API7_SOLTU
ID API7_SOLTU Reviewed; 221 AA.
AC Q41448;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aspartic protease inhibitor 7;
DE AltName: Full=Cathepsin D inhibitor p749;
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 TISSUE=Tuber;
RX PubMed=8278518; DOI=10.1104/pp.101.2.703;
RA Hannapel D.J.;
RT "Nucleotide and deduced amino acid sequence of the 22-kilodalton cathepsin
RT D inhibitor protein of potato (Solanum tuberosum L.).";
RL Plant Physiol. 101:703-704(1993).
RN [2]
RP INDUCTION.
RA Suh S.-C., Stiekema W.J., Hannapel D.J.;
RT "Proteinase-inhibitor activity and wound-inducible gene expression of the
RT 22-kDa potato-tuber proteins.";
RL Planta 184:423-430(1991).
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 -!- TISSUE SPECIFICITY: Tubers, leaves.
CC -!- INDUCTION: By wounding. Also expressed in upper non-wounded systemic
CC leaves. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; M96257; AAA18564.1; -; mRNA.
DR PIR; JQ2246; JQ2246.
DR RefSeq; NP_001275020.1; NM_001288091.1.
DR AlphaFoldDB; Q41448; -.
DR SMR; Q41448; -.
DR MEROPS; I03.002; -.
DR PRIDE; Q41448; -.
DR GeneID; 102577754; -.
DR KEGG; sot:102577754; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q41448; 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 2: Evidence at transcript level;
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_0000016918"
FT CHAIN 33..221
FT /note="Aspartic protease inhibitor 7"
FT /id="PRO_0000016919"
FT MOTIF 26..31
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000250"
FT SITE 99..100
FT /note="Reactive bond for trypsin"
FT SITE 144..145
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..126
FT /evidence="ECO:0000250"
FT DISULFID 175..186
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24485 MW; EE63685B8E09F295 CRC64;
MMKCLFLLCL CLFPILVFSS TFTSQNPINL PSESPVPKRV LDTNGKKLNP NSSYRIISTF
WGALGGDVYL GKSPNSDAPC PDGVFRYNSD VGPSGTPVRF IPLSGANIFE DQLLNIQFNI
PTVKLCGSYT IWKVGNINAH LRTMLLETGG TIGQADSSYF KIVKSSKFGY NLLYCPLTRH
FLCPFCRDDN FCAKVGVVIQ NGKRRLALVN ENPLDVLFQE V