SFTI1_HELAN
ID SFTI1_HELAN Reviewed; 56 AA.
AC Q4GWU5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Trypsin inhibitor 1;
DE AltName: Full=SFTI-1;
DE Flags: Precursor;
GN Name=sfti1 {ECO:0000312|EMBL:CAJ19097.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ19097.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND STRUCTURE BY NMR OF 26-56.
RC TISSUE=Leaf {ECO:0000312|EMBL:CAJ19097.1};
RX PubMed=16036912; DOI=10.1074/jbc.m506060200;
RA Mulvenna J.P., Foley F.M., Craik D.J.;
RT "Discovery, structural determination, and putative processing of the
RT precursor protein that produces the cyclic trypsin inhibitor sunflower
RT trypsin inhibitor 1.";
RL J. Biol. Chem. 280:32245-32253(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 40-53, CROSS-LINK, FUNCTION, MASS SPECTROMETRY, AND
RP STRUCTURE BY NMR OF 40-53.
RC TISSUE=Seed {ECO:0000269|PubMed:10390350};
RX PubMed=10390350; DOI=10.1006/jmbi.1999.2891;
RA Luckett S., Garcia R.S., Barker J.J., Konarev A.V., Shewry P.R.,
RA Clarke A.R., Brady R.L.;
RT "High-resolution structure of a potent, cyclic proteinase inhibitor from
RT sunflower seeds.";
RL J. Mol. Biol. 290:525-533(1999).
RN [3] {ECO:0000305}
RP STRUCTURE BY NMR OF 40-53.
RX PubMed=11493011; DOI=10.1006/jmbi.2001.4887;
RA Korsinczky M.L., Schirra H.J., Rosengren K.J., West J., Condie B.A.,
RA Otvos L., Anderson M.A., Craik D.J.;
RT "Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1
RT from sunflower seeds and an acyclic permutant.";
RL J. Mol. Biol. 311:579-591(2001).
RN [4]
RP STRUCTURE BY NMR OF 40-53, AND DISULFIDE BOND.
RX PubMed=12621047; DOI=10.1074/jbc.m212996200;
RA Marx U.C., Korsinczky M.L.J., Schirra H.J., Jones A., Condie B.,
RA Otvos L. Jr., Craik D.J.;
RT "Enzymatic cyclization of a potent bowman-birk protease inhibitor,
RT sunflower trypsin inhibitor-1, and solution structure of an acyclic
RT precursor peptide.";
RL J. Biol. Chem. 278:21782-21789(2003).
CC -!- FUNCTION: Inhibits trypsin, cathepsin G, elastase, chymotrypsin and
CC thrombin. Does not inhibit factor Xa. {ECO:0000269|PubMed:10390350}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000269|PubMed:10390350}.
CC -!- MASS SPECTROMETRY: Mass=1513; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10390350};
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DR EMBL; AM050587; CAJ19097.1; -; Genomic_DNA.
DR PDB; 1JBL; NMR; -; A=40-53.
DR PDB; 1JBN; NMR; -; A=40-53.
DR PDB; 1O8Y; NMR; -; A=40-53.
DR PDB; 1O8Z; NMR; -; A=40-53.
DR PDB; 1SFI; X-ray; 1.65 A; I=40-53.
DR PDB; 1T9E; NMR; -; A=40-53.
DR PDB; 2AB9; NMR; -; A=26-56.
DR PDB; 3P8F; X-ray; 2.00 A; I=40-53.
DR PDB; 4ABI; X-ray; 1.55 A; B=40-53.
DR PDB; 4ABJ; X-ray; 1.45 A; B=40-53.
DR PDB; 4HGC; X-ray; 1.29 A; I=40-53.
DR PDB; 4K1E; X-ray; 1.30 A; B=40-53.
DR PDB; 4K8Y; X-ray; 1.00 A; B=40-53.
DR PDB; 4KEL; X-ray; 1.15 A; B=40-53.
DR PDB; 4XOJ; X-ray; 0.91 A; B=40-52.
DR PDB; 6BVH; X-ray; 1.93 A; I=40-53.
DR PDB; 6BVU; NMR; -; A=42-50.
DR PDB; 6BVW; NMR; -; A=42-50.
DR PDB; 6BVX; NMR; -; A=42-55.
DR PDB; 6BVY; NMR; -; A=42-50.
DR PDB; 6D3X; X-ray; 1.80 A; C/D=40-53.
DR PDB; 6D3Y; X-ray; 1.32 A; C=40-53.
DR PDB; 6D3Z; X-ray; 2.00 A; C=40-53.
DR PDB; 6D40; X-ray; 1.43 A; C=40-53.
DR PDB; 6Q1U; X-ray; 2.35 A; C/D=40-53.
DR PDB; 6U22; X-ray; 1.42 A; C=40-53.
DR PDB; 6U24; NMR; -; A=40-53.
DR PDB; 6U7Q; NMR; -; A=40-53.
DR PDB; 6U7R; NMR; -; A=40-53.
DR PDB; 6U7S; NMR; -; A=40-53.
DR PDB; 6U7U; NMR; -; A=40-53.
DR PDB; 6U7X; NMR; -; A=40-53.
DR PDB; 6VXY; X-ray; 1.40 A; C=40-53.
DR PDB; 6VY8; NMR; -; A=40-53.
DR PDB; 7ARX; X-ray; 2.42 A; C=40-53.
DR PDBsum; 1JBL; -.
DR PDBsum; 1JBN; -.
DR PDBsum; 1O8Y; -.
DR PDBsum; 1O8Z; -.
DR PDBsum; 1SFI; -.
DR PDBsum; 1T9E; -.
DR PDBsum; 2AB9; -.
DR PDBsum; 3P8F; -.
DR PDBsum; 4ABI; -.
DR PDBsum; 4ABJ; -.
DR PDBsum; 4HGC; -.
DR PDBsum; 4K1E; -.
DR PDBsum; 4K8Y; -.
DR PDBsum; 4KEL; -.
DR PDBsum; 4XOJ; -.
DR PDBsum; 6BVH; -.
DR PDBsum; 6BVU; -.
DR PDBsum; 6BVW; -.
DR PDBsum; 6BVX; -.
DR PDBsum; 6BVY; -.
DR PDBsum; 6D3X; -.
DR PDBsum; 6D3Y; -.
DR PDBsum; 6D3Z; -.
DR PDBsum; 6D40; -.
DR PDBsum; 6Q1U; -.
DR PDBsum; 6U22; -.
DR PDBsum; 6U24; -.
DR PDBsum; 6U7Q; -.
DR PDBsum; 6U7R; -.
DR PDBsum; 6U7S; -.
DR PDBsum; 6U7U; -.
DR PDBsum; 6U7X; -.
DR PDBsum; 6VXY; -.
DR PDBsum; 6VY8; -.
DR PDBsum; 7ARX; -.
DR AlphaFoldDB; Q4GWU5; -.
DR BMRB; Q4GWU5; -.
DR SMR; Q4GWU5; -.
DR MEROPS; I12.002; -.
DR EvolutionaryTrace; Q4GWU5; -.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0002020; F:protease binding; IDA:CAFA.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:CAFA.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..39
FT /evidence="ECO:0000255, ECO:0000269|PubMed:10390350"
FT /id="PRO_0000042672"
FT PEPTIDE 40..53
FT /note="Trypsin inhibitor 1"
FT /id="PRO_0000042673"
FT PROPEP 54..56
FT /id="PRO_0000042674"
FT SITE 44..45
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:P81705"
FT DISULFID 42..50
FT /evidence="ECO:0000269|PubMed:10390350,
FT ECO:0000269|PubMed:12621047"
FT CROSSLNK 40..53
FT /note="Cyclopeptide (Gly-Asp)"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2AB9"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4XOJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2AB9"
SQ SEQUENCE 56 AA; 5971 MW; BF3BAF97C25F19A7 CRC64;
MATTMAKLIT LVVLAILAFV EVSVSGYKTS ISTITIEDNG RCTKSIPPIC FPDGRP
