ID   API10_SOLTU             Reviewed;         219 AA.
AC   Q03197;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Aspartic protease inhibitor 10;
DE   AltName: Full=Wound-induced aspartate proteinase CDI inhibitor;
DE   Flags: Precursor;
GN   Name=CDI;
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 [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=1392612; DOI=10.2307/3869484;
RA   Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J.,
RA   Willmitzer L., Prat S.;
RT   "General roles of abscisic and jasmonic acids in gene activation as a
RT   result of mechanical wounding.";
RL   Plant Cell 4:1157-1170(1992).
CC   -!- FUNCTION: Inhibitor of cathepsin D (aspartic protease) and trypsin
CC       (serine protease). Protects the plant by inhibiting proteases of
CC       invading organisms.
CC   -!- TISSUE SPECIFICITY: In tubers and green buds of untreated plants. After
CC       abscisic acid treatment or mechanical wounding is mostly accumulated in
CC       leaves, to a lesser extent in stems, but not in roots.
CC   -!- INDUCTION: By abscisic acid (ABA), jasmonic acid (JA) and wounding.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   EMBL; X67843; CAA48036.1; -; mRNA.
DR   PIR; JQ1692; JQ1692.
DR   AlphaFoldDB; Q03197; -.
DR   SMR; Q03197; -.
DR   MEROPS; I03.002; -.
DR   PRIDE; Q03197; -.
DR   InParanoid; Q03197; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q03197; baseline.
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   Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PROPEP          24..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016922"
FT   CHAIN           33..219
FT                   /note="Aspartic protease inhibitor 10"
FT                   /id="PRO_0000016923"
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            142..143
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        173..184
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  24035 MW;  8A585CB3E5A09FB5 CRC64;
     MMKCLFLLCL CLVPIVVFSS TFTSQNLIDL PSESPLPKPV LDTNGKELNP NSSYRIISIG
     RGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSGGIFED QLLNIQFNIP
     TVRLCVSYTI WKVGINAYLR TMLLETGGTI GQADSSYFKI VKSSILGYNL LYCPITRPIL
     CPFCRDDDFC AKVGVVIQKG KRRLALVNEN PLDVNFKEV