ITI_FAGTA
ID ITI_FAGTA Reviewed; 86 AA.
AC P86971;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Trypsin inhibitor {ECO:0000303|PubMed:21544554};
DE Short=FtTI {ECO:0000303|PubMed:21544554};
OS Fagopyrum tataricum (Tartarian buckwheat) (Polygonum tataricum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX NCBI_TaxID=62330;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, AND DISULFIDE BONDS.
RC TISSUE=Seed {ECO:0000269|PubMed:21544554};
RX PubMed=21544554; DOI=10.1007/s12010-011-9257-4;
RA Ruan J.J., Zhou M.L., Chen H., Shao J.R.;
RT "Identification and Characterization of a Trypsin Inhibitor from Fagopyrum
RT tataricum Seeds.";
RL Appl. Biochem. Biotechnol. 0:0-0(2011).
CC -!- FUNCTION: Serine protease inhibitor which is active against trypsin.
CC Displays strong antifungal activity against a number of phytopathogenic
CC fungi including M.melonis, A.cucumerina, A.solani, C.glaeosporioides
CC and P.capsici. {ECO:0000269|PubMed:21544554}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 at 37 degrees Celsius. Maintains over 90% of its
CC inhibitory activity from pH 3 to 10. {ECO:0000269|PubMed:21544554};
CC Temperature dependence:
CC Active between 10 and 60 degrees Celsius. 84% activity retained when
CC heated for 30 minutes at 80 degrees Celsius. Incubation at
CC temperatures above 80 degrees Celsius rapidly decreases inhibitory
CC activity. {ECO:0000269|PubMed:21544554};
CC -!- MASS SPECTROMETRY: Mass=13838.50; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21544554};
CC -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC protease inhibitor) family. {ECO:0000255}.
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DR AlphaFoldDB; P86971; -.
DR SMR; P86971; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR InterPro; IPR000864; Prot_inh_pot1.
DR InterPro; IPR036354; Prot_inh_pot1_sf.
DR PANTHER; PTHR33091; PTHR33091; 1.
DR Pfam; PF00280; potato_inhibit; 1.
DR SUPFAM; SSF54654; SSF54654; 1.
DR PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW Plant defense; Protease inhibitor; Serine protease inhibitor.
FT PEPTIDE 1..86
FT /note="Trypsin inhibitor"
FT /evidence="ECO:0000269|PubMed:21544554"
FT /id="PRO_0000412717"
FT SITE 61..62
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:P01051"
FT DISULFID 8..65
FT /evidence="ECO:0000269|PubMed:21544554"
FT DISULFID 49..58
FT /evidence="ECO:0000269|PubMed:21544554"
SQ SEQUENCE 86 AA; 9293 MW; BF417A5EAD2EE2F0 CRC64;
LIYAKVECLT TGVRTYVGKQ SWPELVGTKG KTAAATIDKE NTHVTAVLCP PLTTLAACRT
FDFRCDRVRV LINRIGGVVT KTPTVG