ID   TI_VERHE                Reviewed;          34 AA.
AC   P85981;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Trypsin inhibitor {ECO:0000303|PubMed:17640870};
DE            Short=VhTI {ECO:0000303|PubMed:17640870};
OS   Veronica hederifolia (Ivy-leaved speedwell).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Veroniceae; Veronica;
OC   Veronica subgen. Cochlidiosperma.
OX   NCBI_TaxID=202477;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, REACTIVE BOND, DISULFIDE BONDS, AND X-RAY
RP   CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH BOVINE TRYPSIN.
RC   TISSUE=Seed {ECO:0000269|PubMed:17640870};
RX   PubMed=17640870; DOI=10.1074/jbc.m703871200;
RA   Conners R., Konarev A.V., Forsyth J., Lovegrove A., Marsh J.,
RA   Joseph-Horne T., Shewry P., Brady R.L.;
RT   "An unusual helix-turn-helix protease inhibitory motif in a novel trypsin
RT   inhibitor from seeds of Veronica (Veronica hederifolia L.).";
RL   J. Biol. Chem. 282:27760-27768(2007).
CC   -!- FUNCTION: Inhibits trypsin. {ECO:0000269|PubMed:17640870}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- MISCELLANEOUS: Differs dramatically in structure from all previously
CC       described families of trypsin inhibitors. Consists of a helix-loop-
CC       helix motif with two alpha-helices tightly associated by two disulfide
CC       bonds. {ECO:0000269|PubMed:17640870}.
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DR   PDB; 2CMY; X-ray; 2.25 A; B=1-34.
DR   PDB; 2PLX; X-ray; 1.56 A; B=6-31.
DR   PDBsum; 2CMY; -.
DR   PDBsum; 2PLX; -.
DR   AlphaFoldDB; P85981; -.
DR   SMR; P85981; -.
DR   MEROPS; I73.001; -.
DR   EvolutionaryTrace; P85981; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Secreted; Serine protease inhibitor.
FT   CHAIN           1..34
FT                   /note="Trypsin inhibitor"
FT                   /id="PRO_0000351204"
FT   SITE            15..16
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000269|PubMed:17640870"
FT   DISULFID        7..29
FT                   /evidence="ECO:0000269|PubMed:17640870"
FT   DISULFID        11..25
FT                   /evidence="ECO:0000269|PubMed:17640870"
FT   HELIX           7..13
FT                   /evidence="ECO:0007829|PDB:2PLX"
FT   HELIX           19..29
FT                   /evidence="ECO:0007829|PDB:2PLX"
SQ   SEQUENCE   34 AA;  4050 MW;  BD6BB312733CCE21 CRC64;
     NTDPEQCKVM CYAQRHSSPE LLRRCLDNCE KEHD