ID   API11_SOLTU             Reviewed;         188 AA.
AC   P16348;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Aspartic protease inhibitor 11;
DE   AltName: Full=Cathepsin D inhibitor PDI;
DE   AltName: Allergen=Sola t 2;
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.
RX   PubMed=2753167; DOI=10.1016/0014-5793(89)81435-8;
RA   Mares M., Meloun B., Pavlik M., Kostka V., Baudys M.;
RT   "Primary structure of cathepsin D inhibitor from potatoes and its structure
RT   relationship to soybean trypsin inhibitor family.";
RL   FEBS Lett. 251:94-98(1989).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS), GLYCOSYLATION AT ASN-19, AND
RP   DISULFIDE BONDS.
RX   PubMed=26542926; DOI=10.1016/j.jsb.2015.10.020;
RA   Guo J., Erskine P.T., Coker A.R., Wood S.P., Cooper J.B.;
RT   "Structure of a Kunitz-type potato cathepsin D inhibitor.";
RL   J. Struct. Biol. 192:554-560(2015).
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   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   PIR; S05025; XKPODC.
DR   PDB; 5DZU; X-ray; 2.12 A; A/B=1-188.
DR   PDBsum; 5DZU; -.
DR   AlphaFoldDB; P16348; -.
DR   SMR; P16348; -.
DR   Allergome; 3491; Sola t 2.0101.
DR   Allergome; 640; Sola t 2.
DR   iPTMnet; P16348; -.
DR   PRIDE; P16348; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P16348; 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   3D-structure; Allergen; Aspartic protease inhibitor;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor; Vacuole.
FT   CHAIN           1..188
FT                   /note="Aspartic protease inhibitor 11"
FT                   /id="PRO_0000083313"
FT   SITE            67..68
FT                   /note="Reactive bond for trypsin"
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|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:26542926, ECO:0000269|PubMed:2753167,
FT                   ECO:0007744|PDB:5DZU"
FT   DISULFID        48..93
FT                   /evidence="ECO:0000269|PubMed:26542926,
FT                   ECO:0007744|PDB:5DZU"
FT   DISULFID        142..159
FT                   /evidence="ECO:0000269|PubMed:26542926,
FT                   ECO:0007744|PDB:5DZU"
FT   DISULFID        150..153
FT                   /evidence="ECO:0000269|PubMed:26542926,
FT                   ECO:0007744|PDB:5DZU"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          66..74
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   HELIX           91..97
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          133..141
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          160..167
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          170..178
FT                   /evidence="ECO:0007829|PDB:5DZU"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:5DZU"
SQ   SEQUENCE   188 AA;  20590 MW;  4E8A49113EF6F10D CRC64;
     ESPLPKPVLD TNGKELNPNS SYRIISIGRG ALGGDVYLGK SPNSDAPCPD GVFRYNSDVG
     PSGTPVRFIP LSGGIFEDQL LNIQFNIATV KLCVSYTIWK VGNLNAYFRT MLLETGGTIG
     QADSSYFKIV KLSNFGYNLL YCPITPPFLC PFCRDDNFCA KVGVVIQNGK RRLALVNENP
     LDVLFQEV