LX15B_RAT
ID LX15B_RAT Reviewed; 677 AA.
AC Q8K4F2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Polyunsaturated fatty acid lipoxygenase ALOX15B {ECO:0000305};
DE AltName: Full=15-lipoxygenase 2 {ECO:0000250|UniProtKB:O15296};
DE Short=15-LOX-2 {ECO:0000250|UniProtKB:O15296};
DE AltName: Full=Arachidonate 15-lipoxygenase B;
DE Short=15-LOX-B;
DE EC=1.13.11.33 {ECO:0000269|PubMed:23382512};
DE AltName: Full=Arachidonate 15-lipoxygenase type II;
DE AltName: Full=Linoleate 13-lipoxygenase 15-LOb;
DE EC=1.13.11.- {ECO:0000269|PubMed:23382512};
GN Name=Alox15b {ECO:0000312|RGD:628809};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boeglin W.E., Schneider C., Brash A.R.;
RT "A 15-lipoxygenase in the rat, homolog of human 15-lipoxygenase-2 and mouse
RT 8-lipoxygenase.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23382512; DOI=10.1096/fj.12-217414;
RA Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C.,
RA Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L.,
RA Yaksh T.L., Dennis E.A.;
RT "Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical
RT role for spinal eLOX3 hepoxilin synthase activity in inflammatory
RT hyperalgesia.";
RL FASEB J. 27:1939-1949(2013).
CC -!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the
CC stereo-specific peroxidation of free and esterified polyunsaturated
CC fatty acids (PUFAs) generating a spectrum of bioactive lipid mediators
CC (PubMed:23382512). Inserts a peroxyl group at C15 of arachidonate
CC ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing (15S)-
CC hydroperoxyeicosatetraenoate/(15S)-HPETE (PubMed:23382512). Also
CC peroxidizes linoleate ((9Z,12Z)-octadecadienoate) to 13-
CC hydroperoxyoctadecadienoate/13-HPODE (PubMed:23382512). Oxygenates
CC arachidonyl derivatives such as 2-arachidonoylglycerol (2-AG) leading
CC to the production and extracellular release of 15-
CC hydroxyeicosatetraenoyl glycerol (15-HETE-G) that acts as a peroxisome
CC proliferator-activated receptor alpha agonist.Has the ability to
CC efficiently class-switch ALOX5 pro-inflammatory mediators into anti-
CC inflammatory intermediates. Participates in the sequential oxidations
CC of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate
CC specialized pro-resolving mediators (SPMs) resolvin D5 ((7S,17S)-
CC diHPDHA), which can actively down-regulate the immune response and have
CC anti-aggregation properties with platelets. In addition to free PUFAs
CC hydrolyzed from phospholipids, it directly oxidizes PUFAs esterified to
CC membrane-bound phospholipids. Has no detectable 8S-lipoxygenase
CC activity on arachidonate but reacts with (8S)-HPETE to produce
CC (8S,15S)-diHPETE. May regulate progression through the cell cycle and
CC cell proliferation. May also regulate cytokine secretion by macrophages
CC and therefore play a role in the immune response. May also regulate
CC macrophage differentiation into proatherogenic foam cells (By
CC similarity). {ECO:0000250|UniProtKB:O15296,
CC ECO:0000269|PubMed:23382512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:16869,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57446;
CC EC=1.13.11.33; Evidence={ECO:0000269|PubMed:23382512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16870;
CC Evidence={ECO:0000305|PubMed:23382512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = 13-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:48848, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:90823;
CC Evidence={ECO:0000269|PubMed:23382512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48849;
CC Evidence={ECO:0000305|PubMed:23382512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-
CC hydroxy-(15S)-hydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate;
CC Xref=Rhea:RHEA:53660, ChEBI:CHEBI:15379, ChEBI:CHEBI:90632,
CC ChEBI:CHEBI:137546; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53661;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 5-hydroperoxy-
CC (6E,8Z,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:48844,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:90822;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48845;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S,6R)-dihydroxy-(7E,9E,11Z,14Z)-eicosatetraenoate + O2 =
CC (5S,6R)-dihydroxy-(15S)-hydroperoxy-(7E,9E,11Z,13E)-
CC eicosatetraenoate; Xref=Rhea:RHEA:53656, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:137542, ChEBI:CHEBI:137547;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53657;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 =
CC (5S,15S)-dihydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate;
CC Xref=Rhea:RHEA:53652, ChEBI:CHEBI:15379, ChEBI:CHEBI:57450,
CC ChEBI:CHEBI:137543; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53653;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[15(S)-
CC hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-glycerol;
CC Xref=Rhea:RHEA:53332, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392,
CC ChEBI:CHEBI:137187; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53333;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 =
CC (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate;
CC Xref=Rhea:RHEA:50932, ChEBI:CHEBI:15379, ChEBI:CHEBI:75322,
CC ChEBI:CHEBI:133899; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50933;
CC Evidence={ECO:0000250|UniProtKB:O15296};
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:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50185;
CC Evidence={ECO:0000250|UniProtKB:O15296};
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:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50181;
CC Evidence={ECO:0000250|UniProtKB:O15296};
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:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50189;
CC Evidence={ECO:0000250|UniProtKB:O15296};
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:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50157;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[12-
CC hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl]-glycerol;
CC Xref=Rhea:RHEA:63224, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392,
CC ChEBI:CHEBI:146254; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63225;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-
CC 5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:63264, ChEBI:CHEBI:15379, ChEBI:CHEBI:74965,
CC ChEBI:CHEBI:146283; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63265;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phospho-(1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-
CC 5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol); Xref=Rhea:RHEA:63276, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:75243, ChEBI:CHEBI:146285;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63277;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phospho-
CC (1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-8Z,11Z,13E-
CC eicosatrienoyl)-sn-glycero-3-phospho-(1D-myo-inositol);
CC Xref=Rhea:RHEA:63280, ChEBI:CHEBI:15379, ChEBI:CHEBI:146286,
CC ChEBI:CHEBI:146287; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63281;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phosphoethanolamine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-
CC 5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:63268, ChEBI:CHEBI:15379, ChEBI:CHEBI:78268,
CC ChEBI:CHEBI:146282; Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63269;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + O2 = 1-octadecanoyl-2-(15-hydroperoxy-
CC 5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol); Xref=Rhea:RHEA:63272, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:133606, ChEBI:CHEBI:146284;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63273;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = 15-hydroperoxy-
CC (8Z,11Z,13E)-eicosatrienoate; Xref=Rhea:RHEA:63312,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:146292;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63313;
CC Evidence={ECO:0000250|UniProtKB:O15296};
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:0000250|UniProtKB:O15296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64729;
CC Evidence={ECO:0000250|UniProtKB:O15296};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:O15296,
CC ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:O15296,
CC ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
CC biosynthesis. {ECO:0000269|PubMed:23382512}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O15296}. Cell membrane
CC {ECO:0000250|UniProtKB:O15296}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O15296}. Membrane
CC {ECO:0000250|UniProtKB:O15296}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O15296}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O15296}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O15296}. Nucleus {ECO:0000250|UniProtKB:O15296}.
CC Note=Predominantly cytosolic; becomes enriched at membranes upon
CC calcium binding. {ECO:0000250|UniProtKB:O15296}.
CC -!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
CC association with membranes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AF415240; AAN03708.1; -; mRNA.
DR RefSeq; NP_695213.1; NM_153301.2.
DR AlphaFoldDB; Q8K4F2; -.
DR SMR; Q8K4F2; -.
DR STRING; 10116.ENSRNOP00000010416; -.
DR BindingDB; Q8K4F2; -.
DR ChEMBL; CHEMBL3289; -.
DR PhosphoSitePlus; Q8K4F2; -.
DR PaxDb; Q8K4F2; -.
DR GeneID; 266604; -.
DR KEGG; rno:266604; -.
DR UCSC; RGD:628809; rat.
DR CTD; 247; -.
DR RGD; 628809; Alox15b.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR InParanoid; Q8K4F2; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q8K4F2; -.
DR BRENDA; 1.13.11.33; 5301.
DR Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR UniPathway; UPA00881; -.
DR PRO; PR:Q8K4F2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0036403; F:arachidonate 8(S)-lipoxygenase activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; ISO:RGD.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; ISO:RGD.
DR GO; GO:0008289; F:lipid 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:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:1901696; P:cannabinoid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0071926; P:endocannabinoid signaling pathway; ISS:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:2001303; P:lipoxin A4 biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045926; P:negative regulation of growth; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISO:RGD.
DR CDD; cd01753; PLAT_LOX; 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; 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; PTHR11771; 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; 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 Calcium; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Dioxygenase; Iron; Lipid metabolism; Lipid-binding; Membrane;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..677
FT /note="Polyunsaturated fatty acid lipoxygenase ALOX15B"
FT /id="PRO_0000220702"
FT DOMAIN 2..125
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 126..677
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O15296"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 379
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
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 677
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 677 AA; 76145 MW; 49A47B47C491B8B1 CRC64;
MAKFRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE EDFEVTLPQD
VGTVLMLRIH KAPPEAPLPL LSFPPDAWYC RWFELEWLPG AALRFPCYQW LEGAGELVLR
EGAAKVSWQD HHRTLQDQRQ KELESRKDMY SWKTYIEGWP HCLDHETVKD LDLNIKYSAM
KNAKFFFKAQ SAFTELKFKG LLDRTGLWRS LREMKRMFNF HNTPAAEYVF AHWQEDAFFA
SQFLNGLNPV LIRRCRRLPE NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVQ
TNVINGKPQF SAAPMTLLYQ SPGSGPLLPI AIQLKQTPGP DNPIFLPSDD KWDWLLAKTW
VRNAEFSIHE ALTHLLHAHL IPEVFALATL RQLPHCHPLF KLLIPHTRYT LHINTLAREL
LIAPGKVVDK STGLGIGGFS DLIKRNMEQL SYSVLCLPED IRARDVGDLP GYYYRDDGMQ
IWSAIRSFVS EIVDIYYPSD ASVRDDQELQ AWVGEIFSEG FLSQESSGMP SLLDTQEALV
QYVTMVIFTC SAKHAAVSAS QFDSCVWMPN LPPSMQLPPP TSKGQASPEG FIATLPAVNA
TCDVIIALWL LSKEPGDRRP LGHYPDEHFT EEVPRRSIAA FQRKLIQISS GIRKRNQSLA
LPYTYLDPPL IENSVSI
