UniProtKB - P09917 (LOX5_HUMAN)
Polyunsaturated fatty acid 5-lipoxygenase
ALOX5
Functioni
Catalytic activityi
- EC:1.13.11.342 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 = (5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + O2 = (5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5S)-hydroperoxy-(18S)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5S)-hydroperoxy-(18R)-hydroxy-(6E,8Z,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2O1 Publication1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5S)-hydroperoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate = (5S,6S)-epoxy-18-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate7 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + O2 = (5S)-hydroperoxy-(15S)-hydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = 5-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate1 Publication1 PublicationThis reaction proceeds in the forward2 Publications direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
Cofactori
Activity regulationi
Kineticsi
- KM=13 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=11 µM for arachidonic acid1 Publication
- KM=1.9 µM for arachidonic acid1 Publication
- KM=14 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=5.3 µM for arachidonic acid (in the presence of 200 µM ATP)1 Publication
- KM=19 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (in the presence of 200 µM ATP)1 Publication
- KM=1.6 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid)1 Publication
- KM=4.5 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid in the presence of 200 µM ATP)1 Publication
- Vmax=1 µmol/min/mg enzyme toward arachidonic acid1 Publication
- Vmax=0.33 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- Vmax=4.9 µmol/min/mg enzyme toward arachidonic acid (in the presence of 200 µM ATP)1 Publication
- Vmax=1.6 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (in the presence of 200 µM ATP)1 Publication
- Vmax=0.1 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid)1 Publication
- Vmax=2 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid in the presence of 200 µM ATP)1 Publication
: leukotriene A4 biosynthesis Pathwayi
This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 17 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 18 | Calcium 2; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 19 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 44 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 45 | Calcium 2; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 47 | Calcium 2; structuralBy similarity | 1 | |
Metal bindingi | 79 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Metal bindingi | 80 | Calcium 1; via carbonyl oxygen; structuralBy similarity | 1 | |
Sitei | 103 | Essential for stabilizing binding to COTL11 Publication | 1 | |
Metal bindingi | 368 | Iron; via tele nitrogen; catalyticCombined sources2 Publications | 1 | |
Metal bindingi | 373 | Iron; via tele nitrogen; catalyticCombined sources2 Publications | 1 | |
Metal bindingi | 551 | Iron; via tele nitrogen; catalyticCombined sources2 Publications | 1 | |
Metal bindingi | 555 | Iron; catalyticCombined sources2 Publications | 1 | |
Metal bindingi | 674 | Iron; via carbonyl oxygen; catalyticCombined sources2 Publications | 1 |
GO - Molecular functioni
- arachidonate 5-lipoxygenase activity Source: UniProtKB
- hydrolase activity Source: UniProtKB-KW
- iron ion binding Source: UniProtKB
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: GO_Central
GO - Biological processi
- arachidonic acid metabolic process Source: GO_Central
- cytokine-mediated signaling pathway Source: Reactome
- dendritic cell migration Source: UniProtKB
- glucose homeostasis Source: UniProtKB
- hepoxilin biosynthetic process Source: GO_Central
- humoral immune response Source: UniProtKB
- interleukin-18-mediated signaling pathway Source: Reactome
- leukocyte chemotaxis involved in inflammatory response Source: UniProtKB
- leukocyte migration involved in inflammatory response Source: UniProtKB
- leukotriene A4 biosynthetic process Source: UniProtKB
- leukotriene biosynthetic process Source: UniProtKB
- leukotriene metabolic process Source: Reactome
- leukotriene production involved in inflammatory response Source: Ensembl
- linoleic acid metabolic process Source: GO_Central
- lipid oxidation Source: GO_Central
- lipoxin biosynthetic process Source: UniProtKB
- lipoxygenase pathway Source: GO_Central
- long-chain fatty acid biosynthetic process Source: Reactome
- negative regulation of angiogenesis Source: UniProtKB
- negative regulation of endothelial cell proliferation Source: UniProtKB
- negative regulation of inflammatory response Source: UniProtKB
- negative regulation of response to endoplasmic reticulum stress Source: UniProtKB
- negative regulation of sprouting angiogenesis Source: UniProtKB
- negative regulation of vascular wound healing Source: UniProtKB
- negative regulation of wound healing Source: UniProtKB
- neutrophil degranulation Source: Reactome
- positive regulation of bone mineralization Source: UniProtKB
- positive regulation of leukocyte adhesion to arterial endothelial cell Source: UniProtKB
- regulation of cellular response to oxidative stress Source: UniProtKB
- regulation of cytokine production involved in inflammatory response Source: UniProtKB
- regulation of fat cell differentiation Source: UniProtKB
- regulation of inflammatory response Source: UniProtKB
- regulation of inflammatory response to wounding Source: UniProtKB
- regulation of insulin secretion Source: UniProtKB
- regulation of reactive oxygen species biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Dioxygenase, Hydrolase, Oxidoreductase |
Biological process | Leukotriene biosynthesis |
Ligand | Calcium, Iron, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:HS00336-MONOMER |
BRENDAi | 1.13.11.34, 2681 |
PathwayCommonsi | P09917 |
Reactomei | R-HSA-2142688, Synthesis of 5-eicosatetraenoic acids R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-2142700, Synthesis of Lipoxins (LX) R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling R-HSA-6798695, Neutrophil degranulation R-HSA-9012546, Interleukin-18 signaling R-HSA-9018676, Biosynthesis of D-series resolvins R-HSA-9018682, Biosynthesis of maresins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins R-HSA-9026290, Biosynthesis of DPAn-3-derived maresins R-HSA-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins R-HSA-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives |
SABIO-RKi | P09917 |
SIGNORi | P09917 |
UniPathwayi | UPA00877 |
Chemistry databases
SwissLipidsi | SLP:000000669 |
Names & Taxonomyi
Protein namesi | Recommended name: Polyunsaturated fatty acid 5-lipoxygenaseCurated (EC:1.13.11.-1 Publication)Alternative name(s): Arachidonate 5-lipoxygenase (EC:1.13.11.341 Publication) Short name: 5-LO1 Publication Short name: 5-lipoxygenase1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000012779.10 |
HGNCi | HGNC:435, ALOX5 |
MIMi | 152390, gene |
neXtProti | NX_P09917 |
Subcellular locationi
Cytosol
- cytosol 1 Publication
Nucleus
- Nucleus matrix 1 Publication
- Nucleus membrane 1 Publication; Peripheral membrane protein 1 Publication
- Nucleus envelope 3 Publications
- Nucleus intermembrane space 1 Publication
Other locations
- Cytoplasm By similarity1 Publication
- perinuclear region 1 Publication
Note: Shuttles between cytoplasm and nucleus (PubMed:19233132). Found exclusively in the nucleus, when phosphorylated on Ser-272 (PubMed:18978352). Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association (PubMed:19233132, PubMed:3118366, PubMed:8245774, PubMed:16275640).5 Publications
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: UniProtKB
Nucleus
- nuclear envelope Source: UniProtKB
- nuclear envelope lumen Source: UniProtKB
- nuclear matrix Source: UniProtKB
- nuclear membrane Source: UniProtKB
- nucleoplasm Source: HPA
Other locations
- ficolin-1-rich granule lumen Source: Reactome
- perinuclear region of cytoplasm Source: UniProtKB
- secretory granule lumen Source: Reactome
Keywords - Cellular componenti
Cytoplasm, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 14 | W → A: Impairs interaction with DICER1; when associated with A-76 and A-103. 1 Publication | 1 | |
Mutagenesisi | 76 | W → A: Impairs interaction with DICER1; when associated with A-14 and A-103. 1 Publication | 1 | |
Mutagenesisi | 103 | W → A: Abolishes binding to COTL1. Impairs interaction with DICER; when associated with A-14 and A-76. 2 Publications | 1 | |
Mutagenesisi | 272 | S → A: Loss of phosphorylation site. Permits export from the nucleus. 1 Publication | 1 | |
Mutagenesisi | 359 | D → N: No loss of activity. | 1 | |
Mutagenesisi | 360 | F → W: Loss of (5S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of (5S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form mostly (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with I-425: M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with I-425: M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with I-425: M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with I-425: M-426 and I-604. 2 Publications | 1 | |
Mutagenesisi | 363 | H → S or N: Still some substantial activity. 1 Publication | 1 | |
Mutagenesisi | 368 | H → S, N or A: No activity. 2 Publications | 1 | |
Mutagenesisi | 373 | H → S or N: No activity. 2 Publications | 1 | |
Mutagenesisi | 377 | E → Q: No activity. 1 Publication | 1 | |
Mutagenesisi | 391 | H → A: No activity. 2 Publications | 1 | |
Mutagenesisi | 391 | H → S or N: Still some substantial activity. 2 Publications | 1 | |
Mutagenesisi | 400 | H → A: No activity. 2 Publications | 1 | |
Mutagenesisi | 400 | H → S or N: Still some substantial activity. 2 Publications | 1 | |
Mutagenesisi | 425 | A → I: Loss of (5S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of (5S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; M-426 and I-604. 2 Publications | 1 | |
Mutagenesisi | 426 | N → M: Loss of (5S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and I-425. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and I-604. 2 Publications | 1 | |
Mutagenesisi | 433 | H → N or A: Almost no loss of activity. | 1 | |
Mutagenesisi | 524 | S → A: Prevents phosphorylation by PKA. 1 Publication | 1 | |
Mutagenesisi | 551 | H → N or A: No activity. 1 Publication | 1 | |
Mutagenesisi | 604 | A → I: Loss of (5S)-lipoxygenase activity. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity;when associated with W-360; I-425 and M-426. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and M-426. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of linoleic acid to (13S)- and (9 S)-HODE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and M-426. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and M-426. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and M-426. 2 Publications | 1 | |
Mutagenesisi | 664 | S → A: Does not affect arachidonate 5-lipoxygenase activity. Does not oxygenate arachidonate typical 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine. 1 Publication | 1 | |
Mutagenesisi | 664 | S → D: Enhances affinity for arachidonic acid. Impairs arachidonate 5-lipoxygenase activity. Induces arachidonate 15-lipoxygenase activity. Oxygenates typical arachidonate 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine. Synthesizes lipoxin A4 when incubated with a stable 5-lipoxygenase. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 240 |
MalaCardsi | ALOX5 |
OpenTargetsi | ENSG00000012779 |
PharmGKBi | PA46 |
Miscellaneous databases
Pharosi | P09917, Tclin |
Chemistry databases
ChEMBLi | CHEMBL215 |
DrugBanki | DB14001, alpha-Tocopherol succinate DB00233, Aminosalicylic acid DB01014, Balsalazide DB09061, Cannabidiol DB14002, D-alpha-Tocopherol acetate DB11994, Diacerein DB00586, Diclofenac DB00711, Diethylcarbamazine DB12010, Fostamatinib DB01892, Hyperforin DB04725, Licofelone DB00179, Masoprocol DB00939, Meclofenamic acid DB14009, Medical Cannabis DB00244, Mesalazine DB01017, Minocycline DB05431, MLN-977 DB00471, Montelukast DB09285, Morniflumate DB14011, Nabiximols DB11133, Omega-3 fatty acids DB13168, Omega-6 fatty acids DB02709, Resveratrol DB13174, Rhein DB00795, Sulfasalazine DB00163, Vitamin E DB00744, Zileuton |
DrugCentrali | P09917 |
GuidetoPHARMACOLOGYi | 1385 |
Polymorphism and mutation databases
BioMutai | ALOX5 |
DMDMi | 126407 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000220693 | 1 – 674 | Polyunsaturated fatty acid 5-lipoxygenaseAdd BLAST | 674 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 272 | Phosphoserine; by MAPKAPK22 Publications | 1 | |
Modified residuei | 524 | Phosphoserine; by PKA2 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P09917 |
MassIVEi | P09917 |
MaxQBi | P09917 |
PaxDbi | P09917 |
PeptideAtlasi | P09917 |
PRIDEi | P09917 |
ProteomicsDBi | 52278 [P09917-1] 7233 |
PTM databases
iPTMneti | P09917 |
PhosphoSitePlusi | P09917 |
Expressioni
Gene expression databases
Bgeei | ENSG00000012779, Expressed in blood and 222 other tissues |
ExpressionAtlasi | P09917, baseline and differential |
Genevisiblei | P09917, HS |
Organism-specific databases
HPAi | ENSG00000012779, Tissue enhanced (blood, bone marrow, lymphoid tissue) |
Interactioni
Subunit structurei
Homodimer (PubMed:22516296, PubMed:21233389).
Interacts with ALOX5AP and LTC4S (PubMed:19233132).
Interacts with COTL1, the interaction is required for stability and efficient catalytic activity (PubMed:19807693).
Interacts with PIK3R1; this interaction bridges ALOX5 with CD40 after CD40 ligation in B cells and leads to the production of reactive oxygen species (ROS) (PubMed:21200133).
Interacts (via PLAT domain) with DICER1 (via Dicer dsRNA-binding fold domain); this interaction enhances arachidonate 5-lipoxygenase activity and modifies the miRNA precursor processing activity of DICER1 (PubMed:19022417).
6 PublicationsBinary interactionsi
Hide detailsP09917
Protein-protein interaction databases
BioGRIDi | 106741, 71 interactors |
DIPi | DIP-30950N |
IntActi | P09917, 64 interactors |
MINTi | P09917 |
STRINGi | 9606.ENSP00000363512 |
Chemistry databases
BindingDBi | P09917 |
Miscellaneous databases
RNActi | P09917, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P09917 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09917 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 118 | PLATPROSITE-ProRule annotationAdd BLAST | 117 | |
Domaini | 119 – 674 | LipoxygenasePROSITE-ProRule annotationAdd BLAST | 556 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
GeneTreei | ENSGT00940000156111 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | P09917 |
OMAi | FPDMIKS |
OrthoDBi | 385042at2759 |
PhylomeDBi | P09917 |
TreeFami | TF105320 |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
InterProi | View protein in InterPro IPR000907, LipOase IPR013819, LipOase_C IPR036226, LipOase_C_sf IPR020834, LipOase_CS IPR020833, LipOase_Fe_BS IPR001885, LipOase_mml IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR042062, PLAT_LOX_verte |
PANTHERi | PTHR11771, PTHR11771, 1 hit |
Pfami | View protein in Pfam PF00305, Lipoxygenase, 1 hit PF01477, PLAT, 1 hit |
PRINTSi | PR00087, LIPOXYGENASE PR00467, MAMLPOXGNASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF48484, SSF48484, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS00711, LIPOXYGENASE_1, 1 hit PS00081, LIPOXYGENASE_2, 1 hit PS51393, LIPOXYGENASE_3, 1 hit PS50095, PLAT, 1 hit |
s (5+)i Sequence
Sequence statusi: Complete.
This entry describes 5 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA
60 70 80 90 100
VDSYDVTVDE ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC
110 120 130 140 150
YRWITGDVEV VLRDGRAKLA RDDQIHILKQ HRRKELETRQ KQYRWMEWNP
160 170 180 190 200
GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS
210 220 230 240 250
SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG CNPVLIRRCT
260 270 280 290 300
ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP
310 320 330 340 350
CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL
360 370 380 390 400
AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH
410 420 430 440 450
VRFTIAINTK AREQLICECG LFDKANATGG GGHVQMVQRA MKDLTYASLC
460 470 480 490 500
FPEAIKARGM ESKEDIPYYF YRDDGLLVWE AIRTFTAEVV DIYYEGDQVV
510 520 530 540 550
EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL TVVIFTASAQ
560 570 580 590 600
HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW
610 620 630 640 650
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA
660 670
ERNKKKQLPY YYLSPDRIPN SVAI
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A087X109 | A0A087X109_HUMAN | Polyunsaturated fatty acid 5-lipoxy... | ALOX5 | 139 | Annotation score: |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_028018 | 254 | E → K Decreases arachidonate 5-lipoxygenase activity. Increases leukotriene A4 synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs2228065Ensembl. | 1 | |
Natural variantiVAR_083301 | 337 | P → S Decreases arachidonate 5-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083302 | 447 | A → S Increases arachidonate 5-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083303 | 549 | A → V Decreases arachidonate 5-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083304 | 577 | P → L Does not affect arachidonate 5-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083305 | 591 | T → M Increases arachidonate 5-lipoxygenase activity. Does not affect leukotriene A4 synthase activity. 1 Publication | 1 | |
Natural variantiVAR_083306 | 656 | K → Q Increases arachidonate 5-lipoxygenase activity. 1 Publication | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_053534 | 424 – 455 | Missing in isoform 3. 1 PublicationAdd BLAST | 32 | |
Alternative sequenceiVSP_053535 | 425 – 533 | ANATG…SVKSR → VHGRGGRHLLRGRPGGGGGP GAAGLRERCLRVRHAGPQVL RLPQVGQEPGAAVGVPDRGD LHRLRPARRGQLRPAVPGHV PRRAFYREACEGSHGPIPQE PRGHCQRDC in isoform 4. 1 PublicationAdd BLAST | 109 | |
Alternative sequenceiVSP_053536 | 485 – 674 | Missing in isoform 5. 1 PublicationAdd BLAST | 190 | |
Alternative sequenceiVSP_053537 | 534 – 674 | Missing in isoform 4. 1 PublicationAdd BLAST | 141 | |
Alternative sequenceiVSP_046998 | 559 – 615 | Missing in isoform 2. 2 PublicationsAdd BLAST | 57 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03600 mRNA Translation: AAA36183.1 J03571 mRNA Translation: AAA65450.1 HM592258 mRNA Translation: ADR30798.1 HM592259 mRNA Translation: ADR30799.1 HM592260 mRNA Translation: ADR30800.1 HM592261 mRNA Translation: ADR30801.1 J04520 Genomic DNA Translation: AAA59522.1 AL731567 Genomic DNA No translation available. BC130332 mRNA Translation: AAI30333.1 BC132677 mRNA Translation: AAI32678.1 BC143985 mRNA Translation: AAI43986.1 M38191 Genomic DNA Translation: AAA63212.1 |
CCDSi | CCDS58078.1 [P09917-2] CCDS7212.1 [P09917-1] |
PIRi | A28117, DAHUAL |
RefSeqi | NP_000689.1, NM_000698.4 [P09917-1] NP_001243082.1, NM_001256153.2 [P09917-3] NP_001243083.1, NM_001256154.2 [P09917-2] NP_001307790.1, NM_001320861.1 |
Genome annotation databases
Ensembli | ENST00000374391; ENSP00000363512; ENSG00000012779 [P09917-1] ENST00000542434; ENSP00000437634; ENSG00000012779 [P09917-2] ENST00000610656; ENSP00000484468; ENSG00000275565 [P09917-1] ENST00000622021; ENSP00000479958; ENSG00000275565 [P09917-2] |
GeneIDi | 240 |
KEGGi | hsa:240 |
UCSCi | uc001jce.5, human [P09917-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03600 mRNA Translation: AAA36183.1 J03571 mRNA Translation: AAA65450.1 HM592258 mRNA Translation: ADR30798.1 HM592259 mRNA Translation: ADR30799.1 HM592260 mRNA Translation: ADR30800.1 HM592261 mRNA Translation: ADR30801.1 J04520 Genomic DNA Translation: AAA59522.1 AL731567 Genomic DNA No translation available. BC130332 mRNA Translation: AAI30333.1 BC132677 mRNA Translation: AAI32678.1 BC143985 mRNA Translation: AAI43986.1 M38191 Genomic DNA Translation: AAA63212.1 |
CCDSi | CCDS58078.1 [P09917-2] CCDS7212.1 [P09917-1] |
PIRi | A28117, DAHUAL |
RefSeqi | NP_000689.1, NM_000698.4 [P09917-1] NP_001243082.1, NM_001256153.2 [P09917-3] NP_001243083.1, NM_001256154.2 [P09917-2] NP_001307790.1, NM_001320861.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ABV | model | - | A | 2-674 | [»] | |
3O8Y | X-ray | 2.39 | A/B | 1-674 | [»] | |
3V92 | X-ray | 2.74 | A/B | 1-674 | [»] | |
3V98 | X-ray | 2.07 | A/B | 1-674 | [»] | |
3V99 | X-ray | 2.25 | A/B | 1-674 | [»] | |
6N2W | X-ray | 2.71 | A/B | 1-674 | [»] | |
6NCF | X-ray | 2.87 | A/B/C/D | 1-674 | [»] | |
SMRi | P09917 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106741, 71 interactors |
DIPi | DIP-30950N |
IntActi | P09917, 64 interactors |
MINTi | P09917 |
STRINGi | 9606.ENSP00000363512 |
Chemistry databases
BindingDBi | P09917 |
ChEMBLi | CHEMBL215 |
DrugBanki | DB14001, alpha-Tocopherol succinate DB00233, Aminosalicylic acid DB01014, Balsalazide DB09061, Cannabidiol DB14002, D-alpha-Tocopherol acetate DB11994, Diacerein DB00586, Diclofenac DB00711, Diethylcarbamazine DB12010, Fostamatinib DB01892, Hyperforin DB04725, Licofelone DB00179, Masoprocol DB00939, Meclofenamic acid DB14009, Medical Cannabis DB00244, Mesalazine DB01017, Minocycline DB05431, MLN-977 DB00471, Montelukast DB09285, Morniflumate DB14011, Nabiximols DB11133, Omega-3 fatty acids DB13168, Omega-6 fatty acids DB02709, Resveratrol DB13174, Rhein DB00795, Sulfasalazine DB00163, Vitamin E DB00744, Zileuton |
DrugCentrali | P09917 |
GuidetoPHARMACOLOGYi | 1385 |
SwissLipidsi | SLP:000000669 |
PTM databases
iPTMneti | P09917 |
PhosphoSitePlusi | P09917 |
Polymorphism and mutation databases
BioMutai | ALOX5 |
DMDMi | 126407 |
Proteomic databases
jPOSTi | P09917 |
MassIVEi | P09917 |
MaxQBi | P09917 |
PaxDbi | P09917 |
PeptideAtlasi | P09917 |
PRIDEi | P09917 |
ProteomicsDBi | 52278 [P09917-1] 7233 |
Protocols and materials databases
Antibodypediai | 3906, 749 antibodies |
DNASUi | 240 |
Genome annotation databases
Ensembli | ENST00000374391; ENSP00000363512; ENSG00000012779 [P09917-1] ENST00000542434; ENSP00000437634; ENSG00000012779 [P09917-2] ENST00000610656; ENSP00000484468; ENSG00000275565 [P09917-1] ENST00000622021; ENSP00000479958; ENSG00000275565 [P09917-2] |
GeneIDi | 240 |
KEGGi | hsa:240 |
UCSCi | uc001jce.5, human [P09917-1] |
Organism-specific databases
CTDi | 240 |
DisGeNETi | 240 |
EuPathDBi | HostDB:ENSG00000012779.10 |
GeneCardsi | ALOX5 |
HGNCi | HGNC:435, ALOX5 |
HPAi | ENSG00000012779, Tissue enhanced (blood, bone marrow, lymphoid tissue) |
MalaCardsi | ALOX5 |
MIMi | 152390, gene |
neXtProti | NX_P09917 |
OpenTargetsi | ENSG00000012779 |
PharmGKBi | PA46 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
GeneTreei | ENSGT00940000156111 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | P09917 |
OMAi | FPDMIKS |
OrthoDBi | 385042at2759 |
PhylomeDBi | P09917 |
TreeFami | TF105320 |
Enzyme and pathway databases
UniPathwayi | UPA00877 |
BioCyci | MetaCyc:HS00336-MONOMER |
BRENDAi | 1.13.11.34, 2681 |
PathwayCommonsi | P09917 |
Reactomei | R-HSA-2142688, Synthesis of 5-eicosatetraenoic acids R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-2142700, Synthesis of Lipoxins (LX) R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling R-HSA-6798695, Neutrophil degranulation R-HSA-9012546, Interleukin-18 signaling R-HSA-9018676, Biosynthesis of D-series resolvins R-HSA-9018682, Biosynthesis of maresins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins R-HSA-9026290, Biosynthesis of DPAn-3-derived maresins R-HSA-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins R-HSA-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives |
SABIO-RKi | P09917 |
SIGNORi | P09917 |
Miscellaneous databases
BioGRID-ORCSi | 240, 19 hits in 848 CRISPR screens |
ChiTaRSi | ALOX5, human |
EvolutionaryTracei | P09917 |
GeneWikii | Arachidonate_5-lipoxygenase |
GenomeRNAii | 240 |
Pharosi | P09917, Tclin |
PROi | PR:P09917 |
RNActi | P09917, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000012779, Expressed in blood and 222 other tissues |
ExpressionAtlasi | P09917, baseline and differential |
Genevisiblei | P09917, HS |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
InterProi | View protein in InterPro IPR000907, LipOase IPR013819, LipOase_C IPR036226, LipOase_C_sf IPR020834, LipOase_CS IPR020833, LipOase_Fe_BS IPR001885, LipOase_mml IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR042062, PLAT_LOX_verte |
PANTHERi | PTHR11771, PTHR11771, 1 hit |
Pfami | View protein in Pfam PF00305, Lipoxygenase, 1 hit PF01477, PLAT, 1 hit |
PRINTSi | PR00087, LIPOXYGENASE PR00467, MAMLPOXGNASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF48484, SSF48484, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS00711, LIPOXYGENASE_1, 1 hit PS00081, LIPOXYGENASE_2, 1 hit PS51393, LIPOXYGENASE_3, 1 hit PS50095, PLAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LOX5_HUMAN | |
Accessioni | P09917Primary (citable) accession number: P09917 Secondary accession number(s): B7ZLS0 Q5JQ14 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 213 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations