ESP_ARATH
ID ESP_ARATH Reviewed; 341 AA.
AC Q8RY71; B0LYN4; B0LYN5; B0LYN6; B0LYN7; B0LYN8; B0LYP0; B0LYP2; B0LYP4;
AC B0LYP6; B0LYS4; B0LYT0; B0LYT3; B0LYT8; B0LYT9; B0LYU6; B0LYU8; B0LYV4;
AC B0LYW2; B0LYW3; B0LYW5; B0LYW7; B0LYX3; B0LYX4; B0LYX6; B0LYX7; Q39104;
AC Q93VB6; Q9SYG0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Epithiospecifier protein;
DE Short=AtESP;
DE AltName: Full=Protein EPITHIOSPECIFYING SENESCENCE REGULATOR;
DE Short=AtESR;
GN Name=ESP; Synonyms=ESR, TASTY; OrderedLocusNames=At1g54040;
GN ORFNames=F15I1.12;
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].
RC STRAIN=cv. C24;
RA Quigley F.R.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND POLYMORPHISM.
RC STRAIN=cv. Columbia, cv. Da(1)-12, cv. Ei-2, cv. Landsberg erecta,
RC cv. Ru-0, and cv. Tac-0;
RX PubMed=11752388; DOI=10.2307/3871535;
RA Lambrix V., Reichelt M., Mitchell-Olds T., Kliebenstein D.J.,
RA Gershenzon J.;
RT "The Arabidopsis epithiospecifier protein promotes the hydrolysis of
RT glucosinolates to nitriles and influences Trichoplusia ni herbivory.";
RL Plant Cell 13:2793-2807(2001).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-312, AND POLYMORPHISM.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1,
RC cv. Bor-4, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. CIBC-5,
RC cv. Columbia, cv. Ct-1, cv. Cvi-0, cv. Ed-1, cv. Ed-2, cv. Edi-0, cv. Ei-2,
RC cv. Fab-2, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Goettingen-22,
RC cv. Goettingen-7, cv. Gu-0, cv. Gy-0, cv. HR-10, cv. HR-5, cv. Kas-2,
RC cv. Kin-0, cv. KNO-10, cv. KNO-18, cv. Kon, cv. KZ-1, cv. KZ-9, cv. Ler-1,
RC cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lp2-2, cv. Lp2-6, cv. Lz-0, cv. Mr-0,
RC cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. N13 Konchezero, cv. Nd-1, cv. NFA-10,
RC cv. NFA-8, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pna-10,
RC cv. Pna-17, cv. Pro-0, cv. Pu2-23, cv. Pu2-7, cv. Ra-0, cv. REN-1,
RC cv. REN-11, cv. Rmx-A02, cv. Rmx-A180, cv. RRS-10, cv. RRS-7, cv. Se-0,
RC cv. Sha, cv. Sorbo, cv. Spr1-2, cv. Spr1-6, cv. Sq-1, cv. Sq-8, cv. Tamm-2,
RC cv. Tamm-27, cv. Ts-1, cv. Ts-5, cv. Tsu-1, cv. Ull2-3, cv. Ull2-5,
RC cv. Uod-1, cv. Uod-7, cv. Van-0, cv. Var2-1, cv. Var2-6, cv. Wa-1,
RC cv. Wassilewskija, cv. Wassilewskija-2, cv. Wei-0, cv. Wt-5, cv. Yo-0,
RC cv. Zdr-1, and cv. Zdr-6;
RX PubMed=18245336; DOI=10.1534/genetics.107.083279;
RA Bakker E.G., Traw M.B., Toomajian C., Kreitman M., Bergelson J.;
RT "Low levels of polymorphism in genes that control the activation of defense
RT response in Arabidopsis thaliana.";
RL Genetics 178:2031-2043(2008).
RN [8]
RP INDUCTION BY JASMONATE.
RX PubMed=13677466; DOI=10.1023/a:1025045217859;
RA Mandaokar A., Kumar V.D., Amway M., Browse J.;
RT "Microarray and differential display identify genes involved in jasmonate-
RT dependent anther development.";
RL Plant Mol. Biol. 52:775-786(2003).
RN [9]
RP FUNCTION, AND POLYMORPHISM.
RC STRAIN=cv. Columbia, and cv. Ei-2;
RX PubMed=15845404; DOI=10.1016/j.phytochem.2005.02.026;
RA de Torres-Zabala M., Grant M., Bones A.M., Bennett R., Lim Y.S., Kissen R.,
RA Rossiter J.T.;
RT "Characterisation of recombinant epithiospecifier protein and its over-
RT expression in Arabidopsis thaliana.";
RL Phytochemistry 66:859-867(2005).
RN [10]
RP FUNCTION.
RX PubMed=17061170; DOI=10.1007/s10886-006-9149-1;
RA Burow M., Muller R., Gershenzon J., Wittstock U.;
RT "Altered glucosinolate hydrolysis in genetically engineered Arabidopsis
RT thaliana and its influence on the larval development of Spodoptera
RT littoralis.";
RL J. Chem. Ecol. 32:2333-2349(2006).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=17390109; DOI=10.1007/s11103-007-9143-1;
RA Burow M., Rice M., Hause B., Gershenzon J., Wittstock U.;
RT "Cell- and tissue-specific localization and regulation of the
RT epithiospecifier protein in Arabidopsis thaliana.";
RL Plant Mol. Biol. 64:173-185(2007).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP WRKY53.
RX PubMed=17369373; DOI=10.1105/tpc.106.042705;
RA Miao Y., Zentgraf U.;
RT "The antagonist function of Arabidopsis WRKY53 and ESR/ESP in leaf
RT senescence is modulated by the jasmonic and salicylic acid equilibrium.";
RL Plant Cell 19:819-830(2007).
RN [13]
RP FUNCTION.
RX PubMed=17920088; DOI=10.1016/j.phytochem.2007.08.027;
RA Burow M., Zhang Z.-Y., Ober J.A., Lambrix V.M., Wittstock U.,
RA Gershenzon J., Kliebenstein D.J.;
RT "ESP and ESM1 mediate indol-3-acetonitrile production from indol-3-ylmethyl
RT glucosinolate in Arabidopsis.";
RL Phytochemistry 69:663-671(2008).
RN [14]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Converts glucosinolates both to epithionitriles and to simple
CC nitriles in the presence of myrosinase. Promotes the formation of
CC epithionitriles after hydrolysis of alkenylglucosinolates containing a
CC terminal double bond. Mediates indol-3-acetonitrile (IACN) production
CC from indol-3-ylmethyl glucosinolate. Acts as a negative regulator of
CC senescence. {ECO:0000269|PubMed:11752388, ECO:0000269|PubMed:15845404,
CC ECO:0000269|PubMed:17061170, ECO:0000269|PubMed:17369373,
CC ECO:0000269|PubMed:17920088}.
CC -!- SUBUNIT: Interacts with WRKY53. {ECO:0000269|PubMed:17369373}.
CC -!- INTERACTION:
CC Q8RY71; Q9SUP6: WRKY53; NbExp=6; IntAct=EBI-1997188, EBI-1235980;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17369373}. Nucleus
CC {ECO:0000269|PubMed:17369373}. Note=Brought to the nucleus after
CC interaction with WRKY53.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RY71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RY71-2; Sequence=VSP_036395;
CC -!- TISSUE SPECIFICITY: Expressed in epidermal cells of all above-ground
CC organs except the anthers, in cambial cells of leaf and stem vascular
CC bundles, and in glucosinolates rich S-cells found in stems just below
CC the inflorescence. Absent from roots. {ECO:0000269|PubMed:17390109}.
CC -!- INDUCTION: By jasmonate. {ECO:0000269|PubMed:13677466}.
CC -!- DISRUPTION PHENOTYPE: Accelerated leaf senescence and increased
CC pathogen damages. {ECO:0000269|PubMed:17369373}.
CC -!- MISCELLANEOUS: ESP is functional in cv. Landsberg erecta while the gene
CC encoding the protein is not expressed in cv. Columbia, cv. Da(1)-12 and
CC cv. Ru-0. ESP activity is regulated at the transcriptional, the post-
CC transcriptional and the post-translational levels.
CC -!- MISCELLANEOUS: Not dependent on the presence of Fe(2+) although
CC supplemental Fe(2+) increases nitriles formation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X71915; CAA50730.1; -; mRNA.
DR EMBL; AF416786; AAL14622.1; -; Genomic_DNA.
DR EMBL; AF416790; AAL14625.1; -; Genomic_DNA.
DR EMBL; AF416785; AAL14621.1; -; Genomic_DNA.
DR EMBL; AF416787; AAL14623.1; -; Genomic_DNA.
DR EMBL; AF416789; AAL14624.1; -; Genomic_DNA.
DR EMBL; AC006577; AAD25776.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33039.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33040.1; -; Genomic_DNA.
DR EMBL; AY074550; AAL69516.1; -; mRNA.
DR EMBL; BT033156; ACF75545.1; -; mRNA.
DR EMBL; EU404377; ABY88775.1; -; Genomic_DNA.
DR EMBL; EU404378; ABY88776.1; -; Genomic_DNA.
DR EMBL; EU404379; ABY88777.1; -; Genomic_DNA.
DR EMBL; EU404380; ABY88778.1; -; Genomic_DNA.
DR EMBL; EU404381; ABY88779.1; -; Genomic_DNA.
DR EMBL; EU404382; ABY88780.1; -; Genomic_DNA.
DR EMBL; EU404383; ABY88781.1; -; Genomic_DNA.
DR EMBL; EU404384; ABY88782.1; -; Genomic_DNA.
DR EMBL; EU404385; ABY88783.1; -; Genomic_DNA.
DR EMBL; EU404386; ABY88784.1; -; Genomic_DNA.
DR EMBL; EU404387; ABY88785.1; -; Genomic_DNA.
DR EMBL; EU404388; ABY88786.1; -; Genomic_DNA.
DR EMBL; EU404389; ABY88787.1; -; Genomic_DNA.
DR EMBL; EU404390; ABY88788.1; -; Genomic_DNA.
DR EMBL; EU404391; ABY88789.1; -; Genomic_DNA.
DR EMBL; EU404392; ABY88790.1; -; Genomic_DNA.
DR EMBL; EU404393; ABY88791.1; -; Genomic_DNA.
DR EMBL; EU404394; ABY88792.1; -; Genomic_DNA.
DR EMBL; EU404395; ABY88793.1; -; Genomic_DNA.
DR EMBL; EU404396; ABY88794.1; -; Genomic_DNA.
DR EMBL; EU404397; ABY88795.1; -; Genomic_DNA.
DR EMBL; EU404398; ABY88796.1; -; Genomic_DNA.
DR EMBL; EU404399; ABY88797.1; -; Genomic_DNA.
DR EMBL; EU404400; ABY88798.1; -; Genomic_DNA.
DR EMBL; EU404401; ABY88799.1; -; Genomic_DNA.
DR EMBL; EU404402; ABY88800.1; -; Genomic_DNA.
DR EMBL; EU404403; ABY88801.1; -; Genomic_DNA.
DR EMBL; EU404404; ABY88802.1; -; Genomic_DNA.
DR EMBL; EU404405; ABY88803.1; -; Genomic_DNA.
DR EMBL; EU404406; ABY88804.1; -; Genomic_DNA.
DR EMBL; EU404407; ABY88805.1; -; Genomic_DNA.
DR EMBL; EU404408; ABY88806.1; -; Genomic_DNA.
DR EMBL; EU404409; ABY88807.1; -; Genomic_DNA.
DR EMBL; EU404410; ABY88808.1; -; Genomic_DNA.
DR EMBL; EU404411; ABY88809.1; -; Genomic_DNA.
DR EMBL; EU404412; ABY88810.1; -; Genomic_DNA.
DR EMBL; EU404413; ABY88811.1; -; Genomic_DNA.
DR EMBL; EU404414; ABY88812.1; -; Genomic_DNA.
DR EMBL; EU404415; ABY88813.1; -; Genomic_DNA.
DR EMBL; EU404416; ABY88814.1; -; Genomic_DNA.
DR EMBL; EU404417; ABY88815.1; -; Genomic_DNA.
DR EMBL; EU404418; ABY88816.1; -; Genomic_DNA.
DR EMBL; EU404419; ABY88817.1; -; Genomic_DNA.
DR EMBL; EU404420; ABY88818.1; -; Genomic_DNA.
DR EMBL; EU404421; ABY88819.1; -; Genomic_DNA.
DR EMBL; EU404422; ABY88820.1; -; Genomic_DNA.
DR EMBL; EU404423; ABY88821.1; -; Genomic_DNA.
DR EMBL; EU404424; ABY88822.1; -; Genomic_DNA.
DR EMBL; EU404425; ABY88823.1; -; Genomic_DNA.
DR EMBL; EU404426; ABY88824.1; -; Genomic_DNA.
DR EMBL; EU404427; ABY88825.1; -; Genomic_DNA.
DR EMBL; EU404428; ABY88826.1; -; Genomic_DNA.
DR EMBL; EU404429; ABY88827.1; -; Genomic_DNA.
DR EMBL; EU404430; ABY88828.1; -; Genomic_DNA.
DR EMBL; EU404431; ABY88829.1; -; Genomic_DNA.
DR EMBL; EU404432; ABY88830.1; -; Genomic_DNA.
DR EMBL; EU404433; ABY88831.1; -; Genomic_DNA.
DR EMBL; EU404434; ABY88832.1; -; Genomic_DNA.
DR EMBL; EU404435; ABY88833.1; -; Genomic_DNA.
DR EMBL; EU404436; ABY88834.1; -; Genomic_DNA.
DR EMBL; EU404437; ABY88835.1; -; Genomic_DNA.
DR EMBL; EU404438; ABY88836.1; -; Genomic_DNA.
DR EMBL; EU404439; ABY88837.1; -; Genomic_DNA.
DR EMBL; EU404440; ABY88838.1; -; Genomic_DNA.
DR EMBL; EU404441; ABY88839.1; -; Genomic_DNA.
DR EMBL; EU404443; ABY88840.1; -; Genomic_DNA.
DR EMBL; EU404444; ABY88841.1; -; Genomic_DNA.
DR EMBL; EU404445; ABY88842.1; -; Genomic_DNA.
DR EMBL; EU404446; ABY88843.1; -; Genomic_DNA.
DR EMBL; EU404447; ABY88844.1; -; Genomic_DNA.
DR EMBL; EU404448; ABY88845.1; -; Genomic_DNA.
DR EMBL; EU404450; ABY88846.1; -; Genomic_DNA.
DR EMBL; EU404451; ABY88847.1; -; Genomic_DNA.
DR EMBL; EU404452; ABY88848.1; -; Genomic_DNA.
DR EMBL; EU404453; ABY88849.1; -; Genomic_DNA.
DR EMBL; EU404454; ABY88850.1; -; Genomic_DNA.
DR EMBL; EU404455; ABY88851.1; -; Genomic_DNA.
DR EMBL; EU404456; ABY88852.1; -; Genomic_DNA.
DR EMBL; EU404457; ABY88853.1; -; Genomic_DNA.
DR EMBL; EU404458; ABY88854.1; -; Genomic_DNA.
DR EMBL; EU404459; ABY88855.1; -; Genomic_DNA.
DR EMBL; EU404460; ABY88856.1; -; Genomic_DNA.
DR EMBL; EU404461; ABY88857.1; -; Genomic_DNA.
DR EMBL; EU404462; ABY88858.1; -; Genomic_DNA.
DR EMBL; EU404463; ABY88859.1; -; Genomic_DNA.
DR EMBL; EU404464; ABY88860.1; -; Genomic_DNA.
DR EMBL; EU404465; ABY88861.1; -; Genomic_DNA.
DR EMBL; EU404466; ABY88862.1; -; Genomic_DNA.
DR EMBL; EU404467; ABY88863.1; -; Genomic_DNA.
DR EMBL; EU404468; ABY88864.1; -; Genomic_DNA.
DR EMBL; EU404469; ABY88865.1; -; Genomic_DNA.
DR EMBL; EU404470; ABY88866.1; -; Genomic_DNA.
DR EMBL; EU404471; ABY88867.1; -; Genomic_DNA.
DR EMBL; EU404472; ABY88868.1; -; Genomic_DNA.
DR PIR; A96581; A96581.
DR PIR; S33464; S33464.
DR RefSeq; NP_175806.3; NM_104281.3. [Q8RY71-1]
DR RefSeq; NP_850963.1; NM_180632.2. [Q8RY71-2]
DR PDB; 5GQ0; X-ray; 2.31 A; A/B=1-341.
DR PDBsum; 5GQ0; -.
DR AlphaFoldDB; Q8RY71; -.
DR SMR; Q8RY71; -.
DR BioGRID; 27067; 2.
DR IntAct; Q8RY71; 1.
DR STRING; 3702.AT1G54040.2; -.
DR PaxDb; Q8RY71; -.
DR PRIDE; Q8RY71; -.
DR ProteomicsDB; 222295; -. [Q8RY71-1]
DR EnsemblPlants; AT1G54040.1; AT1G54040.1; AT1G54040. [Q8RY71-2]
DR EnsemblPlants; AT1G54040.2; AT1G54040.2; AT1G54040. [Q8RY71-1]
DR GeneID; 841842; -.
DR Gramene; AT1G54040.1; AT1G54040.1; AT1G54040. [Q8RY71-2]
DR Gramene; AT1G54040.2; AT1G54040.2; AT1G54040. [Q8RY71-1]
DR KEGG; ath:AT1G54040; -.
DR Araport; AT1G54040; -.
DR TAIR; locus:2014400; AT1G54040.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_030461_0_0_1; -.
DR InParanoid; Q8RY71; -.
DR OMA; NTWENPE; -.
DR PhylomeDB; Q8RY71; -.
DR BioCyc; ARA:AT1G54040-MON; -.
DR BioCyc; MetaCyc:AT1G54040-MON; -.
DR PRO; PR:Q8RY71; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY71; baseline and differential.
DR Genevisible; Q8RY71; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic process; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0080028; P:nitrile biosynthetic process; IBA:GO_Central.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF01344; Kelch_1; 3.
DR SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Kelch repeat; Nucleus;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..341
FT /note="Epithiospecifier protein"
FT /id="PRO_0000363988"
FT REPEAT 34..82
FT /note="Kelch 1"
FT REPEAT 87..133
FT /note="Kelch 2"
FT REPEAT 139..194
FT /note="Kelch 3"
FT REPEAT 203..249
FT /note="Kelch 4"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.6"
FT /id="VSP_036395"
FT VARIANT 13
FT /note="G -> E (in strain: cv. Ei-2 and cv. Tac-0)"
FT VARIANT 18
FT /note="T -> S (in strain: cv. Ei-2 and cv. Tac-0)"
FT VARIANT 308
FT /note="A -> P (in strain: cv. Ag-0, cv. Br-0, cv. CIBC-5,
FT cv. Ei-2, cv. Gy-0, cv. HR-10, cv. HR-5, cv. Kin-0, cv.
FT KNO-10, cv. KNO-18, cv. Lz-0, cv. NFA-8, cv. NFA-10, cv.
FT Pna-10, cv. Ra-0, cv. Rmx-A180, cv. RRS-10, cv. Se-0, cv.
FT Sq-1, cv. Tac-0, cv. Van-0, cv. Var2-6 and cv. Yo-0)"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:5GQ0"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:5GQ0"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5GQ0"
SQ SEQUENCE 341 AA; 37008 MW; 2423B2AD685E72DF CRC64;
MAPTLQGQWI KVGQKGGTGP GPRSSHGIAA VGDKLYSFGG ELTPNKHIDK DLYVFDFNTQ
TWSIAQPKGD APTVSCLGVR MVAVGTKIYI FGGRDENRNF ENFRSYDTVT SEWTFLTKLD
EVGGPEARTF HSMASDENHV YVFGGVSKGG TMNTPTRFRT IEAYNIADGK WAQLPDPGDN
FEKRGGAGFA VVQGKIWVVY GFATSIVPGG KDDYESNAVQ FYDPASKKWT EVETTGAKPS
ARSVFAHAVV GKYIIIFAGE VWPDLNGHYG PGTLSNEGYA LDTETLVWEK LGEEGAPAIP
RGWTAYTAAT VDGKNGLLMH GGKLPTNERT DDLYFYAVNS A
