ALOXE3
entrez
59344
canonical
uniprot
Q9BYJ1
canonical
ensembl
ENSG00000179148
resolver
ensp
ENSP00000400581
resolver
ensp
ENSP00000519433
resolver
enst
ENST00000714144
resolver
genesymbol
ALOXE3
resolver
hgnc
HGNC:13743
resolver
uniprot
A0AAQ5BHH1
resolver
uniprot
B2R981
resolver
uniprot
B7Z3W0
resolver
uniprot
Q3ZB74
resolver
uniprot
Q9H4F2
resolver
uniprot
Q9HC22
resolver
uniprot_entry
A0AAQ5BHH1_HUMAN
resolver
uniprot_entry
LOXE3_HUMAN
resolver
uniprot_sec
B2R981
resolver
uniprot_sec
B7Z3W0
resolver
uniprot_sec
Q3ZB74
resolver
uniprot_sec
Q9H4F2
resolver
uniprot_sec
Q9HC22
resolver
activity_regulation
ACTIVITY REGULATION: Lipoxygenase activity is activated by 13(S)-HPODE leading to an active free ferric enzyme (PubMed:20921226). The lipoxygenase and hydroperoxide isomerase activities are in competition and are reciprocally regulated by oxygen (PubMed:20923767). The oxygen reacts with an epoxyallylic radical intermediate leading to an epoxyallylic peroxyl radical, which, due to its limited reactivity within the enzyme active site, it dissociates and leaves the enzyme in the activated free ferric state (PubMed:20923767). {ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767}.
uniprot
proteins
amino_acid_sequence
MAVYRLCVTTGPYLRAGTLDNISVTLVGTCGESPKQRLDRMGRDFAPGSVQKYKVRCTAELGELLLLRVHKERYAFFRKDSWYCSRICVTEPDGSVSHFPCYQWIEGYCTVELRPGTARTICQDSLPLLLDHRTRELRARQECYRWKIYAPGFPCMVDVNSFQEMESDKKFALTKTTTCVDQGDSSGNRYLPGFPMKIDIPSLMYMEPNVRYSATKTISLLFNAIPASLGMKLRGLLDRKGSWKKLDDMQNIFWCHKTFTTKYVTEHWCEDHFFGYQYLNGVNPVMLHCISSLPSKLPVTNDMVAPLLGQDTCLQTELERGNIFLADYWILAEAPTHCLNGRQQYVAAPLCLLWLSPQGALVPLAIQLSQTPGPDSPIFLPTDSEWDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFAMATLRQLPLCHPIYKLLLPHTRYTLQVNTIARATLLNPEGLVDQVTSIGRQGLIYLMSTGLAHFTYTNFCLPDSLRARGVLAIPNYHYRDDGLKIWAAIESFVSEIVGYYYPSDASVQQDSELQAWTGEIFAQAFLGRESSGFPSRLCTPGEMVKFLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGTTTLKTYLDTLPEVNISCNNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRRSIAAFQSRLAQISRDIQERNQGLALPYTYLDPPLIENSVSI
uniprot
proteins
disease_involvement
DISEASE: Ichthyosis, congenital, autosomal recessive 3 (ARCI3) [MIM:606545]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:11773004, ECO:0000269|PubMed:15629692, ECO:0000269|PubMed:16116617, ECO:0000269|PubMed:19131948, ECO:0000269|PubMed:19890349}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
4.2.1.152
uniprot
proteins
ec_number
5.4.4.7
uniprot
proteins
function
FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity (PubMed:12881489, PubMed:17045234, PubMed:20921226, PubMed:20923767). The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones (PubMed:12881489, PubMed:17045234, PubMed:20923767). In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides (PubMed:20921226). 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 (PubMed:21558561). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:21558561). In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (PubMed:21558561). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (By similarity). {ECO:0000250|UniProtKB:D3ZKX9, ECO:0000250|UniProtKB:Q9WV07, ECO:0000269|PubMed:12881489, ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767, ECO:0000269|PubMed:21558561}.
uniprot
proteins
mass_dalton
80543
uniprot
proteins
mutagenesis
MUTAGEN 451; /note="A->G: Increases the O2-dependent dioxygenase activity."; /evidence="ECO:0000269|PubMed:20921226, ECO:0000269|PubMed:20923767
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:12881489}.; PATHWAY: Lipid metabolism; sphingolipid metabolism.
uniprot
proteins
protein_family
Lipoxygenase family
uniprot
proteins
pubmed
11350124
uniprot
proteins
pubmed
11773004
uniprot
proteins
pubmed
12881489
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15629692
uniprot
proteins
pubmed
16116617
uniprot
proteins
pubmed
17045234
uniprot
proteins
pubmed
19131948
uniprot
proteins
pubmed
19890349
uniprot
proteins
pubmed
20921226
uniprot
proteins
pubmed
20923767
uniprot
proteins
pubmed
21558561
uniprot
proteins
sequence_length
711
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
uniprot
proteins