ID   IP27_SOLTU              Reviewed;         154 AA.
AC   Q43652;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Proteinase inhibitor type-2 CM7;
DE   AltName: Full=Proteinase inhibitor type II CM7;
DE   Flags: Precursor;
GN   Name=PIN2-CM7;
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].
RC   STRAIN=cv. Arran Banner; TISSUE=Leaf;
RX   PubMed=7846166; DOI=10.1104/pp.106.4.1681;
RA   Murray C., Christeller J.T.;
RT   "Genomic nucleotide sequence of a proteinase inhibitor II gene.";
RL   Plant Physiol. 106:1681-1681(1994).
CC   -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC       proteinase inhibitor) family. {ECO:0000305}.
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DR   EMBL; X78275; CAA55082.1; -; Genomic_DNA.
DR   PIR; S43105; S43105.
DR   AlphaFoldDB; Q43652; -.
DR   SMR; Q43652; -.
DR   MEROPS; I20.950; -.
DR   PRIDE; Q43652; -.
DR   InParanoid; Q43652; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43652; 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   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..154
FT                   /note="Proteinase inhibitor type-2 CM7"
FT                   /id="PRO_0000025317"
FT   REPEAT          31..87
FT                   /note="1"
FT   REPEAT          88..147
FT                   /note="2"
FT   SITE            36..37
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000305"
FT   SITE            93..94
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000305"
FT   DISULFID        34..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..139
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  16868 MW;  9EE8CCB7A26099C2 CRC64;
     MDVHKEVNFV AYLLIVLGIF LLVSVVEHVD AKICTKECGN LGFGICPRSE GSPKNPICIN
     CCSGYKGCNY YSVFGRFICE GESDLKNPKA CPLNCDTNIA YSRCPHSEGK SLIYPTGCTT
     CCTGYKGCYY FGKNGKFVCE GESDEPKANM YPAM