JOX4_ARATH
ID JOX4_ARATH Reviewed; 353 AA.
AC O80449; Q8LCL0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Jasmonate-induced oxygenase 4 {ECO:0000303|PubMed:28559313};
DE EC=1.14.11.- {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase JOX4 {ECO:0000305};
DE AltName: Full=Anthocyanidin synthase {ECO:0000305};
DE AltName: Full=Jasmonic acid oxidase 4 {ECO:0000303|PubMed:28760569};
GN Name=JOX4 {ECO:0000303|PubMed:28559313};
GN Synonyms=ANS {ECO:0000305}, JAO4 {ECO:0000303|PubMed:28760569};
GN OrderedLocusNames=At2g38240 {ECO:0000312|Araport:AT2G38240};
GN ORFNames=F16M14.17 {ECO:0000312|EMBL:AAC27173.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY SALT STRESS.
RX PubMed=11351099; DOI=10.1104/pp.126.1.363;
RA Gong Z., Koiwa H., Cushman M.A., Ray A., Bufford D., Kore-eda S.,
RA Matsumoto T.K., Zhu J., Cushman J.C., Bressan R.A., Hasegawa P.M.;
RT "Genes that are uniquely stress regulated in salt overly sensitive (sos)
RT mutants.";
RL Plant Physiol. 126:363-375(2001).
RN [6]
RP INDUCTION BY BACTERIAL INFECTION.
RX PubMed=16553894; DOI=10.1111/j.1365-313x.2006.02725.x;
RA Thilmony R., Underwood W., He S.Y.;
RT "Genome-wide transcriptional analysis of the Arabidopsis thaliana
RT interaction with the plant pathogen Pseudomonas syringae pv. tomato DC3000
RT and the human pathogen Escherichia coli O157:H7.";
RL Plant J. 46:34-53(2006).
RN [7]
RP INDUCTION.
RX PubMed=17587374; DOI=10.1111/j.1469-8137.2007.02092.x;
RA Hectors K., Prinsen E., De Coen W., Jansen M.A., Guisez Y.;
RT "Arabidopsis thaliana plants acclimated to low dose rates of ultraviolet B
RT radiation show specific changes in morphology and gene expression in the
RT absence of stress symptoms.";
RL New Phytol. 175:255-270(2007).
RN [8]
RP INDUCTION BY WOUNDING.
RX PubMed=17675405; DOI=10.1105/tpc.107.050708;
RA Yan Y., Stolz S., Chetelat A., Reymond P., Pagni M., Dubugnon L.,
RA Farmer E.E.;
RT "A downstream mediator in the growth repression limb of the jasmonate
RT pathway.";
RL Plant Cell 19:2470-2483(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RX PubMed=28760569; DOI=10.1016/j.molp.2017.07.010;
RA Smirnova E., Marquis V., Poirier L., Aubert Y., Zumsteg J., Menard R.,
RA Miesch L., Heitz T.;
RT "Jasmonic acid oxidase 2 hydroxylates jasmonic acid and represses basal
RT defense and resistance responses against Botrytis cinerea infection.";
RL Mol. Plant 10:1159-1173(2017).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28559313; DOI=10.1073/pnas.1701101114;
RA Caarls L., Elberse J., Awwanah M., Ludwig N.R., de Vries M., Zeilmaker T.,
RA Van Wees S.C.M., Schuurink R.C., Van den Ackerveken G.;
RT "Arabidopsis JASMONATE-INDUCED OXYGENASES down-regulate plant immunity by
RT hydroxylation and inactivation of the hormone jasmonic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6388-6393(2017).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the
CC oxidation of jasmonate (JA), a stress-induced phytohormone synthesized
CC in response to attack by pathogens and herbivores, which triggers the
CC activation of defense responses via the JA-mediated signaling pathway
CC (PubMed:28760569, PubMed:28559313). Converts JA to 12-hydroxyjasmonate
CC (12OH-JA), an inactive form of JA (PubMed:28760569, PubMed:28559313).
CC Is specific to free JA, and cannot oxidize the bioactive form
CC jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates
CC (PubMed:28760569). Prevents over-accumulation of JA and indirectly its
CC bioactive form JA-Ile under stress response (PubMed:28760569,
CC PubMed:28559313). Acts as negative regulator of JA-mediated defense
CC signaling, by contributing to 12OH-JA accumulation, which represses JA
CC defense responses upon infection by the fungal pathogen Botrytis
CC cinerea (PubMed:28760569, PubMed:28559313). Acts as negative regulator
CC of JA-mediated defense responses upon infestation by the herbivorous
CC caterpillar Mamestra brassicae (PubMed:28559313).
CC {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + jasmonate + O2 = (1R,2R)-12-hydroxyjasmonate
CC + CO2 + succinate; Xref=Rhea:RHEA:67144, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58431, ChEBI:CHEBI:132022;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67145;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- INDUCTION: Induced by infection with the bacterial pathogen Pseudomonas
CC syringae pv. tomato (PubMed:16553894). Induced by wounding
CC (PubMed:17675405, PubMed:28760569). Induced by infection with the
CC fungal pathogen Botrytis cinerea (PubMed:28760569, PubMed:28559313).
CC Induced by methyl jasmonate (MeJA) (PubMed:28559313). Induced by
CC infestation with the caterpillar Mamestra brassicae (PubMed:28559313).
CC Induced by salt stress (PubMed:11351099). Down-regulated by UV-B
CC (PubMed:17587374). {ECO:0000269|PubMed:11351099,
CC ECO:0000269|PubMed:16553894, ECO:0000269|PubMed:17587374,
CC ECO:0000269|PubMed:17675405, ECO:0000269|PubMed:28559313,
CC ECO:0000269|PubMed:28760569}.
CC -!- DISRUPTION PHENOTYPE: The quadruple mutant jox1, jox2, jox3 and jox4
CC exhibit reduced root and shoot growth, delayed flowering, reduced seed
CC production, constitutively elevated jasmonate and jasmonoyl-L-
CC isoleucine levels, and enhanced resistance to the necrotrophic fungal
CC pathogen Botrytis cinerea and the herbivorous caterpillar Mamestra
CC brassicae. {ECO:0000269|PubMed:28559313}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC003028; AAC27173.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09512.1; -; Genomic_DNA.
DR EMBL; AY062643; AAL32721.1; -; mRNA.
DR EMBL; AY093302; AAM13301.1; -; mRNA.
DR EMBL; AY086539; AAM63604.1; -; mRNA.
DR PIR; T01256; T01256.
DR RefSeq; NP_181359.1; NM_129381.4.
DR AlphaFoldDB; O80449; -.
DR SMR; O80449; -.
DR STRING; 3702.AT2G38240.1; -.
DR PaxDb; O80449; -.
DR PRIDE; O80449; -.
DR ProteomicsDB; 222153; -.
DR EnsemblPlants; AT2G38240.1; AT2G38240.1; AT2G38240.
DR GeneID; 818403; -.
DR Gramene; AT2G38240.1; AT2G38240.1; AT2G38240.
DR KEGG; ath:AT2G38240; -.
DR Araport; AT2G38240; -.
DR TAIR; locus:2042942; AT2G38240.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_0_1; -.
DR InParanoid; O80449; -.
DR OMA; TCRKIIA; -.
DR OrthoDB; 1005149at2759; -.
DR PhylomeDB; O80449; -.
DR PRO; PR:O80449; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80449; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0120091; F:jasmonic acid hydrolase; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900366; P:negative regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IGI:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Jasmonic acid signaling pathway; Metal-binding;
KW Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..353
FT /note="Jasmonate-induced oxygenase 4"
FT /id="PRO_0000438434"
FT DOMAIN 202..302
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 209
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 211
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 283
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 293
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 295
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 332
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 336
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT CONFLICT 127
FT /note="K -> R (in Ref. 4; AAM63604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39681 MW; 92C5DF2C5EF9CC5C CRC64;
MATCWPEPIV SVQSLSQTGV PTVPNRYVKP AHQRPVFNTT QSDAGIEIPV LDMNDVWGKP
EGLRLVRSAC EEWGFFQMVN HGVTHSLMER VRGAWREFFE LPLEEKRKYA NSPDTYEGYG
SRLGVVKDAK LDWSDYFFLN YLPSSIRNPS KWPSQPPKIR ELIEKYGEEV RKLCERLTET
LSESLGLKPN KLMQALGGGD KVGASLRTNF YPKCPQPQLT LGLSSHSDPG GITILLPDEK
VAGLQVRRGD GWVTIKSVPN ALIVNIGDQL QILSNGIYKS VEHQVIVNSG MERVSLAFFY
NPRSDIPVGP IEELVTANRP ALYKPIRFDE YRSLIRQKGP CGKNQVDSLL LTR
