ID   PGRP2_MOUSE             Reviewed;         530 AA.
AC   Q8VCS0; Q8K4I8; Q9QXZ1; Q9QXZ2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
DE   AltName: Full=Peptidoglycan recognition protein 2;
DE   AltName: Full=Peptidoglycan recognition protein long;
DE            Short=PGRP-L;
DE   AltName: Full=TagL;
DE   Flags: Precursor;
GN   Name=Pglyrp2; Synonyms=Pglyrpl, Pgrpl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-37.
RC   STRAIN=C57BL/6J;
RX   PubMed=12821140; DOI=10.1016/s0006-291x(03)01096-9;
RA   Gelius E., Persson C., Karlsson J., Steiner H.;
RT   "A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-
RT   alanine amidase activity.";
RL   Biochem. Biophys. Res. Commun. 306:988-994(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX   PubMed=12559914; DOI=10.1016/s0022-2836(02)01401-8;
RA   Kibardin A.V., Mirkina I.I., Baranova E.V., Zakeyeva I.R., Georgiev G.P.,
RA   Kiselev S.L.;
RT   "The differentially spliced mouse tagL gene, homolog of tag7/PGRP gene
RT   family in mammals and Drosophila, can recognize Gram-positive and Gram-
RT   negative bacterial cell wall independently of T phage lysozyme homology
RT   domain.";
RL   J. Mol. Biol. 326:467-474(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
CC   -!- FUNCTION: May play a scavenger role by digesting biologically active
CC       peptidoglycan (PGN) into biologically inactive fragments. Has no direct
CC       bacteriolytic activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00806};
CC   -!- SUBCELLULAR LOCATION: Secreted. Membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=TagL-alpha;
CC         IsoId=Q8VCS0-1; Sequence=Displayed;
CC       Name=2; Synonyms=TagL-beta;
CC         IsoId=Q8VCS0-2; Sequence=VSP_009081;
CC       Name=3; Synonyms=TagL-epsilon;
CC         IsoId=Q8VCS0-3; Sequence=VSP_009079, VSP_009080;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY282722; AAP22283.1; -; mRNA.
DR   EMBL; AF392055; AAM73674.1; -; mRNA.
DR   EMBL; AF149837; AAF22233.1; -; mRNA.
DR   EMBL; AF149838; AAF22234.1; -; mRNA.
DR   EMBL; BC019396; AAH19396.1; -; mRNA.
DR   CCDS; CCDS37557.1; -. [Q8VCS0-1]
DR   CCDS; CCDS89065.1; -. [Q8VCS0-3]
DR   RefSeq; NP_001258405.1; NM_001271476.1. [Q8VCS0-1]
DR   RefSeq; NP_001258407.1; NM_001271478.1. [Q8VCS0-3]
DR   RefSeq; NP_001258408.1; NM_001271479.1.
DR   RefSeq; NP_067294.2; NM_021319.5. [Q8VCS0-1]
DR   RefSeq; XP_006524777.1; XM_006524714.3. [Q8VCS0-3]
DR   AlphaFoldDB; Q8VCS0; -.
DR   SMR; Q8VCS0; -.
DR   STRING; 10090.ENSMUSP00000158365; -.
DR   GlyCosmos; Q8VCS0; 5 sites, No reported glycans.
DR   GlyGen; Q8VCS0; 5 sites.
DR   iPTMnet; Q8VCS0; -.
DR   PhosphoSitePlus; Q8VCS0; -.
DR   CPTAC; non-CPTAC-5616; -.
DR   EPD; Q8VCS0; -.
DR   MaxQB; Q8VCS0; -.
DR   PaxDb; 10090-ENSMUSP00000129964; -.
DR   PeptideAtlas; Q8VCS0; -.
DR   ProteomicsDB; 288107; -. [Q8VCS0-1]
DR   ProteomicsDB; 288108; -. [Q8VCS0-2]
DR   ProteomicsDB; 288109; -. [Q8VCS0-3]
DR   Antibodypedia; 43600; 107 antibodies from 23 providers.
DR   DNASU; 57757; -.
DR   Ensembl; ENSMUST00000170392.9; ENSMUSP00000129964.2; ENSMUSG00000079563.11. [Q8VCS0-1]
DR   Ensembl; ENSMUST00000236386.2; ENSMUSP00000158365.2; ENSMUSG00000079563.11. [Q8VCS0-1]
DR   Ensembl; ENSMUST00000237130.2; ENSMUSP00000157771.2; ENSMUSG00000079563.11. [Q8VCS0-3]
DR   GeneID; 57757; -.
DR   KEGG; mmu:57757; -.
DR   UCSC; uc008bxa.3; mouse. [Q8VCS0-1]
DR   UCSC; uc008bxc.3; mouse. [Q8VCS0-3]
DR   AGR; MGI:1928099; -.
DR   CTD; 114770; -.
DR   MGI; MGI:1928099; Pglyrp2.
DR   VEuPathDB; HostDB:ENSMUSG00000079563; -.
DR   eggNOG; ENOG502QR3D; Eukaryota.
DR   GeneTree; ENSGT00940000158718; -.
DR   HOGENOM; CLU_038892_0_0_1; -.
DR   InParanoid; Q8VCS0; -.
DR   OMA; TLTQQVW; -.
DR   OrthoDB; 2282228at2759; -.
DR   PhylomeDB; Q8VCS0; -.
DR   TreeFam; TF323898; -.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   BioGRID-ORCS; 57757; 2 hits in 77 CRISPR screens.
DR   PRO; PR:Q8VCS0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8VCS0; Protein.
DR   Bgee; ENSMUSG00000079563; Expressed in left lobe of liver and 42 other cell types or tissues.
DR   ExpressionAtlas; Q8VCS0; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; ISO:MGI.
DR   GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
DR   GO; GO:0016019; F:peptidoglycan immune receptor activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:MGI.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; IMP:MGI.
DR   GO; GO:0032689; P:negative regulation of type II interferon production; IMP:MGI.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022:SF66; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   Genevisible; Q8VCS0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:12821140"
FT   CHAIN           23..530
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /id="PRO_0000023921"
FT   DOMAIN          386..512
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         502
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         510
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   SITE            427
FT                   /note="Important for catalytic activity; essential for
FT                   amidase activity and zinc hydrate coordination"
FT                   /evidence="ECO:0000250|UniProtKB:P00806"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PD5"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16944957"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        399..405
FT                   /evidence="ECO:0000250|UniProtKB:Q96PD5"
FT   VAR_SEQ         338..366
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12559914"
FT                   /id="VSP_009081"
FT   VAR_SEQ         428..450
FT                   /note="SFVVGSDGYLYQGRGWHWVGAHT -> RLKTKNSFERPLKIQEVLSLMIL
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12559914"
FT                   /id="VSP_009079"
FT   VAR_SEQ         451..530
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12559914"
FT                   /id="VSP_009080"
FT   CONFLICT        486
FT                   /note="Missing (in Ref. 2; AAF22233/AAF22234)"
FT                   /evidence="ECO:0000305"
SQ   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
//