SPI1_SOLTU
ID SPI1_SOLTU Reviewed; 221 AA.
AC P58514; Q66LL1; Q8L5X2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine protease inhibitor 1;
DE AltName: Full=PSPI-21;
DE AltName: Full=PSPI-21-6.3;
DE Contains:
DE RecName: Full=Serine protease inhibitor 1 chain A;
DE Contains:
DE RecName: Full=Serine protease inhibitor 1 chain B;
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. Provita; TISSUE=Tuber;
RX PubMed=12783302; DOI=10.1007/s00438-003-0860-0;
RA Heibges A., Glaczinski H., Ballvora A., Salamini F., Gebhardt C.;
RT "Structural diversity and organization of three gene families for Kunitz-
RT type enzyme inhibitors from potato tubers (Solanum tuberosum L.).";
RL Mol. Genet. Genomics 269:526-534(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-221.
RC STRAIN=cv. Istrinskii;
RA Speransky A.S., Krinitsina A.A., Poltronieri P., Fasano L., Santino A.,
RA Valueva T.A., Shevelev A.B.;
RT "Kunitz-type proteinase inhibitor group B genes from Solanum tuberosum cv.
RT Istrinskii and Solanum brevidens.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 29-178 AND 185-221, MASS SPECTROMETRY, AND DISULFIDE
RP BONDS.
RC STRAIN=cv. Istrinskii;
RX PubMed=11209756; DOI=10.1515/bc.2000.149;
RA Valueva T.A., Revina T.A., Mosolov V.V., Mentele R.;
RT "Primary structure of potato Kunitz-type serine proteinase inhibitor.";
RL Biol. Chem. 381:1215-1221(2000).
RN [4]
RP PROTEIN SEQUENCE OF 29-53 AND 185-194.
RC STRAIN=cv. Istrinskii;
RX PubMed=9598993; DOI=10.1016/s0014-5793(98)00321-4;
RA Valueva T.A., Revina T.A., Kladnitskaya G.V., Mosolov V.V.;
RT "Kunitz-type proteinase inhibitors from intact and Phytophthora-infected
RT potato tubers.";
RL FEBS Lett. 426:131-134(1998).
CC -!- FUNCTION: Potent inhibitor of serine proteases (chymotrypsin and
CC trypsin). Inhibits tightly human leukocyte elastase (HLE). Does not
CC inhibit papain, pepsin nor cathepsin D (cysteine and aspartic
CC proteases). Protects the plant by inhibiting proteases of invading
CC organisms, decreasing both hyphal growth and zoospores germination of
CC Phytophthora infestans.
CC -!- SUBUNIT: Heterodimer of chains A and B; disulfide-linked. Double-headed
CC inhibitor able to form triple complexes with target proteases, by
CC binding simultaneously one molecule of trypsin and one molecule of
CC chymotrypsin. {ECO:0000269|PubMed:11209756}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Tubers.
CC -!- INDUCTION: By infection with Phytophthora infestans.
CC -!- PTM: Synthesized as a single-chain precursor which is cleaved to form
CC chain A and chain B.
CC -!- MASS SPECTROMETRY: Mass=20262; Mass_error=20; Method=Electrospray;
CC Note=The measured mass is that of the native protein composed of the 2
CC chains A and B. The measured ranges are 29-178, 185-221.;
CC Evidence={ECO:0000269|PubMed:11209756};
CC -!- MASS SPECTROMETRY: [Serine protease inhibitor 1 chain A]: Mass=16078;
CC Mass_error=16; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11209756};
CC -!- MASS SPECTROMETRY: [Serine protease inhibitor 1 chain B]: Mass=4282;
CC Mass_error=4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11209756};
CC -!- MISCELLANEOUS: The serine protease inhibitor PSPI-21 comprises two
CC protein species with pI 5.2 and 6.3, denoted as PSPI-21-5.2 and PSPI-
CC 21-6.3. They may be encoded by two alleles at the same gene locus.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; AF495585; AAM21646.1; -; mRNA.
DR EMBL; AY693424; AAU09272.1; -; mRNA.
DR AlphaFoldDB; P58514; -.
DR SMR; P58514; -.
DR MEROPS; I03.020; -.
DR PRIDE; P58514; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P58514; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor; Signal; Vacuole.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..28
FT /evidence="ECO:0000255"
FT /id="PRO_0000230276"
FT CHAIN 29..178
FT /note="Serine protease inhibitor 1 chain A"
FT /id="PRO_0000016899"
FT PROPEP 179..184
FT /note="Linker peptide"
FT /evidence="ECO:0000269|PubMed:11209756,
FT ECO:0000269|PubMed:9598993"
FT /id="PRO_0000230277"
FT CHAIN 185..221
FT /note="Serine protease inhibitor 1 chain B"
FT /id="PRO_0000016900"
FT MOTIF 25..30
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000250"
FT SITE 95..96
FT /note="Reactive bond for trypsin"
FT SITE 143..144
FT /note="Reactive bond for chymotrypsin or HLE"
FT DISULFID 76..125
FT /evidence="ECO:0000269|PubMed:11209756"
FT DISULFID 174..191
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000269|PubMed:11209756"
SQ SEQUENCE 221 AA; 24009 MW; 20FB0F00971290F9 CRC64;
MKCLFLVCLC LVPIVVFSST FTSQNPINLP SDATPVLDVT GKELDSRLSY RIISTFWGAL
GGDVYLGKSP NSDAPCANGV FRYNSDVGPS GTPVRFIGSS SHFGQGIFEN ELLNIQFAIS
TSKLCVSYTI WKVGDYDASL GTMLLETGGT IGQADSSWFK IVKSSQLGYN LLYCPVTSTM
SCPFSSDDQF CLKVGVVHQN GKRRLALVKD NPLDISFKQV Q
