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PDOC00255
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* Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature *
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The soybean trypsin inhibitor (Kunitz) family [1] is one of the numerous
families of serine proteinase inhibitors. This family is currently known to
group the following proteins:
- Trypsin inhibitors A, B, C, KTI1, and KTI2 from soybean.
- Trypsin inhibitor DE3 from coral beans (Erythrina sp.).
- Trypsin inhibitor DE5 from sandal bead tree.
- Trypsin inhibitors 1A (WTI-1A), 1B (WTI-1B), and 2 (WTI-2) from goa bean.
- Trypsin inhibitor from Acacia confusa.
- Trypsin inhibitor from silk tree.
- Chymotrypsin inhibitor 3 (WCI-3) from goa bean.
- Cathepsin D inhibitors PDI and NDI from potato [2], which inhibit both
cathepsin D (aspartic protease) and trypsin.
- Alpha-amylase/subtilisin inhibitors from barley and wheat.
- Albumin-1 (WBA-1) from goa bean seeds [3].
- Miraculin from Richadella dulcifica [4], a sweet taste protein.
- Sporamin from sweet potato [5], the major tuberous root protein.
- Potato tuber protein P340 [6].
- Wound responsive protein gwin3 from poplar tree [7].
- 21 kd seed protein from cocoa [8].
All these proteins contain from 170 to 200 amino acid residues and one or two
intrachain disulfide bonds. The best conserved region is found in their N-
terminal section and is used as a signature pattern.
-Consensus pattern: [LIVM]-x-D-x-[EDNTY]-[DG]-[RKHDENQ]-x-[LIVM]-x(5)-Y-x-
[LIVM]
-Sequences known to belong to this class detected by the pattern: ALL, except
for potato tuber protein P340.
-Other sequence(s) detected in SWISS-PROT: 8 RuBisCO small chains and a
chloroplast hypothetical protein from Oenothera bertiana.
-Last update: October 1993 / Text revised.
[ 1] Laskowski M., Kato I.
Annu. Rev. Biochem. 49:593-626(1980).
[ 2] Ritonja A., Krizaj I., Mesko P., Kopitar M., Lucovnik P., Strukelj B.,
Pungercar J., Buttle D.J., Barret A.J., Turk V.
FEBS Lett. 267:13-15(1990).
[ 3] Kortt A.A., Strike P.M., de Jersey J.
Eur. J. Biochem. 181:403-408(1989).
[ 4] Theerasilp S., Hitotsuya H., Nakajo S., Nakaja K., Nakamura Y.,
Kurihara Y.
J. Biol. Chem. 264:6655-6659(1989).
[ 5] Hattori T., Yoshida N., Nakamura K.
Plant Mol. Biol. 13:563-572(1989).
[ 6] Stiekema W.J., Heidekamp F., Dirkse W.G., van Beckum J., de Haan P.,
Ten Bosch C., Louwerse J.D.
Plant Mol. Biol. 11:255-269(1988).
[ 7] Bradshaw H.D., Hollick J.B., Parsons T.J., Clarke H.R.G., Gordon M.P.
Plant Mol. Biol. 14:51-59(1989).
[ 8] Tai H., McHenry L., Fritz P.J., Furtek D.B.
Plant Mol. Biol. 16:913-915(1991).