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 03-MAR-2009, entry version 40. DE RecName: Full=Inducible metalloproteinase inhibitor protein; DE Contains: DE RecName: Full=IMPI alpha; DE Flags: Precursor; GN Name=IMPI; OS Galleria mellonella (Wax moth). OC Eukaryota; Metazoa; 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., 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 MEDLINE=98409271; PubMed=9738891; 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. CC -!- INDUCTION: During humoral immune response. By lipopolysaccharide CC (LPS). CC -!- PTM: Cleaved (Probable). 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 Source=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 MEROPS; I08.006; -. 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:0042060; P:wound healing; NAS:UniProtKB. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Signal. FT SIGNAL 1 19 Potential. 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 (Probable). FT CARBOHYD 48 48 N-linked (GlcNAc...). FT CARBOHYD 149 149 N-linked (GlcNAc...) (Potential). 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 //