KTI5_ARATH
ID KTI5_ARATH Reviewed; 196 AA.
AC Q9LMU2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Kunitz trypsin inhibitor 5 {ECO:0000303|PubMed:30042779};
DE Short=AtKTI5 {ECO:0000303|PubMed:30042779};
DE AltName: Full=Kunitz trypsin inhibitor 2 {ECO:0000305};
DE Short=AtKTI2 {ECO:0000305};
DE Flags: Precursor;
GN Name=KTI5 {ECO:0000303|PubMed:30042779}; Synonyms=KTI2 {ECO:0000305};
GN OrderedLocusNames=At1g17860 {ECO:0000312|Araport:AT1G17860};
GN ORFNames=F2H15.9 {ECO:0000312|EMBL:AAF97266.1};
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].
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 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: Can inhibit both serine proteases and cysteine proteases
CC (PubMed:30042779). May be involved in the modulation of the proteases
CC that participate in the hydrolysis of dietary proteins in the gut of
CC spider mites (PubMed:30042779). {ECO:0000269|PubMed:30042779}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:30042779}.
CC -!- INDUCTION: Induced by infestation with spider mites.
CC {ECO:0000269|PubMed:30042779}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; AC034106; AAF97266.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29645.1; -; Genomic_DNA.
DR EMBL; AF332416; AAG48779.1; -; mRNA.
DR EMBL; AF370535; AAK48962.1; -; mRNA.
DR EMBL; AF410274; AAK95260.1; -; mRNA.
DR EMBL; AY081529; AAM10091.1; -; mRNA.
DR EMBL; AY097369; AAM19885.1; -; mRNA.
DR PIR; G86313; G86313.
DR RefSeq; NP_173228.1; NM_101649.2.
DR AlphaFoldDB; Q9LMU2; -.
DR SMR; Q9LMU2; -.
DR IntAct; Q9LMU2; 2.
DR STRING; 3702.AT1G17860.1; -.
DR MEROPS; I03.030; -.
DR PaxDb; Q9LMU2; -.
DR PRIDE; Q9LMU2; -.
DR ProteomicsDB; 237035; -.
DR EnsemblPlants; AT1G17860.1; AT1G17860.1; AT1G17860.
DR GeneID; 838365; -.
DR Gramene; AT1G17860.1; AT1G17860.1; AT1G17860.
DR KEGG; ath:AT1G17860; -.
DR Araport; AT1G17860; -.
DR TAIR; locus:2030923; AT1G17860.
DR eggNOG; ENOG502QWSQ; Eukaryota.
DR HOGENOM; CLU_090145_1_0_1; -.
DR InParanoid; Q9LMU2; -.
DR OMA; CDICRVM; -.
DR OrthoDB; 1343928at2759; -.
DR PhylomeDB; Q9LMU2; -.
DR PRO; PR:Q9LMU2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMU2; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0009625; P:response to insect; IMP: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.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Plant defense; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..196
FT /note="Kunitz trypsin inhibitor 5"
FT /id="PRO_5007717122"
FT DISULFID 156..167
FT /evidence="ECO:0000250|UniProtKB:P01070"
SQ SEQUENCE 196 AA; 22082 MW; A047EFBF70DE583E CRC64;
MSSLLYIFLL LAVFISHRGV TTEAAVEPVK DINGKSLLTG VNYYILPVIR GRGGGLTMSN
LKTETCPTSV IQDQFEVSQG LPVKFSPYDK SRTIPVSTDV NIKFSPTSIW ELANFDETTK
QWFISTCGVE GNPGQKTVDN WFKIDKFEKD YKIRFCPTVC NFCKVICRDV GVFVQDGKRR
LALSDVPLKV MFKRAY
