ID   PGRP_TRINI              Reviewed;         182 AA.
AC   O76537;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Peptidoglycan recognition protein;
DE   Flags: Precursor;
GN   Name=PGRP;
OS   Trichoplusia ni (Cabbage looper).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Plusiinae; Trichoplusia.
OX   NCBI_TaxID=7111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-21, TISSUE SPECIFICITY,
RP   AND INDUCTION.
RC   TISSUE=Larva;
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).
CC   -!- FUNCTION: Binds specifically to peptidoglycan and triggers the
CC       propenoloxidase cascade which is an important insect innate immune
CC       defense mechanism.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in fat body with weak expression
CC       observed in hemocyte. No expression detected in gut.
CC       {ECO:0000269|PubMed:9707603}.
CC   -!- INDUCTION: By bacterial challenge. {ECO:0000269|PubMed:9707603}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF076481; AAC31820.1; -; mRNA.
DR   AlphaFoldDB; O76537; -.
DR   SMR; O76537; -.
DR   Proteomes; UP000322000; Genome assembly.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; 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   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:9707603"
FT   CHAIN           17..182
FT                   /note="Peptidoglycan recognition protein"
FT                   /id="PRO_0000023919"
FT   DOMAIN          39..166
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   DISULFID        18..140
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..60
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   182 AA;  20572 MW;  56631E762AE34794 CRC64;
     MEILFVLFFV FVTVSGDCGV VTKDEWDGLT PIHVEYLARP VELVIIQHTV TSTCNTDAAC
     AQIVRNIQSY HMDNLNYWDI GSSFIIGGNG KVYEGAGWLH VGAHTYGYNR KSIGITFIGN
     YNNDKPTQKS LDALRALLRC GVERGHLTAN YHIVGHRQLI STESPGRKLY NEIRRWDHFL
     DN