SPI6_SOLTU
ID SPI6_SOLTU Reviewed; 221 AA.
AC Q41433;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable serine protease inhibitor 6;
DE AltName: Full=AM66;
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 [MRNA].
RC STRAIN=cv. Keszthelyi 855 (White lady); TISSUE=Etiolated shoot;
RX PubMed=8925888; DOI=10.1016/0014-5793(96)00234-7;
RA Banfalvi Z., Molnar A., Molnar G., Lakatos L., Szabo L.;
RT "Starch synthesis, and tuber storage protein genes are differently
RT expressed in Solanum tuberosum and in Solanum brevidens.";
RL FEBS Lett. 383:159-164(1996).
CC -!- FUNCTION: Inhibitor of trypsin (serine protease). May protect the plant
CC by inhibiting proteases of invading organisms (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- INDUCTION: By sucrose.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; U30814; AAC49602.1; -; mRNA.
DR PIR; S66277; S66277.
DR AlphaFoldDB; Q41433; -.
DR SMR; Q41433; -.
DR MEROPS; I03.020; -.
DR PRIDE; Q41433; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q41433; baseline.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PROPEP 23..28
FT /evidence="ECO:0000250"
FT /id="PRO_0000016906"
FT CHAIN 29..221
FT /note="Probable serine protease inhibitor 6"
FT /id="PRO_0000016907"
FT MOTIF 25..30
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000250"
FT SITE 95..96
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 DISULFID 76..125
FT /evidence="ECO:0000250"
FT DISULFID 174..191
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24097 MW; 98C6CE610D8A93D2 CRC64;
MKCLFLLCLC LFPIVVFSST FTSQNPINLP SDATPVLDVT GKELDPRLSY HIISTFWGAL
GGDVYLGKSP NSDAPCANGI FRYNSDVGPS GTPVRFIGSS SHFGQGIFEN ELLNIQFAIS
TSKLCVSYTI WKVGDYDASL GTMLLETGGT IGQADSSWFK IVQSSQFGYN LLYCPVTSTM
SCPFSSDDQF CLKVGVVHQN GKRRLALVKD NPLDVSFKQV Q