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Kunitz trypsin inhibitor 1 (AtKTI1) (Trypsin protease inhibitor)

 KTI1_ARATH              Reviewed;         215 AA.
Q8RXD5; Q8H190; Q93Y29; Q9CAT9;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
10-OCT-2018, entry version 112.
RecName: Full=Kunitz trypsin inhibitor 1 {ECO:0000303|PubMed:19825555};
Short=AtKTI1 {ECO:0000303|PubMed:19825555};
AltName: Full=Trypsin protease inhibitor {ECO:0000303|PubMed:16236154};
Flags: Precursor;
Name=KTI1 {ECO:0000303|PubMed:19825555};
Synonyms=TPI {ECO:0000303|PubMed:16236154};
OrderedLocusNames=At1g73260 {ECO:0000312|Araport:AT1G73260};
ORFNames=T18K17.7 {ECO:0000312|EMBL:AAG52121.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
TISSUE SPECIFICITY, AND REGULATION BY NEMATODE.
PubMed=16236154; DOI=10.1111/j.1365-313X.2005.02532.x;
Jammes F., Lecomte P., de Almeida-Engler J., Bitton F.,
Martin-Magniette M.L., Renou J.P., Abad P., Favery B.;
"Genome-wide expression profiling of the host response to root-knot
nematode infection in Arabidopsis.";
Plant J. 44:447-458(2005).
[6]
INDUCTION BY PIERIS BRASSICAE OVIPOSITION.
PubMed=17142483; DOI=10.1104/pp.106.090837;
Little D., Gouhier-Darimont C., Bruessow F., Reymond P.;
"Oviposition by pierid butterflies triggers defense responses in
Arabidopsis.";
Plant Physiol. 143:784-800(2007).
[7]
FUNCTION, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, AND DISRUPTION
PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=19825555; DOI=10.1093/mp/ssn013;
Li J., Brader G., Palva E.T.;
"Kunitz trypsin inhibitor: an antagonist of cell death triggered by
phytopathogens and fumonisin b1 in Arabidopsis.";
Mol. Plant 1:482-495(2008).
-!- FUNCTION: Exhibits Kunitz trypsin protease inhibitor activity.
Involved in modulating programmed cell death (PCD) in plant-
pathogen interactions. {ECO:0000269|PubMed:19825555}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8RXD5-1; Sequence=Displayed;
Name=2;
IsoId=Q8RXD5-2; Sequence=VSP_058577;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:AAK96757.1};
-!- TISSUE SPECIFICITY: Expressed in roots.
{ECO:0000269|PubMed:16236154}.
-!- INDUCTION: Down-regulated after root-knot nematode infection
(PubMed:16236154). Accumulates locally within 72 hours after
P.brassicae butterflies oviposition (PubMed:17142483). Induced
late in response to bacterial and fungal elicitors (e.g. Pst
DC3000 and Ecc culture filtrates), and upon wounding, salicylic
acid (SA) and hydrogen peroxide H(2)O(2) treatments
(PubMed:19825555). {ECO:0000269|PubMed:16236154,
ECO:0000269|PubMed:17142483, ECO:0000269|PubMed:19825555}.
-!- DISRUPTION PHENOTYPE: Enhanced lesion development after
infiltration of leaf tissue with the programmed cell death (PCD)-
eliciting fungal toxin fumonisin B1 (FB1) or the avirulent
bacterial pathogen P.syringae pv. tomato DC3000 carrying avrB (Pst
avrB). Enhanced resistance to the virulent pathogen E.carotovora
subsp. carotovora SCC1. {ECO:0000269|PubMed:19825555}.
-!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous
Kunitz-type inhibitor) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG52121.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC010556; AAG52121.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE35435.1; -; Genomic_DNA.
EMBL; AY054566; AAK96757.1; -; mRNA.
EMBL; AY081323; AAL91212.1; -; mRNA.
EMBL; BT000366; AAN15685.1; -; mRNA.
EMBL; BT002548; AAO00908.1; -; mRNA.
EMBL; AK230302; BAF02103.1; -; mRNA.
PIR; G96758; G96758.
RefSeq; NP_565061.1; NM_105985.3. [Q8RXD5-1]
UniGene; At.21000; -.
ProteinModelPortal; Q8RXD5; -.
SMR; Q8RXD5; -.
IntAct; Q8RXD5; 1.
STRING; 3702.AT1G73260.1; -.
MEROPS; I03.031; -.
PaxDb; Q8RXD5; -.
PRIDE; Q8RXD5; -.
EnsemblPlants; AT1G73260.1; AT1G73260.1; AT1G73260. [Q8RXD5-1]
GeneID; 843660; -.
Gramene; AT1G73260.1; AT1G73260.1; AT1G73260. [Q8RXD5-1]
KEGG; ath:AT1G73260; -.
Araport; AT1G73260; -.
TAIR; locus:2197249; AT1G73260.
eggNOG; ENOG410IWBP; Eukaryota.
eggNOG; ENOG410YHN1; LUCA.
HOGENOM; HOG000006442; -.
InParanoid; Q8RXD5; -.
OMA; PCPYDIV; -.
OrthoDB; EOG09360O64; -.
PhylomeDB; Q8RXD5; -.
PRO; PR:Q8RXD5; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8RXD5; baseline and differential.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0012501; P:programmed cell death; IMP:TAIR.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
GO; GO:0009625; P:response to insect; IEP:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
GO; GO:0009624; P:response to nematode; IEP:UniProtKB.
GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
CDD; cd00178; STI; 1.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR002160; Prot_inh_Kunz-lg.
PANTHER; PTHR33107; PTHR33107; 1.
Pfam; PF00197; Kunitz_legume; 1.
PRINTS; PR00291; KUNITZINHBTR.
SMART; SM00452; STI; 1.
SUPFAM; SSF50386; SSF50386; 1.
PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
2: Evidence at transcript level;
Alternative splicing; Apoptosis; Complete proteome; Disulfide bond;
Glycoprotein; Plant defense; Protease inhibitor; Reference proteome;
Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 215 Kunitz trypsin inhibitor 1.
/FTId=PRO_5007714371.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 165 176 {ECO:0000250|UniProtKB:P01070}.
VAR_SEQ 200 215 VMFKKANVTEVSSKTM -> GYVQKS (in isoform
2).
/FTId=VSP_058577.
CONFLICT 128 128 K -> R (in Ref. 3; AAN15685/AAK96757).
{ECO:0000305}.
SEQUENCE 215 AA; 23793 MW; A3799CCA9B25322A CRC64;
MTKTTKTMNP KFYLVLALTA VLASNAYGAV VDIDGNAMFH ESYYVLPVIR GRGGGLTLAG
RGGQPCPYDI VQESSEVDEG IPVKFSNWRL KVAFVPESQN LNIETDVGAT ICIQSTYWRV
GEFDHERKQY FVVAGPKPEG FGQDSLKSFF KIEKSGEDAY KFVFCPRTCD SGNPKCSDVG
IFIDELGVRR LALSDKPFLV MFKKANVTEV SSKTM


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