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Potato locus serine protease inhibitor
Locus details | Download GMOD XML | Note to Editors | Annotation guidelines |
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L06137 Solanum tuberosum proteinase inhibitor 1 (pin1) mRNA, complete cds.
L06985 Solanum tuberosum proteinase inhibitor I mRNA, 3' end.
X67675 S.tuberosum mRNA for proteinase inhibitor I.
X67950 S.tuberosum pin1 mRNA for proteinase inhibitor I.
L06606 Solanum tuberosum proteinase inhibitor I mRNA, complete cds.
AY496262 Solanum tuberosum serine protease inhibitor (PI-1) mRNA, partial cds.
DQ087221 Solanum tuberosum proteinase inhibitor 1 PPI3B2 (PPI3B2) mRNA, complete cds.
DQ087222 Solanum tuberosum proteinase inhibitor 1 PPI2C1A (PPI2C1A) mRNA, complete cds.
DQ087223 Solanum tuberosum proteinase inhibitor 1 PPI2C4 (PPI2C4) mRNA, complete cds.
DQ168322 Solanum tuberosum clone 066E06 proteinase inhibitor I precursor, mRNA, complete cds.
U30861 Solanum tuberosum wound-inducible proteinase inhibitor I mRNA, partial cds.
L06985 Solanum tuberosum proteinase inhibitor I mRNA, 3' end.
X67675 S.tuberosum mRNA for proteinase inhibitor I.
X67950 S.tuberosum pin1 mRNA for proteinase inhibitor I.
L06606 Solanum tuberosum proteinase inhibitor I mRNA, complete cds.
AY496262 Solanum tuberosum serine protease inhibitor (PI-1) mRNA, partial cds.
DQ087221 Solanum tuberosum proteinase inhibitor 1 PPI3B2 (PPI3B2) mRNA, complete cds.
DQ087222 Solanum tuberosum proteinase inhibitor 1 PPI2C1A (PPI2C1A) mRNA, complete cds.
DQ087223 Solanum tuberosum proteinase inhibitor 1 PPI2C4 (PPI2C4) mRNA, complete cds.
DQ168322 Solanum tuberosum clone 066E06 proteinase inhibitor I precursor, mRNA, complete cds.
U30861 Solanum tuberosum wound-inducible proteinase inhibitor I mRNA, partial cds.
Other genome matches | None |
![]() ![]() | [Associate publication] [Matching publications] |
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop.
Journal of molecular evolution (1994)
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A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBL/Genbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319-324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family.
Beuning, LL. Spriggs, TW. Christeller, JT.
Journal of molecular evolution.
1994.
39(6).
644-54.
Isolation of a cDNA for proteinase inhibitor I.
Plant physiology (1993)
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Beuning, LL. Christeller, JT.
Plant physiology.
1993.
102(3).
1061.
Starch synthesis, and tuber storage protein genes are differently expressed in Solanum tuberosum and in Solanum brevidens.
FEBS letters (1996)
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Studying in vitro stem cuttings of Solanum tuberosum induced for tuberization and those of a non-tuberizing Solanum species, differences both in morphology and in gene expression were detected. Stolon formation essentially depended on light while tuberization was triggered by the elevated level of sucrose in the medium. Genes involved in starch synthesis were induced by sucrose in both species, however, starch granules were detected only in potato. A new tuber specific cDNA clone, GM7, encoding a putative metallocarboxypeptidase inhibitor and the cDNA of a proline rich cell wall protein with S. brevidens specific expression were isolated by differential screening. Sucrose mediated transcription of the tuber storage proteins like patatin and proteinase inhibitors (Kunitz-type, winI, GM7) failed in S. brevidens.
Bánfalvi, Z. Molnar, A. Molnar, G. Lakatos, L. Szabo, L.
FEBS letters.
1996.
383(3).
159-64.
Structural characterization of potato protease inhibitor I (Cv. Bintje) after expression in Pichia pastoris.
Journal of agricultural and food chemistry (2004)
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In the present study the structural properties of potato protease inhibitor 1 (PI-1) were studied as a function of temperature to elucidate its precipitation mechanism upon heating. A cDNA coding for PI-1 from cv. Bintje was cloned and expressed in Pichia pastoris. Using the recombinant PI-1 it was suggested that PI-1 behaves as a hexameric protein rather than as a pentamer, as previously proposed in the literature. The recombinant protein seems either to have a predominantly unordered structure or to belong to the beta-II proteins. Differential scanning calorimetry analysis of PI-1 revealed that its thermal unfolding occurs via one endothermic transition in which the hexameric PI-1 probably unfolds, having a dimer instead of a monomer as cooperative unit. The transition temperature for the recombinant PI-1 was 88 degrees C. Similar results were obtained for a partially purified pool of native PI-1 from cv. Bintje.
van den Broek, LA. Pouvreau, L. Lommerse, G. Schipper, B. Van Koningsveld, GA. Gruppen, H.
Journal of agricultural and food chemistry.
2004.
52(15).
4928-34.
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