ID   API5_SOLTU              Reviewed;         220 AA.
AC   P58519;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Aspartic protease inhibitor 5;
DE   AltName: Full=PI-13;
DE   AltName: Full=pi13;
DE   Flags: Precursor;
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.
RC   STRAIN=cv. Pentland squire; TISSUE=Tuber;
RX   PubMed=1515078; DOI=10.1515/bchm3.1992.373.2.477;
RA   Strukelj B., Pungercar J., Mesko P., Barlic-Maganja D., Gubensek F.,
RA   Kregar I., Turk V.;
RT   "Characterization of aspartic proteinase inhibitors from potato at the
RT   gene, cDNA and protein levels.";
RL   Biol. Chem. Hoppe-Seyler 373:477-482(1992).
CC   -!- FUNCTION: Inhibitor of cathepsin D (aspartic protease). May also
CC       inhibit trypsin and chymotrypsin (serine proteases). Protects the plant
CC       by inhibiting proteases of invading organisms.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   PIR; S24186; S24186.
DR   AlphaFoldDB; P58519; -.
DR   SMR; P58519; -.
DR   PRIDE; P58519; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P58519; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00178; STI; 1.
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   3: Inferred from homology;
KW   Aspartic protease inhibitor; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal;
KW   Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PROPEP          24..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016916"
FT   CHAIN           33..220
FT                   /note="Aspartic protease inhibitor 5"
FT                   /id="PRO_0000016917"
FT   MOTIF           26..31
FT                   /note="Vacuolar targeting signal"
FT                   /evidence="ECO:0000250"
FT   SITE            99..100
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            143..144
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..185
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  24303 MW;  41D2D499139019E6 CRC64;
     MMKCLFLLCL CLLPIVVFSS TFTSQNLIDL PSESPVPKPV LDTNGKELNP NSSYRIISIG
     RGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSTNIFED QLLNIQFNIP
     TVKLCVSYTI WKVGNLNAHL RTMLLETGGT IGQADSSYFK IVKSSKFGYN LLYCPITRHF
     LCPFCRDDNF CAKVGVVIQN GKRRLALVNE NPLDVLFQEV