IP22_SOLLC
ID IP22_SOLLC Reviewed; 223 AA.
AC Q43710;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Proteinase inhibitor type-2 TR8;
DE AltName: Full=Proteinase inhibitor type II TR8;
DE Flags: Precursor;
GN Name=ARPI;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. VFN8; TISSUE=Seedling root;
RX PubMed=7903168; DOI=10.1007/bf00021815;
RA Taylor B.H., Young R.J., Scheuring C.F.;
RT "Induction of a proteinase inhibitor II-class gene by auxin in tomato
RT roots.";
RL Plant Mol. Biol. 23:1005-1014(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. VFN8;
RX PubMed=8159801; DOI=10.1104/pp.104.2.811;
RA Young R.J., Scheuring C.F., Harris-Haller L., Taylor B.H.;
RT "An auxin-inducible proteinase inhibitor gene from tomato.";
RL Plant Physiol. 104:811-812(1994).
CC -!- INDUCTION: By auxin.
CC -!- SIMILARITY: Belongs to the protease inhibitor I20 (potato type II
CC proteinase inhibitor) family. {ECO:0000305}.
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DR EMBL; L21194; AAA16881.1; -; mRNA.
DR EMBL; L25128; AAC37397.1; -; Unassigned_DNA.
DR PIR; S43338; S43338.
DR RefSeq; NP_001234661.1; NM_001247732.1.
DR AlphaFoldDB; Q43710; -.
DR SMR; Q43710; -.
DR STRING; 4081.Solyc11g021060.1.1; -.
DR PaxDb; Q43710; -.
DR PRIDE; Q43710; -.
DR EnsemblPlants; Solyc11g021060.2.1; Solyc11g021060.2.1; Solyc11g021060.2.
DR GeneID; 543962; -.
DR Gramene; Solyc11g021060.2.1; Solyc11g021060.2.1; Solyc11g021060.2.
DR KEGG; sly:543962; -.
DR eggNOG; ENOG502SBHN; Eukaryota.
DR HOGENOM; CLU_118313_0_0_1; -.
DR InParanoid; Q43710; -.
DR OMA; TYICDGE; -.
DR OrthoDB; 941883at2759; -.
DR PhylomeDB; Q43710; -.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR003465; Prot_inh_I20.
DR Pfam; PF02428; Prot_inhib_II; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..223
FT /note="Proteinase inhibitor type-2 TR8"
FT /id="PRO_0000025311"
FT REPEAT 24..81
FT /note="1"
FT REPEAT 88..145
FT /note="2"
FT REPEAT 152..209
FT /note="3"
FT SITE 29..30
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000305"
FT SITE 93..94
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000305"
FT SITE 157..158
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000305"
FT DISULFID 27..120
FT /evidence="ECO:0000250"
FT DISULFID 31..116
FT /evidence="ECO:0000250"
FT DISULFID 40..126
FT /evidence="ECO:0000250"
FT DISULFID 52..95
FT /evidence="ECO:0000250"
FT DISULFID 55..73
FT /evidence="ECO:0000250"
FT DISULFID 56..91
FT /evidence="ECO:0000250"
FT DISULFID 62..104
FT /evidence="ECO:0000250"
FT DISULFID 119..137
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 24697 MW; 8F6173C4BE536F9E CRC64;
MAIYKVALLL LFGMILLASD FEHAKACTKE CDTRIDFGIC PLLETKRVEG LCTNCCAGKK
GCKYFSKDGT YICDGESEWV SEKNNNLKKA CTKECDTRID FGICPLLETK RVEGLCTNCC
AGKKGCKYFS KDGTYICDGE SEWVSEKDNN LEKDCTKECD TRIDFGICPL LETKRVKGLC
TNCCAGKKGC KYFSADGTYI CDGESEWVSE GENDLQKSNV AIS
