ID   PGRP1_BOSIN             Reviewed;         190 AA.
AC   B5T255;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Peptidoglycan recognition protein 1;
DE   Flags: Precursor;
GN   Name=PGLYRP1;
OS   Bos indicus (Zebu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 23, and Isolate 86;
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).
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   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; EU746449; ACH92778.1; -; Genomic_DNA.
DR   EMBL; EU746453; ACH92782.1; -; Genomic_DNA.
DR   RefSeq; XP_019834179.1; XM_019978620.1.
DR   AlphaFoldDB; B5T255; -.
DR   SMR; B5T255; -.
DR   PRIDE; B5T255; -.
DR   GeneID; 109572082; -.
DR   KEGG; biu:109572082; -.
DR   CTD; 8993; -.
DR   OrthoDB; 1110472at2759; -.
DR   Proteomes; UP000515132; Chromosome 18.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Immunity;
KW   Innate immunity; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..190
FT                   /note="Peptidoglycan recognition protein 1"
FT                   /id="PRO_0000363765"
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:0000250|UniProtKB:Q8SPP7"
FT   DISULFID        24..148
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..67
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  21037 MW;  9AA7DAEF85542361 CRC64;
     MSRRYTPLAW VLLALLGLGA AQDCGSIVSR GKWGALASKC SQRLRQPVRY VVVSHTAGSV
     CNTPASCQRQ AQNVQHYHVR ERGWCDVGYN FLIGEDGLVY EGRGWNTLGA HSGPTWNPIA
     IGISFMGNYM HRVPPASALR AAQSLLACGA ARGYLTPNYE VKGHRDVQQT LSPGDELYKI
     IQQWPHYRRV