ITRA_MOMCH
ID ITRA_MOMCH Reviewed; 28 AA.
AC P30709;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Trypsin inhibitor A;
OS Momordica charantia (Bitter gourd) (Balsam pear).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX NCBI_TaxID=3673;
RN [1]
RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=1551419; DOI=10.1016/0014-5793(92)80346-i;
RA Huang Q., Liu S., Tang Y., Zeng F., Qian R.;
RT "Amino acid sequencing of a trypsin inhibitor by refined 1.6 A X-ray
RT crystal structure of its complex with porcine beta-trypsin.";
RL FEBS Lett. 297:143-146(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.
CC -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC protease inhibitor) family. {ECO:0000305}.
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DR PIR; S20393; S20393.
DR PDB; 1MCT; X-ray; 1.60 A; I=1-28.
DR PDBsum; 1MCT; -.
DR AlphaFoldDB; P30709; -.
DR SMR; P30709; -.
DR MINT; P30709; -.
DR MEROPS; I07.018; -.
DR EvolutionaryTrace; P30709; -.
DR Proteomes; UP000504603; 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 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 3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor.
FT PEPTIDE 1..28
FT /note="Trypsin inhibitor A"
FT /id="PRO_0000044389"
FT SITE 5..6
FT /note="Reactive bond"
FT DISULFID 3..20
FT DISULFID 10..22
FT DISULFID 16..27
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1MCT"
SQ SEQUENCE 28 AA; 3133 MW; 67E8E6A2D404FEDF CRC64;
RSCPRIWMEC TRDSDCMAKC ICVAGHCG