ID   ITRY_SINAR              Reviewed;         130 AA.
AC   P38057;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Trypsin inhibitor;
DE   AltName: Full=TISA;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor small chain;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor large chain;
OS   Sinapis arvensis (Charlock mustard) (Brassica kaber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=29728;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=8070965; DOI=10.1111/j.1399-3011.1994.tb00540.x;
RA   Svendsen I.B., Nicolova D., Goshev I., Genov N.;
RT   "Primary structure, spectroscopic and inhibitory properties of a two-chain
RT   trypsin inhibitor from the seeds of charlock (Sinapis arvensis L), a member
RT   of the napin protein family.";
RL   Int. J. Pept. Protein Res. 43:425-430(1994).
CC   -!- FUNCTION: Inhibits trypsin with a Ki of 7 x 10(-6) M.
CC   -!- SUBUNIT: The protein consists of two chains linked by disulfide bonds.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P38057; -.
DR   SMR; P38057; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; PTHR35496; 2.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Seed storage protein;
KW   Storage protein.
FT   CHAIN           1..39
FT                   /note="Trypsin inhibitor small chain"
FT                   /id="PRO_0000032172"
FT   CHAIN           40..130
FT                   /note="Trypsin inhibitor large chain"
FT                   /id="PRO_0000032173"
FT   REGION          27..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         32
FT                   /note="R -> M"
FT   VARIANT         53..57
FT                   /note="Missing (in form II)"
FT   VARIANT         73
FT                   /note="A -> S"
FT   VARIANT         77
FT                   /note="K -> R"
FT   VARIANT         81
FT                   /note="Q -> R"
FT   VARIANT         87
FT                   /note="H -> Q"
FT   VARIANT         89
FT                   /note="Q -> H"
FT   VARIANT         91
FT                   /note="G -> Q"
FT   VARIANT         97
FT                   /note="E -> M"
FT   VARIANT         98
FT                   /note="I -> V"
FT   VARIANT         99
FT                   /note="R -> S"
FT   VARIANT         106
FT                   /note="T -> K"
FT   VARIANT         123
FT                   /note="N -> Q"
FT   VARIANT         124
FT                   /note="K -> G"
FT   VARIANT         126
FT                   /note="M -> V"
FT   NON_CONS        39..40
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   130 AA;  14682 MW;  EC02E4B26D180DF2 CRC64;
     PAGPFRLPRC RKEFQQAQHL RACQQWLHKQ ARQSGSGPSP QGPQQRPPLL QQCCNELHQE
     EPLCVCPTLK GAAKAVKQQI QQQGQQHGQQ GQQLQHEIRR IYQTATHLPK VCNIPQVQVC
     PFNKTMPGPS