SPI4_SOLTU
ID SPI4_SOLTU Reviewed; 103 AA.
AC P58517;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine protease inhibitor 4;
DE Short=PI-4;
DE Flags: Fragment;
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 serine protease. May protect the plant by
CC inhibiting proteases of invading organisms (By similarity).
CC {ECO:0000250}.
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; S24187; S24187.
DR AlphaFoldDB; P58517; -.
DR SMR; P58517; -.
DR PRIDE; P58517; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P58517; baseline.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Disulfide bond; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Vacuole.
FT CHAIN <1..103
FT /note="Serine protease inhibitor 4"
FT /id="PRO_0000016903"
FT SITE 25..26
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 56..73
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 103 AA; 11349 MW; D328692B166B21C4 CRC64;
ISTSKLCVSY TIWKVGDYDA SLGTMLLETG GTIGQADSSW FKIVQSSQFG YNLLYCPVTS
TMSCPFSLDD QFCLKVGVVH QNGKRRLALV NGNPLECLFK QVQ