LOXE3_MOUSE
ID LOXE3_MOUSE Reviewed; 711 AA.
AC Q9WV07; B1ASX3;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hydroperoxide isomerase ALOXE3 {ECO:0000305};
DE AltName: Full=Epidermis-type lipoxygenase 3 {ECO:0000303|PubMed:10366447};
DE Short=Epidermal LOX-3;
DE Short=e-LOX-3 {ECO:0000303|PubMed:10366447};
DE Short=eLOX-3;
DE AltName: Full=Hydroperoxy dehydratase ALOXE3 {ECO:0000305};
DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE EC=4.2.1.152 {ECO:0000269|PubMed:17045234};
DE AltName: Full=Hydroperoxy icosatetraenoate isomerase;
DE EC=5.4.4.7 {ECO:0000269|PubMed:17045234};
GN Name=Aloxe3 {ECO:0000312|MGI:MGI:1345140};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NMRI; TISSUE=Skin;
RX PubMed=10366447; DOI=10.1006/geno.1999.5816;
RA Kinzig A., Heidt M., Fuerstenberger G., Marks F., Krieg P.;
RT "cDNA cloning, genomic structure and chromosomal localization of a novel
RT epidermis-type lipoxygenase.";
RL Genomics 58:158-164(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION AS A HYDROPEROXIDE ISOMERASE, AND CATALYTIC ACTIVITY.
RX PubMed=17045234; DOI=10.1016/j.abb.2006.09.002;
RA Yu Z., Schneider C., Boeglin W.E., Brash A.R.;
RT "Human and mouse eLOX3 have distinct substrate specificities: implications
RT for their linkage with lipoxygenases in skin.";
RL Arch. Biochem. Biophys. 455:188-196(2006).
RN [5]
RP FUNCTION IN PPARG ACTIVATION.
RX PubMed=20530198; DOI=10.1128/mcb.01806-08;
RA Hallenborg P., Joergensen C., Petersen R.K., Feddersen S., Araujo P.,
RA Markt P., Langer T., Furstenberger G., Krieg P., Koppen A., Kalkhoven E.,
RA Madsen L., Kristiansen K.;
RT "Epidermis-type lipoxygenase 3 regulates adipocyte differentiation and
RT peroxisome proliferator-activated receptor gamma activity.";
RL Mol. Cell. Biol. 30:4077-4091(2010).
RN [6]
RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE.
RX PubMed=22832496; DOI=10.1038/jid.2012.250;
RA Krieg P., Rosenberger S., de Juanes S., Latzko S., Hou J., Dick A.,
RA Kloz U., van der Hoeven F., Hausser I., Esposito I., Rauh M., Schneider H.;
RT "Aloxe3 knockout mice reveal a function of epidermal lipoxygenase-3 as
RT hepoxilin synthase and its pivotal role in barrier formation.";
RL J. Invest. Dermatol. 133:172-180(2013).
CC -!- FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in
CC that it displays a prominent hydroperoxide isomerase activity and a
CC reduced lipoxygenases activity (PubMed:17045234). The hydroperoxide
CC isomerase activity catalyzes the isomerization of hydroperoxides,
CC derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-
CC type epoxyalcohols and ketones (PubMed:17045234). In presence of
CC oxygen, oxygenates polyunsaturated fatty acids, including arachidonic
CC acid, to produce fatty acid hydroperoxides. In the skin, acts
CC downstream of ALOX12B on the linoleate moiety of esterified omega-
CC hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone
CC derivative, a crucial step in the conjugation of omega-hydroxyceramide
CC to membrane proteins (By similarity). Therefore plays a crucial role in
CC the synthesis of corneocytes lipid envelope and the establishment of
CC the skin barrier to water loss (PubMed:22832496). In parallel, it may
CC have a signaling function in barrier formation through the production
CC of hepoxilins metabolites (By similarity). Also plays a role in
CC adipocyte differentiation through hepoxilin A3 and hepoxilin B3
CC production which in turn activate PPARG (PubMed:20530198). Through the
CC production of hepoxilins in the spinal cord, it may regulate
CC inflammatory tactile allodynia (By similarity).
CC {ECO:0000250|UniProtKB:D3ZKX9, ECO:0000250|UniProtKB:Q9BYJ1,
CC ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20530198,
CC ECO:0000269|PubMed:22832496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxyeicosatetraenoate = a hydroxy-epoxy-
CC eicosatetraenoate; Xref=Rhea:RHEA:55560, ChEBI:CHEBI:59720,
CC ChEBI:CHEBI:137328; EC=5.4.4.7;
CC Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55561;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = (10R)-
CC hydroxy-(8S,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:37931, ChEBI:CHEBI:75322, ChEBI:CHEBI:75327;
CC EC=5.4.4.7; Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37932;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-
CC hydroxy-(11R,12R)-epoxy-(5Z,9E,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:37939, ChEBI:CHEBI:75230, ChEBI:CHEBI:75232;
CC EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37940;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-
CC hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:37955, ChEBI:CHEBI:57444, ChEBI:CHEBI:75233;
CC EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37956;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (10R)-
CC hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:37951, ChEBI:CHEBI:57444, ChEBI:CHEBI:75234;
CC EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37952;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (13R)-
CC hydroxy-(14S,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:37959, ChEBI:CHEBI:57446, ChEBI:CHEBI:75235;
CC EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37960;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 11-hydroxy-
CC (12S,13S)-epoxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:50212,
CC ChEBI:CHEBI:57466, ChEBI:CHEBI:132064;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50213;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 7R-
CC hydroxy-5S,6S-epoxy-(8Z,11Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:41251, ChEBI:CHEBI:57450, ChEBI:CHEBI:77919;
CC Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41252;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-[omega-(9R)-hydroperoxy-(10E,12Z)-octadecadienoyloxy]acyl-
CC beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine = N-[omega-(9R,10R)-
CC epoxy-(13R)-hydroxy-(11E)-octadecadienoyloxy]acyl-beta-D-glucosyl-
CC (1<->1)-octadecasphing-4E-enine; Xref=Rhea:RHEA:40503,
CC ChEBI:CHEBI:134624, ChEBI:CHEBI:134626;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40504;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate
CC octadecasphing-4E-enine = N-acyl-(9R,10R)-epoxy-(13R)-hydroxy-(11E)-
CC octadecenoate (4E)-octadecasphin-4-enine; Xref=Rhea:RHEA:41243,
CC ChEBI:CHEBI:77889, ChEBI:CHEBI:77891;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41244;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate +
CC H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720,
CC ChEBI:CHEBI:131859; EC=4.2.1.152;
CC Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-
CC (5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37935,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57447, ChEBI:CHEBI:75326;
CC EC=4.2.1.152; Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37936;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-
CC (5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37927,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:75322, ChEBI:CHEBI:75326;
CC EC=4.2.1.152; Evidence={ECO:0000269|PubMed:17045234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37928;
CC Evidence={ECO:0000305|PubMed:17045234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37943,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:75230, ChEBI:CHEBI:75231;
CC EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37944;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
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; hydroperoxy eicosatetraenoic acid
CC biosynthesis. {ECO:0000269|PubMed:17045234}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q9BYJ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC -!- TISSUE SPECIFICITY: Skin specific.
CC -!- DISRUPTION PHENOTYPE: Mice die within 5 to 12 hours after birth due to
CC defective skin barrier function loosing around 2.5% of body weight per
CC hour. Dehydratation through the skin is increased 4 folds. The outside-
CC in barrier acquisition is also affected, the skin remaining permeable
CC at 18.5 dpc while it is impermeable in wild-type mice. The stratum
CC corneum is more tightly packed while other layers are unaffected.
CC Hyperkeratosis of the skin is observed but it is not associated with
CC defects in epidermal differentiation while the ceramide composition of
CC the epidermis is altered with an absence of ester-bound ceramides.
CC {ECO:0000269|PubMed:22832496}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; Y14695; CAB46101.1; -; mRNA.
DR EMBL; AL645527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466601; EDL10481.1; -; Genomic_DNA.
DR CCDS; CCDS24884.1; -.
DR RefSeq; NP_035916.2; NM_011786.2.
DR AlphaFoldDB; Q9WV07; -.
DR SMR; Q9WV07; -.
DR BioGRID; 204721; 1.
DR IntAct; Q9WV07; 1.
DR STRING; 10090.ENSMUSP00000021268; -.
DR SwissLipids; SLP:000000661; -.
DR iPTMnet; Q9WV07; -.
DR PhosphoSitePlus; Q9WV07; -.
DR PaxDb; Q9WV07; -.
DR PRIDE; Q9WV07; -.
DR ProteomicsDB; 291959; -.
DR Antibodypedia; 24534; 164 antibodies from 21 providers.
DR DNASU; 23801; -.
DR Ensembl; ENSMUST00000021268; ENSMUSP00000021268; ENSMUSG00000020892.
DR GeneID; 23801; -.
DR KEGG; mmu:23801; -.
DR UCSC; uc007jpj.2; mouse.
DR CTD; 59344; -.
DR MGI; MGI:1345140; Aloxe3.
DR VEuPathDB; HostDB:ENSMUSG00000020892; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR GeneTree; ENSGT00940000156796; -.
DR HOGENOM; CLU_004282_3_3_1; -.
DR InParanoid; Q9WV07; -.
DR OMA; LCEAFSM; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q9WV07; -.
DR TreeFam; TF105320; -.
DR BRENDA; 4.2.1.152; 3474.
DR BRENDA; 5.4.4.7; 3474.
DR Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00881; -.
DR BioGRID-ORCS; 23801; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Aloxe3; mouse.
DR PRO; PR:Q9WV07; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WV07; protein.
DR Bgee; ENSMUSG00000020892; Expressed in esophagus and 77 other tissues.
DR ExpressionAtlas; Q9WV07; baseline and differential.
DR Genevisible; Q9WV07; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; ISA:MGI.
DR GO; GO:0051120; F:hepoxilin A3 synthase activity; IDA:UniProtKB.
DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0106255; F:hydroperoxy icosatetraenoate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0050486; F:intramolecular transferase activity, transferring hydroxy groups; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:UniProtKB.
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 Cytoplasm; Dioxygenase; Fatty acid metabolism; Iron; Isomerase;
KW Lipid metabolism; Lyase; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..711
FT /note="Hydroperoxide isomerase ALOXE3"
FT /id="PRO_0000220692"
FT DOMAIN 2..119
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 120..711
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 408
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 413
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 588
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 592
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 711
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 138
FT /note="Q -> R (in Ref. 1; CAB46101)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="G -> S (in Ref. 1; CAB46101)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="V -> F (in Ref. 1; CAB46101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 80473 MW; 85A75EE2AFF3000E CRC64;
MAVYRLCVTT GSYLKAGTLD NIYATLVGTC GESPKQKLDR VGRDFASGSV QKYKVRCEAE
LGEILLLRLH KERFAFFCKD PWYCSRICVT APDGSAVHFP CYQWIDGYCT VELRPGTART
ICQDSLPLLL DHRKRELQAR QECYRWKIFA PGFPRMVDVS SFQEMESDKK FALTKTVPCA
EQDDNSGNRY LPGFPMKIDI PSLLHMEPNI RYSATKTASL IFNALPASFG MKIRGLLDRK
GSWKRLDDIR NIFWCHKTFT SEYVTEHWCE DSFFGYQYLN GVNPVMLHCL SSLPSKLPVT
NDMVAPLLGP GTCLQTELER GHIFLADYWI LAEAPVHCIN GLQQYVTAPL CLLWLNPQGV
LLPLAIQLSQ TPGPESPIFL PTDCELDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFS
MATLRQLPLC HPVYKLLLPH TRYTLQVNTI ARATLLNPDG LVDKVTSIGR QGLIYLMSTG
LAHFTYTDFC LPDSIRARGV LTIPNYHYRD DGLKIWAAIE RFVSEIVSYY YPSDASVQQD
CELQAWVGEI FAQAFLGRES SGFPSRLCTP GELVKYLTAI IFNCSAQHAA VNSGQHDFGA
WMPNAPSSMR QPPPQTKGDT TMKSYLDTLP EVNTTCRNLL LFWLVSQEPK DQRPLGTYPD
EHFTEEAPRQ SIAAFQNCLA QISKDIRERN QSLALPYAYL DPPLIENSVS I
