Aminopeptidase B (RNPEP)
The protein contains 650 amino acids for an estimated molecular weight of 72596 Da.
Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). (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.
- 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.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs3820439 |
No binding partner found
Biological Process
Leukotriene biosynthetic process
Negative regulation of blood pressure
Peptide catabolic process
Proteolysis
Cellular Component
Extracellular exosome
Extracellular region
Extracellular space
Plasma membrane
Secretory granule
The reference OMIM entry for this protein is 602675
Arginyl aminopeptidase; rnpep
Aminopeptidase b
CLONING
Aminopeptidase B (EC 3.4.11.6) was originally defined as an exopeptidase capable of trimming basic amino acid residues from the NH2 terminus of peptide substrates (Hopsu et al., 1964). Cadel et al. (1995) demonstrated that it is a Zn(2+)-dependent exopeptidase that selectively removes arginine and/or lysine residues from the N terminus of several peptide substrates. Structurally it is related to leukotriene A4 hydrolase (151570), an important enzyme of the arachidonic acid pathway. The structural relationship has its functional counterpart in the capacity of aminopeptidase B to hydrolyze leukotriene A4 (Cadel et al., 1997). Antibodies raised against the isolated peptidase show that it is widely distributed in a number of tissues, including endocrine and nonendocrine cell types. It is secreted by rat PC12 pheochromocytoma cells and associated with the external face of their plasma membrane. Together these data strongly argue in favor of participation of this ubiquitous and in vitro bifunctional enzyme in the final stages of precursor processing mechanisms occurring either during the intracellular transport along the secretory pathway or at the plasma membrane level, or both (Aurich-Costa et al., 1997).MAPPING
By fluorescence in situ hybridization, Aurich-Costa et al. (1997) mapped the RNPEP gene to chromosome 1q32.1-q32.2. ... 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 602675 was added.