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Potato locus Kunitz-type proteinase inhibitor

Locus details

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Locus synonyms 8: PKI1 PKPI-B1 PKPI-B10 PKPI-B2 PKPI-B9 POTPIB POTPIC POTPIE [Add/Remove]

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

Potato-TXB 1992

Links to external databases

Kunitz-type proteinase inhibitor is on PhyloGenes

Registry name:

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Notes and figures (0)

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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 PGSC0003DMT400026257

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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AF492359 Solanum tuberosum putative kunitz-type proteinase inhibitor precursor P1H5 mRNA, complete cds.
AF492769 Solanum tuberosum putative kunitz-type proteinase inhibitor S1C1 mRNA, complete cds.
AF495581 Solanum tuberosum clone P1G7 putative Kunitz-type proteinase inhibitor mRNA, complete cds.
AF495582 Solanum tuberosum clone P2F10 putative Kunitz-type proteinase inhibitor mRNA, complete cds.
AF495583 Solanum tuberosum clone P2G2 putative Kunitz-type proteinase inhibitor mRNA, complete cds.
AF495584 Solanum tuberosum clone P4D11 putative Kunitz-type proteinase inhibitor mRNA, complete cds.
AF495585 Solanum tuberosum clone P7D8 putative Kunitz-type proteinase inhibitor mRNA, complete cds.
X64370 S.tuberosum gene for aspartic proteinase inhibitor homologue.
AF536175 Solanum tuberosum Kunitz-type proteinase inhibitor precursor (PKPI-B10) gene, partial cds.
AY166690 Solanum tuberosum serine protease inhibitor mRNA, complete cds.
D17329 Solanum tuberosum mRNA for proteinase inhibitor, complete cds, clone:pF4.
D17332 Solanum tuberosum mRNA for proteinase inhibitor, complete cds, clone:gCDT-B1.
D17330 Solanum tuberosum mRNA for proteinase inhibitor, complete cds, clone:pKEN14-28.
AY692479 Solanum tuberosum Kunitz-type proteinase inhibitor (PKPI-B1) mRNA, partial cds.
AY693423 Solanum tuberosum Kunitz-type proteinase inhibitor group B (PKPI-B2) mRNA, partial cds.
AY693424 Solanum tuberosum Kunitz-type proteinase inhibitor group B (PKPI-B9) mRNA, partial cds.
DQ087220 Solanum tuberosum putative Kunitz-type proteinase inhibitor PKI1 (PKI1) gene, complete cds.
DQ168319 Solanum tuberosum clone 057D04 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168329 Solanum tuberosum clone 168H02 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168330 Solanum tuberosum clone 031D06 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168331 Solanum tuberosum clone 051E07 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168332 Solanum tuberosum clone 061B03 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ168333 Solanum tuberosum clone 159G09 Kunitz-type protease inhibitor precursor, mRNA, complete cds.
DQ268834 Solanum tuberosum clone 112D01 Kunitz-type protease inhibitor-like protein mRNA, complete cds.
DQ268836 Solanum tuberosum clone 117G04 Kunitz-type protease inhibitor-like protein mRNA, complete cds.
U30814 Solanum tuberosum Kunitz-type proteinase inhibitor mRNA, complete cds.

Other genome matches

None

Literature annotations [6]

[Associate publication] [Matching publications]

Isolation and sequence analysis of the genomic DNA fragment encoding an aspartic proteinase inhibitor homologue from potato (Solanum tuberosum L.). Plant molecular biology (1992)
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A genomic DNA clone encoding an aspartic proteinase inhibitor of potato was isolated from a lambda EMBL3 phage library using the aspartic proteinase inhibitor cDNA as a hybridization probe. The gene has all characteristic sequences normally found in eucaryotic genes. Typical CAAT and TATA box sequences were found in the 5'-upstream region. In this part are also two putative regulatory AGGA box sequences located. In the genomic sequence there are no intron sequences interrupting the coding region. An open reading frame of the gene encodes a precursor protein of 217 amino acids which shows high percent identity with the aspartic proteinase inhibitor cDNA.

Maganja, DB. Strukelj, B. Pungercar, J. Gubensek, F. Turk, V. Kregar, I. Plant molecular biology. 1992. 20(2). 311-3.

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.

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 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.

The most abundant protease inhibitor in potato tuber (cv. Elkana) is a serine protease inhibitor from the Kunitz family. Journal of agricultural and food chemistry (2003)
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The gene of the most abundant protease inhibitor in potato cv. Elkana was isolated and sequenced. The deduced amino acid sequence of this gene showed 98% identity with potato serine protease inhibitor (PSPI), a member of the Kunitz family. Therefore, the most abundant protease inhibitor was considered to be one of the isoforms of PSPI. The PSPI group represents approximately 22% of the total amount of proteins in potato cv. Elkana and is composed of seven different isoforms that slightly differ in isoelectric point. Antibodies were raised against the two most abundant isoforms of PSPI. The binding of these antibodies to PSPI isoforms and protease inhibitors from different groups of protease inhibitor in potato showed that approximately 70% of the protease inhibitors present in potato juice belong to the Kunitz family.

Pouvreau, L. Gruppen, H. Van Koningsveld, GA. Van Den Broek, LA. Voragen, AG. Journal of agricultural and food chemistry. 2003. 51(17). 5001-5.

Protein trypsin inhibitor from potato tubers. Biochemistry. Biokhimii͡a (2010)
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A protein of 22 kDa designated as PKTI-22 was isolated from potato tubers (Solanum tuberosum L., cv. Istrinskii) and purified to homogeneity using CM-Sepharose CL-6B ion-exchange chromatography. The protein efficiently suppressed the activity of trypsin, affected chymotrypsin less, and did not affect subtilisin Carlsberg. The N-terminal sequence of PKTI-22 (20 amino acid residues) was found to be highly homologous with the amino acid sequences of the potato Kunitz-type proteinase inhibitors of group B (PKPI-B) that were aligned from the corresponding gene sequences and was identical to the sequence (from the 2nd to the 20th residue) of the recombinant protein PKPI-B10. These data together with the observed similarity of the properties of two proteins indicate that the PKTI-22 protein is encoded by the PKPI-B10 gene.

Revina, TA. Kladnitskaya, GV. Gerasimova, NG. Gvozdeva, EL. Valueva, TA. Biochemistry. Biokhimii͡a. 2010. 75(1). 36-40.

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Accessions	Seedlots
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