LOX2_ARATH
ID LOX2_ARATH Reviewed; 896 AA.
AC P38418; Q0WLR8; Q56WG6; Q8GW45; Q8W4E4; Q9M1U5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Lipoxygenase 2, chloroplastic;
DE Short=AtLOX2;
DE EC=1.13.11.12 {ECO:0000269|PubMed:18949503};
DE Flags: Precursor;
GN Name=LOX2; OrderedLocusNames=At3g45140; ORFNames=T14D3.80;
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].
RX PubMed=8290626; DOI=10.1104/pp.103.4.1133;
RA Bell E., Mullet J.E.;
RT "Characterization of an Arabidopsis lipoxygenase gene responsive to methyl
RT jasmonate and wounding.";
RL Plant Physiol. 103:1133-1137(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-125.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-896.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7567995; DOI=10.1073/pnas.92.19.8675;
RA Bell E., Creelman R.A., Mullet J.E.;
RT "A chloroplast lipoxygenase is required for wound-induced jasmonic acid
RT accumulation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8675-8679(1995).
RN [8]
RP INDUCTION BY WOUNDING.
RX PubMed=11090221; DOI=10.2307/3871117;
RA Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.;
RT "Involvement of phospholipase D in wound-induced accumulation of jasmonic
RT acid in arabidopsis.";
RL Plant Cell 12:2237-2246(2000).
RN [9]
RP INTERACTION WITH EIF4E2, AND SUBCELLULAR LOCATION.
RX PubMed=11117257; DOI=10.1023/a:1006494628892;
RA Freire M.A., Tourneur C., Granier F., Camonis J., El Amrani A.,
RA Browning K.S., Robaglia C.;
RT "Plant lipoxygenase 2 is a translation initiation factor-4E-binding
RT protein.";
RL Plant Mol. Biol. 44:129-140(2000).
RN [10]
RP INDUCTION BY APHIDS AND WOUNDING.
RX PubMed=11161062; DOI=10.1104/pp.125.2.1074;
RA Moran P.J., Thompson G.A.;
RT "Molecular responses to aphid feeding in Arabidopsis in relation to plant
RT defense pathways.";
RL Plant Physiol. 125:1074-1085(2001).
RN [11]
RP INDUCTION BY JASMONATE.
RX PubMed=11874572; DOI=10.1046/j.0960-7412.2001.01241.x;
RA Jensen A.B., Raventos D., Mundy J.;
RT "Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis.";
RL Plant J. 29:595-606(2002).
RN [12]
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 [13]
RP INDUCTION BY NITRIC OXIDE.
RX PubMed=14716563; DOI=10.1007/s00425-003-1178-1;
RA Huang X., Stettmaier K., Michel C., Hutzler P., Mueller M.J., Durner J.;
RT "Nitric oxide is induced by wounding and influences jasmonic acid signaling
RT in Arabidopsis thaliana.";
RL Planta 218:938-946(2004).
RN [14]
RP INDUCTION BY LEAF VOLATILES.
RX PubMed=15879447; DOI=10.1093/pcp/pci122;
RA Kishimoto K., Matsui K., Ozawa R., Takabayashi J.;
RT "Volatile C6-aldehydes and allo-ocimene activate defense genes and induce
RT resistance against Botrytis cinerea in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1093-1102(2005).
RN [15]
RP INDUCTION BY MYZUS PERSICAE AND BREVICORYNE BRASSICAE.
RX PubMed=17545220; DOI=10.1093/jxb/erm043;
RA Kusnierczyk A., Winge P., Midelfart H., Armbruster W.S., Rossiter J.T.,
RA Bones A.M.;
RT "Transcriptional responses of Arabidopsis thaliana ecotypes with different
RT glucosinolate profiles after attack by polyphagous Myzus persicae and
RT oligophagous Brevicoryne brassicae.";
RL J. Exp. Bot. 58:2537-2552(2007).
RN [16]
RP INDUCTION BY BACTERIAL PATHOGENS.
RX PubMed=17313166; DOI=10.1094/mpmi-20-2-0146;
RA Jakob K., Kniskern J.M., Bergelson J.;
RT "The role of pectate lyase and the jasmonic acid defense response in
RT Pseudomonas viridiflava virulence.";
RL Mol. Plant Microbe Interact. 20:146-158(2007).
RN [17]
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 [18]
RP REPRESSION BY WRKY62.
RX PubMed=17510065; DOI=10.1093/pcp/pcm058;
RA Mao P., Duan M., Wei C., Li Y.;
RT "WRKY62 transcription factor acts downstream of cytosolic NPR1 and
RT negatively regulates jasmonate-responsive gene expression.";
RL Plant Cell Physiol. 48:833-842(2007).
RN [19]
RP INDUCTION BY CATERPILLAR.
RX PubMed=18487634; DOI=10.1093/jxb/ern108;
RA Weech M.-H., Chapleau M., Pan L., Ide C., Bede J.C.;
RT "Caterpillar saliva interferes with induced Arabidopsis thaliana defence
RT responses via the systemic acquired resistance pathway.";
RL J. Exp. Bot. 59:2437-2448(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [21]
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. Required for the
CC wound-induced synthesis of jasmonic acid (JA) in leaves.
CC {ECO:0000269|PubMed:18949503, ECO:0000269|PubMed:7567995}.
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. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Interacts with EIF4E2. {ECO:0000269|PubMed:11117257}.
CC -!- INTERACTION:
CC P38418; O04663: EIF(ISO)4E; NbExp=7; IntAct=EBI-1770437, EBI-1770425;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}. Cytoplasm. Note=The unprocessed form is
CC cytoplasmic whereas the cleaved form is chloroplastic.
CC -!- TISSUE SPECIFICITY: In leaves and inflorescences but not abundant in
CC seeds, roots and stems. {ECO:0000269|PubMed:17369372}.
CC -!- DEVELOPMENTAL STAGE: Expression is sharply reduced in leaves during
CC leaf senescence. {ECO:0000269|PubMed:11891244}.
CC -!- INDUCTION: By methyl jasmonate (MeJA) and wounding, probably through
CC nitric oxide-mediated (NO) induction. Slightly locally induced upon
CC herbivors infestation such as aphids (Myzus persicae and Brevicoryne
CC brassicae), or caterpillar (Spodoptera exigua). Induced by leaf-
CC volatiles generated by herbivors-mediated wounding such as (E)-2-
CC hexenal, (Z)-3-hexenal, (Z)-3-hexenol or allo-ocimene (2,6-dimethyl-
CC 2,4,6-octatriene). Increased levels by bacterial pathogens (e.g.
CC P.viridiflava and P.syringae pv. tomato). Repressed by WRKY62.
CC {ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:11161062,
CC ECO:0000269|PubMed:11874572, ECO:0000269|PubMed:14716563,
CC ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:17313166,
CC ECO:0000269|PubMed:17510065, ECO:0000269|PubMed:17545220,
CC ECO:0000269|PubMed:18487634}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB72152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L23968; AAA32749.1; -; mRNA.
DR EMBL; AL138649; CAB72152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77997.1; -; Genomic_DNA.
DR EMBL; AY062611; AAL32689.1; -; mRNA.
DR EMBL; AK119093; BAC43666.1; -; mRNA.
DR EMBL; AK222075; BAD94917.1; -; mRNA.
DR EMBL; AK230124; BAF01939.1; -; mRNA.
DR PIR; JQ2391; JQ2391.
DR PIR; T47454; T47454.
DR RefSeq; NP_566875.1; NM_114383.3.
DR AlphaFoldDB; P38418; -.
DR SMR; P38418; -.
DR BioGRID; 8970; 5.
DR IntAct; P38418; 4.
DR STRING; 3702.AT3G45140.1; -.
DR iPTMnet; P38418; -.
DR SWISS-2DPAGE; P38418; -.
DR PaxDb; P38418; -.
DR PRIDE; P38418; -.
DR ProteomicsDB; 238417; -.
DR EnsemblPlants; AT3G45140.1; AT3G45140.1; AT3G45140.
DR GeneID; 823650; -.
DR Gramene; AT3G45140.1; AT3G45140.1; AT3G45140.
DR KEGG; ath:AT3G45140; -.
DR Araport; AT3G45140; -.
DR TAIR; locus:2096915; AT3G45140.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; P38418; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; P38418; -.
DR BioCyc; ARA:AT3G45140-MON; -.
DR BioCyc; MetaCyc:AT3G45140-MON; -.
DR BRENDA; 1.13.11.12; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:P38418; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P38418; baseline and differential.
DR Genevisible; P38418; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
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:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:TAIR.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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; 2.
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; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..896
FT /note="Lipoxygenase 2, chloroplastic"
FT /id="PRO_0000018326"
FT DOMAIN 79..199
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 202..896
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 175..232
FT /note="EIF4E2 binding"
FT BINDING 554
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 559
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 746
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 750
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 896
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 119..125
FT /note="ITVEDYA -> EYTFFFL (in Ref. 5; BAC43666)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="W -> C (in Ref. 4; AAL32689)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="L -> V (in Ref. 6; BAF01939)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="L -> F (in Ref. 6; BAF01939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 102046 MW; F32822205C8F9F22 CRC64;
MYCRESLSSL QTLNVAKSLS SLFPKQSALI NPISAGRRNN LPRPNLRRRC KVTASRANIE
QEGNTVKEPI QNIKVKGYIT AQEEFLEGIT WSRGLDDIAD IRGRSLLVEL ISAKTDQRIT
VEDYAQRVWA EAPDEKYECE FEMPEDFGPV GAIKIQNQYH RQLFLKGVEL KLPGGSITFT
CESWVAPKSV DPTKRIFFSD KSYLPSQTPE PLKKYRKEEL ETLQGKNREE VGEFTKFERI
YDYDVYNDVG DPDNDPELAR PVIGGLTHPY PRRCKTGRKP CETDPSSEQR YGGEFYVPRD
EEFSTAKGTS FTGKAVLAAL PSIFPQIESV LLSPQEPFPH FKAIQNLFEE GIQLPKDAGL
LPLLPRIIKA LGEAQDDILQ FDAPVLINRD RFSWLRDDEF ARQTLAGLNP YSIQLVEEWP
LISKLDPAVY GDPTSLITWE IVEREVKGNM TVDEALKNKR LFVLDYHDLL LPYVNKVREL
NNTTLYASRT LFFLSDDSTL RPVAIELTCP PNINKPQWKQ VFTPGYDATS CWLWNLAKTH
AISHDAGYHQ LISHWLRTHA CTEPYIIAAN RQLSAMHPIY RLLHPHFRYT MEINARARQS
LVNGGGIIET CFWPGKYALE LSSAVYGKLW RFDQEGLPAD LIKRGLAEED KTAEHGVRLT
IPDYPFANDG LILWDAIKEW VTDYVKHYYP DEELITSDEE LQGWWSEVRN IGHGDKKDEP
WWPVLKTQDD LIGVVTTIAW VTSGHHAAVN FGQYGYGGYF PNRPTTTRIR MPTEDPTDEA
LKEFYESPEK VLLKTYPSQK QATLVMVTLD LLSTHSPDEE YIGEQQEASW ANEPVINAAF
ERFKGKLQYL EGVIDERNVN ITLKNRAGAG VVKYELLKPT SEHGVTGMGV PYSISI
