PGRP3_MOUSE
ID PGRP3_MOUSE Reviewed; 347 AA.
AC A1A547; E9QMH8; Q6R1Z2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Peptidoglycan recognition protein 3;
DE AltName: Full=Peptidoglycan recognition protein I-alpha;
DE Short=PGLYRPIalpha;
DE Short=PGRP-I-alpha;
DE AltName: Full=Peptidoglycan recognition protein intermediate alpha;
DE Flags: Precursor;
GN Name=Pglyrp3; Synonyms=Gm420, Pgrpia;
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], AND TISSUE SPECIFICITY.
RX PubMed=15177568; DOI=10.1016/j.ygeno.2004.01.003;
RA Mathur P., Murray B., Crowell T., Gardner H., Allaire N., Hsu Y.-M.,
RA Thill G., Carulli J.P.;
RT "Murine peptidoglycan recognition proteins PglyrpIalpha and PglyrpIbeta are
RT encoded in the epidermal differentiation complex and are expressed in
RT epidermal and hematopoietic tissues.";
RL Genomics 83:1151-1163(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of
CC Gram-positive bacteria. Has bactericidal activity towards Gram-positive
CC bacteria. May kill Gram-positive bacteria by interfering with
CC peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and
CC has bacteriostatic activity towards Gram-negative bacteria. Plays a
CC role in innate immunity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked. Heterodimer with
CC PGLYRP4; disulfide-linked (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in lung, spleen and stomach, and at low
CC levels in eye, heart, thymus and testis. {ECO:0000269|PubMed:15177568}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AY518698; AAS49172.1; -; mRNA.
DR EMBL; AC163215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128291; AAI28292.1; -; mRNA.
DR CCDS; CCDS17545.1; -.
DR RefSeq; NP_997130.2; NM_207247.4.
DR AlphaFoldDB; A1A547; -.
DR SMR; A1A547; -.
DR STRING; 10090.ENSMUSP00000035737; -.
DR GlyGen; A1A547; 1 site.
DR PhosphoSitePlus; A1A547; -.
DR PaxDb; A1A547; -.
DR PRIDE; A1A547; -.
DR ProteomicsDB; 287922; -.
DR Antibodypedia; 34121; 72 antibodies from 25 providers.
DR DNASU; 242100; -.
DR Ensembl; ENSMUST00000047660; ENSMUSP00000035737; ENSMUSG00000042244.
DR GeneID; 242100; -.
DR KEGG; mmu:242100; -.
DR UCSC; uc008qdi.2; mouse.
DR CTD; 114771; -.
DR MGI; MGI:2685266; Pglyrp3.
DR VEuPathDB; HostDB:ENSMUSG00000042244; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000162657; -.
DR HOGENOM; CLU_037559_1_0_1; -.
DR InParanoid; A1A547; -.
DR OMA; WHIQGSH; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; A1A547; -.
DR TreeFam; TF323898; -.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 242100; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pglyrp3; mouse.
DR PRO; PR:A1A547; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A1A547; protein.
DR Bgee; ENSMUSG00000042244; Expressed in esophagus and 11 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
DR GO; GO:0016019; F:peptidoglycan immune receptor activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0016045; P:detection of bacterium; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
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 CDD; cd06583; PGRP; 2.
DR Gene3D; 3.40.80.10; -; 2.
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; 2.
DR SMART; SM00644; Ami_2; 2.
DR SMART; SM00701; PGRP; 2.
DR SUPFAM; SSF55846; SSF55846; 2.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..347
FT /note="Peptidoglycan recognition protein 3"
FT /id="PRO_0000295274"
FT DOMAIN 77..185
FT /note="N-acetylmuramoyl-L-alanine amidase 1"
FT /evidence="ECO:0000255"
FT DOMAIN 206..328
FT /note="N-acetylmuramoyl-L-alanine amidase 2"
FT /evidence="ECO:0000255"
FT REGION 270..275
FT /note="Interaction with murein"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="peptidoglycan"
FT /ligand_id="ChEBI:CHEBI:8005"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="peptidoglycan"
FT /ligand_id="ChEBI:CHEBI:8005"
FT /evidence="ECO:0000250"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 184..306
FT /evidence="ECO:0000250"
FT DISULFID 200..244
FT /evidence="ECO:0000250"
FT DISULFID 220..226
FT /evidence="ECO:0000250"
FT CONFLICT 149
FT /note="F -> S (in Ref. 1; AAS49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Y -> H (in Ref. 1; AAS49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="I -> T (in Ref. 1; AAS49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> G (in Ref. 1; AAS49172 and 3; AAI28292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38503 MW; 1AAEF71374B66F4C CRC64;
MLVSWDHPKM LPRLLGFLAL SLLACGNPTI VSRKEWGASS LTCRVPLSLP VPYLIIEQVT
RMQCQDQITC SQVVRVLQSQ YVHNKGWCDI AFNFLVGDDG KVYEGVGWYV QGLHTQGYNN
VSLGIAFFGS KIGSPSPAAL SATEDLIFFA IQNGYLSPKY IQPFLLKEET CLVPQHSEIP
KKACPNITPR SAWEARETHC PQMNLPAKFV IIIHTAGKSC NESADCLVRV RDTQSFHIDN
QDFCDIAYHF LVGQDGEVYE GVGWNIEGSH TYGYNDIALG IAFMGNFVEK PPNEASLKAA
QSLIQCAVAK GYLTSNYLLM GHSDVSNILS PGQALYNIIK TWPHFKH
