ID API5_SOLTU Reviewed; 220 AA.
AC P58519;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Aspartic protease inhibitor 5;
DE AltName: Full=PI-13;
DE AltName: Full=pi13;
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.
RC STRAIN=cv. Pentland squire; TISSUE=Tuber;
RX PubMed=1515078; DOI=10.1515/bchm3.1992.373.2.477;
RA Strukelj B., Pungercar J., Mesko P., Barlic-Maganja D., Gubensek F.,
RA Kregar I., Turk V.;
RT "Characterization of aspartic proteinase inhibitors from potato at the
RT gene, cDNA and protein levels.";
RL Biol. Chem. Hoppe-Seyler 373:477-482(1992).
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 -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR PIR; S24186; S24186.
DR AlphaFoldDB; P58519; -.
DR SMR; P58519; -.
DR STRING; 4113.P58519; -.
DR InParanoid; P58519; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P58519; 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 Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; KUNITZ TRYPSIN INHIBITOR 2; 1.
DR PANTHER; PTHR33107:SF38; SERINE PROTEASE INHIBITOR 5; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; STI-like; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 3: Inferred from homology;
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_0000016916"
FT CHAIN 33..220
FT /note="Aspartic protease inhibitor 5"
FT /id="PRO_0000016917"
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..185
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 24303 MW; 41D2D499139019E6 CRC64;
MMKCLFLLCL CLLPIVVFSS TFTSQNLIDL PSESPVPKPV LDTNGKELNP NSSYRIISIG
RGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSTNIFED QLLNIQFNIP
TVKLCVSYTI WKVGNLNAHL RTMLLETGGT IGQADSSYFK IVKSSKFGYN LLYCPITRHF
LCPFCRDDNF CAKVGVVIQN GKRRLALVNE NPLDVLFQEV
//
