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N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Peptidoglycan recognition protein 2) (Peptidoglycan recognition protein long) (PGRP-L) (TagL)

 PGRP2_MOUSE             Reviewed;         530 AA.
Q8VCS0; Q8K4I8; Q9QXZ1; Q9QXZ2;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
28-FEB-2018, entry version 134.
RecName: Full=N-acetylmuramoyl-L-alanine amidase;
EC=3.5.1.28;
AltName: Full=Peptidoglycan recognition protein 2;
AltName: Full=Peptidoglycan recognition protein long;
Short=PGRP-L;
AltName: Full=TagL;
Flags: Precursor;
Name=Pglyrp2; Synonyms=Pglyrpl, Pgrpl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-37.
STRAIN=C57BL/6J;
PubMed=12821140; DOI=10.1016/S0006-291X(03)01096-9;
Gelius E., Persson C., Karlsson J., Steiner H.;
"A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-
L-alanine amidase activity.";
Biochem. Biophys. Res. Commun. 306:988-994(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=12559914; DOI=10.1016/S0022-2836(02)01401-8;
Kibardin A.V., Mirkina I.I., Baranova E.V., Zakeyeva I.R.,
Georgiev G.P., Kiselev S.L.;
"The differentially spliced mouse tagL gene, homolog of tag7/PGRP gene
family in mammals and Drosophila, can recognize Gram-positive and
Gram-negative bacterial cell wall independently of T phage lysozyme
homology domain.";
J. Mol. Biol. 326:467-474(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
-!- FUNCTION: May play a scavenger role by digesting biologically
active peptidoglycan (PGN) into biologically inactive fragments.
Has no direct bacteriolytic activity.
-!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl
residues and L-amino acid residues in certain cell-wall
glycopeptides.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P00806};
-!- SUBCELLULAR LOCATION: Secreted. Membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=TagL-alpha;
IsoId=Q8VCS0-1; Sequence=Displayed;
Name=2; Synonyms=TagL-beta;
IsoId=Q8VCS0-2; Sequence=VSP_009081;
Name=3; Synonyms=TagL-epsilon;
IsoId=Q8VCS0-3; Sequence=VSP_009079, VSP_009080;
-!- TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver.
-!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2
family. {ECO:0000305}.
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EMBL; AY282722; AAP22283.1; -; mRNA.
EMBL; AF392055; AAM73674.1; -; mRNA.
EMBL; AF149837; AAF22233.1; -; mRNA.
EMBL; AF149838; AAF22234.1; -; mRNA.
EMBL; BC019396; AAH19396.1; -; mRNA.
CCDS; CCDS37557.1; -. [Q8VCS0-1]
RefSeq; NP_001258405.1; NM_001271476.1. [Q8VCS0-1]
RefSeq; NP_001258407.1; NM_001271478.1. [Q8VCS0-3]
RefSeq; NP_001258408.1; NM_001271479.1.
RefSeq; NP_067294.2; NM_021319.5. [Q8VCS0-1]
RefSeq; XP_006524777.1; XM_006524714.3. [Q8VCS0-3]
UniGene; Mm.86752; -.
ProteinModelPortal; Q8VCS0; -.
SMR; Q8VCS0; -.
STRING; 10090.ENSMUSP00000110099; -.
iPTMnet; Q8VCS0; -.
PhosphoSitePlus; Q8VCS0; -.
EPD; Q8VCS0; -.
PaxDb; Q8VCS0; -.
PeptideAtlas; Q8VCS0; -.
PRIDE; Q8VCS0; -.
Ensembl; ENSMUST00000114455; ENSMUSP00000110099; ENSMUSG00000079563. [Q8VCS0-1]
Ensembl; ENSMUST00000170392; ENSMUSP00000129964; ENSMUSG00000079563. [Q8VCS0-1]
GeneID; 57757; -.
KEGG; mmu:57757; -.
UCSC; uc008bxa.3; mouse. [Q8VCS0-1]
UCSC; uc008bxc.3; mouse. [Q8VCS0-3]
CTD; 114770; -.
MGI; MGI:1928099; Pglyrp2.
eggNOG; ENOG410IIH1; Eukaryota.
eggNOG; ENOG4111PAY; LUCA.
GeneTree; ENSGT00390000016833; -.
HOGENOM; HOG000276878; -.
HOVERGEN; HBG053578; -.
InParanoid; Q8VCS0; -.
KO; K01446; -.
OMA; TEAFLGC; -.
OrthoDB; EOG091G0O6Z; -.
PhylomeDB; Q8VCS0; -.
TreeFam; TF323898; -.
Reactome; R-MMU-6803157; Antimicrobial peptides.
PRO; PR:Q8VCS0; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000079563; -.
CleanEx; MM_PGLYRP2; -.
Genevisible; Q8VCS0; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; ISO:MGI.
GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
GO; GO:0016019; F:peptidoglycan receptor activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
GO; GO:0044117; P:growth of symbiont in host; IMP:MGI.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:MGI.
GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; IMP:MGI.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
CDD; cd06583; PGRP; 1.
Gene3D; 3.40.80.10; -; 1.
InterPro; IPR036505; Amidase/PGRP_sf.
InterPro; IPR002502; Amidase_domain.
InterPro; IPR015510; PGRP.
InterPro; IPR006619; PGRP_domain_met/bac.
PANTHER; PTHR11022; PTHR11022; 1.
Pfam; PF01510; Amidase_2; 1.
SMART; SM00644; Ami_2; 1.
SMART; SM00701; PGRP; 1.
SUPFAM; SSF55846; SSF55846; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Immunity; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Secreted; Signal;
Zinc.
SIGNAL 1 22 {ECO:0000269|PubMed:12821140}.
CHAIN 23 530 N-acetylmuramoyl-L-alanine amidase.
/FTId=PRO_0000023921.
METAL 390 390 Zinc; via pros nitrogen.
{ECO:0000250|UniProtKB:Q8INK6}.
METAL 502 502 Zinc; via pros nitrogen.
{ECO:0000250|UniProtKB:Q8INK6}.
METAL 510 510 Zinc. {ECO:0000250|UniProtKB:Q8INK6}.
SITE 427 427 Important for catalytic activity;
essential for amidase activity and zinc
hydrate coordination.
{ECO:0000250|UniProtKB:P00806}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:Q96PD5}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 465 465 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 399 405 {ECO:0000250|UniProtKB:Q96PD5}.
VAR_SEQ 338 366 Missing (in isoform 2).
{ECO:0000303|PubMed:12559914}.
/FTId=VSP_009081.
VAR_SEQ 428 450 SFVVGSDGYLYQGRGWHWVGAHT -> RLKTKNSFERPLKI
QEVLSLMIL (in isoform 3).
{ECO:0000303|PubMed:12559914}.
/FTId=VSP_009079.
VAR_SEQ 451 530 Missing (in isoform 3).
{ECO:0000303|PubMed:12559914}.
/FTId=VSP_009080.
CONFLICT 486 486 Missing (in Ref. 2; AAF22233/AAF22234).
{ECO:0000305}.
SEQUENCE 530 AA; 57707 MW; D3BF52597CE5D1F9 CRC64;
MKAWGALWIV LGLLLWPEPG AASSLPLLMD SIIQALAELE QKVPVTEASI TASAWILSAK
NSSTHNSLHQ RLLLKAPSHN TTEPDPHSLS PELQALISEV AQHDVQNGRE YGVVLAPDGS
TVAVKPLLFG LEAGLQAHSV ANLPSDCLAI PCDTGDTLAN IRATWPGLMD AFPNASSPDV
GATLPNDKAK TPTTVDRLLA ITLAGDLGLT FLHRSQTWSP PGLGTEGCWD QLTAPRVFTL
LDPQASRLTM AFLNGALDGA LLGNHLSQIP RPHPPLSHLL REYYGAGVNG DPVFRSNFRR
QNGAALTSAP TLAQQVWEAL VLLQKLEPEH LQLQNISQEQ LAQVATLATK EFTEAFLGCP
AIHPRCRWGA APYRGHPTPL RLPLGFLYVH HTYVPAPPCT TFQSCAADMR SMQRFHQDVR
KWDDIGYSFV VGSDGYLYQG RGWHWVGAHT RGYNSRGFGV AFVGNYTGSL PNEAALNTVR
DALPSCAIRA GLLRPDYKLL GHRQLVLTHC PGNALFNLLR TWPHFTEVEN


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