[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1105/tpc.1.4.427; PubMed=2562563 [NCBI, ExPASy, EBI, Israel, Japan] Jofuku K.D., Schipper R.D., Goldberg R.B.; "A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation in soybean embryos."; Plant Cell 1:427-435(1989).
[2]	PROTEIN SEQUENCE OF 25-205 (VARIANT A). PubMed=4734969 [NCBI, ExPASy, EBI, Israel, Japan] Koide T., Ikenaka T.; "Studies on soybean trypsin inhibitors. 3. Amino-acid sequences of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz)."; Eur. J. Biochem. 32:417-431(1973).
[3]	PROTEIN SEQUENCE OF 25-205 (VARIANT C), AND SEQUENCE REVISION (VARIANT A). STRAIN=cv. Raiden; PubMed=3905784 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.-H., Hara S., Hase S., Ikenaka T., Toda H., Kitamura K., Kaizuma N.; "Comparative study on amino acid sequences of Kunitz-type soybean trypsin inhibitors, Tia, Tib, and Tic."; J. Biochem. 98:435-448(1985).
[4]	PROTEIN SEQUENCE OF 25-56. PubMed=8318586 [NCBI, ExPASy, EBI, Israel, Japan] Coronel C.E., Novella M.L., Winnica D.E., Lardy H.A.; "Isolation and characterization of a 54-kilodalton precursor of caltrin, the calcium transport inhibitor protein from seminal vesicles of the rat."; Biol. Reprod. 48:1326-1333(1993).
[5]	DISULFIDE BONDS. DOI=10.1016/0006-291X(66)90766-2; PubMed=6006643 [NCBI, ExPASy, EBI, Israel, Japan] Brown J.R., Lerman N., Bohak Z.; "The amino acid sequences around the disulfide bonds of soybean trypsin inhibitor."; Biochem. Biophys. Res. Commun. 23:561-565(1966).
[6]	INHIBITORY SITE. PubMed=5950769 [NCBI, ExPASy, EBI, Israel, Japan] Ozawa K., Laskowski M. Jr.; "The reactive site of trypsin inhibitors."; J. Biol. Chem. 241:3955-3961(1966).
[7]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1021/bi00717a024; PubMed=4472048 [NCBI, ExPASy, EBI, Israel, Japan] Sweet R.M., Wright H.T., Janin J., Chothia C.H., Blow D.M.; "Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution."; Biochemistry 13:4212-4228(1974).
[8]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1107/S0907444997015849; PubMed=9761854 [NCBI, ExPASy, EBI, Israel, Japan] de Meester P., Brick P., Lloyd L.F., Blow D.M., Onesti S.; "Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator."; Acta Crystallogr. D 54:589-597(1998).
[9]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1006/jmbi.1997.1469; PubMed=9466914 [NCBI, ExPASy, EBI, Israel, Japan] Song H.K., Suh S.W.; "Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator."; J. Mol. Biol. 275:347-363(1998).

Comments

FUNCTION: Inhibition of trypsin.
MISCELLANEOUS: The sequence of variant A is shown.
MISCELLANEOUS: Electrophoresis identifies three genetically distinct variants, A, B, and C, that are inherited as codominant alleles.
SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-type inhibitor) family [view classification].
CAUTION: Ref.4 sequence was originally thought to be rat caltrin. A number of peptide fragments were derived from a trypsin digest of caltrin and soybean trypsin inhibitor was used to stop the digestion. It appears that some of the inhibitor was also digested and sequenced.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S45092; AAB23464.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ0968; JQ0968.

UniGene

Gma.29257

3D structure databases

PDB

1AVU; X-ray; 2.30 A; A=25-205.	[ExPASy / RCSB / EBI]
1AVW; X-ray; 1.75 A; B=25-201.	[ExPASy / RCSB / EBI]
1AVX; X-ray; 1.90 A; B=25-201.	[ExPASy / RCSB / EBI]
1BA7; X-ray; 2.50 A; A/B=25-205.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AVU; -.
1AVW; -.
1AVX; -.
1BA7; -.

ModBase

P01070.

Protein-protein interaction databases

DIP

DIP:6101N; -.

Protein family/group databases

MEROPS

I03.001; -.

Ontologies

GO:0004867;	Molecular function: serine-type endopeptidase inhibitor activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002160; Prot_inh_Kunz-lg.
Graphical view of domain structure.

Pfam

PF00197; Kunitz_legume; 1.
Pfam graphical view of domain structure.

PRINTS

PR00291; KUNITZINHBTR.

ProDom

PD000891; Prot_inh_Kunz-lg; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00452; STI; 1.
SMART graphical view of domain structure.

PROSITE

PS00283; SOYBEAN_KUNITZ; 1.

Other

P01070; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Protease inhibitor; Serine protease inhibitor; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 205`	`181`	`Trypsin inhibitor A.`	`PRO_0000016889`
`PROPEP`	`206 216`	`11`		`PRO_0000016890`
`SITE`	`87 88`	`2`	`Reactive bond for trypsin.`
`DISULFID`	`63 110`
`DISULFID`	`160 169`
`VARIANT`	`79 79`	`1`	`G -> E (in variant C).`
`CONFLICT`	`25 25`		`D -> S (in Ref. 4; AA sequence).`
`TURN`	`30 32`	`3`
`STRAND`	`39 46`	`8`
`STRAND`	`53 56`	`4`
`STRAND`	`66 69`	`4`
`STRAND`	`80 83`	`4`
`STRAND`	`85 87`	`3`
`STRAND`	`97 101`	`5`
`HELIX`	`108 110`	`3`
`STRAND`	`118 120`	`3`
`STRAND`	`126 130`	`5`
`STRAND`	`140 146`	`7`
`STRAND`	`155 161`	`7`
`STRAND`	`170 176`	`7`
`STRAND`	`178 180`	`3`
`STRAND`	`183 188`	`6`
`STRAND`	`195 199`	`5`

Sequence information

Length: 216 AA [This is the length of the unprocessed precursor]

Molecular weight: 24005 Da [This is the MW of the unprocessed precursor]

CRC64: 1251FE0DE46CCA96 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKSTIFFLFL FCAFTTSYLP SAIADFVLDN EGNPLENGGT YYILSDITAF GGIRAAPTGN 

        70         80         90        100        110        120 
ERCPLTVVQS RNELDKGIGT IISSPYRIRF IAEGHPLSLK FDSFAVIMLC VGIPTEWSVV 

       130        140        150        160        170        180 
EDLPEGPAVK IGENKDAMDG WFRLERVSDD EFNNYKLVFC PQQAEDDKCG DIGISIDHDD 

       190        200        210 
GTRRLVVSKN KPLVVQFQKL DKESLAKKNH GLSRSE

P01070 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools