ID   ICI_LINUS               Reviewed;          69 AA.
AC   P82381;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Proteinase inhibitor;
DE   AltName: Full=LUTI;
OS   Linum usitatissimum (Flax) (Linum humile).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Linaceae; Linum.
OX   NCBI_TaxID=4006;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, ACETYLATION AT SER-1, ACTIVE
RP   BOND, AND DISULFIDE BOND.
RX   PubMed=11828426;
RX   DOI=10.1002/1439-7633(20010105)2:1<45::aid-cbic45>3.0.co;2-%23;
RA   Lorenc-Kubis I., Kowalska J., Pochron B., Zuzlo A., Wilusz T.;
RT   "Isolation and amino acid sequence of a serine proteinase inhibitor from
RT   common flax (Linum usitatissimum) seeds.";
RL   ChemBioChem 2:45-51(2001).
CC   -!- FUNCTION: In vitro, strong inhibitor of bovine beta-trypsin, weak
CC       inhibitor of alpha-chymotrypsin, subtilisin BPN', subtilisin Carlsberg
CC       and cathepsin G. {ECO:0000269|PubMed:11828426}.
CC   -!- MASS SPECTROMETRY: Mass=7655.0; Mass_error=0.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11828426};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease 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   PDB; 1DWM; NMR; -; A=1-69.
DR   PDBsum; 1DWM; -.
DR   AlphaFoldDB; P82381; -.
DR   SMR; P82381; -.
DR   iPTMnet; P82381; -.
DR   EvolutionaryTrace; P82381; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR   InterPro; IPR000864; Prot_inh_pot1.
DR   InterPro; IPR036354; Prot_inh_pot1_sf.
DR   PANTHER; PTHR33091; PTHR33091; 1.
DR   Pfam; PF00280; potato_inhibit; 1.
DR   PRINTS; PR00292; POTATOINHBTR.
DR   SUPFAM; SSF54654; SSF54654; 1.
DR   PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..69
FT                   /note="Proteinase inhibitor"
FT                   /id="PRO_0000217652"
FT   SITE            45..46
FT                   /note="Reactive bond"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:11828426"
FT   DISULFID        4..49
FT                   /evidence="ECO:0000269|PubMed:11828426"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1DWM"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:1DWM"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:1DWM"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:1DWM"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:1DWM"
SQ   SEQUENCE   69 AA;  7613 MW;  9E441A9742FF8055 CRC64;
     SRRCPGKNAW PELVGKSGNM AAATVERENR NVHAIVLKEG SAMTKDFRCD RVWVIVNDHG
     VVTSVPHIT