ITR4_CUCMA
ID ITR4_CUCMA Reviewed; 32 AA.
AC P07853;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Trypsin inhibitor 4;
DE AltName: Full=CMTI-IV;
DE AltName: Full=Trypsin inhibitor IV;
DE Contains:
DE RecName: Full=Trypsin inhibitor 3;
DE AltName: Full=CMTI-III;
DE AltName: Full=ITD-III;
DE AltName: Full=Trypsin inhibitor III;
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 (CMT-IV).
RC TISSUE=Seed;
RX PubMed=3977882; DOI=10.1016/0006-291x(85)90233-5;
RA Wieczorek M., Otlewski J., Cook J., Parks K., Leluk J., Wilimowska-Pelc A.,
RA Polanowski A., Wilusz T., Laskowski M. Jr.;
RT "The squash family of serine proteinase inhibitors. Amino acid sequences
RT and association equilibrium constants of inhibitors from squash, summer
RT squash, zucchini, and cucumber seeds.";
RL Biochem. Biophys. Res. Commun. 126:646-652(1985).
RN [2]
RP PROTEIN SEQUENCE (CMT-III).
RC TISSUE=Seed;
RX PubMed=6840699; DOI=10.1515/bchm2.1983.364.1.93;
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 from
RT squash seeds (Cucurbita maxima).";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:93-95(1983).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE (CMT-III).
RC TISSUE=Seed;
RX PubMed=7275008;
RA Nowak K., Slominska A., Polanowski A., Wieczorek M., Wilusz T.;
RT "Trypsin inhibitor III from squash seeds (Cucurbita maxima), its reactive
RT site and proposed amino acid sequence.";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:1017-1019(1981).
RN [4]
RP STRUCTURE BY NMR OF CMT-III.
RX PubMed=1731946; DOI=10.1021/bi00118a036;
RA Krishnamoorthi R., Gong Y., Lin C.-L.S., Vandervelde D.;
RT "Two-dimensional NMR studies of squash family inhibitors. Sequence-specific
RT proton assignments and secondary structure of reactive-site hydrolyzed
RT Cucurbita maxima trypsin inhibitor III.";
RL Biochemistry 31:898-904(1992).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC protease inhibitor) family. {ECO:0000305}.
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DR PIR; B01313; TIPU3.
DR PIR; S07156; S07156.
DR AlphaFoldDB; P07853; -.
DR BMRB; P07853; -.
DR SMR; P07853; -.
DR MEROPS; I07.007; -.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00150; PlantTI; 1.
DR InterPro; IPR000737; Prot_inh_squash.
DR InterPro; IPR011052; Proteinase_amylase_inhib_sf.
DR Pfam; PF00299; Squash; 1.
DR PRINTS; PR00293; SQUASHINHBTR.
DR SUPFAM; SSF57027; SSF57027; 1.
DR PROSITE; PS00286; SQUASH_INHIBITOR; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor.
FT PEPTIDE 1..32
FT /note="Trypsin inhibitor 4"
FT /id="PRO_0000033197"
FT PEPTIDE 4..32
FT /note="Trypsin inhibitor 3"
FT /id="PRO_0000033198"
FT SITE 8..9
FT /note="Reactive bond"
FT DISULFID 6..23
FT /evidence="ECO:0000250"
FT DISULFID 13..25
FT /evidence="ECO:0000250"
FT DISULFID 19..31
FT /evidence="ECO:0000250"
SQ SEQUENCE 32 AA; 3669 MW; 0F591120B0137512 CRC64;
HEERVCPRIL MKCKKDSDCL AECVCLEHGY CG
