PGRP2_MOUSE
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 03-AUG-2022, entry version 157.
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}.
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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.ENSMUSP00000129964; -.
DR GlyGen; Q8VCS0; 5 sites.
DR iPTMnet; Q8VCS0; -.
DR PhosphoSitePlus; Q8VCS0; -.
DR CPTAC; non-CPTAC-5616; -.
DR EPD; Q8VCS0; -.
DR MaxQB; Q8VCS0; -.
DR PaxDb; Q8VCS0; -.
DR PeptideAtlas; Q8VCS0; -.
DR PRIDE; Q8VCS0; -.
DR ProteomicsDB; 288107; -. [Q8VCS0-1]
DR ProteomicsDB; 288108; -. [Q8VCS0-2]
DR ProteomicsDB; 288109; -. [Q8VCS0-3]
DR Antibodypedia; 43600; 99 antibodies from 22 providers.
DR DNASU; 57757; -.
DR Ensembl; ENSMUST00000170392; ENSMUSP00000129964; ENSMUSG00000079563. [Q8VCS0-1]
DR Ensembl; ENSMUST00000236386; ENSMUSP00000158365; ENSMUSG00000079563. [Q8VCS0-1]
DR Ensembl; ENSMUST00000237130; ENSMUSP00000157771; ENSMUSG00000079563. [Q8VCS0-3]
DR GeneID; 57757; -.
DR KEGG; mmu:57757; -.
DR UCSC; uc008bxa.3; mouse. [Q8VCS0-1]
DR UCSC; uc008bxc.3; mouse. [Q8VCS0-3]
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; RCAADMR; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q8VCS0; -.
DR TreeFam; TF323898; -.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 57757; 2 hits in 72 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 tissues.
DR ExpressionAtlas; Q8VCS0; baseline and differential.
DR Genevisible; Q8VCS0; MM.
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:0032689; P:negative regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; 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; -; 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; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
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
