ID   IP2K_SOLTU              Reviewed;         153 AA.
AC   P01080; P11429;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Proteinase inhibitor type-2 K;
DE   AltName: Full=Proteinase inhibitor type II K;
DE            Short=IIK;
DE   Contains:
DE     RecName: Full=Proteinase inhibitor PCI-1;
DE     AltName: Full=Proteinase inhibitor PCI-I;
DE   Flags: Precursor;
GN   Name=PIN2K;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16593809; DOI=10.1073/pnas.84.3.744;
RA   Thornburg R.W., An G., Cleveland T.E., Johnson R., Ryan C.A.;
RT   "Wound-inducible expression of a potato inhibitor II-chloramphenicol
RT   acetyltransferase gene fusion in transgenic tobacco plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:744-748(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3016659; DOI=10.1093/nar/14.14.5641;
RA   Keil M., Sanchez-Serrano J., Schell J., Willmitzer L.;
RT   "Primary structure of a proteinase inhibitor II gene from potato (Solanum
RT   tuberosum).";
RL   Nucleic Acids Res. 14:5641-5650(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 55-106.
RX   PubMed=7074039; DOI=10.1021/bi00533a027;
RA   Hass G.M., Hermodson M.A., Ryan C.A., Gentry L.;
RT   "Primary structures of two low molecular weight proteinase inhibitors from
RT   potatoes.";
RL   Biochemistry 21:752-756(1982).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 55-106.
RX   PubMed=2494344; DOI=10.1016/0022-2836(89)90376-8;
RA   Greenblatt H.M., Ryan C.A., James M.N.G.;
RT   "Structure of the complex of Streptomyces griseus proteinase B and
RT   polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at
RT   2.1-A resolution.";
RL   J. Mol. Biol. 205:201-228(1989).
CC   -!- FUNCTION: Inhibitor of trypsin and chymotrypsin.
CC   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; M15186; AAA33815.1; -; Genomic_DNA.
DR   EMBL; X03778; CAA27408.1; -; mRNA.
DR   EMBL; X04118; CAA27730.1; -; Genomic_DNA.
DR   PIR; A26584; XKPOC1.
DR   PDB; 4SGB; X-ray; 2.10 A; I=55-105.
DR   PDBsum; 4SGB; -.
DR   AlphaFoldDB; P01080; -.
DR   SMR; P01080; -.
DR   MINT; P01080; -.
DR   MEROPS; I20.001; -.
DR   MEROPS; I20.950; -.
DR   PRIDE; P01080; -.
DR   InParanoid; P01080; -.
DR   EvolutionaryTrace; P01080; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P01080; baseline and differential.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR003465; Prot_inh_I20.
DR   Pfam; PF02428; Prot_inhib_II; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Protease inhibitor; Reference proteome;
KW   Repeat; Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..153
FT                   /note="Proteinase inhibitor type-2 K"
FT                   /id="PRO_0000025313"
FT   CHAIN           55..106
FT                   /note="Proteinase inhibitor PCI-1"
FT                   /id="PRO_0000025314"
FT   REPEAT          30..86
FT                   /note="1"
FT   REPEAT          87..146
FT                   /note="2"
FT   SITE            35..36
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            92..93
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        33..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..94
FT   DISULFID        60..78
FT   DISULFID        61..90
FT   DISULFID        67..103
FT   DISULFID        120..138
FT                   /evidence="ECO:0000250"
FT   CONFLICT        27
FT                   /note="D -> EH (in Ref. 2; CAA27408/CAA27730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34..35
FT                   /note="IR -> TL (in Ref. 2; CAA27408/CAA27730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="P -> R (in Ref. 2; CAA27408/CAA27730)"
FT                   /evidence="ECO:0000305"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:4SGB"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:4SGB"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:4SGB"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:4SGB"
SQ   SEQUENCE   153 AA;  16505 MW;  8027499652E8BA06 CRC64;
     MDVHKEVNFV AYLLIVLGLL VLVSAMDVDA KACIRECGNL GFGICPRSEG SPENPICTNC
     CAGYKGCNYY SANGAFICEG QSDPKKPKAC PLNCDPHIAY SKCPRSEGKS LIYPTGCTTC
     CTGYKGCYYF GKNGKFVCEG ESDEPKANMY PAM