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   27-MAR-2024, entry version 157.
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; Evidence={ECO:0000255|PROSITE-
CC         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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9LNR3; -.
DR   SwissLipids; SLP:000001766; -.
DR   PaxDb; 3702-AT1G17420-1; -.
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; AT1G17420; LOX3.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   InParanoid; Q9LNR3; -.
DR   OMA; ILIWNAS; -.
DR   OrthoDB; 462210at2759; -.
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   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: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; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF181; LIPOXYGENASE 3, CHLOROPLASTIC; 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; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   Genevisible; Q9LNR3; AT.
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
//