ID   ITR1_CUCMA              Reviewed;          29 AA.
AC   P01074;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 65.
DE   RecName: Full=Trypsin inhibitor 1;
DE   AltName: Full=Trypsin inhibitor I;
DE   AltName: Full=CMTI-I;
DE   AltName: Full=ITD-I;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   MEDLINE=83184077; PubMed=6840699;
RA   Wilusz T., Wieczorek M., Polanowski A., Denton A., Cook J.,
RA   Laskowski M. Jr.;
RT   "Amino-acid sequence of two trypsin isoinhibitors, ITD I and ITD III
RT   from squash seeds (Cucurbita maxima).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:93-95(1983).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=89121085; PubMed=2914611; DOI=10.1016/0014-5793(89)80486-7;
RA   Bode W., Greyling H.J., Huber R., Otlewski J., Wilusz T.;
RT   "The refined 2.0 A X-ray crystal structure of the complex formed
RT   between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from
RT   squash seeds (Cucurbita maxima). Topological similarity of the squash
RT   seed inhibitors with the carboxypeptidase A inhibitor from potatoes.";
RL   FEBS Lett. 242:285-292(1989).
RN   [3]
RP   STRUCTURE BY NMR.
RX   MEDLINE=90133915; PubMed=2614837; DOI=10.1016/0022-2836(89)90137-X;
RA   Holak T.A., Gondol D., Otlewski J., Wilusz T.;
RT   "Determination of the complete three-dimensional structure of the
RT   trypsin inhibitor from squash seeds in aqueous solution by nuclear
RT   magnetic resonance and a combination of distance geometry and
RT   dynamical simulated annealing.";
RL   J. Mol. Biol. 210:635-648(1989).
RN   [4]
RP   STRUCTURE BY NMR.
RX   MEDLINE=20178923; PubMed=10716179;
RA   Zhukov I., Jaroszewski L., Bierzynski A.;
RT   "Conservative mutation Met8 --> Leu affects the folding process and
RT   structural stability of squash trypsin inhibitor CMTI-I.";
RL   Protein Sci. 9:273-279(2000).
CC   -!- FUNCTION: Inhibits trypsin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type
CC       serine protease inhibitor) family.
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DR   PIR; A01313; TIPU.
DR   PDB; 1CTI; NMR; -; A=1-29.
DR   PDB; 1LU0; X-ray; 1.03 A; A/B=1-29.
DR   PDB; 1PPE; X-ray; 2.00 A; I=1-29.
DR   PDB; 2CTI; NMR; -; A=1-29.
DR   PDB; 2STA; X-ray; 1.80 A; I=1-29.
DR   PDB; 2V1V; NMR; -; A=1-29.
DR   PDB; 3CTI; NMR; -; A=1-29.
DR   PDBsum; 1CTI; -.
DR   PDBsum; 1LU0; -.
DR   PDBsum; 1PPE; -.
DR   PDBsum; 2CTI; -.
DR   PDBsum; 2STA; -.
DR   PDBsum; 2V1V; -.
DR   PDBsum; 3CTI; -.
DR   MEROPS; I07.005; -.
DR   LinkHub; P01074; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   InterPro; IPR000737; Prot_inh_squash.
DR   Pfam; PF00299; Squash; 1.
DR   PRINTS; PR00293; SQUASHINHBTR.
DR   ProDom; PD003401; Prot_inh_squash; 1.
DR   SMART; SM00286; PTI; 1.
DR   PROSITE; PS00286; SQUASH_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Knottin; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   PEPTIDE       1     29       Trypsin inhibitor 1.
FT                                /FTId=PRO_0000044376.
FT   SITE          5      6       Reactive bond.
FT   DISULFID      3     20
FT   DISULFID     10     22
FT   DISULFID     16     28
FT   HELIX        13     15
FT   STRAND       26     28
SQ   SEQUENCE   29 AA;  3275 MW;  CD509120BA52C01F CRC64;
     RVCPRILMEC KKDSDCLAEC VCLEHGYCG
//