KTI6_ARATH
ID KTI6_ARATH Reviewed; 203 AA.
AC Q0WNE5; A0A178VKP9; A0A1I9LR55; Q7Y212; Q9M8Y8;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Kunitz trypsin inhibitor 6 {ECO:0000303|PubMed:30042779};
DE Short=AtKTI6 {ECO:0000303|PubMed:30042779};
DE Flags: Precursor;
GN Name=KTI6 {ECO:0000303|PubMed:30042779};
GN OrderedLocusNames=At3g04320 {ECO:0000312|Araport:AT3G04320};
GN ORFNames=T6K12.6 {ECO:0000312|EMBL:AAF26782.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF26782.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP40451.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ANM65063.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC016829; AAF26782.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74066.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65063.1; ALT_INIT; Genomic_DNA.
DR EMBL; BT008630; AAP40451.1; ALT_INIT; mRNA.
DR EMBL; AK229498; BAF01355.1; -; mRNA.
DR RefSeq; NP_001327060.1; NM_001337512.1.
DR RefSeq; NP_187082.2; NM_111303.6.
DR AlphaFoldDB; Q0WNE5; -.
DR SMR; Q0WNE5; -.
DR STRING; 3702.AT3G04320.1; -.
DR MEROPS; I03.017; -.
DR PaxDb; Q0WNE5; -.
DR PRIDE; Q0WNE5; -.
DR ProteomicsDB; 177106; -.
DR ProteomicsDB; 216404; -.
DR EnsemblPlants; AT3G04320.1; AT3G04320.1; AT3G04320.
DR GeneID; 819587; -.
DR Gramene; AT3G04320.1; AT3G04320.1; AT3G04320.
DR KEGG; ath:AT3G04320; -.
DR Araport; AT3G04320; -.
DR TAIR; locus:2103080; AT3G04320.
DR HOGENOM; CLU_1350546_0_0_1; -.
DR InParanoid; Q0WNE5; -.
DR OrthoDB; 1420434at2759; -.
DR PRO; PR:Q0WNE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WNE5; baseline and differential.
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 SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..203
FT /note="Kunitz trypsin inhibitor 6"
FT /id="PRO_5015097008"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
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 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 70..115
FT /evidence="ECO:0000250|UniProtKB:P01070"
SQ SEQUENCE 203 AA; 22932 MW; 561D42257ACA9F31 CRC64;
MKTFQLMMIS FLFVAITTTS GVVSEGNDVV YDGEGDPVKP NVPYYISFMT SDYNMWICRM
QYGSTDPNSC PQQPLMVTHP NLAAPTPVMF VLANKSDVVR ESAKLKIKFV GPRQCGKSGF
WKVVQRNSSE GEVFLNGSKS MSHNDSTFAI HKTNEYYKFT FGDGDYPTTI SMTNDYPIYR
LLSKRLSGEM EIYFYKNLTT SEG
