ITRA_SOYBN
ID ITRA_SOYBN Reviewed; 216 AA.
AC P01070; Q9QV66;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Trypsin inhibitor A;
DE AltName: Full=Kunitz-type trypsin inhibitor A;
DE Flags: Precursor;
GN Name=KTI3;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2562563; DOI=10.2307/3869103;
RA Jofuku K.D., Schipper R.D., Goldberg R.B.;
RT "A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation
RT in soybean embryos.";
RL Plant Cell 1:427-435(1989).
RN [2]
RP PROTEIN SEQUENCE OF 25-205 (VARIANT A).
RX PubMed=4734969; DOI=10.1111/j.1432-1033.1973.tb02624.x;
RA Koide T., Ikenaka T.;
RT "Studies on soybean trypsin inhibitors. 3. Amino-acid sequences of the
RT carboxyl-terminal region and the complete amino-acid sequence of soybean
RT trypsin inhibitor (Kunitz).";
RL Eur. J. Biochem. 32:417-431(1973).
RN [3]
RP PROTEIN SEQUENCE OF 25-205 (VARIANT C), AND SEQUENCE REVISION (VARIANT A).
RC STRAIN=cv. Raiden;
RX PubMed=3905784; DOI=10.1093/oxfordjournals.jbchem.a135298;
RA Kim S.-H., Hara S., Hase S., Ikenaka T., Toda H., Kitamura K., Kaizuma N.;
RT "Comparative study on amino acid sequences of Kunitz-type soybean trypsin
RT inhibitors, Tia, Tib, and Tic.";
RL J. Biochem. 98:435-448(1985).
RN [4]
RP PROTEIN SEQUENCE OF 25-56.
RX PubMed=8318586; DOI=10.1095/biolreprod48.6.1326;
RA Coronel C.E., Novella M.L., Winnica D.E., Lardy H.A.;
RT "Isolation and characterization of a 54-kilodalton precursor of caltrin,
RT the calcium transport inhibitor protein from seminal vesicles of the rat.";
RL Biol. Reprod. 48:1326-1333(1993).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=6006643; DOI=10.1016/0006-291x(66)90766-2;
RA Brown J.R., Lerman N., Bohak Z.;
RT "The amino acid sequences around the disulfide bonds of soybean trypsin
RT inhibitor.";
RL Biochem. Biophys. Res. Commun. 23:561-565(1966).
RN [6]
RP INHIBITORY SITE.
RX PubMed=5950769; DOI=10.1016/s0021-9258(18)99798-x;
RA Ozawa K., Laskowski M. Jr.;
RT "The reactive site of trypsin inhibitors.";
RL J. Biol. Chem. 241:3955-3961(1966).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=4472048; DOI=10.1021/bi00717a024;
RA Sweet R.M., Wright H.T., Janin J., Chothia C.H., Blow D.M.;
RT "Crystal structure of the complex of porcine trypsin with soybean trypsin
RT inhibitor (Kunitz) at 2.6-A resolution.";
RL Biochemistry 13:4212-4228(1974).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9761854; DOI=10.1107/s0907444997015849;
RA de Meester P., Brick P., Lloyd L.F., Blow D.M., Onesti S.;
RT "Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication
RT for the interactions between members of the STI family and tissue-
RT plasminogen activator.";
RL Acta Crystallogr. D 54:589-597(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9466914; DOI=10.1006/jmbi.1997.1469;
RA Song H.K., Suh S.W.;
RT "Kunitz-type soybean trypsin inhibitor revisited: refined structure of its
RT complex with porcine trypsin reveals an insight into the interaction
RT between a homologous inhibitor from Erythrina caffra and tissue-type
RT plasminogen activator.";
RL J. Mol. Biol. 275:347-363(1998).
CC -!- FUNCTION: Inhibition of trypsin.
CC -!- MISCELLANEOUS: The sequence of variant A is shown.
CC -!- MISCELLANEOUS: Electrophoresis identifies three genetically distinct
CC variants, A, B, and C, that are inherited as codominant alleles.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC -!- CAUTION: PubMed:8318586 sequence was originally thought to be rat
CC caltrin. A number of peptide fragments were derived from a trypsin
CC digest of caltrin and soybean trypsin inhibitor was used to stop the
CC digestion. It appears that some of the inhibitor was also digested and
CC sequenced. {ECO:0000305}.
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DR EMBL; S45092; AAB23464.1; -; mRNA.
DR PIR; JQ0968; JQ0968.
DR RefSeq; NP_001238611.1; NM_001251682.1.
DR PDB; 1AVU; X-ray; 2.30 A; A=25-205.
DR PDB; 1AVW; X-ray; 1.75 A; B=25-201.
DR PDB; 1AVX; X-ray; 1.90 A; B=25-201.
DR PDB; 1BA7; X-ray; 2.50 A; A/B=25-205.
DR PDB; 6NTT; X-ray; 2.40 A; A/B=1-216.
DR PDB; 6O1F; X-ray; 2.15 A; I=25-216.
DR PDBsum; 1AVU; -.
DR PDBsum; 1AVW; -.
DR PDBsum; 1AVX; -.
DR PDBsum; 1BA7; -.
DR PDBsum; 6NTT; -.
DR PDBsum; 6O1F; -.
DR AlphaFoldDB; P01070; -.
DR BMRB; P01070; -.
DR PCDDB; P01070; -.
DR SMR; P01070; -.
DR DIP; DIP-6101N; -.
DR MINT; P01070; -.
DR STRING; 3847.GLYMA08G45531.1; -.
DR Allergome; 1144; Gly m TI.
DR MEROPS; I03.001; -.
DR GeneID; 547831; -.
DR KEGG; gmx:547831; -.
DR InParanoid; P01070; -.
DR OrthoDB; 1481039at2759; -.
DR EvolutionaryTrace; P01070; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3905784,
FT ECO:0000269|PubMed:4734969, ECO:0000269|PubMed:8318586"
FT CHAIN 25..205
FT /note="Trypsin inhibitor A"
FT /id="PRO_0000016889"
FT PROPEP 206..216
FT /id="PRO_0000016890"
FT SITE 87..88
FT /note="Reactive bond for trypsin"
FT DISULFID 63..110
FT /evidence="ECO:0000269|PubMed:6006643"
FT DISULFID 160..169
FT /evidence="ECO:0000269|PubMed:6006643"
FT VARIANT 79
FT /note="G -> E (in variant C)"
FT CONFLICT 25
FT /note="D -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1AVU"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6O1F"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6NTT"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1AVW"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6NTT"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1AVX"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1AVW"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6O1F"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1AVW"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1AVW"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6O1F"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1AVW"
SQ SEQUENCE 216 AA; 24005 MW; 1251FE0DE46CCA96 CRC64;
MKSTIFFLFL FCAFTTSYLP SAIADFVLDN EGNPLENGGT YYILSDITAF GGIRAAPTGN
ERCPLTVVQS RNELDKGIGT IISSPYRIRF IAEGHPLSLK FDSFAVIMLC VGIPTEWSVV
EDLPEGPAVK IGENKDAMDG WFRLERVSDD EFNNYKLVFC PQQAEDDKCG DIGISIDHDD
GTRRLVVSKN KPLVVQFQKL DKESLAKKNH GLSRSE
