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N-acetylmuramoyl-L-alanine amidase; peptidoglycan recognition protein long; PGRP-L; peptidoglycan recognition protein 2 (PGLYRP2, PGLYRPL, PGRPL, UNQ3103/PRO10102)
Function:
1) scavenger
2) digests biologically active peptidoglycan into biologically inactive fragments
3) no direct bacteriolytic activity
4) hydrolyzes link between N-acetylmuramoyl residues & L-amino acid residues in certain cell-wall glycopeptides
Cofactor: Zn+2
Structure:
- belongs to the N-acetylmuramoyl-L-alanine amidase 2 family
Compartment: secreted, membrane
Alternative splicing:
- named isoforms=2;
- may be due to an intron retention
Expression:
- expressed in adult liver & fetal liver & secreted into plasma
- expressed to a much lesser extent in transverse colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach, testis
- isoform 2 is not detected in the liver or plasma
General
glycoprotein
hydrolase
metalloprotein
phosphoprotein
Properties
SIZE: MW = 62 kD
entity length = 576 aa
MOTIF: signal sequence {1-21}
N-glycosylation site {N77}
Ser phosphorylation site {S239}
N-glycosylation site {N367}
Zn+2-binding site
SITE: 411-411
cysteine residue {C419}
MODIFICATION: cysteine residue {C425}
cysteine residue {C425}
MODIFICATION: cysteine residue {C419}
Zn+2-binding site
SITE: 447-447
N-glycosylation site {N485}
Zn+2-binding site
SITE: 522-522
Zn+2-binding site
SITE: 530-530
Database Correlations
OMIM 608199
UniProt Q96PD5
Pfam PF01510
Entrez Gene 114770
Kegg hsa:114770
ENZYME 3.5.1.28
References
UniProt :accession Q96PD5