ID   LDTI_HIRME              Reviewed;          46 AA.
AC   P80424;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Leech-derived tryptase inhibitor C;
DE            Short=LDTI-C;
DE   Contains:
DE     RecName: Full=Leech-derived tryptase inhibitor B;
DE              Short=LDTI-B;
DE   Contains:
DE     RecName: Full=Leech-derived tryptase inhibitor A;
DE              Short=LDTI-A;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7888081; DOI=10.1515/bchm3.1994.375.10.685;
RA   Sommerhoff C.P., Soellner C., Mentele R., Piechottka G.P., Auerswald E.A.,
RA   Fritz H.;
RT   "A Kazal-type inhibitor of human mast cell tryptase: isolation from the
RT   medical leech Hirudo medicinalis, characterization, and sequence
RT   analysis.";
RL   Biol. Chem. Hoppe-Seyler 375:685-694(1994).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=7988692; DOI=10.1016/0014-5793(94)01225-3;
RA   Muehlhahn P., Czisch M., Morenweiser R., Habermann B., Engh R.A.,
RA   Sommerhoff C.P., Auerswald E.A., Holak T.A.;
RT   "Structure of leech derived tryptase inhibitor (LDTI-C) in solution.";
RL   FEBS Lett. 355:290-296(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH TRYPSIN.
RX   PubMed=9242660; DOI=10.1074/jbc.272.32.19931;
RA   Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R.,
RA   Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.;
RT   "The three-dimensional structure of recombinant leech-derived tryptase
RT   inhibitor in complex with trypsin. Implications for the structure of human
RT   mast cell tryptase and its inhibition.";
RL   J. Biol. Chem. 272:19931-19937(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF COMPLEX WITH TRYPSIN.
RX   PubMed=9384562; DOI=10.1016/s0969-2126(97)00296-7;
RA   di Marco S., Priestle J.P.;
RT   "Structure of the complex of leech-derived tryptase inhibitor (LDTI) with
RT   trypsin and modeling of the LDTI-tryptase system.";
RL   Structure 5:1465-1474(1997).
CC   -!- FUNCTION: Acts as an inhibitor of human tryptase, trypsin and
CC       chymotrypsin. Probably acts to block host defense mechanisms.
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DR   PIR; S50015; S50015.
DR   PDB; 1AN1; X-ray; 2.03 A; I=1-46.
DR   PDB; 1LDT; X-ray; 1.90 A; L=1-46.
DR   PDB; 2KMO; NMR; -; A=1-44.
DR   PDB; 2KMP; NMR; -; A=1-44.
DR   PDB; 2KMQ; NMR; -; A=1-44.
DR   PDB; 2KMR; NMR; -; A=1-44.
DR   PDBsum; 1AN1; -.
DR   PDBsum; 1LDT; -.
DR   PDBsum; 2KMO; -.
DR   PDBsum; 2KMP; -.
DR   PDBsum; 2KMQ; -.
DR   PDBsum; 2KMR; -.
DR   AlphaFoldDB; P80424; -.
DR   BMRB; P80424; -.
DR   SMR; P80424; -.
DR   DIP; DIP-6084N; -.
DR   IntAct; P80424; 1.
DR   MINT; P80424; -.
DR   MEROPS; I01.021; -.
DR   EvolutionaryTrace; P80424; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..46
FT                   /note="Leech-derived tryptase inhibitor C"
FT                   /id="PRO_0000045882"
FT   CHAIN           1..43
FT                   /note="Leech-derived tryptase inhibitor B"
FT                   /id="PRO_0000045883"
FT   CHAIN           1..42
FT                   /note="Leech-derived tryptase inhibitor A"
FT                   /id="PRO_0000045884"
FT   DOMAIN          1..42
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            8..9
FT                   /note="Reactive bond (tryptase)"
FT   DISULFID        4..29
FT   DISULFID        6..25
FT   DISULFID        14..40
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:1LDT"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1AN1"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1LDT"
FT   HELIX           24..30
FT                   /evidence="ECO:0007829|PDB:1LDT"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:1LDT"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1LDT"
SQ   SEQUENCE   46 AA;  4744 MW;  9FC4383FF5C009A1 CRC64;
     KKVCACPKIL KPVCGSDGRT YANSCIARCN GVSIKSEGSC PTGILN