IBBA_PEA
ID IBBA_PEA Reviewed; 96 AA.
AC Q41065;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Seed trypsin/chymotrypsin inhibitor IVA;
DE Short=PSTI IVA;
DE AltName: Full=TI12-36;
DE Contains:
DE RecName: Full=Seed trypsin/chymotrypsin inhibitor I;
DE Short=PSTI I;
DE Flags: Precursor; Fragment;
GN Name=TI1236;
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], AND PROTEIN SEQUENCE OF 25-56.
RC STRAIN=cv. Birte, and cv. JI 2;
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).
RN [2]
RP PROTEIN SEQUENCE OF 25-96.
RC STRAIN=cv. Frilene; TISSUE=Seed;
RX PubMed=8593187; DOI=10.1007/bf01888141;
RA Ferrasson E., Quillien L., Gueguen J.;
RT "Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea
RT seeds.";
RL J. Protein Chem. 14:467-475(1995).
RN [3]
RP PROTEOLYTIC PROCESSING.
RC STRAIN=cv. Frilene; TISSUE=Seed;
RX PubMed=9155090; DOI=10.1023/a:1026326808553;
RA Quillien L., Ferrasson E., Molle D., Gueguen J.;
RT "Trypsin inhibitor polymorphism: multigene family expression and
RT posttranslational modification.";
RL J. Protein Chem. 16:195-203(1997).
CC -!- FUNCTION: Inhibitor of trypsin and of chymotrypsin. May function as a
CC natural phytochemical defense against predators.
CC -!- TISSUE SPECIFICITY: Seed.
CC -!- DEVELOPMENTAL STAGE: During desiccation stage of seed development
CC increasing activity seems to be associated with appearance of isoform I
CC (PSTI I) which has a stronger affinity for trypsin.
CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC family. {ECO:0000305}.
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DR EMBL; X83211; CAA58213.1; -; mRNA.
DR PIR; S69007; S69007.
DR AlphaFoldDB; Q41065; -.
DR SMR; Q41065; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Serine protease inhibitor; Signal.
FT SIGNAL <1..10
FT /evidence="ECO:0000255"
FT PROPEP 11..24
FT /evidence="ECO:0000255"
FT /id="PRO_0000003271"
FT CHAIN 25..96
FT /note="Seed trypsin/chymotrypsin inhibitor IVA"
FT /id="PRO_0000003272"
FT CHAIN 25..87
FT /note="Seed trypsin/chymotrypsin inhibitor I"
FT /id="PRO_0000003273"
FT PROPEP 88..96
FT /note="Removed in PSTI I"
FT /id="PRO_0000003274"
FT SITE 40..41
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT SITE 66..67
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 32..85
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 33..48
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 36..81
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 38..46
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 55..62
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 59..74
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT DISULFID 64..72
FT /evidence="ECO:0000250|UniProtKB:P80321"
FT CONFLICT 52
FT /note="R -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 96 AA; 10544 MW; 654F0E00069FB8F2 CRC64;
LSFAANVVNA RFDSTSFITQ VLSNGDDVKS ACCDTCLCTK SNPPTCRCVD VRETCHSACD
SCICAYSNPP KCQCFDTHKF CYKACHNSEV EEVIKN
