{"metadata":{"accession":"Q9WV07","id":"LOXE3_MOUSE","source_organism":{"taxId":"10090","scientificName":"Mus musculus","fullName":"Mus musculus (Mouse)"},"name":"Hydroperoxide isomerase ALOXE3","description":["Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity (PubMed:17045234). The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones (PubMed:17045234). 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 (By similarity). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:22832496). In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (PubMed:20530198). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (By similarity)"],"length":711,"sequence":"MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFASGSVQKYKVRCEAELGEILLLRLHKERFAFFCKDPWYCSRICVTAPDGSAVHFPCYQWIDGYCTVELRPGTARTICQDSLPLLLDHRKRELQARQECYRWKIFAPGFPRMVDVSSFQEMESDKKFALTKTVPCAEQDDNSGNRYLPGFPMKIDIPSLLHMEPNIRYSATKTASLIFNALPASFGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPVMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCINGLQQYVTAPLCLLWLNPQGVLLPLAIQLSQTPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRQGLIYLMSTGLAHFTYTDFCLPDSIRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPSDASVQQDCELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGDTTMKSYLDTLPEVNTTCRNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQNCLAQISKDIRERNQSLALPYAYLDPPLIENSVSI","proteome":"UP000000589","gene":"Aloxe3","go_terms":[{"identifier":"GO:0005515","name":"protein binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0016702","name":"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0046872","name":"metal ion binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0034440","name":"lipid oxidation","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0005506","name":"iron ion binding","category":{"code":"F","name":"molecular_function"}}],"protein_evidence":1,"source_database":"reviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"5ebc5f3429d72c7e8ce2bc55a89d35e7644e0f31","counters":{"domain_architectures":10307,"entries":25,"isoforms":0,"proteomes":1,"sets":2,"structures":0,"taxa":1,"dbEntries":{"ssf":2,"cathgene3d":3,"smart":1,"cdd":1,"profile":2,"pfam":2,"panther":1,"prosite":2,"prints":2,"interpro":9},"proteome":1,"taxonomy":1,"similar_proteins":10307}}}