, which they called bisphosphate 3-prime-nucleotidase, or BPntase (EC 3.1.3.7). The predicted 309-amino acid human protein is 92% identical to mouse BPntase. Northern blot analysis revealed that the 2.5-kb human BPntase mRNA was expressed in all tissues tested, with the highest level observed in kidney.GENE FUNCTION
Spiegelberg et al. (1999) found that both native and recombinant BPntase exhibited intrinsic magnesium-dependent bisphosphate nucleotidase activity. Lithium acted as an uncompetitive inhibitor of the enzyme. Inositol 1,4-bisphosphate was a competitive inhibitor, suggesting that BPntase's physiologic role in nucleotide metabolism may be regulated by inositol signaling pathways. Expression of mammalian BPntase complemented mutations in the S. cerevisiae HAL2 gene, which encodes a protein involved in methionine biosynthesis and sodium tolerance. Spiegelberg et al. (1999) noted that the high expression of BPntase in kidney, as found by Northern blot analysis, is consistent with the hypothesis that increases in nucleotidase activity are associated with resistance to salt. They proposed that inhibition of human BPntase may account for lithium-induced nephrotoxicity.MAPPING
Gross (2014) mapped the BPNT1 gene to chromosome 1q41 based on an alignment of the BPNT1 sequence (GenBank GENBANK BC017801) with the genomic sequence (GRCh37). ... 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 15, 2016: Protein entry updated
Automatic update: OMIM entry 604053 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed