LCM_LOCMI
ID LCM_LOCMI Reviewed; 92 AA.
AC P80060; P80058;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protease inhibitors;
DE Contains:
DE RecName: Full=Protease inhibitor LCMI-I;
DE AltName: Full=PARS intercerebralis major peptide D2;
DE Short=PMP-D2;
DE Contains:
DE RecName: Full=Protease inhibitor LCMI-II;
DE AltName: Full=PARS intercerebralis major peptide C;
DE Short=PMP-C;
DE Flags: Precursor;
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body;
RA Lagueux M.L.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-16.
RC TISSUE=Fat body;
RX PubMed=8019577; DOI=10.1016/0965-1748(94)90013-2;
RA Kromer E., Nakakura N., Lagueux M.;
RT "Cloning of a Locusta cDNA encoding a precursor peptide for two
RT structurally related proteinase inhibitors.";
RL Insect Biochem. Mol. Biol. 24:329-331(1994).
RN [3]
RP PROTEIN SEQUENCE OF 20-54 AND 57-92.
RC TISSUE=Pars intercerebralis;
RX PubMed=1740125; DOI=10.1111/j.1432-1033.1992.tb16617.x;
RA Nakakura N., Hietter H., van Dorsselaer A., Luu B.;
RT "Isolation and structural determination of three peptides from the insect
RT Locusta migratoria. Identification of a deoxyhexose-linked peptide.";
RL Eur. J. Biochem. 204:147-153(1992).
RN [4]
RP PROTEIN SEQUENCE OF 20-54 AND 57-92.
RC TISSUE=Hemolymph;
RX PubMed=1472051; DOI=10.1016/0006-291x(92)92271-x;
RA Boigegrain R.-A., Mattras H., Brehelin M., Paroutaud P.,
RA Coletti-Previero M.-A.;
RT "Insect immunity: two proteinase inhibitors from hemolymph of Locusta
RT migratoria.";
RL Biochem. Biophys. Res. Commun. 189:790-793(1992).
RN [5]
RP STRUCTURE BY NMR OF LMCI-I, AND DISULFIDE BONDS.
RX PubMed=7803403; DOI=10.1021/bi00255a021;
RA Mer G., Kellenberger C., Koehl P., Stote R., Sorokine O.,
RA van Dorsselaer A., Luu B., Hietter H., Lefevre J.-F.;
RT "Solution structure of PMP-D2, a 35-residue peptide isolated from the
RT insect Locusta migratoria.";
RL Biochemistry 33:15397-15407(1994).
RN [6]
RP STRUCTURE BY NMR OF LMCI-II.
RX PubMed=8548454; DOI=10.1038/nsb0196-45;
RA Mer G., Hietter H., Lefevre J.-F.;
RT "Stabilization of proteins by glycosylation examined by NMR analysis of a
RT fucosylated proteinase inhibitor.";
RL Nat. Struct. Biol. 3:45-53(1996).
RN [7]
RP STRUCTURE BY NMR OF LMCI-II.
RX PubMed=8613985; DOI=10.1006/jmbi.1996.0240;
RA Mer G., Hietter H., Kellenberger C., Renatus M., Luu B., Lefevre J.-F.;
RT "Solution structure of PMP-C: a new fold in the group of small serine
RT proteinase inhibitors.";
RL J. Mol. Biol. 258:158-171(1996).
CC -!- FUNCTION: Both LCMI I and II are inhibitors of chymotrypsin and
CC elastase (in vitro). They both inhibit the prophenol oxidase activation
CC cascade.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Brain and fat body.
CC -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00776}.
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DR EMBL; Z22805; CAA80462.1; -; mRNA.
DR PIR; S36658; S36658.
DR PDB; 1GL0; X-ray; 3.00 A; I=20-54.
DR PDB; 1GL1; X-ray; 2.10 A; I/J/K=57-92.
DR PDB; 1PMC; NMR; -; A=57-92.
DR PDBsum; 1GL0; -.
DR PDBsum; 1GL1; -.
DR PDBsum; 1PMC; -.
DR AlphaFoldDB; P80060; -.
DR SMR; P80060; -.
DR MINT; P80060; -.
DR MEROPS; I19.001; -.
DR MEROPS; I19.011; -.
DR iPTMnet; P80060; -.
DR EvolutionaryTrace; P80060; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR008037; Pacifastin_dom.
DR InterPro; IPR036201; Pacifastin_dom_sf.
DR InterPro; IPR016307; Prtase-inh_pacifastin.
DR Pfam; PF05375; Pacifastin_I; 2.
DR PIRSF; PIRSF001625; Prot_inhib_pacifastin; 1.
DR SUPFAM; SSF57283; SSF57283; 2.
DR PROSITE; PS51446; PACIFASTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1472051,
FT ECO:0000269|PubMed:1740125"
FT PEPTIDE 20..54
FT /note="Protease inhibitor LCMI-I"
FT /id="PRO_0000026708"
FT PEPTIDE 57..92
FT /note="Protease inhibitor LCMI-II"
FT /id="PRO_0000026709"
FT DOMAIN 20..54
FT /note="Pacifastin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DOMAIN 57..92
FT /note="Pacifastin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT SITE 48..49
FT /note="Reactive bond"
FT SITE 86..87
FT /note="Reactive bond"
FT CARBOHYD 65
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000269|PubMed:8613985"
FT DISULFID 23..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT DISULFID 33..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT DISULFID 36..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT DISULFID 60..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT DISULFID 70..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT DISULFID 73..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776,
FT ECO:0000269|PubMed:7803403"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1GL0"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1GL0"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1GL0"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1GL1"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1GL1"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1GL1"
SQ SEQUENCE 92 AA; 9760 MW; 2A53F9E3D97D290A CRC64;
MKFALALCAA VLLVVLVQAE EKCTPGQVKQ QDCNTCTCTP TGVWGCTRKG CQPAKREISC
EPGKTFKDKC NTCRCGADGK SAACTLKACP NQ
