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ALOXE3

Gene
ALOXE3
Protein
Hydroperoxide isomerase ALOXE3
Organism
Homo sapiens
Length
711 amino acids
Function
Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.
Similarity
Belongs to the lipoxygenase family.
Mass
80.543 kDa
Sequence
MAVYRLCVTTGPYLRAGTLDNISVTLVGTCGESPKQRLDRMGRDFAPGSVQKYKVRCTAELGELLLLRVHKERYAFFRKDSWYCSRICVTEPDGSVSHFPCYQWIEGYCTVELRPGTARTICQDSLPLLLDHRTRELRARQECYRWKIYAPGFPCMVDVNSFQEMESDKKFALTKTTTCVDQGDSSGNRYLPGFPMKIDIPSLMYMEPNVRYSATKTISLLFNAIPASLGMKLRGLLDRKGSWKKLDDMQNIFWCHKTFTTKYVTEHWCEDHFFGYQYLNGVNPVMLHCISSLPSKLPVTNDMVAPLLGQDTCLQTELERGNIFLADYWILAEAPTHCLNGRQQYVAAPLCLLWLSPQGALVPLAIQLSQTPGPDSPIFLPTDSEWDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFAMATLRQLPLCHPIYKLLLPHTRYTLQVNTIARATLLNPEGLVDQVTSIGRQGLIYLMSTGLAHFTYTNFCLPDSLRARGVLAIPNYHYRDDGLKIWAAIESFVSEIVGYYYPSDASVQQDSELQAWTGEIFAQAFLGRESSGFPSRLCTPGEMVKFLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGTTTLKTYLDTLPEVNISCNNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRRSIAAFQSRLAQISRDIQERNQGLALPYTYLDPPLIENSVSI

Gene
Aloxe3
Protein
Hydroperoxide isomerase ALOXE3
Organism
Mus musculus
Length
711 amino acids
Function
Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.
Similarity
Belongs to the lipoxygenase family.
Mass
80.473 kDa
Sequence
MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFASGSVQKYKVRCEAELGEILLLRLHKERFAFFCKDPWYCSRICVTAPDGSAVHFPCYQWIDGYCTVELRPGTARTICQDSLPLLLDHRKRELQARQECYRWKIFAPGFPRMVDVSSFQEMESDKKFALTKTVPCAEQDDNSGNRYLPGFPMKIDIPSLLHMEPNIRYSATKTASLIFNALPASFGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPVMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCINGLQQYVTAPLCLLWLNPQGVLLPLAIQLSQTPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRQGLIYLMSTGLAHFTYTDFCLPDSIRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPSDASVQQDCELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGDTTMKSYLDTLPEVNTTCRNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQNCLAQISKDIRERNQSLALPYAYLDPPLIENSVSI

Gene
Aloxe3
Protein
Hydroperoxide isomerase ALOXE3
Organism
Rattus norvegicus
Length
711 amino acids
Function
Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activates PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.
Similarity
Belongs to the lipoxygenase family.
Mass
80.44 kDa
Sequence
MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCLNGRQQYVTAPLCLLWLNPQGVLLPLAIQLSQIPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRRGLIYLMSTGLAHFTYTDFCLPDSLRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPNDACVQQDSELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGNTTMESYLETLPEVNTTCSNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQKCLAQISKDIRARNESLALPYAYLDPPLIENSVSI