PGRP1_MOUSE
ID PGRP1_MOUSE Reviewed; 182 AA.
AC O88593; Q62185;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Peptidoglycan recognition protein 1;
DE AltName: Full=Cytokine tag7;
DE AltName: Full=Peptidoglycan recognition protein short;
DE Short=PGRP-S;
DE Flags: Precursor;
GN Name=Pglyrp1; Synonyms=Pglyrp, Pgrp, Pgrps, Tag7;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=9707603; DOI=10.1073/pnas.95.17.10078;
RA Kang D., Liu G., Lundstroem A., Gelius E., Steiner H.;
RT "A peptidoglycan recognition protein in innate immunity conserved from
RT insects to humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10078-10082(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9660837; DOI=10.1074/jbc.273.29.18633;
RA Kiselev S.L., Kustikova O.S., Korobko E.V., Prokhortchouk E.B.,
RA Kabishev A.A., Lukanidin E.M., Georgiev G.P.;
RT "Molecular cloning and characterization of the mouse tag7 gene encoding a
RT novel cytokine.";
RL J. Biol. Chem. 273:18633-18639(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Slayton W.B., Rigaa A., Hancock J.D., Zaugg J.K., Le T.V., Trautman M.S.,
RA Spangrude G.J., Carroll W.L., Schibler K.R.;
RT "Granulocyte-colony stimulating factor up-regulates expression of murine
RT tag7 during myeloid differentiation.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=129/Sv;
RX PubMed=12649138; DOI=10.1182/blood-2002-12-3853;
RA Dziarski R., Platt K.A., Gelius E., Steiner H., Gupta D.;
RT "Defect in neutrophil killing and increased susceptibility to infection
RT with nonpathogenic Gram-positive bacteria in peptidoglycan recognition
RT protein-S (PGRP-S)-deficient mice.";
RL Blood 102:689-697(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
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).
RN [7]
RP INTERACTION WITH HSPA1A, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14585845; DOI=10.1074/jbc.m307513200;
RA Sashchenko L.P., Dukhanina E.A., Yashin D.V., Shatalov Y.V., Romanova E.A.,
RA Korobko E.V., Demin A.V., Lukyanova T.I., Kabanova O.D., Khaidukov S.V.,
RA Kiselev S.L., Gabibov A.G., Gnuchev N.V., Georgiev G.P.;
RT "Peptidoglycan recognition protein tag7 forms a cytotoxic complex with heat
RT shock protein 70 in solution and in lymphocytes.";
RL J. Biol. Chem. 279:2117-2124(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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
CC (PubMed:9707603, PubMed:9660837, PubMed:12649138). Forms an equimolar
CC complex with heat shock protein HSPA1A and induces programmed cell
CC death through apoptosis and necroptosis in tumor cell lines by
CC activating the TNFR1 receptor on the target cell membrane
CC (PubMed:14585845). In addition, acts in complex with the Ca(2+)-binding
CC protein S100A4 as a chemoattractant able to induce lymphocyte movement.
CC Mechanistically, this complex acts as a ligand of the chemotactic
CC receptors CCR5 and CXCR3 which are present on the cells of the immune
CC system. Promotes also the activation of lymphocytes that become able to
CC kill virus-infected cells as well as tumor cells by modulating the
CC spectrum of their target-cell specificity. Induction of cytotoxicity on
CC monocyte surface requires interaction with TREM1 receptor (By
CC similarity). {ECO:0000250|UniProtKB:O75594,
CC ECO:0000269|PubMed:12649138, ECO:0000269|PubMed:14585845,
CC ECO:0000269|PubMed:9660837, ECO:0000269|PubMed:9707603}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with HSPA1A; this
CC interaction forms a cytotoxic complex that is released by lymphokine-
CC activated killer cells (PubMed:14585845). Interacts with HSPBP1; this
CC interaction blocks the cytotoxic activity of the PGLYRP1-HSPA1A complex
CC (PubMed:14585845). {ECO:0000269|PubMed:14585845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9660837}. Secreted
CC {ECO:0000269|PubMed:14585845, ECO:0000269|PubMed:9660837}. Note=Exists
CC in both soluble and membrane-associated forms.
CC -!- TISSUE SPECIFICITY: Strongly expressed in spleen and lung. Also
CC detected in brain and thymus. In the lung, expressed in the
CC intraalveolar space, in the brain, expressed in the Purkinje cells of
CC the cerebellum and in certain layers of neurons in the hippocampus.
CC Also detected in cells filling the space within the intestinal villus.
CC {ECO:0000269|PubMed:9707603}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA60133.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF076482; AAC31821.1; -; mRNA.
DR EMBL; X86374; CAA60133.1; ALT_FRAME; mRNA.
DR EMBL; Y12088; CAA72803.1; -; Genomic_DNA.
DR EMBL; AF193843; AAF06335.1; -; mRNA.
DR EMBL; AY144361; AAN52146.1; -; Genomic_DNA.
DR EMBL; AY144360; AAN52146.1; JOINED; Genomic_DNA.
DR EMBL; AK008335; BAB25611.1; -; mRNA.
DR EMBL; BC005582; AAH05582.1; -; mRNA.
DR CCDS; CCDS20881.1; -.
DR RefSeq; NP_033428.1; NM_009402.2.
DR AlphaFoldDB; O88593; -.
DR SMR; O88593; -.
DR STRING; 10090.ENSMUSP00000032573; -.
DR PhosphoSitePlus; O88593; -.
DR PaxDb; O88593; -.
DR PeptideAtlas; O88593; -.
DR PRIDE; O88593; -.
DR ProteomicsDB; 288187; -.
DR Antibodypedia; 18065; 354 antibodies from 35 providers.
DR DNASU; 21946; -.
DR Ensembl; ENSMUST00000032573; ENSMUSP00000032573; ENSMUSG00000030413.
DR GeneID; 21946; -.
DR KEGG; mmu:21946; -.
DR UCSC; uc009fjv.1; mouse.
DR CTD; 8993; -.
DR MGI; MGI:1345092; Pglyrp1.
DR VEuPathDB; HostDB:ENSMUSG00000030413; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000161006; -.
DR HOGENOM; CLU_037559_3_2_1; -.
DR InParanoid; O88593; -.
DR OMA; FKGDHSS; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; O88593; -.
DR TreeFam; TF323898; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 21946; 4 hits in 72 CRISPR screens.
DR PRO; PR:O88593; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88593; protein.
DR Bgee; ENSMUSG00000030413; Expressed in granulocyte and 129 other tissues.
DR ExpressionAtlas; O88593; baseline and differential.
DR Genevisible; O88593; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
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: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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:0050728; P:negative regulation of inflammatory response; IMP: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 GO; GO:0009617; P:response to bacterium; IEP: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; 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; Apoptosis; Cytokine; Cytoplasm; Disulfide bond;
KW Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..182
FT /note="Peptidoglycan recognition protein 1"
FT /id="PRO_0000023902"
FT DOMAIN 39..167
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DISULFID 17..141
FT /evidence="ECO:0000250"
FT DISULFID 33..78
FT /evidence="ECO:0000250"
FT DISULFID 54..60
FT /evidence="ECO:0000250"
FT CONFLICT 141
FT /note="C -> S (in Ref. 2; CAA60133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20489 MW; 9844E2137F047F14 CRC64;
MLFACALLAL LGLATSCSFI VPRSEWRALP SECSSRLGHP VRYVVISHTA GSFCNSPDSC
EQQARNVQHY HKNELGWCDV AYNFLIGEDG HVYEGRGWNI KGDHTGPIWN PMSIGITFMG
NFMDRVPAKR ALRAALNLLE CGVSRGFLRS NYEVKGHRDV QSTLSPGDQL YQVIQSWEHY
RE
