ID   KTI4_ARATH              Reviewed;         215 AA.
AC   Q8RXD5; Q8H190; Q93Y29; Q9CAT9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Kunitz trypsin inhibitor 4 {ECO:0000303|PubMed:30042779};
DE            Short=AtKTI4 {ECO:0000303|PubMed:30042779};
DE   AltName: Full=Kunitz trypsin inhibitor 1 {ECO:0000303|PubMed:19825555};
DE            Short=AtKTI1 {ECO:0000303|PubMed:19825555};
DE   AltName: Full=Trypsin protease inhibitor {ECO:0000303|PubMed:16236154};
DE   Flags: Precursor;
GN   Name=KTI4 {ECO:0000303|PubMed:30042779};
GN   Synonyms=KTI1 {ECO:0000303|PubMed:19825555}, TPI
GN   {ECO:0000303|PubMed:16236154};
GN   OrderedLocusNames=At1g73260 {ECO:0000312|Araport:AT1G73260};
GN   ORFNames=T18K17.7 {ECO:0000312|EMBL:AAG52121.1};
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] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
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   TISSUE SPECIFICITY, AND REGULATION BY NEMATODE.
RX   PubMed=16236154; DOI=10.1111/j.1365-313x.2005.02532.x;
RA   Jammes F., Lecomte P., de Almeida-Engler J., Bitton F.,
RA   Martin-Magniette M.L., Renou J.P., Abad P., Favery B.;
RT   "Genome-wide expression profiling of the host response to root-knot
RT   nematode infection in Arabidopsis.";
RL   Plant J. 44:447-458(2005).
RN   [6]
RP   INDUCTION BY PIERIS BRASSICAE OVIPOSITION.
RX   PubMed=17142483; DOI=10.1104/pp.106.090837;
RA   Little D., Gouhier-Darimont C., Bruessow F., Reymond P.;
RT   "Oviposition by pierid butterflies triggers defense responses in
RT   Arabidopsis.";
RL   Plant Physiol. 143:784-800(2007).
RN   [7]
RP   FUNCTION, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=19825555; DOI=10.1093/mp/ssn013;
RA   Li J., Brader G., Palva E.T.;
RT   "Kunitz trypsin inhibitor: an antagonist of cell death triggered by
RT   phytopathogens and fumonisin b1 in Arabidopsis.";
RL   Mol. Plant 1:482-495(2008).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY SPIDER MITES, GENE FAMILY, AND
RP   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       (PubMed:19825555). Involved in modulating programmed cell death (PCD)
CC       in plant-pathogen interactions (PubMed:19825555). Can inhibit both
CC       serine proteases and cysteine proteases (PubMed:30042779). May be
CC       involved in the modulation of the proteases that participate in the
CC       hydrolysis of dietary proteins in the gut of spider mites
CC       (PubMed:30042779). {ECO:0000269|PubMed:19825555,
CC       ECO:0000269|PubMed:30042779}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:30042779}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8RXD5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8RXD5-2; Sequence=VSP_058577;
CC   -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:16236154}.
CC   -!- INDUCTION: Down-regulated after root-knot nematode infection
CC       (PubMed:16236154). Accumulates locally within 72 hours after
CC       P.brassicae butterflies oviposition (PubMed:17142483). Induced late in
CC       response to bacterial and fungal elicitors (e.g. Pst DC3000 and Ecc
CC       culture filtrates), and upon wounding, salicylic acid (SA) and hydrogen
CC       peroxide H(2)O(2) treatments (PubMed:19825555). Induced by infestation
CC       with spider mites (PubMed:30042779). {ECO:0000269|PubMed:16236154,
CC       ECO:0000269|PubMed:17142483, ECO:0000269|PubMed:19825555,
CC       ECO:0000269|PubMed:30042779}.
CC   -!- DISRUPTION PHENOTYPE: Enhanced lesion development after infiltration of
CC       leaf tissue with the programmed cell death (PCD)-eliciting fungal toxin
CC       fumonisin B1 (FB1) or the avirulent bacterial pathogen P.syringae pv.
CC       tomato DC3000 carrying avrB (Pst avrB). Enhanced resistance to the
CC       virulent pathogen E.carotovora subsp. carotovora SCC1.
CC       {ECO:0000269|PubMed:19825555}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52121.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC010556; AAG52121.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE35435.1; -; Genomic_DNA.
DR   EMBL; AY054566; AAK96757.1; -; mRNA.
DR   EMBL; AY081323; AAL91212.1; -; mRNA.
DR   EMBL; BT000366; AAN15685.1; -; mRNA.
DR   EMBL; BT002548; AAO00908.1; -; mRNA.
DR   EMBL; AK230302; BAF02103.1; -; mRNA.
DR   PIR; G96758; G96758.
DR   RefSeq; NP_565061.1; NM_105985.3. [Q8RXD5-1]
DR   AlphaFoldDB; Q8RXD5; -.
DR   SMR; Q8RXD5; -.
DR   IntAct; Q8RXD5; 1.
DR   STRING; 3702.Q8RXD5; -.
DR   MEROPS; I03.031; -.
DR   GlyCosmos; Q8RXD5; 1 site, No reported glycans.
DR   PaxDb; 3702-AT1G73260-1; -.
DR   ProteomicsDB; 237034; -. [Q8RXD5-1]
DR   EnsemblPlants; AT1G73260.1; AT1G73260.1; AT1G73260. [Q8RXD5-1]
DR   GeneID; 843660; -.
DR   Gramene; AT1G73260.1; AT1G73260.1; AT1G73260. [Q8RXD5-1]
DR   KEGG; ath:AT1G73260; -.
DR   Araport; AT1G73260; -.
DR   TAIR; AT1G73260; KTI1.
DR   eggNOG; ENOG502QWSQ; Eukaryota.
DR   HOGENOM; CLU_090145_1_0_1; -.
DR   InParanoid; Q8RXD5; -.
DR   OMA; PCPYDIV; -.
DR   OrthoDB; 1216061at2759; -.
DR   PhylomeDB; Q8RXD5; -.
DR   PRO; PR:Q8RXD5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8RXD5; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:TAIR.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR   GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR   GO; GO:0009624; P:response to nematode; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR   CDD; cd00178; STI; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   PANTHER; PTHR33107; KUNITZ TRYPSIN INHIBITOR 2; 1.
DR   PANTHER; PTHR33107:SF12; KUNITZ TRYPSIN INHIBITOR 4; 1.
DR   Pfam; PF00197; Kunitz_legume; 1.
DR   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; STI-like; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Plant defense; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..215
FT                   /note="Kunitz trypsin inhibitor 4"
FT                   /id="PRO_5007714371"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        66..112
FT                   /evidence="ECO:0000250|UniProtKB:P01070"
FT   DISULFID        165..176
FT                   /evidence="ECO:0000250|UniProtKB:P01070"
FT   VAR_SEQ         200..215
FT                   /note="VMFKKANVTEVSSKTM -> GYVQKS (in isoform 2)"
FT                   /id="VSP_058577"
FT   CONFLICT        128
FT                   /note="K -> R (in Ref. 3; AAN15685/AAK96757)"
FT                   /evidence="ECO:0000305"
SQ   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
//