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PGRP4_MOUSE
ID   PGRP4_MOUSE             Reviewed;         374 AA.
AC   Q0VB07; Q6R1Z1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Peptidoglycan recognition protein 4;
DE   AltName: Full=Peptidoglycan recognition protein I-beta;
DE            Short=PGLYRPIbeta;
DE            Short=PGRP-I-beta;
DE   AltName: Full=Peptidoglycan recognition protein intermediate beta;
DE   Flags: Precursor;
GN   Name=Pglyrp4; Synonyms=Pgrpib;
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 MRNA].
RC   TISSUE=Brain;
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: Homodimer; disulfide-linked. Heterodimer with PGLYRP3;
CC       disulfide-linked (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {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; AY518699; AAS49173.1; -; mRNA.
DR   EMBL; BC120840; AAI20841.1; -; mRNA.
DR   CCDS; CCDS17544.1; -.
DR   RefSeq; NP_997146.2; NM_207263.2.
DR   AlphaFoldDB; Q0VB07; -.
DR   SMR; Q0VB07; -.
DR   STRING; 10090.ENSMUSP00000040755; -.
DR   GlyGen; Q0VB07; 3 sites.
DR   iPTMnet; Q0VB07; -.
DR   PhosphoSitePlus; Q0VB07; -.
DR   jPOST; Q0VB07; -.
DR   PaxDb; Q0VB07; -.
DR   PRIDE; Q0VB07; -.
DR   ProteomicsDB; 288188; -.
DR   Antibodypedia; 34122; 181 antibodies from 26 providers.
DR   DNASU; 384997; -.
DR   Ensembl; ENSMUST00000047745; ENSMUSP00000040755; ENSMUSG00000042250.
DR   GeneID; 384997; -.
DR   KEGG; mmu:384997; -.
DR   UCSC; uc008qdg.2; mouse.
DR   CTD; 57115; -.
DR   MGI; MGI:2686324; Pglyrp4.
DR   VEuPathDB; HostDB:ENSMUSG00000042250; -.
DR   eggNOG; ENOG502S2KY; Eukaryota.
DR   GeneTree; ENSGT00940000162349; -.
DR   InParanoid; Q0VB07; -.
DR   OMA; AREAHCP; -.
DR   TreeFam; TF323898; -.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   BioGRID-ORCS; 384997; 4 hits in 73 CRISPR screens.
DR   PRO; PR:Q0VB07; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q0VB07; protein.
DR   Bgee; ENSMUSG00000042250; Expressed in esophagus and 10 other tissues.
DR   ExpressionAtlas; Q0VB07; baseline and differential.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..374
FT                   /note="Peptidoglycan recognition protein 4"
FT                   /id="PRO_0000295275"
FT   DOMAIN          76..212
FT                   /note="N-acetylmuramoyl-L-alanine amidase 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          233..359
FT                   /note="N-acetylmuramoyl-L-alanine amidase 2"
FT                   /evidence="ECO:0000255"
FT   REGION          294..303
FT                   /note="Interaction with murein"
FT                   /evidence="ECO:0000250"
FT   REGION          354..355
FT                   /note="Interaction with murein"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="peptidoglycan"
FT                   /ligand_id="ChEBI:CHEBI:8005"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        211..333
FT                   /evidence="ECO:0000250"
FT   DISULFID        227..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..253
FT                   /evidence="ECO:0000250"
FT   CONFLICT        334
FT                   /note="A -> T (in Ref. 1; AAS49173)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  41190 MW;  A677F7E1BD621532 CRC64;
     MLSWLLVFSI LVLLAQGVSS WENPQTDQVS EGLQQLFGNI SQLFEKGILG RDDVFTMVSR
     EEWGAEAIGC SSKLSRPVDV LVIHHIPGLE CHNKTVCSQK LRELQAYHIH NSWCDVAYNF
     LVGDDGRVYE GVGWNVQGSH DQGYKNISLG VAFFGTQEGH SPSPVALSAM KGLISYAVKK
     GHLSSKYIQP LLAKSEDCLV PPQKGKQKKA CPHIVPRSVW GARDSHCSRM TLPAKYAIIL
     HTAGRTCSQP DECRLLVRDL QSFFMNRLNA CDIGYNFLVG QDGGVYEGVG WNNQGSKTDS
     YNDISLSITF MGTFTGSPPN AAALEAAQDL IRCAVVKGYL TPNYLLMGHS DVSNTLSPGQ
     ALYNIIKTWP HFKH
 
 
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