ID   IBB2_PEA                Reviewed;         114 AA.
AC   Q41066;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Seed trypsin/chymotrypsin inhibitor TI5-72;
DE   Flags: Precursor;
GN   Name=TI572;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Birte;
RX   PubMed=7875292; DOI=10.1016/0014-5793(95)00070-p;
RA   Domoney C., Welham T., Sidebottom C., Firmin J.-L.;
RT   "Multiple isoforms of Pisum trypsin inhibitors result from modification of
RT   two primary gene products.";
RL   FEBS Lett. 360:15-20(1995).
CC   -!- FUNCTION: Inhibitor of trypsin and of chymotrypsin. May function as a
CC       natural phytochemical defense against predators.
CC   -!- TISSUE SPECIFICITY: Seed.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; X83210; CAA58212.1; -; mRNA.
DR   PIR; S69006; S69006.
DR   AlphaFoldDB; Q41066; -.
DR   SMR; Q41066; -.
DR   MEROPS; I12.018; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00023; BBI; 1.
DR   Gene3D; 2.10.69.10; -; 1.
DR   InterPro; IPR035995; Bowman-Birk_prot_inh.
DR   InterPro; IPR000877; Prot_inh_BBI.
DR   Pfam; PF00228; Bowman-Birk_leg; 1.
DR   SMART; SM00269; BowB; 1.
DR   SUPFAM; SSF57247; SSF57247; 1.
DR   PROSITE; PS00281; BOWMAN_BIRK; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Serine protease inhibitor; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..42
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003278"
FT   CHAIN           43..114
FT                   /note="Seed trypsin/chymotrypsin inhibitor TI5-72"
FT                   /id="PRO_0000003279"
FT   SITE            58..59
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            84..85
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..103
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        54..99
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        56..64
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        73..80
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        77..92
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        82..90
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   114 AA;  12598 MW;  B60FC0768E8AB2A3 CRC64;
     MELMNKKVMM KLALMVFLLS FAANVVNARF DSTSFITQVL SNGDDVKSAC CDTCLCTKSD
     PPTCRCVDVG ETCHSACDSC ICALSYPPQC QCFDTHKFCY KACHNSEVEE VIKN