PGRP1_RAT
ID PGRP1_RAT Reviewed; 183 AA.
AC Q9JLN4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Peptidoglycan recognition protein 1;
DE AltName: Full=Peptidoglycan recognition protein short;
DE Short=PGRP-S;
DE Flags: Precursor;
GN Name=Pglyrp1; Synonyms=Pglyrp, Pgrp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX PubMed=11145837; DOI=10.1006/cyto.2000.0800;
RA Rehman A., Taishi P., Fang J., Majde J.A., Krueger J.M.;
RT "The cloning of a rat peptidoglycan recognition protein (PGRP) and its
RT induction in brain by sleep deprivation.";
RL Cytokine 13:8-17(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Innate immunity protein that plays several important
CC functions in antimicrobial and antitumor defense systems. Acts as a
CC pattern receptor that binds to murein peptidoglycans (PGN) of Gram-
CC positive bacteria and thus provides bactericidal activity. Forms an
CC equimolar complex with heat shock protein HSPA1A and induces programmed
CC cell death through apoptosis and necroptosis in tumor cell lines by
CC activating the TNFR1 receptor on the target cell membrane. In addition,
CC acts in complex with the Ca(2+)-binding protein S100A4 as a
CC chemoattractant able to induce lymphocyte movement. Mechanistically,
CC this complex acts as a ligand of the chemotactic receptors CCR5 and
CC CXCR3 which are present on the cells of the immune system. Promotes
CC also the activation of lymphocytes that become able to kill virus-
CC infected cells as well as tumor cells by modulating the spectrum of
CC their target-cell specificity. Induction of cytotoxicity on monocyte
CC surface requires interaction with TREM1 receptor.
CC {ECO:0000250|UniProtKB:O75594}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all regions of the brain.
CC -!- INDUCTION: By sleep deprivation in the brain stem and in the
CC hypothalamus.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AF154114; AAF73252.1; -; mRNA.
DR RefSeq; NP_445825.1; NM_053373.1.
DR AlphaFoldDB; Q9JLN4; -.
DR SMR; Q9JLN4; -.
DR BioGRID; 249930; 1.
DR IntAct; Q9JLN4; 1.
DR STRING; 10116.ENSRNOP00000018233; -.
DR iPTMnet; Q9JLN4; -.
DR PhosphoSitePlus; Q9JLN4; -.
DR PaxDb; Q9JLN4; -.
DR PRIDE; Q9JLN4; -.
DR GeneID; 84387; -.
DR KEGG; rno:84387; -.
DR UCSC; RGD:621429; rat.
DR CTD; 8993; -.
DR RGD; 621429; Pglyrp1.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR InParanoid; Q9JLN4; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q9JLN4; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR PRO; PR:Q9JLN4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:RGD.
DR GO; GO:0051701; P:biological process involved in interaction with host; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0016045; P:detection of bacterium; ISO:RGD.
DR GO; GO:0006955; P:immune response; TAS:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; ISO:RGD.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEP:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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; IPR017331; Peptidoglycan_recognition.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR PIRSF; PIRSF037945; PGRPs; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Disulfide bond; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..183
FT /note="Peptidoglycan recognition protein 1"
FT /id="PRO_0000023903"
FT DOMAIN 40..168
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DISULFID 18..142
FT /evidence="ECO:0000250"
FT DISULFID 34..79
FT /evidence="ECO:0000250"
FT DISULFID 55..61
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20591 MW; 5B9C1B7AA8A2EC21 CRC64;
MLFAWAPFPA LLGLADSCCF VVPRSEWKAL PSECSKGLKK PVRYVVISHT AGSFCSSPDS
CEQQARNVQL YQMKQLGWCD VAYNFLIGED GHVYEGRGWT IKGDHTGPIW NPMSIGITFM
GDYSHRVPAK RALRAALNLL KCGVSEGFLR SNYEVKGHRD VQSTLSPGDQ LYEIIQSWDH
YRE
