ITR6_CYCPE
ID ITR6_CYCPE Reviewed; 30 AA.
AC P83397;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Trypsin inhibitor 6 {ECO:0000303|PubMed:16635550};
DE AltName: Full=CyPTI-VI {ECO:0000303|PubMed:16635550};
DE AltName: Full=Trypsin inhibitor VI {ECO:0000303|PubMed:16635550};
OS Cyclanthera pedata (Achocha) (Caihua).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Cyclanthera.
OX NCBI_TaxID=198836;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND REACTIVE SITE.
RC TISSUE=Seed {ECO:0000269|PubMed:16635550};
RX PubMed=16635550; DOI=10.1016/j.bbagen.2006.03.011;
RA Kowalska J., Zablocka A., Wilusz T.;
RT "Isolation and primary structures of seven serine proteinase inhibitors
RT from Cyclanthera pedata seeds.";
RL Biochim. Biophys. Acta 1760:1054-1063(2006).
CC -!- FUNCTION: Strongly inhibits trypsin, weakly inhibits chymotrypsin.
CC {ECO:0000269|PubMed:16635550}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P01074}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC protease inhibitor) family. {ECO:0000255}.
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DR AlphaFoldDB; P83397; -.
DR SMR; P83397; -.
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 Secreted; Serine protease inhibitor.
FT PEPTIDE 1..30
FT /note="Trypsin inhibitor 6"
FT /evidence="ECO:0000269|PubMed:16635550"
FT /id="PRO_0000044379"
FT SITE 6..7
FT /note="Reactive bond"
FT /evidence="ECO:0000269|PubMed:16635550"
FT DISULFID 4..21
FT /evidence="ECO:0000250|UniProtKB:P01074"
FT DISULFID 11..23
FT /evidence="ECO:0000250|UniProtKB:P01074"
FT DISULFID 17..29
FT /evidence="ECO:0000250|UniProtKB:P01074"
SQ SEQUENCE 30 AA; 3373 MW; D5F383AE41F8787E CRC64;
ARICPRILMK CKKDSDCLAE CICEEHGFCG