ID   API1_SOLTU              Reviewed;         221 AA.
AC   Q41480; Q41483;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Aspartic protease inhibitor 1;
DE            Short=pA1;
DE   AltName: Full=STPIA;
DE   AltName: Full=STPID;
DE   AltName: Full=gCDI-A1;
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 / MRNA], AND PROTEIN SEQUENCE OF 33-42.
RC   STRAIN=cv. Danshaku;
RX   PubMed=8069493;
RA   Ishikawa A., Ohta S., Matsuoka K., Hattori T., Nakamura K.;
RT   "A family of potato genes that encode Kunitz-type proteinase inhibitors:
RT   structural comparisons and differential expression.";
RL   Plant Cell Physiol. 35:303-312(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, young leaves and flower bud. Not detected
CC       in root, stem or mature leaves.
CC   -!- INDUCTION: By methyl jasmonate and wounding; but not by sucrose.
CC   -!- MISCELLANEOUS: Has a single chain structure.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   EMBL; D17328; BAA04148.1; -; mRNA.
DR   EMBL; D17331; BAA04151.1; -; Genomic_DNA.
DR   PIR; T07411; T07411.
DR   PIR; T07413; T07413.
DR   AlphaFoldDB; Q41480; -.
DR   SMR; Q41480; -.
DR   MEROPS; I03.002; -.
DR   PRIDE; Q41480; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41480; 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   1: Evidence at protein level;
KW   Aspartic protease inhibitor; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor; Signal; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PROPEP          24..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016910"
FT   CHAIN           33..221
FT                   /note="Aspartic protease inhibitor 1"
FT                   /id="PRO_0000016911"
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..186
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  24546 MW;  D8EE8290F6E29199 CRC64;
     MMKCLFFLCL CLFPILVFSS TFTSQNPINL PSESPVPKPV LDTNGKKLNP NSSYRIISTF
     WGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSTNIFED QLLNIQFNIP
     TVKLCVSYTI WKVGNLNTHL WTMLLETGGT IGKADSSYFK IVKSSKFGYN LLYCPITRPP
     IVCPFCRDDD FCAKVGVVIQ NGKRRLALVN ENPLDVLFQE V