ID   ITH5_CUCMA              Reviewed;          68 AA.
AC   P19873;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Inhibitor of trypsin and hageman factor;
DE   AltName: Full=CMTI-V;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   TISSUE=Seed;
RX   PubMed=2226848; DOI=10.1016/0014-5793(90)81075-y;
RA   Krishnamoorthi R., Gong Y.X., Richardson M.;
RT   "A new protein inhibitor of trypsin and activated Hageman factor from
RT   pumpkin (Cucurbita maxima) seeds.";
RL   FEBS Lett. 273:163-167(1990).
RN   [2]
RP   STRUCTURE BY NMR.
RC   TISSUE=Seed;
RX   PubMed=8634282; DOI=10.1021/bi952466d;
RA   Liu J., Prakash O., Cai M., Gong Y.X., Huang Y., Wen L., Wen J.J.,
RA   Huang J.-K., Krishnamoorthi R.;
RT   "Solution structure and backbone dynamics of recombinant Cucurbita maxima
RT   trypsin inhibitor-V determined by NMR spectroscopy.";
RL   Biochemistry 35:1516-1524(1996).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=7547948; DOI=10.1021/bi00038a001;
RA   Cai M., Gong Y.X., Prakash O., Krishnamoorthi R.;
RT   "Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function,
RT   thermodynamic stability, and NMR solution structure.";
RL   Biochemistry 34:12087-12094(1995).
CC   -!- FUNCTION: Specifically inhibits both trypsin and activated Hageman
CC       factor.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   PIR; S12897; S12897.
DR   PDB; 1HYM; NMR; -; A=1-44, B=45-68.
DR   PDB; 1MIT; NMR; -; A=1-68.
DR   PDB; 1TIN; NMR; -; A=1-68.
DR   PDBsum; 1HYM; -.
DR   PDBsum; 1MIT; -.
DR   PDBsum; 1TIN; -.
DR   AlphaFoldDB; P19873; -.
DR   SMR; P19873; -.
DR   MEROPS; I13.008; -.
DR   iPTMnet; P19873; -.
DR   EvolutionaryTrace; P19873; -.
DR   Proteomes; UP000504608; Unplaced.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; 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   PRINTS; PR00292; POTATOINHBTR.
DR   SUPFAM; SSF54654; SSF54654; 1.
DR   PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..68
FT                   /note="Inhibitor of trypsin and hageman factor"
FT                   /id="PRO_0000217655"
FT   SITE            44..45
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2226848"
FT   DISULFID        3..48
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:1HYM"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:1HYM"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:1HYM"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:1HYM"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:1HYM"
SQ   SEQUENCE   68 AA;  7363 MW;  AF000AB56B0DFA6E CRC64;
     SSCPGKSSWP HLVGVGGSVA KAIIERQNPN VKAVILEEGT PVTKDFRCNR VRIWVNKRGL
     VVSPPRIG