ID   IECI_ERYVA              Reviewed;         179 AA.
AC   P34952;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Chymotrypsin inhibitor ECI;
OS   Erythrina variegata (Indian coral tree) (Erythrina indica).
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; indigoferoid/millettioid clade; Phaseoleae; Erythrina.
OX   NCBI_TaxID=3845;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   STRAIN=Var. Orientalis; TISSUE=Seed;
RX   PubMed=7763417; DOI=10.1271/bbb.57.102;
RA   Kimura M., Kouzuma Y., Yamasaki N.;
RT   "Amino acid sequence of chymotrypsin inhibitor ECI from the seeds of
RT   Erythrina variegata (Linn.) var. Orientalis.";
RL   Biosci. Biotechnol. Biochem. 57:102-106(1993).
CC   -!- FUNCTION: Inhibition of chymotrypsin.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   PIR; JC1487; JC1487.
DR   AlphaFoldDB; P34952; -.
DR   SMR; P34952; -.
DR   MEROPS; I03.005; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00178; STI; 1.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   PANTHER; PTHR33107; PTHR33107; 1.
DR   Pfam; PF00197; Kunitz_legume; 1.
DR   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; SSF50386; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Pyrrolidone carboxylic acid; Serine protease inhibitor.
FT   CHAIN           1..179
FT                   /note="Chymotrypsin inhibitor ECI"
FT                   /id="PRO_0000083291"
FT   SITE            64..65
FT                   /note="Reactive bond for chymotrypsin"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:7763417"
FT   DISULFID        40..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..143
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   179 AA;  19851 MW;  E772FCAD905EC839 CRC64;
     QPLVDLEGNL VENGGTYYLL PHIWALGGGI EAARTGKETC PLTVVQSPFE VSNGEPIRIA
     SQFLSTFIPD GSPYAIGFAN PPSCAASPWW TVVETSEGLA VKLLEHKTPE EDDTKFKFQK
     VSSPNRYVYN LSYCQREDDD LKCDQYIGIR RDAKGYRRLV VTNDNPLELV LVKANSPSQ