ID   KTI1_ARATH              Reviewed;         209 AA.
AC   Q39091;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Kunitz trypsin inhibitor 1 {ECO:0000303|PubMed:30042779};
DE            Short=AtKTI1 {ECO:0000303|PubMed:30042779};
DE   AltName: Full=Protein DROUGHT-REPRESSED 4 {ECO:0000303|PubMed:7823904};
DE            Short=AtDR4 {ECO:0000303|PubMed:7823904};
DE   Flags: Precursor;
GN   Name=KTI1 {ECO:0000303|PubMed:30042779};
GN   Synonyms=DR4 {ECO:0000303|PubMed:7823904};
GN   OrderedLocusNames=At1g73330 {ECO:0000312|Araport:AT1G73330};
GN   ORFNames=T9L24.45 {ECO:0000312|EMBL:AAG30985.1};
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 [MRNA], AND INDUCTION.
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=7823904; DOI=10.1007/bf00290128;
RA   Gosti F., Bertauche N., Vartanian N., Giraudat J.;
RT   "Abscisic acid-dependent and -independent regulation of gene expression by
RT   progressive drought in Arabidopsis thaliana.";
RL   Mol. Gen. Genet. 246:10-18(1995).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   INDUCTION BY SPIDER MITES, 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   -!- INDUCTION: Induced by infestation with spider mites (PubMed:30042779).
CC       Down-regulated in roots in response to drought stress (PubMed:7823904).
CC       {ECO:0000269|PubMed:30042779, ECO:0000269|PubMed:7823904}.
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; X78586; CAA55323.1; -; mRNA.
DR   EMBL; AC012396; AAG30985.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35444.1; -; Genomic_DNA.
DR   EMBL; AF370184; AAK43999.1; -; mRNA.
DR   EMBL; AY059142; AAL15248.1; -; mRNA.
DR   PIR; S51480; S51480.
DR   RefSeq; NP_177476.1; NM_105993.3.
DR   AlphaFoldDB; Q39091; -.
DR   SMR; Q39091; -.
DR   STRING; 3702.AT1G73330.1; -.
DR   MEROPS; I03.015; -.
DR   iPTMnet; Q39091; -.
DR   PaxDb; Q39091; -.
DR   PRIDE; Q39091; -.
DR   ProteomicsDB; 187765; -.
DR   EnsemblPlants; AT1G73330.1; AT1G73330.1; AT1G73330.
DR   GeneID; 843668; -.
DR   Gramene; AT1G73330.1; AT1G73330.1; AT1G73330.
DR   KEGG; ath:AT1G73330; -.
DR   Araport; AT1G73330; -.
DR   TAIR; locus:2206905; AT1G73330.
DR   HOGENOM; CLU_090145_1_1_1; -.
DR   OMA; EICPLDI; -.
DR   OrthoDB; 1266966at2759; -.
DR   PhylomeDB; Q39091; -.
DR   PRO; PR:Q39091; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q39091; baseline and differential.
DR   GO; GO:0030414; F:peptidase inhibitor activity; ISS:TAIR.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009414; P:response to water deprivation; 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   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; SSF50386; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..209
FT                   /note="Kunitz trypsin inhibitor 1"
FT                   /id="PRO_5014309041"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        63..107
FT                   /evidence="ECO:0000250|UniProtKB:P01070"
FT   DISULFID        154..162
FT                   /evidence="ECO:0000250|UniProtKB:P01070"
SQ   SEQUENCE   209 AA;  23113 MW;  77F06364730FDBCF CRC64;
     MKATISITTI FLVVALAAPS LARPDNHVED SVGRLLRPGQ TYHIVPANPE TGGGIFSNSE
     EICPLDIFQS NNPLDLGLPI KFKSELWFVK EMNSITIEFE APNWFLCPKE SKGWRVVYSE
     EFKKSLIIST GGSSNPSGFQ IHRVDGGAYK IVYCTNISTT TCMNVGIFTD ISGARRLALT
     SDEALLVKFQ KAATPKADLK TKLRMFPFY