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Potato locus cathepsin D inhibitor,

Locus details

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Locus synonyms 4: Cdi POTPIA POTPID StCDI [Add/Remove]

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Created on: 2006-12-21 Last updated on: 2011-12-16 by

Potato-TXB 1992

Links to external databases

cathepsin D inhibitor, is on PhyloGenes

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Accessions and images (0)

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Alleles (0)

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Associated loci (0)

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Associated loci - graphical view

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unprocessed genomic sequence region underlying this gene

mRNA PGSC0003DMT400024598

Ontology terms

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terms associated with this mRNA

cDNA sequence

spliced cDNA sequence, including UTRs

Protein sequence

translated polypeptide sequence

Gene model matches

SGN Unigenes

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GenBank accessions

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M96257 Potato cathepsin D inhibitor protein mRNA, complete cds.
AY083348 Solanum tuberosum Kunitz-type enzyme inhibitor P4E1 precursor, mRNA, complete cds.
AY083349 Solanum tuberosum aspartic proteinase inhibitor P2B4 mRNA, partial cds.
AF490593 Solanum tuberosum aspartic proteinase inhibitor precursor P1E9 mRNA, complete cds.
AY089959 Solanum tuberosum aspartic proteinase inhibitor precursor P7E9 mRNA, complete cds.
AY089960 Solanum tuberosum aspartic proteinase inhibitor precursor P8G5 mRNA, complete cds.
X53470 Solanum tuberosum mRNA for presumed inhibitor of aspartic proteinase.
X67843 S.tuberosum Cdi mRNA for cathepsin D inhibitor.
AB061246 Solanum tuberosum StCDI mRNA for cathepsin D inhibitor, complete cds.
X74985 S.tuberosum gene for cathepsin D inhibitor.
D17331 Solanum tuberosum mRNA for proteinase inhibitor, complete cds, clone:gCDT-A1.
D17328 Solanum tuberosum mRNA for proteinase inhibitor, complete cds, clone:pA1.
DQ168311 Solanum tuberosum clone 002D05 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168316 Solanum tuberosum clone 033A10 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168317 Solanum tuberosum clone 033D02 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168318 Solanum tuberosum clone 048E06 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168324 Solanum tuberosum clone 093E09 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168325 Solanum tuberosum clone 134F08 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168327 Solanum tuberosum clone 150D02 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ207847 Solanum tuberosum clone 073D02 kunitz-type protease inhibitor mRNA, complete cds.
X62095 S.tuberosum mRNA for aspartic proteinase inhibitor homologue.

Other genome matches

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Literature annotations [7]

[Associate publication] [Matching publications]

General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. The Plant cell (1992)
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Exogenous application of abscisic acid (ABA) has been shown to induce a systemic pattern of proteinase inhibitor II (pin2) mRNA accumulation identical to that induced by mechanical wounding. Evidence is presented that the ABA-specific response is not restricted to pin2 genes but appears to be part of a general reaction to wound stress. Four other wound-induced, ABA-responsive genes that encode two additional proteinase inhibitors, the proteolytic enzyme leucine aminopeptidase, and the biosynthetic enzyme threonine deaminase were isolated from potato plants. Wounding or treatment with ABA resulted in a pattern of accumulation of these mRNAs very similar to that of pin2. ABA-deficient plants did not accumulate any of the mRNAs upon wounding, although they showed normal levels of expression upon ABA treatment. Also, application of methyl jasmonate (MeJA) induced a strong accumulation of these transcripts, both in wild-type and in ABA-deficient plants, thus supporting a role for jasmonic acid as an intermediate in the signaling pathway that leads from ABA accumulation in response to wounding to the transcriptional activation of the genes.

Hildmann, T. Ebneth, M. Peña, Cortés. Sánchez, Serrano. Willmitzer, L. Prat, S. The Plant cell. 1992. 4(9). 1157-70.

Nucleotide and deduced amino acid sequence of an aspartic proteinase inhibitor homologue from potato tubers (Solanum tuberosum L.). Nucleic acids research (1990)
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Strukelj, B. Pungercar, J. Ritonja, A. Krizaj, I. Gubensek, F. Kregar, I. Turk, V. Nucleic acids research. 1990. 18(15). 4605.

Cloning and characterization of a cathepsin D inhibitor gene from Solanum tuberosum L. Plant molecular biology (1994)
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A DNA clone encoding a cathepsin D inhibitor CathInh was isolated from a potato genomic library using a CathInh cDNA as hybridization probe. The amino acid sequence of the coding region is nearly identical with a CathInh cDNA and CathInh proteins previously isolated from a tuber-specific cDNA library and from tubers, respectively. Analysis of GUS activity resulting from expression of chimeric CathInh promoter-GUS genes in transgenic potato plants revealed expression exclusively confined to potato tubers. No GUS activity could be detected in any other organ of the transgenic plants either constitutively or after wounding or treatment with abscisic and jasmonic acid (JA). Interestingly, part of the promoter region of the CathInh gene, essential for GUS activity in tubers, shows striking similarity to promoter regions of tuber-specific class I patatin genes.

Herbers, K. Prat, S. Willmitzer, L. Plant molecular biology. 1994. 26(1). 73-83.

A family of potato genes that encode Kunitz-type proteinase inhibitors: structural comparisons and differential expression. Plant & cell physiology (1994)
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Potato tubers contain a complex group of proteins of 20 to 24 kDa that exhibit homology to Kunitz-type proteinase inhibitors. We isolated three cDNAs and two genomic clones that encode members of the potato Kunitz-type proteinase inhibitor (PKPI) family. Comparison of the structures of these and other cloned genes indicated that genes of the PKPI family can be classified into three major homology groups, namely, A, B and C. The PKPI-A and -B genes exhibit higher homology to one another than to the PKPI-C genes. Determination of the N-terminal amino acid sequences of 18 polypeptides from the complex group of 20- to 24-kDa proteins that had been separated by column chromatography and subsequently gel electrophoresis revealed three different sequences that corresponded to PKPI-A, -B, and -C. PKPI-A genes include those coding for a cathepsin D inhibitor, while PKPI-B and -C genes include those coding for trypsin and/or chymotrypsin inhibitors and a subtilisin inhibitor. Precursors to PKPIs are synthesized with an N-terminal extra peptide that appears to contain, in addition to the signal peptide, a short propeptide with a highly conserved Asn-Pro-Ile-Xxx-Leu-Pro motif that is identical to the potential vacuolar-sorting determinant in the N-terminal propeptide of a precursor to sporamin of sweet potato. Expression of the PKPI-A and -B genes is differentially regulated: PKPI-A mRNA but not PKPI-B mRNA were induced in leaves after wounding or upon treatment with methyl jasmonate. Nuclear genes for PKPI-A and -B do not contain introns, and the homology between the two types of gene extends only 72 bp upstream from the site of initiation of transcription.

Ishikawa, A. Ohta, S. Matsuoka, K. Hattori, T. Nakamura, K. Plant & cell physiology. 1994. 35(2). 303-12.

Nucleotide and deduced amino acid sequence of the 22-kilodalton cathepsin D inhibitor protein of potato (Solanum tuberosum L.). Plant physiology (1993)
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Hannapel, DJ. Plant physiology. 1993. 101(2). 703-4.

Molecular cloning and immunocytochemical localization of jasmonic acid inducible cathepsin D inhibitors from potato. Advances in experimental medicine and biology (1995)
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Strukelj, B. Ravnikar, M. Mesko, P. Poljsak, Prijatelj. Pungercar, J. Kopitar, G. Kregar, I. Turk, V. Advances in experimental medicine and biology. 1995. 362(). 293-8.

Structural diversity and organization of three gene families for Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.). Molecular genetics and genomics : MGG (2003)
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In the potato, Kunitz-type enzyme inhibitors are abundant and highly polymorphic small proteins found in tubers. DNA sequence analysis of 1596 unselected ESTs (expressed sequence tags) from mature tubers of the cultivars Provita and Saturna resulted in the identification of 55 different DNA sequences with high sequence similarity to Kunitz-type enzyme inhibitors. The frequency of Kunitz-type inhibitor ESTs in Provita was four times higher than in Saturna tubers, and none of the Provita ESTs was identical to any of the Saturna ESTs. A phenogram constructed from the deduced amino acid sequences of the inhibitors revealed three major homology groups-A, B and C. Group A inhibitors were all derived from Provita ESTs. Inhibitor groups A and B were more similar to each other than to group C inhibitors, and for most members within-group similarity was at least 90%. Non-conservative amino acid substitutions and insertion/deletion polymorphisms suggest functional differentiation between members of the gene family. A minimum of 21 genes for Kunitz-type enzyme inhibitors (six for group A, nine for group B and six for group C) was estimated to exist in the potato genome. Genetic mapping and the identification of BAC (bacterial artificial chromosome) clones containing more than one member of the gene family indicated that most inhibitor genes of groups A, B and C are organized in a cluster that maps to a single region on potato chromosome III.

Heibges, A. Glaczinski, H. Ballvora, A. Salamini, F. Gebhardt, C. Molecular genetics and genomics : MGG. 2003. 269(4). 526-34.

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Accessions	Seedlots
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