KTI2_ARATH
ID KTI2_ARATH Reviewed; 215 AA.
AC Q9C7S6;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kunitz trypsin inhibitor 2 {ECO:0000303|PubMed:30042779};
DE Short=AtKTI2 {ECO:0000303|PubMed:30042779};
DE AltName: Full=Cysteine protease inhibitor WSCP {ECO:0000305};
DE AltName: Full=Kunitz-type cysteine protease inhibitor WSCP {ECO:0000305};
DE AltName: Full=Water-soluble chlorophyll protein {ECO:0000303|PubMed:26016527};
DE Short=AtWSCP {ECO:0000303|PubMed:26016527};
DE Flags: Precursor;
GN Name=KTI2 {ECO:0000303|PubMed:30042779};
GN Synonyms=WSCP {ECO:0000303|PubMed:26016527};
GN OrderedLocusNames=At1g72290 {ECO:0000312|Araport:AT1G72290};
GN ORFNames=T9N14.19 {ECO:0000312|EMBL:AAG51801.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=11577184; DOI=10.1093/pcp/pce117;
RA Satoh H., Uchida A., Nakayama K., Okada M.;
RT "Water-soluble chlorophyll protein in Brassicaceae plants is a stress-
RT induced chlorophyll-binding protein.";
RL Plant Cell Physiol. 42:906-911(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=26289422; DOI=10.1186/s13104-015-1333-3;
RA Takahashi S., Aizawa K., Nakayama K., Satoh H.;
RT "Water-soluble chlorophyll-binding proteins from Arabidopsis thaliana and
RT Raphanus sativus target the endoplasmic reticulum body.";
RL BMC Res. Notes 8:365-365(2015).
RN [7]
RP FUNCTION, INTERACTION WITH RD21A; RD21B AND RD21C, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26160583; DOI=10.1093/jxb/erv327;
RA Boex-Fontvieille E., Rustgi S., Reinbothe S., Reinbothe C.;
RT "A Kunitz-type protease inhibitor regulates programmed cell death during
RT flower development in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:6119-6135(2015).
RN [8]
RP FUNCTION, INTERACTION WITH RD21A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26016527; DOI=10.1073/pnas.1507714112;
RA Boex-Fontvieille E., Rustgi S., von Wettstein D., Reinbothe S.,
RA Reinbothe C.;
RT "Water-soluble chlorophyll protein is involved in herbivore resistance
RT activation during greening of Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7303-7308(2015).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=30042779; DOI=10.3389/fpls.2018.00986;
RA Arnaiz A., Talavera-Mateo L., Gonzalez-Melendi P., Martinez M., Diaz I.,
RA Santamaria M.E.;
RT "Arabidopsis Kunitz trypsin inhibitors in defense against spider mites.";
RL Front. Plant Sci. 9:986-986(2018).
CC -!- FUNCTION: Water-soluble and chlorophyll-binding protein that probably
CC does not function as a chloroplast chlorophyll carrier and is not
CC involved in photosynthesis (PubMed:11577184, PubMed:26160583). Involved
CC in the control of cell death in the transmitting tract and septum
CC epidermis during flower development. Binds and inhibits the activity of
CC the cysteine protease RD21A as a pro-death protein (PubMed:26160583).
CC May play a role in herbivore resistance activation during seedling
CC greening (PubMed:26016527). {ECO:0000269|PubMed:11577184,
CC ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}.
CC -!- SUBUNIT: Interacts with RD21A (PubMed:26160583, PubMed:26016527).
CC Interacts with RD21B and RD21C (PubMed:26160583).
CC {ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:26016527,
CC ECO:0000269|PubMed:26160583}. Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:26289422}. Note=Targeted to ER bodies.
CC {ECO:0000269|PubMed:26289422}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular bundles of the carpels, the
CC transmitting tract of the style and septum epidermis (PubMed:26160583).
CC Expressed in etiolated seedlings (PubMed:26016527).
CC {ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}.
CC -!- DEVELOPMENTAL STAGE: During flower development, expressed in the
CC transmitting tract of the septum from stage 12 to stage 15.
CC {ECO:0000269|PubMed:26160583}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:26016527}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; AC067754; AAG51801.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35299.1; -; Genomic_DNA.
DR EMBL; AY084376; AAM60956.1; -; mRNA.
DR EMBL; BT025277; ABF19030.1; -; mRNA.
DR PIR; F96746; F96746.
DR RefSeq; NP_177373.1; NM_105888.2.
DR AlphaFoldDB; Q9C7S6; -.
DR SMR; Q9C7S6; -.
DR STRING; 3702.AT1G72290.1; -.
DR MEROPS; I03.028; -.
DR PaxDb; Q9C7S6; -.
DR PRIDE; Q9C7S6; -.
DR ProteomicsDB; 243082; -.
DR EnsemblPlants; AT1G72290.1; AT1G72290.1; AT1G72290.
DR GeneID; 843561; -.
DR Gramene; AT1G72290.1; AT1G72290.1; AT1G72290.
DR KEGG; ath:AT1G72290; -.
DR Araport; AT1G72290; -.
DR TAIR; locus:2207041; AT1G72290.
DR HOGENOM; CLU_075927_0_0_1; -.
DR InParanoid; Q9C7S6; -.
DR OMA; PFVGTDY; -.
DR OrthoDB; 1208843at2759; -.
DR PhylomeDB; Q9C7S6; -.
DR PRO; PR:Q9C7S6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7S6; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:TAIR.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; IMP:UniProtKB.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Plant defense; Protease inhibitor; Reference proteome; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..215
FT /note="Kunitz trypsin inhibitor 2"
FT /id="PRO_5006751521"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 67..114
FT /evidence="ECO:0000250|UniProtKB:P01070"
SQ SEQUENCE 215 AA; 23096 MW; 08D4C25BB3407D97 CRC64;
MKNPSVISFL IILLFAATIC THGNEPVKDT AGNPLNTREQ YFIQPVKTES KNGGGLVPAA
ITVLPFCPLG ITQTLLPYQP GLPVSFVLAL GVGSTVMTSS AVNIEFKSNI WPFCKEFSKF
WEVDDSSSAP KEPSILIGGK MGDRNSSFKI EKAGEGARAN VYKLTTFYGT VGAIPGVWLS
APQLIITKDT AKTLLVKFKK VDDATTATSN LYFPG
