{PDOC00255}
{PS00283; SOYBEAN_KUNITZ}
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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  proteinase  inhibitors.  It  comprise  plant  proteins which have
inhibitory activity against serine proteinases from the trypsin and subtilisin
families, thiol proteinases and aspartic proteinases as well  as some proteins
that are  probably involved in seed storage. 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 proteinase) 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.
 - Thiol proteinase inhibitor PCPI 8.3 (P340) from potato tuber [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-{EK}-[EDNTY]-[DG]-[RKHDENQ]-x-[LIVM]-x-{E}-{Q}-
                    x(2)-Y-x-[LIVM]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for 2 sequences.
-Other sequence(s) detected in Swiss-Prot: 20.
-Last update: April 2006 / Pattern revised.

[ 1] Laskowski M. Jr., Kato I.
     "Protein inhibitors of proteinases."
     Annu. Rev. Biochem. 49:593-626(1980).
     PubMed=6996568; DOI=10.1146/annurev.bi.49.070180.003113
[ 2] Ritonja A., Krizaj I., Mesko P., Kopitar M., Lucovnik P., Strukelj B.,
     Pungercar J., Buttle D.J., Barrett A.J., Turk V.
     "The amino acid sequence of a novel inhibitor of cathepsin D from
     potato."
     FEBS Lett. 267:13-15(1990).
     PubMed=2365079
[ 3] Kortt A.A., Strike P.M., De Jersey J.
     "Amino acid sequence of a crystalline seed albumin (winged bean
     albumin-1) from Psophocarpus tetragonolobus (L.) DC. Sequence
     similarity with Kunitz-type seed inhibitors and 7S storage
     globulins."
     Eur. J. Biochem. 181:403-408(1989).
     PubMed=2653830
[ 4] Theerasilp S., Hitotsuya H., Nakajo S., Nakaya K., Nakamura Y.,
     Kurihara Y.
     "Complete amino acid sequence and structure characterization of the
     taste-modifying protein, miraculin."
     J. Biol. Chem. 264:6655-6659(1989).
     PubMed=2708331
[ 5] Hattori T., Yoshida N., Nakamura K.
     "Structural relationship among the members of a multigene family
     coding for the sweet potato tuberous root storage protein."
     Plant Mol. Biol. 13:563-572(1989).
     PubMed=2491673
[ 6] Krizaj I., Drobnic-Kosorok M., Brzin J., Jerala R., Turk V.
     "The primary structure of inhibitor of cysteine proteinases from
     potato."
     FEBS Lett. 333:15-20(1993).
     PubMed=8224155
[ 7] Bradshaw H.D. Jr., Hollick J.B., Parsons T.J., Clarke H.R.G., Gordon M.P.
     "Systemically wound-responsive genes in poplar trees encode proteins
     similar to sweet potato sporamins and legume Kunitz trypsin
     inhibitors."
     Plant Mol. Biol. 14:51-59(1990).
     PubMed=2101311
[ 8] Tai H., McHenry L., Fritz P.J., Furtek D.B.
     "Nucleic acid sequence of a 21 kDa cocoa seed protein with homology to
     the soybean trypsin inhibitor (Kunitz) family of protease
     inhibitors."
     Plant Mol. Biol. 16:913-915(1991).
     PubMed=1859871

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