ID IMPI_GALME Reviewed; 170 AA. AC P82176; Q67FQ9; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 28-JUN-2023, entry version 81. DE RecName: Full=Inducible metalloproteinase inhibitor protein; DE Contains: DE RecName: Full=IMPI alpha; DE Flags: Precursor; GN Name=IMPI; OS Galleria mellonella (Greater wax moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea; OC Pyralidae; Galleriinae; Galleria. OX NCBI_TaxID=7137; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION. RX PubMed=15115439; DOI=10.1042/bj20031923; RA Clermont A., Wedde M., Seitz V., Podsiadlowski L., Lenze D., Hummel M., RA Vilcinskas A.; RT "Cloning and expression of an inhibitor of microbial metalloproteinases RT from insects contributing to innate immunity."; RL Biochem. J. 382:315-322(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Weise C., Bender O., Kopacek P., Hucho F.; RT "Hemolymph proteins of the greater wax moth, Galleria mellonella."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 57-82, FUNCTION, INDUCTION, BLOCKAGE OF N-TERMINUS, AND RP GLYCOSYLATION AT ASN-48. RC TISSUE=Larval hemolymph; RX PubMed=9738891; DOI=10.1046/j.1432-1327.1998.2550535.x; RA Wedde M., Weise C., Kopacek P., Franke P., Vilcinskas A.; RT "Purification and characterization of an inducible metalloprotease RT inhibitor from the hemolymph of greater wax moth larvae, Galleria RT mellonella."; RL Eur. J. Biochem. 255:535-543(1998). RN [4] RP SEQUENCE REVISION TO 63, AND MASS SPECTROMETRY. RA Weise C.; RL Submitted (JUL-2003) to UniProtKB. RN [5] {ECO:0000305} RP DEVELOPMENTAL STAGE, AND INDUCTION BY A.NIGER ALPHA-1,3-GLUCAN. RX PubMed=34443685; DOI=10.3390/molecules26165097; RA Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P., RA Skrzypiec K., Cytrynska M.; RT "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in RT the Insect Model Host Galleria mellonella."; RL Molecules 26:5097-5097(2021). CC -!- FUNCTION: Inhibits thermolysin, bacillolysin and pseudolysin, CC B.polymyxa metalloprotease and human MMP1 and MMP3. No activity on CC trypsin or cysteine protease papain. {ECO:0000269|PubMed:15115439, CC ECO:0000269|PubMed:9738891}. CC -!- DEVELOPMENTAL STAGE: Expressed in fat body of last instar larvae. CC {ECO:0000269|PubMed:34443685}. CC -!- INDUCTION: During humoral immune response (PubMed:9738891). By CC lipopolysaccharide (LPS) (PubMed:15115439). Induced by A.niger alpha- CC 1,3-glucan (PubMed:34443685). {ECO:0000269|PubMed:15115439, CC ECO:0000269|PubMed:34443685, ECO:0000269|PubMed:9738891}. CC -!- PTM: Cleaved. {ECO:0000305}. CC -!- PTM: Five disulfide bonds are present. When artificially cleaved by CC thermolysin between Asn-56 and Ile-57, the two obtained chains (called CC heavy and light chains) remain linked. CC -!- PTM: The N-terminus is blocked. CC -!- MASS SPECTROMETRY: [IMPI alpha]: Mass=8360; Method=MALDI; CC Evidence={ECO:0000269|Ref.4}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY330624; AAQ73240.1; -; mRNA. DR EMBL; AJ577749; CAE12200.1; -; mRNA. DR PDB; 3SSB; X-ray; 1.80 A; C/D=19-56, I/J=57-88. DR PDBsum; 3SSB; -. DR AlphaFoldDB; P82176; -. DR SMR; P82176; -. DR MEROPS; I08.006; -. DR GlyCosmos; P82176; 2 sites, No reported glycans. DR iPTMnet; P82176; -. DR InParanoid; P82176; -. DR EvolutionaryTrace; P82176; -. DR Proteomes; UP000504614; Unplaced. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0009653; P:anatomical structure morphogenesis; NAS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB. DR GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0042060; P:wound healing; NAS:UniProtKB. DR CDD; cd19941; TIL; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR InterPro; IPR036084; Ser_inhib-like_sf. DR InterPro; IPR002919; TIL_dom. DR Pfam; PF01826; TIL; 1. DR SUPFAM; SSF57567; Serine protease inhibitors; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor; KW Reference proteome; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..170 FT /note="Inducible metalloproteinase inhibitor protein" FT /id="PRO_0000021511" FT CHAIN 20..88 FT /note="IMPI alpha" FT /id="PRO_0000021512" FT SITE 88..89 FT /note="Cleavage" FT /evidence="ECO:0000305" FT CARBOHYD 48 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:9738891" FT CARBOHYD 149 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT STRAND 26..34 FT /evidence="ECO:0007829|PDB:3SSB" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:3SSB" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:3SSB" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:3SSB" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:3SSB" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:3SSB" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:3SSB" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:3SSB" SQ SEQUENCE 170 AA; 18759 MW; 1A5B272846AD129A CRC64; MKCLLYLCLW CYCVLVSSSI VLICNGGHEY YECGGACDNV CADLHIQNKT NCPIINIRCN DKCYCEDGYA RDVNGKCIPI KDCPKIRSRR SIGIPVDKKC CTGPNEHYDE EKVSCPPETC ISLVAKFSCI DSPPPSPGCS CNSGYLRLNL TSPCIPICDC PQMQHSPDCQ //