ID   API9_SOLTU              Reviewed;         187 AA.
AC   P58521;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Aspartic protease inhibitor 9;
DE   AltName: Full=Novel inhibitor of cathepsin D;
DE            Short=NID;
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   PROTEIN SEQUENCE.
RC   TISSUE=Tuber;
RX   PubMed=2365079; DOI=10.1016/0014-5793(90)80275-n;
RA   Ritonja A., Krizaj I., Mesko P., Kopitar M., Lucovnik P., Strukelj B.,
RA   Pungercar J., Buttle D.J., Barrett A.J., Turk V.;
RT   "The amino acid sequence of a novel inhibitor of cathepsin D from potato.";
RL   FEBS Lett. 267:13-15(1990).
CC   -!- FUNCTION: Inhibitor of cathepsin D (aspartic protease) and trypsin
CC       (serine protease). May protect the plant by inhibiting proteases of
CC       invading organisms.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Tubers.
CC   -!- PTM: Glycosylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P58521; -.
DR   SMR; P58521; -.
DR   MEROPS; I03.002; -.
DR   PRIDE; P58521; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P58521; 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.
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; Vacuole.
FT   CHAIN           1..187
FT                   /note="Aspartic protease inhibitor 9"
FT                   /id="PRO_0000083312"
FT   SITE            67..68
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            111..112
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        142..158
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20368 MW;  D088A6EB241EDD29 CRC64;
     ESPLPKPVLD TNGKELNPNS SYRIISIGAG ALGGDVYLGK SPNSDAPCPD GVFRYNSDVG
     PSGTPVRFIP LSGGIFEDQL LNIQFNIPTV KLCVSYTIWK VGNLNAYFRT MLLETGGTIG
     QADNSYFKIV KLSNFGYNLL SCPFTSIICL RCPEDQFCAK VGVVIQNGKR RLALVNENPL
     DVLFQEV