LOX4_ARATH
ID LOX4_ARATH Reviewed; 926 AA.
AC Q9FNX8; Q9CAG9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lipoxygenase 4, chloroplastic;
DE Short=AtLOX4;
DE EC=1.13.11.12 {ECO:0000269|PubMed:18949503};
DE AltName: Full=LOX3-like protein;
DE Flags: Precursor;
GN Name=LOX4; Synonyms=LOX3; OrderedLocusNames=At1g72520;
GN ORFNames=F28P22.29, T10D10.1;
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].
RC TISSUE=Leaf;
RA Kunze S., Fritsche K., Feussner I.;
RT "AtLOX4, the third chloroplastic jasmonate-inducible 13-LOX from
RT Arabidopsis leaves.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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 DEVELOPMENTAL STAGE.
RX PubMed=11891244; DOI=10.1104/pp.010843;
RA He Y., Fukushige H., Hildebrand D.F., Gan S.;
RT "Evidence supporting a role of jasmonic acid in Arabidopsis leaf
RT senescence.";
RL Plant Physiol. 128:876-884(2002).
RN [6]
RP INDUCTION BY BACTERIAL PATHOGENS AND WOUNDING.
RX PubMed=12609040; DOI=10.1046/j.1365-313x.2003.01653.x;
RA de Torres M., Sanchez P., Fernandez-Delmond I., Grant M.;
RT "Expression profiling of the host response to bacterial infection: the
RT transition from basal to induced defence responses in RPM1-mediated
RT resistance.";
RL Plant J. 33:665-676(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17369372; DOI=10.1105/tpc.106.046052;
RA Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L.,
RA Hamberg M., Castresana C.;
RT "Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate
RT lateral root development and defense responses through a specific signaling
RT cascade.";
RL Plant Cell 19:831-846(2007).
RN [8]
RP INDUCTION BY OZONE.
RX PubMed=19054359; DOI=10.1111/j.1365-313x.2008.03756.x;
RA Ahlfors R., Brosche M., Kollist H., Kangasjaervi J.;
RT "Nitric oxide modulates ozone-induced cell death, hormone biosynthesis and
RT gene expression in Arabidopsis thaliana.";
RL Plant J. 58:1-12(2009).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18949503; DOI=10.1007/s11745-008-3245-7;
RA Bannenberg G., Martinez M., Hamberg M., Castresana C.;
RT "Diversity of the enzymatic activity in the lipoxygenase gene family of
RT Arabidopsis thaliana.";
RL Lipids 44:85-95(2009).
CC -!- FUNCTION: Plant lipoxygenases may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure (By similarity). 13S-lipoxygenase that can use linolenic acid
CC as substrates. {ECO:0000255|PROSITE-ProRule:PRU00726,
CC ECO:0000269|PubMed:18949503}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC Evidence={ECO:0000269|PubMed:18949503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12; Evidence={ECO:0000269|PubMed:18949503};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:17369372}.
CC -!- DEVELOPMENTAL STAGE: Expression is greatly increased in leaves during
CC leaf senescence. {ECO:0000269|PubMed:11891244}.
CC -!- INDUCTION: Induced by bacterial pathogens (e.g. Pseudomonas syringae
CC pv. tomato), ozone O(3), and wounding. {ECO:0000269|PubMed:12609040,
CC ECO:0000269|PubMed:19054359}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AJ302042; CAC19364.1; -; mRNA.
DR EMBL; AC010926; AAG51846.1; -; Genomic_DNA.
DR EMBL; AC016529; AAG52571.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35334.1; -; Genomic_DNA.
DR EMBL; AY056166; AAL07015.1; -; mRNA.
DR EMBL; AY091193; AAM14132.1; -; mRNA.
DR PIR; E96749; E96749.
DR RefSeq; NP_177396.1; NM_105911.5.
DR AlphaFoldDB; Q9FNX8; -.
DR SMR; Q9FNX8; -.
DR BioGRID; 28803; 1.
DR STRING; 3702.AT1G72520.1; -.
DR SwissLipids; SLP:000001765; -.
DR PaxDb; Q9FNX8; -.
DR PRIDE; Q9FNX8; -.
DR ProteomicsDB; 238497; -.
DR EnsemblPlants; AT1G72520.1; AT1G72520.1; AT1G72520.
DR GeneID; 843584; -.
DR Gramene; AT1G72520.1; AT1G72520.1; AT1G72520.
DR KEGG; ath:AT1G72520; -.
DR Araport; AT1G72520; -.
DR TAIR; locus:2030215; AT1G72520.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q9FNX8; -.
DR OMA; QKDHPSK; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q9FNX8; -.
DR BRENDA; 1.13.11.12; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q9FNX8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FNX8; baseline and differential.
DR Genevisible; Q9FNX8; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0009901; P:anther dehiscence; IGI:TAIR.
DR GO; GO:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0010193; P:response to ozone; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0080086; P:stamen filament development; IGI:TAIR.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..926
FT /note="Lipoxygenase 4, chloroplastic"
FT /id="PRO_0000380593"
FT DOMAIN 106..228
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 231..926
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 585
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 590
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 777
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 781
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 926
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 926 AA; 104814 MW; 3592FB6ECDCCC4A4 CRC64;
MALANEIMGS RLIFERSSSL ASPFHSRFSI KKKTQRTQFS INPFDPRPMR AVNSSGVVAA
ISEDLVKTLR ISTVGRKQEK EEEEEKSVKF KVRAVATVRN KNKEDFKETL VKHLDAFTDK
IGRNVVLELM STQVDPKTNE PKKSKAAVLK DWSKKSNSKA ERVHYTAEFT VDSAFGSPGA
ITVTNKHQKE FFLESITIEG FACGPVHFPC NSWVQSQKDH PSKRILFTNQ PYLPSETPSG
LRTLREKELE NLRGNGKGER KLSDRIYDYD VYNDIGNPDI SRELARPTLG GREFPYPRRC
RTGRSSTDTD MMSERRVEKP LPMYVPRDEQ FEESKQNTFA ACRLKAVLHN LIPSLKASIL
AEDFANFGEI DSLYKEGLLL KLGFQDDMFK KFPLPKIVTT LQKSSEGLLR YDTPKIVSKD
KYAWLRDDEF ARQAIAGINP VNIERVTSYP PVSNLDPEIY GPGLHSALTE DHIIGQLDGL
TVQQALETNR LFMVDYHDIY LPFLDRINAL DGRKAYATRT ILFLTRLGTL KPIAIELSLP
SQSSSNQKSK RVVTPPVDAT SNWMWQLAKA HVGSNDAGVH QLVNHWLRTH ACLEPFILAA
HRQLSAMHPI FKLLDPHMRY TLEINAVARQ TLISADGVIE SCFTAGQYGL EISSAAYKNK
WRFDMEGLPA DLIRRGMAVP DPTQPHGLKL LVEDYPYAND GLLLWSAIQT WVRTYVERYY
ANSNLIQTDT ELQAWYSESI NVGHADHRDA EWWPKLSTVE DLVSVITTII WLASAQHAAL
NFGQYPYGGY VPNRPPLMRR LIPDESDPEF TSFIEDPQKY FFSSMPSLLQ TTKFMAVVDT
LSTHSPDEEY IGERQQPSIW TGDAEIVDAF YGFSAEIGRI EKEIDKRNRD PSRRNRCGAG
VLPYELMAPS SEPGVTCRGV PNSVSI
