ID   ITRB_SOYBN              Reviewed;         181 AA.
AC   P01071;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Trypsin inhibitor B;
DE   AltName: Full=Kunitz-type trypsin inhibitor B;
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Norin No. 2;
RX   PubMed=3905784; DOI=10.1093/oxfordjournals.jbchem.a135298;
RA   Kim S.-H., Hara S., Hase S., Ikenaka T., Toda H., Kitamura K., Kaizuma N.;
RT   "Comparative study on amino acid sequences of Kunitz-type soybean trypsin
RT   inhibitors, Tia, Tib, and Tic.";
RL   J. Biochem. 98:435-448(1985).
CC   -!- FUNCTION: Inhibition of trypsin.
CC   -!- MISCELLANEOUS: Electrophoresis identifies three genetically distinct
CC       variants, A, B, and C, that are inherited as codominant alleles.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A01310; TISYB.
DR   AlphaFoldDB; P01071; -.
DR   BMRB; P01071; -.
DR   SMR; P01071; -.
DR   PRIDE; P01071; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00178; STI; 1.
DR   DisProt; DP01971; -.
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   Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..181
FT                   /note="Trypsin inhibitor B"
FT                   /id="PRO_0000083285"
FT   SITE            63..64
FT                   /note="Reactive bond for trypsin"
FT   DISULFID        39..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..145
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20041 MW;  C134E9891866C787 CRC64;
     DFVLDNEGNP LSNGGTYYIL SDITAFGGIR AAPTGNERCP LTVVQSRNEL DKGIGTIISS
     PFRIRFIAEG NPLRLKFDSF AVIMLCVGIP TEWSVVEDLP EGPAVKIGEN KDAVDGWFRI
     ERVSDDEFNN YKLVFCTQQA EDDKCGDIGI SIDHDDGTRR LVVSKNKPLV VQFQKVDKES
     L