KTI2_SOYBN
ID KTI2_SOYBN Reviewed; 204 AA.
AC P25273;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Kunitz-type trypsin inhibitor KTI2;
DE Flags: Precursor;
GN Name=KTI2;
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 [GENOMIC DNA].
RC STRAIN=cv. Forrest;
RX PubMed=2562561; DOI=10.2307/3869025;
RA Jofuku K.D., Goldberg R.B.;
RT "Kunitz trypsin inhibitor genes are differentially expressed during the
RT soybean life cycle and in transformed tobacco plants.";
RL Plant Cell 1:1079-1093(1989).
CC -!- FUNCTION: Has probably no trypsin inhibitor activity. KTi2 is
CC responsible for most of the Kunitz trypsin inhibitor activity and
CC protein found in soybean seeds.
CC -!- TISSUE SPECIFICITY: Seed, and at low levels in leaf, root, and stem.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis and in mature
CC plant.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; S45035; AAB23483.1; -; Genomic_DNA.
DR PIR; JQ1092; JQ1092.
DR AlphaFoldDB; P25273; -.
DR SMR; P25273; -.
DR MEROPS; I03.001; -.
DR PRIDE; P25273; -.
DR InParanoid; P25273; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..204
FT /note="Kunitz-type trypsin inhibitor KTI2"
FT /id="PRO_0000016892"
FT DISULFID 65..112
FT /evidence="ECO:0000250"
FT DISULFID 160..169
FT /evidence="ECO:0000250"
SQ SEQUENCE 204 AA; 22800 MW; E22D38BA565A99BE CRC64;
MKSTIFFALF LVCAFTISYL PSATAQFVLD TDDDPLQNGG TYYMLPVMRG KSGGIEGNST
GKEICPLTVV QSPNKHNKGI GLVFKSPLHA LFIAERYPLS IKFDSFAVIP LCGVMPTKWA
IVEREGLQAV TLAARDTVDG WFNIERVSRE YNDYYKLVFC PQEAEDNKCE DIGIQIDNDG
IRRLVLSKNK PLVVEFQKFR SSTA