N-acetylmuramoyl-L-alanine amidase (PGLYRP2)
The protein contains 576 amino acids for an estimated molecular weight of 62217 Da.
May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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:rs3813135 | |
| dbSNP:rs733731 | |
| dbSNP:rs28404490 | |
| dbSNP:rs892145 | |
| dbSNP:rs34440547 | |
| dbSNP:rs2304200 |
No binding partner found
Biological Process
Antimicrobial humoral response
Biological process involved in interaction with host
Defense response to Gram-positive bacterium
Detection of bacterium
Growth of symbiont in host
Innate immune response
Negative regulation of interferon-gamma production
Negative regulation of natural killer cell differentiation involved in immune response
Peptide amidation
Peptidoglycan catabolic process
Regulation of inflammatory response
The reference OMIM entry for this protein is 608199
Peptidoglycan recognition protein 2; pglyrp2
Peptidoglycan recognition protein, long; pgrpl
DESCRIPTION
Peptidoglycan recognition proteins, such as PGRPL, are part of the innate immune system and recognize peptidoglycan, a ubiquitous component of bacterial cell walls.CLONING
By searching an EST database for homologs of PGRPS (PGLYRP1; 604963), followed by PCR of a pooled cDNA library and a liver cDNA library, Liu et al. (2001) cloned full-length PGRPL. The deduced 576-amino acid precursor protein contains an N-terminal signal peptide, followed by 2 transmembrane segments and an extracellular C terminus containing PGRP domains III, II, and I. PGRPL shares 40%, 33%, and 32% identity with PGRPS, PGRPI-alpha (608197), and PGRPI-beta (608198), respectively. RNA dot blot analysis detected strong PGRPL expression in adult liver and weak expression in fetal liver. Northern blot analysis detected 2.1- and 0.8-kb transcripts expressed in adult and fetal liver. PCR also detected low expression in transverse colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach, and testis. Transiently transfected COS-7 and human embryonic kidney cells expressed PGRPL as a Triton X-100-soluble membrane protein with an apparent molecular mass of 65 kD.GENE FUNCTION
Liu et al. (2001) determined that recombinant PGRPL expressed by COS-7 cells and human embryonic kidney cells bound to gram-positive bacteria, B. subtilis and M. luteus, with high affinity. Xu et al. (2004) determined that murine Pgrpl is a secreted serum protein that can form multimers, most likely homodimers.GENE STRUCTURE
Liu et al. (2001) determined that the PGRPL gene contains 5 exons.MAPPING
By genomic sequence analysis, Liu et al. (2001) mapped the PGRPL gene to chromosome 19.ANIMAL MODEL
Xu et al. (2004) created Pgrpl-deficient mice. They found that Pgrpl contributed little to systemic challenge using gram-negative bacteria, gram-positive bacteria, or yeast. Peritoneal macrophages from Pgrpl-deficient mice produced decreased amounts of the inflammatory cytokines Il6 (147620) and Tnfa (191160) when stimulated with E. coli or lipopolysaccharide, but comparable amounts when stimulated with S. aureus, C. albicans, or their cell wall components. The cells produced similar amounts of cytokines when challenged with gram-positive or gram-negative peptidoglycans. Xu et al. (2004) concluded that, in contrast to its critical role in immunity in flies, Pgrpl is largely dispensable for mammalian immunity against bacteria and fungi. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 608199 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).