ID   API2_SOLTU              Reviewed;         220 AA.
AC   Q43646;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Aspartic protease inhibitor 2;
DE   AltName: Full=CathIhn;
DE   AltName: Full=Cathepsin D inhibitor;
DE            Short=CathDinh;
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 [GENOMIC DNA].
RC   STRAIN=cv. AM 80.5793; TISSUE=Leaf;
RX   PubMed=7948907; DOI=10.1007/bf00039521;
RA   Herbers K., Prat S., Willmitzer L.;
RT   "Cloning and characterization of a cathepsin D inhibitor gene from Solanum
RT   tuberosum L.";
RL   Plant Mol. Biol. 26:73-83(1994).
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   -!- TISSUE SPECIFICITY: Tubers.
CC   -!- INDUCTION: Not induced by abscisic acid, jasmonic acid and wounding.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   EMBL; X74985; CAA52919.1; -; Genomic_DNA.
DR   PIR; S52656; S52656.
DR   AlphaFoldDB; Q43646; -.
DR   SMR; Q43646; -.
DR   MEROPS; I03.002; -.
DR   PRIDE; Q43646; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43646; 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   2: Evidence at transcript level;
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_0000016912"
FT   CHAIN           33..220
FT                   /note="Aspartic protease inhibitor 2"
FT                   /id="PRO_0000016913"
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            144..145
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;  24199 MW;  33D6E866EA0C5DD5 CRC64;
     MMKCLFLLCL CLLPIVVFSS TFTSQNLIDL PSESPLPKPV LDTNGKELNP NSSYRIISIG
     RGALGGDVYL GKSPNSDGPC PDGVFRYNSD VGPSGTFVRF IPLSGGIFED QLLNIQFNIA
     TVKLCVSYTI WKVGNLNAYF RTMLLETGGT IGQADSSYFK IVKLSNFGYN LLYCPITPPF
     LCPFCRDDNF CAKVGVVIQN GKRRLALVNE NPLDVLFQEV