KTI7_ARATH
ID KTI7_ARATH Reviewed; 202 AA.
AC Q9M8Y9;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kunitz trypsin inhibitor 7 {ECO:0000303|PubMed:30042779};
DE Short=AtKTI7 {ECO:0000303|PubMed:30042779};
DE Flags: Precursor;
GN Name=KTI7 {ECO:0000303|PubMed:30042779};
GN OrderedLocusNames=At3g04330 {ECO:0000312|Araport:AT3G04330};
GN ORFNames=T6K12.5 {ECO:0000312|EMBL:AAF26781.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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: Exhibits Kunitz trypsin protease inhibitor activity.
CC {ECO:0000250|UniProtKB:Q8RXD5}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC016829; AAF26781.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74067.1; -; Genomic_DNA.
DR RefSeq; NP_187083.1; NM_111304.2.
DR AlphaFoldDB; Q9M8Y9; -.
DR SMR; Q9M8Y9; -.
DR MEROPS; I03.017; -.
DR PaxDb; Q9M8Y9; -.
DR PRIDE; Q9M8Y9; -.
DR EnsemblPlants; AT3G04330.1; AT3G04330.1; AT3G04330.
DR GeneID; 819588; -.
DR Gramene; AT3G04330.1; AT3G04330.1; AT3G04330.
DR KEGG; ath:AT3G04330; -.
DR Araport; AT3G04330; -.
DR TAIR; locus:2103070; AT3G04330.
DR HOGENOM; CLU_1350546_0_0_1; -.
DR InParanoid; Q9M8Y9; -.
DR OMA; EMEVLFY; -.
DR OrthoDB; 1420434at2759; -.
DR PhylomeDB; Q9M8Y9; -.
DR PRO; PR:Q9M8Y9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8Y9; baseline and differential.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..202
FT /note="Kunitz trypsin inhibitor 7"
FT /id="PRO_5015099902"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 69..115
FT /evidence="ECO:0000250|UniProtKB:P01070"
SQ SEQUENCE 202 AA; 22914 MW; 485A2C8472CD3792 CRC64;
MKTFRSMLIS LLLVAITTTS GVVEGNYVVY DGEGDQVKPN VPYYISFMTS DYNMWICRKK
WRSNDPNSCP QQPLMVTHPN MAAPTPVMFV LSNKSETVVR ESAKLKIKFV DPRPCGESGF
WRVVQRTSSE GEVVLNGSES TSDNASTFAI EQTNEYYKFT FGDGPDYLTT ISLSNDYPIY
RLLSKKFSGE MEIYFYKNLT MG
