ID   A0A341ASR6_NEOAA        Unreviewed;       663 AA.
AC   A0A341ASR6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JUL-2024, entry version 24.
DE   RecName: Full=Polyunsaturated fatty acid lipoxygenase ALOX15 {ECO:0000256|ARBA:ARBA00040850};
DE            EC=1.13.11.12 {ECO:0000256|ARBA:ARBA00038988};
DE            EC=1.13.11.31 {ECO:0000256|ARBA:ARBA00038997};
DE            EC=1.13.11.33 {ECO:0000256|ARBA:ARBA00038998};
DE   AltName: Full=12/15-lipoxygenase {ECO:0000256|ARBA:ARBA00042534};
DE   AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type {ECO:0000256|ARBA:ARBA00041889};
DE   AltName: Full=Arachidonate 15-lipoxygenase {ECO:0000256|ARBA:ARBA00043170};
DE   AltName: Full=Arachidonate omega-6 lipoxygenase {ECO:0000256|ARBA:ARBA00043163};
DE   AltName: Full=Hepoxilin A3 synthase Alox15 {ECO:0000256|ARBA:ARBA00041403};
DE   AltName: Full=Linoleate 13S-lipoxygenase {ECO:0000256|ARBA:ARBA00041853};
GN   Name=ALOX15 {ECO:0000313|RefSeq:XP_024592292.1};
OS   Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS   (Neophocaena phocaenoides subsp. asiaeorientalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Phocoenidae; Neophocaena.
OX   NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024592292.1};
RN   [1] {ECO:0000313|RefSeq:XP_024592292.1}
RP   IDENTIFICATION.
RC   TISSUE=Meat {ECO:0000313|RefSeq:XP_024592292.1};
RG   RefSeq;
RL   Submitted (APR-2024) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8S)-
CC         hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50216, ChEBI:CHEBI:57444, ChEBI:CHEBI:132129;
CC         Evidence={ECO:0000256|ARBA:ARBA00036803};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50217;
CC         Evidence={ECO:0000256|ARBA:ARBA00036803};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-
CC         hydroperoxy-(14R,15S)-epoxy-(5Z,8Z,10E)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50276, ChEBI:CHEBI:15379, ChEBI:CHEBI:131965,
CC         ChEBI:CHEBI:132063; Evidence={ECO:0000256|ARBA:ARBA00036582};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50277;
CC         Evidence={ECO:0000256|ARBA:ARBA00036582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (5S)-
CC         hydroperoxy-(14R,15S)-epoxy-(6E,8Z,11Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50280, ChEBI:CHEBI:15379, ChEBI:CHEBI:131965,
CC         ChEBI:CHEBI:132067; Evidence={ECO:0000256|ARBA:ARBA00036208};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50281;
CC         Evidence={ECO:0000256|ARBA:ARBA00036208};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-
CC         hydroperoxy-(14S,15R)-epoxy-(5Z,8Z,10E)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50284, ChEBI:CHEBI:15379, ChEBI:CHEBI:131964,
CC         ChEBI:CHEBI:132065; Evidence={ECO:0000256|ARBA:ARBA00036149};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50285;
CC         Evidence={ECO:0000256|ARBA:ARBA00036149};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (8S)-
CC         hydroperoxy-(14S,15R)-epoxy-(5Z,9E,11Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50288, ChEBI:CHEBI:15379, ChEBI:CHEBI:131964,
CC         ChEBI:CHEBI:132068; Evidence={ECO:0000256|ARBA:ARBA00035753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50289;
CC         Evidence={ECO:0000256|ARBA:ARBA00035753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC         (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:50152,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:82626;
CC         Evidence={ECO:0000256|ARBA:ARBA00035941};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50153;
CC         Evidence={ECO:0000256|ARBA:ARBA00035941};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate =
CC         (14S,15S)-epoxy-(5Z,8Z,10E,12E)-eicosatetraenoate + H2O;
CC         Xref=Rhea:RHEA:50140, ChEBI:CHEBI:15377, ChEBI:CHEBI:57446,
CC         ChEBI:CHEBI:132070; Evidence={ECO:0000256|ARBA:ARBA00036658};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50141;
CC         Evidence={ECO:0000256|ARBA:ARBA00036658};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 = 14-hydroperoxy-
CC         (4Z,7Z,10Z,12E,16Z)-docosapentaenoate; Xref=Rhea:RHEA:50824,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:77226, ChEBI:CHEBI:133799;
CC         Evidence={ECO:0000256|ARBA:ARBA00036369};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50825;
CC         Evidence={ECO:0000256|ARBA:ARBA00036369};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (11S)-
CC         hydroperoxy-(4Z,7Z,9E,13Z,16Z,19Z)-docosahexaenoate;
CC         Xref=Rhea:RHEA:64732, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC         ChEBI:CHEBI:156131; Evidence={ECO:0000256|ARBA:ARBA00036202};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64733;
CC         Evidence={ECO:0000256|ARBA:ARBA00036202};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-
CC         hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate;
CC         Xref=Rhea:RHEA:41332, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC         ChEBI:CHEBI:78048; Evidence={ECO:0000256|ARBA:ARBA00036495};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41333;
CC         Evidence={ECO:0000256|ARBA:ARBA00036495};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-
CC         hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate;
CC         Xref=Rhea:RHEA:50840, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC         ChEBI:CHEBI:133795; Evidence={ECO:0000256|ARBA:ARBA00035958};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50841;
CC         Evidence={ECO:0000256|ARBA:ARBA00035958};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (14R,15S)-
CC         dihydroperoxy-(5Z,8Z,10E,12E)-eicosatetraenoate;
CC         Xref=Rhea:RHEA:50928, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:133900; Evidence={ECO:0000256|ARBA:ARBA00036568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50929;
CC         Evidence={ECO:0000256|ARBA:ARBA00036568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (8S,15S)-
CC         dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate;
CC         Xref=Rhea:RHEA:50924, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:133899; Evidence={ECO:0000256|ARBA:ARBA00036449};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50925;
CC         Evidence={ECO:0000256|ARBA:ARBA00036449};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2
CC         = (7S,14S)-dihydroperoxy-(4Z,8E,10Z,12E,16Z,19Z)-docosahexaenoate;
CC         Xref=Rhea:RHEA:64724, ChEBI:CHEBI:15379, ChEBI:CHEBI:156049,
CC         ChEBI:CHEBI:156082; Evidence={ECO:0000256|ARBA:ARBA00035888};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64725;
CC         Evidence={ECO:0000256|ARBA:ARBA00035888};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2
CC         = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoate;
CC         Xref=Rhea:RHEA:64728, ChEBI:CHEBI:15379, ChEBI:CHEBI:140349,
CC         ChEBI:CHEBI:156049; Evidence={ECO:0000256|ARBA:ARBA00036949};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64729;
CC         Evidence={ECO:0000256|ARBA:ARBA00036949};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 = 14-hydroperoxy-
CC         (7Z,10Z,12E,16Z,19Z)-docosapentaenoate; Xref=Rhea:RHEA:50836,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:77224, ChEBI:CHEBI:133798;
CC         Evidence={ECO:0000256|ARBA:ARBA00036752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50837;
CC         Evidence={ECO:0000256|ARBA:ARBA00036752};
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:0000256|ARBA:ARBA00035889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781;
CC         Evidence={ECO:0000256|ARBA:ARBA00035889};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(12S)-
CC         hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-alanine;
CC         Xref=Rhea:RHEA:50172, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071,
CC         ChEBI:CHEBI:132074; Evidence={ECO:0000256|ARBA:ARBA00035947};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50173;
CC         Evidence={ECO:0000256|ARBA:ARBA00035947};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-
CC         hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanine;
CC         Xref=Rhea:RHEA:50184, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071,
CC         ChEBI:CHEBI:132077; Evidence={ECO:0000256|ARBA:ARBA00036420};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50185;
CC         Evidence={ECO:0000256|ARBA:ARBA00036420};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 =
CC         N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-gamma-
CC         aminobutanoate; Xref=Rhea:RHEA:50176, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:132072, ChEBI:CHEBI:132075;
CC         Evidence={ECO:0000256|ARBA:ARBA00036852};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50177;
CC         Evidence={ECO:0000256|ARBA:ARBA00036852};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 =
CC         N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-gamma-
CC         aminobutanoate; Xref=Rhea:RHEA:50180, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:132072, ChEBI:CHEBI:132078;
CC         Evidence={ECO:0000256|ARBA:ARBA00035867};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50181;
CC         Evidence={ECO:0000256|ARBA:ARBA00035867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(12S)-
CC         hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-glycine;
CC         Xref=Rhea:RHEA:50168, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002,
CC         ChEBI:CHEBI:132073; Evidence={ECO:0000256|ARBA:ARBA00036768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50169;
CC         Evidence={ECO:0000256|ARBA:ARBA00036768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-
CC         hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycine;
CC         Xref=Rhea:RHEA:50188, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002,
CC         ChEBI:CHEBI:132076; Evidence={ECO:0000256|ARBA:ARBA00036165};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50189;
CC         Evidence={ECO:0000256|ARBA:ARBA00036165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(12S)-
CC         hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-taurine;
CC         Xref=Rhea:RHEA:50160, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060,
CC         ChEBI:CHEBI:132061; Evidence={ECO:0000256|ARBA:ARBA00036438};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50161;
CC         Evidence={ECO:0000256|ARBA:ARBA00036438};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-
CC         hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurine;
CC         Xref=Rhea:RHEA:50156, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060,
CC         ChEBI:CHEBI:132062; Evidence={ECO:0000256|ARBA:ARBA00036945};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50157;
CC         Evidence={ECO:0000256|ARBA:ARBA00036945};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601885-1};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR601885-1};
CC   -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00037897}.
CC   -!- SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13,
CC       prevents the interaction of PEBP1 with RAF1 to activate the ERK
CC       signaling cascade. {ECO:0000256|ARBA:ARBA00038731}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC       cytosol {ECO:0000256|ARBA:ARBA00004514}. Lipid droplet
CC       {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|RuleBase:RU003974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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   RefSeq; XP_024592292.1; XM_024736524.1.
DR   STRING; 1706337.A0A341ASR6; -.
DR   KEGG; nasi:112394032; -.
DR   InParanoid; A0A341ASR6; -.
DR   OrthoDB; 999249at2759; -.
DR   Proteomes; UP000252040; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004052; F:arachidonate 12(S)-lipoxygenase activity; IEA:UniProt.
DR   GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IEA:TreeGrafter.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProt.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IEA:TreeGrafter.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0019372; P:lipoxygenase pathway; IEA:UniProt.
DR   CDD; cd01753; PLAT_LOX; 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; IPR020833; LipOase_Fe_BS.
DR   InterPro; IPR001885; LipOase_mml.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR042062; PLAT_LOX_verte.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF33; POLYUNSATURATED FATTY ACID LIPOXYGENASE ALOX15; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00467; MAMLPOXGNASE.
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; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601885-2};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601885-1};
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601885-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252040}.
FT   DOMAIN          2..115
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          115..663
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         361
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         366
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         663
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   SITE            100
FT                   /note="Essential for stabilizing binding to COTL1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ   SEQUENCE   663 AA;  75005 MW;  C5A301355200191C CRC64;
     MGLYRVRASS GSSLCAGSNN KVQLWLVGQH GEVALGWRVR PMRGKEAEFE VDVSEYLGPL
     LFVKLSKWHL LQDDAWFCNW ISVQGPGASG DQFRFPCYRW LEGKGILSLP EGTGRTVVDD
     PQGLFKKHRE EEPEERRKLY WWGNWKDELI LNMAGATICD LPTDERFLED KRIDFEASLV
     KGLADLAIKD SSNILTSWNS LDDFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGSNPM
     LLRCSNHLPA RLEFPPGMEE LQAQLEKELQ GGTLFEADVS LLDGIKANVI LCSQQYLAAP
     LVMLKLQPDG KLLPMVIQLQ LPCKGSLPPL LFLPMDPPMA WLLAKCWVRS SDFQLHELQS
     HLLRGHLVAE VIAVATVRCL PSIHPMFKLL ILHIRYTTEI NLRARTGLVA DLGIFDQVVS
     TGGGGHVDLF KRAGAFLTYS SFCXPDDLAE RGLLGVKSPF YVQDALRLWE IISHYVEGIV
     SLHYKTDKSV KEDLELQAWC XEITEIGLLG AQDRGFPIAL QSKDQLCHFX TTCIFTCTGQ
     YSSNHLDQLD WYAWVPNAPC TMRLPLPTTK DVTLETAMAT LPNFHQASLQ MSITWQLGRR
     QSIMVALDQH EEEYFSGPEP KAALKKFREE LAALEKGIEI WNAKLDLPYE YLWPSLVENS
     VAI
//