Alox8
entrez
11688
canonical
uniprot
O35936
canonical
ensembl
ENSMUSG00000020891
resolver
ensp
ENSMUSP00000021262
resolver
enst
ENSMUST00000021262
resolver
genesymbol
Alox8
resolver
genesymbol_syn
Alox15b
resolver
uniprot
B1ASX5
resolver
uniprot_entry
ALOX8_MOUSE
resolver
uniprot_sec
B1ASX5
resolver
amino_acid_sequence
MAKCRVRVSTGEACGAGTWDKVSVSIVGTHGESPLVPLDHLGKEFSAGAEEDFEVTLPQDVGTVLMLRVHKAPPEVSLPLMSFRSDAWFCRWFELEWLPGAALHFPCYQWLEGAGELVLREGAAKVSWQDHHPTLQDQRQKELESRQKMYSWKTYIEGWPRCLDHETVKDLDLNIKYSAMKNAKLFFKAHSAYTELKVKGLLDRTGLWRSLREMRRLFNFRKTPAAEYVFAHWQEDAFFASQFLNGINPVLIRRCHSLPNNFPVTDEMVAPVLGPGTSLQAELEKGSLFLVDHGILSGVHTNILNGKPQFSAAPMTLLHQSSGSGPLLPIAIQLKQTPGPDNPIFLPSDDTWDWLLAKTWVRNSEFYIHEAVTHLLHAHLIPEVFALATLRQLPRCHPLFKLLIPHIRYTLHINTLARELLVAPGKLIDKSTGLGTGGFSDLIKRNMEQLNYSVLCLPEDIRARGVEDIPGYYYRDDGMQIWGAIKSFVSEIVSIYYPSDTSVQDDQELQAWVREIFSEGFLGRESSGMPSLLDTREALVQYITMVIFTCSAKHAAVSSGQFDSCVWMPNLPPTMQLPPPTSKGQARPESFIATLPAVNSSSYHIIALWLLSAEPGDQRPLGHYPDEHFTEDAPRRSVAAFQRKLIQISKGIRERNRGLALPYTYLDPPLIENSVSI
uniprot
proteins
ec_number
1.13.11.-
uniprot
proteins
ec_number
1.13.11.58
uniprot
proteins
function
FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:10625675, PubMed:10965849, PubMed:15558016, PubMed:16112079, PubMed:16143298, PubMed:27435673, PubMed:9305900). Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively (PubMed:10625675, PubMed:10965849, PubMed:15558016, PubMed:16112079, PubMed:16143298, PubMed:27435673, PubMed:9305900). In addition to generate (8S)-HPETE from free arachidonic acid (AA), may produce other HETE isomers from phospholipid-esterified polyunsaturated fatty acids and minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE (PubMed:16112079, PubMed:16143298, PubMed:27435673). With free arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity (PubMed:10625675, PubMed:10965849, PubMed:15558016, PubMed:16112079, PubMed:16143298, PubMed:9305900). However may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE and when oxidizes directly arachidonic acid esterified to membrane-bound phospholipids to produce a phospholipid-esterified 15-HpETE (PubMed:16112079, PubMed:16143298, PubMed:27435673). May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE (PubMed:16112079). May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway (PubMed:10965849). {ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:10965849, ECO:0000269|PubMed:15558016, ECO:0000269|PubMed:16112079, ECO:0000269|PubMed:16143298, ECO:0000269|PubMed:27435673, ECO:0000269|PubMed:9305900}.
uniprot
proteins
mass_dalton
76230
uniprot
proteins
mutagenesis
MUTAGEN 374; /note="H->L: Loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:16143298"; MUTAGEN 558; /note="S->A,H,N: Retains catalytic activity indicating it is not required for iron ligand-binding."; /evidence="ECO:0000269|PubMed:11368335"; MUTAGEN 603; /note="Y->D: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with V-604."; /evidence="ECO:0000269|PubMed:10625675"; MUTAGEN 604; /note="H->V: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with D-603."; /evidence="ECO:0000269|PubMed:10625675
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:9305900}.
uniprot
proteins
protein_family
Lipoxygenase family
uniprot
proteins
pubmed
10625675
uniprot
proteins
pubmed
10965849
uniprot
proteins
pubmed
11368335
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15558016
uniprot
proteins
pubmed
16112079
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16143298
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
27435673
uniprot
proteins
pubmed
9305900
uniprot
proteins
pubmed
9518531
uniprot
proteins
sequence_length
677
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15296}. Membrane {ECO:0000250|UniProtKB:O15296}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15296}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. {ECO:0000250|UniProtKB:O15296}.
uniprot
proteins