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 01-OCT-2014, entry version 58. 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; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Pyraloidea; 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., RA Hummel M., Vilcinskas A.; RT "Cloning and expression of an inhibitor of microbial RT metalloproteinases 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 RP N-TERMINUS, AND GLYCOSYLATION. 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. 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 -!- INDUCTION: During humoral immune response. By lipopolysaccharide CC (LPS). {ECO:0000269|PubMed:15115439, ECO:0000269|PubMed:9738891}. CC -!- PTM: Cleaved. {ECO:0000305}. CC -!- PTM: Five disulfide bonds are present. When artificially cleaved CC by thermolysin between Asn-56 and Ile-57, the two obtained chains CC (called heavy and light chains) remain linked. CC -!- PTM: The N-terminus is blocked. CC -!- MASS SPECTROMETRY: Mass=8360; Method=MALDI; Range=20-88; 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 ProteinModelPortal; P82176; -. DR MEROPS; I08.006; -. DR EvolutionaryTrace; P82176; -. 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:0010951; P:negative regulation of endopeptidase activity; IDA:GOC. DR GO; GO:0042060; P:wound healing; NAS:UniProtKB. DR InterPro; IPR002919; TIL_dom. DR Pfam; PF01826; TIL; 1. DR SUPFAM; SSF57567; SSF57567; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Metalloenzyme inhibitor; Metalloprotease inhibitor; KW Protease inhibitor; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 170 Inducible metalloproteinase inhibitor FT protein. FT /FTId=PRO_0000021511. FT CHAIN 20 88 IMPI alpha. FT /FTId=PRO_0000021512. FT SITE 88 89 Cleavage. {ECO:0000305}. FT CARBOHYD 48 48 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:9738891}. FT CARBOHYD 149 149 N-linked (GlcNAc...). {ECO:0000255}. FT STRAND 26 34 FT HELIX 41 43 FT TURN 44 46 FT STRAND 49 51 FT STRAND 60 65 FT STRAND 69 71 FT STRAND 77 79 FT HELIX 80 82 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 //