PGRP1_BOVIN
ID PGRP1_BOVIN Reviewed; 190 AA.
AC Q8SPP7; A5PJC0; B5T256; B5T261;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peptidoglycan recognition protein 1;
DE AltName: Full=Oligosaccharide-binding protein;
DE Short=OBP;
DE AltName: Full=Peptidoglycan recognition protein short;
DE Short=PGRP-S;
DE Flags: Precursor;
GN Name=PGLYRP1; Synonyms=PGLYRP, PGRP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-43; 50-55; 83-88;
RP 127-145; 141-146 AND 178-190, TISSUE SPECIFICITY, FUNCTION, PYROGLUTAMATE
RP FORMATION AT GLN-22, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11880375; DOI=10.1074/jbc.m200659200;
RA Tydell C.C., Yount N., Tran D., Yuan J., Selsted M.E.;
RT "Isolation, characterization, and antimicrobial properties of bovine
RT oligosaccharide-binding protein. A microbicidal granule protein of
RT eosinophils and neutrophils.";
RL J. Biol. Chem. 277:19658-19664(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 44, Isolate 74, Isolate 80, and Isolate JEW38;
RX PubMed=18639626; DOI=10.1016/j.ygeno.2008.06.005;
RA Seabury C.M., Womack J.E.;
RT "Analysis of sequence variability and protein domain architectures for
RT bovine peptidoglycan recognition protein 1 and Toll-like receptors 2 and
RT 6.";
RL Genomics 92:235-245(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Mammary gland;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16394004; DOI=10.4049/jimmunol.176.2.1154;
RA Tydell C.C., Yuan J., Tran P., Selsted M.E.;
RT "Bovine peptidoglycan recognition protein-S: antimicrobial activity,
RT localization, secretion, and binding properties.";
RL J. Immunol. 176:1154-1162(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
CC (PubMed:11880375, PubMed:16394004). Forms an equimolar complex with
CC heat shock protein HSPA1A and induces programmed cell death through
CC apoptosis and necroptosis in tumor cell lines by activating the TNFR1
CC receptor on the target cell membrane. In addition, acts in complex with
CC the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce
CC lymphocyte movement. Mechanistically, this complex acts as a ligand of
CC the chemotactic receptors CCR5 and CXCR3 which are present on the cells
CC of the immune system. Promotes also the activation of lymphocytes that
CC become able to kill virus-infected cells as well as tumor cells by
CC modulating the spectrum of their target-cell specificity. Induction of
CC cytotoxicity on monocyte surface requires interaction with TREM1
CC receptor (By similarity). {ECO:0000250|UniProtKB:O75594,
CC ECO:0000269|PubMed:11880375, ECO:0000269|PubMed:16394004}.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16394004}.
CC Cytoplasmic granule {ECO:0000269|PubMed:16394004}.
CC -!- TISSUE SPECIFICITY: Synthesized only in bone marrow. The mature protein
CC is stored in the cytoplasmic granules of eosinophils and neutrophils
CC but is absent from monocytes, lymphocytes, or platelets.
CC {ECO:0000269|PubMed:11880375}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AY083309; AAL87002.1; -; mRNA.
DR EMBL; EU746450; ACH92779.1; -; Genomic_DNA.
DR EMBL; EU746451; ACH92780.1; -; Genomic_DNA.
DR EMBL; EU746452; ACH92781.1; -; Genomic_DNA.
DR EMBL; EU746455; ACH92784.1; -; Genomic_DNA.
DR EMBL; BC142042; AAI42043.1; -; mRNA.
DR RefSeq; NP_776998.1; NM_174573.3.
DR AlphaFoldDB; Q8SPP7; -.
DR SMR; Q8SPP7; -.
DR STRING; 9913.ENSBTAP00000003414; -.
DR PaxDb; Q8SPP7; -.
DR PeptideAtlas; Q8SPP7; -.
DR PRIDE; Q8SPP7; -.
DR Ensembl; ENSBTAT00000003414; ENSBTAP00000003414; ENSBTAG00000002635.
DR GeneID; 282305; -.
DR KEGG; bta:282305; -.
DR CTD; 8993; -.
DR VEuPathDB; HostDB:ENSBTAG00000002635; -.
DR VGNC; VGNC:32791; PGLYRP1.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000161006; -.
DR HOGENOM; CLU_037559_3_2_1; -.
DR InParanoid; Q8SPP7; -.
DR OMA; FKGDHSS; -.
DR OrthoDB; 1110472at2759; -.
DR TreeFam; TF323898; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000002635; Expressed in thymus and 82 other tissues.
DR ExpressionAtlas; Q8SPP7; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0016045; P:detection of bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
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; Direct protein sequencing; Disulfide bond;
KW Fungicide; Immunity; Innate immunity; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..190
FT /note="Peptidoglycan recognition protein 1"
FT /id="PRO_0000023899"
FT DOMAIN 46..174
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11880375"
FT DISULFID 24..148
FT DISULFID 40..85
FT DISULFID 61..67
FT VARIANT 184
FT /note="W -> G (in strain: Isolate JEW38)"
SQ SEQUENCE 190 AA; 21063 MW; 2BA7D659438F4ED7 CRC64;
MSRRYTPLAW VLLALLGLGA AQDCGSIVSR GKWGALASKC SQRLRQPVRY VVVSHTAGSV
CNTPASCQRQ AQNVQYYHVR ERGWCDVGYN FLIGEDGLVY EGRGWNTLGA HSGPTWNPIA
IGISFMGNYM HRVPPASALR AAQSLLACGA ARGYLTPNYE VKGHRDVQQT LSPGDELYKI
IQQWPHYRRV
