IMPI_GALME
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 25-MAY-2022, entry version 77.
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};
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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 iPTMnet; 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:0042060; P:wound healing; NAS:UniProtKB.
DR InterPro; IPR036084; Ser_inhib-like_sf.
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; 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
