ID   API3_SOLTU              Reviewed;         169 AA.
AC   P58518;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Aspartic protease inhibitor 3;
DE            Short=API-3;
DE   Flags: Fragment;
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. Desiree;
RX   PubMed=9055446; DOI=10.1016/s0031-9422(96)00668-1;
RA   Kreft S., Ravnikar M., Mesko P., Pungercar J., Umek A., Kregar I.,
RA   Strukelj B.;
RT   "Jasmonic acid inducible aspartic proteinase inhibitors from potato.";
RL   Phytochemistry 44:1001-1006(1997).
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   -!- INDUCTION: By jasmonate.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P58518; -.
DR   SMR; P58518; -.
DR   ProMEX; P58518; -.
DR   EnsemblPlants; RHC03H1G1796.2.1; RHC03H1G1796.2.1.cds.1; RHC03H1G1796.2.
DR   Gramene; RHC03H1G1796.2.1; RHC03H1G1796.2.1.cds.1; RHC03H1G1796.2.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P58518; baseline and differential.
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.
PE   2: Evidence at transcript level;
KW   Aspartic protease inhibitor; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor; Vacuole.
FT   CHAIN           <1..169
FT                   /note="Aspartic protease inhibitor 3"
FT                   /id="PRO_0000083310"
FT   SITE            49..50
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            93..94
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        1
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..134
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   169 AA;  18578 MW;  96B1765DFF7483D0 CRC64;
     NSSYRIISIG RGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSTNIFED
     QLLNIQFNIP TVKLCVSYTI WKVGNLNAYF RTMLLETGGT IGQADNSYFK IVKSSKIGYN
     LLSCPFTSII CLRCPEDQFC AKVGVVIQNG KRRLALVNEN PLDVLFQEV