Summary: Pacifastin inhibitor (LCMII)
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Pacifastin inhibitor (LCMII) Provide feedback
Structures of members of this family show that they are comprised of a triple-stranded antiparallel beta-sheet connected by three disulfide bridges, which defines this as a novel family of serine protease inhibitors [1,2].
Simonet G, Claeys I, Broeck JV; , Comp Biochem Physiol B Biochem Mol Biol 2002;132:247-255.: Structural and functional properties of a novel serine protease inhibiting peptide family in arthropods. PUBMED:11997226 EPMC:11997226
Roussel A, Mathieu M, Dobbs A, Luu B, Cambillau C, Kellenberger C; , J Biol Chem 2001;276:38893-38898.: Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity. PUBMED:11495915 EPMC:11495915
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This tab holds annotation information from the InterPro database.
InterPro entry IPR008037
They were first isolated from Locusta migratoria migratoria(migratory locust). These were HI, LMCI-1 (PMP-D2) and LMCI-2 (PMP-C) [PUBMED:1472051, PUBMED:1740125, PUBMED:10696590]; five additional members SGPI-1 to 5 were identified in Schistocerca gregaria (desert locust) [PUBMED:9475173, PUBMED:11856311], and a heterodimeric serine protease inhibitor (pacifastin) was isolated from the hemolymph of Pacifastacus leniusculus (Signal crayfish) [PUBMED:9192625].
Pacifastin is a 155kDa composed of two covalently linked subunits, which are separately encoded. The heavy chain of pacifastin (105 kDa) is related to transferrins, containing three transferrin lobes, two of which seem to be active for iron binding [PUBMED:9192625]. A number of the members of the transferrin family are also serine peptidases belong to MEROPS peptidase family S60 (INTERPRO). The light chain of pacifastin (44 kDa) is the proteinase inhibitory subunit, and has nine cysteine-rich inhibitory domains that are homologous to each other. The locust inhibitors share a conserved array of six cysteine residues with the pacifastin light chain. The structure of members of this family reveal that they are comprised of a triple-stranded antiparallel beta-sheet connected by three disulphide bridges [PUBMED:9192625].
The biological function(s) of the locust inhibitors is (are) not fully understood. LMCI-1 and LMCI-2 were shown to inhibit the endogenous proteolytic activating cascade of prophenoloxidase [PUBMED:11997226]. Expression analysis shows that the genes encoding the SGPI precursors are differentially expressed in a time-, stage- and hormone-dependent manner.
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|Molecular function||peptidase inhibitor activity (GO:0030414)|
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|Seed source:||Pfam-B_35181 (release 7.8)|
|Number in seed:||36|
|Number in full:||437|
|Average length of the domain:||38.40 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||26.50 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pacifastin_I domain has been found. There are 12 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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