LOX3_ARATH
ID LOX3_ARATH Reviewed; 919 AA.
AC Q9LNR3; Q9LQJ5; Q9SMW1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Lipoxygenase 3, chloroplastic;
DE Short=AtLOX3;
DE EC=1.13.11.12 {ECO:0000269|PubMed:18949503};
DE Flags: Precursor;
GN Name=LOX3; OrderedLocusNames=At1g17420; ORFNames=F28G4.10;
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].
RA Fritsche K., Feussner I.;
RT "The second chloroplastic jasmonate-inducible 13-LOX from Arabidopsis
RT leaves.";
RL Submitted (SEP-1999) 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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [7]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=18156220; DOI=10.1105/tpc.106.045898;
RA Rossel J.B., Wilson P.B., Hussain D., Woo N.S., Gordon M.J., Mewett O.P.,
RA Howell K.A., Whelan J., Kazan K., Pogson B.J.;
RT "Systemic and intracellular responses to photooxidative stress in
RT Arabidopsis.";
RL Plant Cell 19:4091-4110(2007).
RN [8]
RP INDUCTION BY WOUNDING.
RX PubMed=17786451; DOI=10.1007/s00299-007-0410-z;
RA Wang Z., Cao G., Wang X., Miao J., Liu X., Chen Z., Qu L.-J., Gu H.;
RT "Identification and characterization of COI1-dependent transcription factor
RT genes involved in JA-mediated response to wounding in Arabidopsis plants.";
RL Plant Cell Rep. 27:125-135(2008).
RN [9]
RP INDUCTION BY JASMONATE.
RX PubMed=18216250; DOI=10.1073/pnas.0711203105;
RA Pauwels L., Morreel K., De Witte E., Lammertyn F., Van Montagu M.,
RA Boerjan W., Inze D., Goossens A.;
RT "Mapping methyl jasmonate-mediated transcriptional reprogramming of
RT metabolism and cell cycle progression in cultured Arabidopsis cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1380-1385(2008).
RN [10]
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: 13S-lipoxygenase that can use linolenic acid as substrates.
CC Plant lipoxygenases may be involved in a number of diverse aspects of
CC plant physiology including growth and development, pest resistance, and
CC senescence or responses to wounding. Catalyzes the hydroperoxidation of
CC lipids containing a cis,cis-1,4-pentadiene structure (By similarity).
CC {ECO:0000250, 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781;
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34496;
CC 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 roots and leaves.
CC {ECO:0000269|PubMed:17369372}.
CC -!- DEVELOPMENTAL STAGE: First observed in lateral root primordia (LRP),
CC from the first pericycle divisions. Later expressed in lateral roots.
CC Expression is greatly increased in leaves during leaf senescence.
CC {ECO:0000269|PubMed:11891244, ECO:0000269|PubMed:17369372}.
CC -!- INDUCTION: Induced by methyl jasmonate (MeJA), bacterial pathogens
CC (e.g. Pseudomonas syringae pv. tomato), high light and wounding.
CC {ECO:0000269|PubMed:17786451, ECO:0000269|PubMed:18156220,
CC ECO:0000269|PubMed:18216250}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ249794; CAB56692.1; -; mRNA.
DR EMBL; AC007843; AAF97315.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC022492; AAF79461.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29585.1; -; Genomic_DNA.
DR EMBL; AY075625; AAL91636.1; -; mRNA.
DR EMBL; BT006348; AAP21156.1; -; mRNA.
DR RefSeq; NP_564021.1; NM_101603.3.
DR AlphaFoldDB; Q9LNR3; -.
DR SMR; Q9LNR3; -.
DR BioGRID; 23554; 2.
DR IntAct; Q9LNR3; 1.
DR STRING; 3702.AT1G17420.1; -.
DR SwissLipids; SLP:000001766; -.
DR PaxDb; Q9LNR3; -.
DR PRIDE; Q9LNR3; -.
DR ProteomicsDB; 238670; -.
DR EnsemblPlants; AT1G17420.1; AT1G17420.1; AT1G17420.
DR GeneID; 838314; -.
DR Gramene; AT1G17420.1; AT1G17420.1; AT1G17420.
DR KEGG; ath:AT1G17420; -.
DR Araport; AT1G17420; -.
DR TAIR; locus:2018848; AT1G17420.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q9LNR3; -.
DR OMA; AYGMEMS; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q9LNR3; -.
DR BRENDA; 1.13.11.12; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q9LNR3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNR3; baseline and differential.
DR Genevisible; Q9LNR3; 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:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; 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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..919
FT /note="Lipoxygenase 3, chloroplastic"
FT /id="PRO_0000380592"
FT DOMAIN 86..222
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 225..919
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 272..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 578
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 583
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 770
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 774
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 919
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 374
FT /note="L -> P (in Ref. 1; CAB56692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 103726 MW; 194A0B150273E44C CRC64;
MALAKELMGY PLITERSSLV SSASHFKKRT QSTQFSINPF DRRPRKTKSG VVAAISEDLV
KTLRFSTTTG DRKSEEEEKA AVKFKVRAVV TVRNKNKEDL KETLVKHLDA FADKIGRNIV
LELISTQLDP KTKLPKKSNA AVLKDWSKKS KTKAERVHYT AEFTVDAAFG SPGAITVMNK
HQKEFFLESI TIEGFALGPV HFPCNSWVQS QKDHPDKRIF FTNQPYLPNE TPSGLRVLRE
KELKNLRGDG SGVRKLSDRI YDFDVYNDLG NPDKSSELSR PKLGGKEVPY PRRCRTGRQS
TVSDKDAESR VEKPLPMYVP RDEQFEESKQ DTFAAGRLKA VLHHLIPSLK ASIVAEDFAD
FGEIDRLYKE GLLLKLGFQD DIFKKFPLPK VVVDTLQEST KGLLKYDTPK ILSKDKNAWL
RDDEFARQAI AGINPVNIER VKTFPPVSNL DPKIYGPQHS ALTDDHIIGH LDGFSVQQAL
EENRLYMLDY HDIFLPFLDR INALDGRKAY ATRTIFFLTR LGTLKPVAIE LSLPPHGPKH
RSKRVLTPPV DATSNWMWQL AKAHVSSNDA GVHQLVNHWL RTHACLEPFI LAAHRQLSAM
HPIFKLLDPH MRYTLEINAL ARQSLISADG VIEGGFTAGA YGMEMSAAAY KSSWRFDMEG
LPADLIRRGM AIPDATQPHG LKLLIEDYPY ANDGLLLWSA IQTWVRTYVE RYYPNPNLIK
TDSELQSWYS ESINVGHADL RDADWWPELS TVDDLVSILT TLIWLASAQH AALNFGQYPY
GGYVPNRPPL MRRLIPDESD PEYASFISHP EKYYFSSMPS LAQTSKFMAV VDTLSTHSPD
EEYIGERQQP SIWTGDAEIV EAFYGFAAEI GRIEKEIEKR NADPDRRNRC GAGVLPYELL
VPSSEPGVTC RGVPNSVSI
