UniProtKB - P16050 (LOX15_HUMAN)
Protein
Polyunsaturated fatty acid lipoxygenase ALOX15
Gene
ALOX15
Organism
Homo sapiens (Human)
Status
Functioni
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:1944593, PubMed:8334154, PubMed:17052953, PubMed:24282679, PubMed:25293588, PubMed:32404334). It inserts peroxyl groups at C12 or C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing both 12-hydroperoxyeicosatetraenoate/12-HPETE and 15-hydroperoxyeicosatetraenoate/15-HPETE (PubMed:1944593, PubMed:8334154, PubMed:17052953, PubMed:24282679). It may then act on 12-HPETE to produce hepoxilins, which may show proinflammatory properties (By similarity). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to 13-hydroperoxyoctadecadienoate/13-HPODE (PubMed:8334154). May participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs)like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively downregulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). Can convert epoxy fatty acids to hydroperoxy-epoxides derivatives followed by an intramolecular nucleophilic substitution leading to the formation of monocyclic endoperoxides (PubMed:25293588). Plays an important role during the maintenance of self-tolerance by peroxidizing membrane-bound phosphatidylethanolamine which can then signal the sorting process for clearance of apoptotic cells during inflammation and prevent an autoimmune response. In addition to its role in the immune and inflammatory responses, this enzyme may play a role in epithelial wound healing in the cornea through production of lipoxin A4 (LXA4) and docosahexaenoic acid-derived neuroprotectin D1 (NPD1; 10R,17S-HDHA), both lipid autacoids exhibit anti-inflammatory and neuroprotective properties. Furthermore, it may regulate actin polymerization which is crucial for several biological processes such as the phagocytosis of apoptotic cells. It is also implicated in the generation of endogenous ligands for peroxisome proliferator activated receptor (PPAR-gamma), hence modulating macrophage development and function. It may also exert a negative effect on skeletal development by regulating bone mass through this pathway. As well as participates in ER stress and downstream inflammation in adipocytes, pancreatic islets, and liver (By similarity). Finally, it is also involved in the cellular response to IL13/interleukin-13 (PubMed:21831839).By similarity7 Publications
Catalytic activityi
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate1 PublicationEC:1.13.11.311 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate4 PublicationsEC:1.13.11.334 PublicationsThis reaction proceeds in the forward1 Publication direction.
- EC:1.13.11.121 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (14R,15S)-dihydroperoxy-(5Z,8Z,10E,12E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (8S)-hydroperoxy-(14S,15R)-epoxy-(5Z,9E,11Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14S,15R)-epoxy-(5Z,8Z,10E)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (5S)-hydroperoxy-(14R,15S)-epoxy-(6E,8Z,11Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14R,15S)-epoxy-(5Z,8Z,10E)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (14S,15S)-epoxy-(5Z,8Z,10E,12E)-eicosatetraenoate + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8S)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity 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 = (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,14S)-dihydroperoxy-(4Z,8E,10Z,12E,16Z,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (11S)-hydroperoxy-(4Z,7Z,9E,13Z,16Z,19Z)-docosahexaenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 = 14-hydroperoxy-(7Z,10Z,12E,16Z,19Z)-docosapentaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 = 14-hydroperoxy-(4Z,7Z,10Z,12E,16Z)-docosapentaenoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-taurineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-γ-aminobutanoate + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-γ-aminobutanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-glycineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-alanineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-γ-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-γ-aminobutanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanineBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Fe cationPROSITE-ProRule annotationBy similarityNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotationBy similarity
Activity regulationi
Activity is increased by binding phosphatidylinositol phosphates, especially phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate (PubMed:17052953). Inactivated at 37 degrees Celsius by (13S)-hydroperoxy-(9Z,11E)-octadecadienoate (PubMed:8334154).2 Publications
Kineticsi
kcat is 14.4 sec(-1) with (9Z,12Z)-octadecadienoate as substrate.1 Publication
- KM=3 µM for (9Z,12Z)-octadecadienoate1 Publication
- KM=12 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=3.8 µM for (9Z,12Z)-octadecadienoate1 Publication
- Vmax=10.6 µmol/min/mg enzyme toward (9Z,12Z)-octadecadienoate1 Publication
- Vmax=5.6 µmol/min/mg enzyme toward (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
pH dependencei
Optimum pH is 7 with (9Z,12Z)-octadecadienoate as substrate.1 Publication
: hydroperoxy eicosatetraenoic acid biosynthesis Pathwayi
This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 360 | Iron; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 365 | Iron; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 540 | Iron; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 544 | Iron; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 662 | Iron; via carboxylate; catalyticPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- arachidonate 12(S)-lipoxygenase activity Source: UniProtKB
- arachidonate 15-lipoxygenase activity Source: UniProtKB
- hepoxilin A3 synthase activity Source: Ensembl
- hepoxilin-epoxide hydrolase activity Source: Ensembl
- iron ion binding Source: UniProtKB
- linoleate 13S-lipoxygenase activity Source: UniProtKB
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: GO_Central
- phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
GO - Biological processi
- apoptotic cell clearance Source: UniProtKB
- arachidonic acid metabolic process Source: UniProtKB
- bone mineralization Source: UniProtKB
- cellular response to calcium ion Source: UniProtKB
- cellular response to interleukin-13 Source: UniProtKB
- cytokine-mediated signaling pathway Source: Reactome
- fatty acid oxidation Source: UniProtKB
- hepoxilin biosynthetic process Source: UniProtKB
- inflammatory response Source: ProtInc
- leukotriene metabolic process Source: Reactome
- linoleic acid metabolic process Source: UniProtKB
- lipid metabolic process Source: UniProtKB
- lipid oxidation Source: GO_Central
- lipoxin A4 biosynthetic process Source: UniProtKB
- lipoxygenase pathway Source: UniProtKB
- long-chain fatty acid biosynthetic process Source: Reactome
- negative regulation of adaptive immune response Source: UniProtKB
- ossification Source: UniProtKB
- phosphatidylethanolamine biosynthetic process Source: UniProtKB
- positive regulation of actin filament polymerization Source: UniProtKB
- positive regulation of cell-substrate adhesion Source: UniProtKB
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of heterotypic cell-cell adhesion Source: Ensembl
- regulation of engulfment of apoptotic cell Source: UniProtKB
- regulation of inflammatory response Source: UniProtKB
- regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
- response to endoplasmic reticulum stress Source: UniProtKB
- wound healing Source: UniProtKB
Keywordsi
Molecular function | Dioxygenase, Oxidoreductase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Ligand | Calcium, Iron, Lipid-binding, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:HS08621-MONOMER |
BRENDAi | 1.13.11.33, 2681 |
PathwayCommonsi | P16050 |
Reactomei | R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-2142712, Synthesis of 12-eicosatetraenoic acid derivatives R-HSA-2142770, Synthesis of 15-eicosatetraenoic acid derivatives R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling R-HSA-9018677, Biosynthesis of DHA-derived SPMs R-HSA-9018681, Biosynthesis of protectins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins R-HSA-9025106, Biosynthesis of DPAn-6 SPMs R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins |
SABIO-RKi | P16050 |
SIGNORi | P16050 |
UniPathwayi | UPA00881 |
Chemistry databases
SwissLipidsi | SLP:000000667 |
Names & Taxonomyi
Protein namesi | Recommended name: Polyunsaturated fatty acid lipoxygenase ALOX15CuratedAlternative name(s): 12/15-lipoxygenaseBy similarity Arachidonate 12-lipoxygenase, leukocyte-typeBy similarity (EC:1.13.11.311 Publication) Short name: 12-LOX Arachidonate omega-6 lipoxygenase1 Publication Hepoxilin A3 synthase Alox15By similarity (EC:1.13.11.-By similarity) Linoleate 13S-lipoxygenase (EC:1.13.11.121 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
HGNCi | HGNC:433, ALOX15 |
MIMi | 152392, gene |
neXtProti | NX_P16050 |
VEuPathDBi | HostDB:ENSG00000161905.12 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
Cytosol
- cytosol 2 Publications
Other locations
- Lipid droplet 1 Publication
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding (By similarity). Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells (By similarity).By similarity
Cytosol
- cytosol Source: UniProtKB
Plasma Membrane
- extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- lipid droplet Source: UniProtKB
- membrane Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Lipid droplet, MembranePathology & Biotechi
Involvement in diseasei
Disease susceptibility may be associated with variants affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (PubMed:17959182).1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 418 | M → V: Catalyzes 15- and 12-lipoxygenation. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 246 |
OpenTargetsi | ENSG00000161905 |
PharmGKBi | PA48 |
Miscellaneous databases
Pharosi | P16050, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2903 |
DrugBanki | DB08492, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID DB09061, Cannabidiol DB14009, Medical Cannabis DB14011, Nabiximols DB02709, Resveratrol |
DrugCentrali | P16050 |
GuidetoPHARMACOLOGYi | 1388 |
Genetic variation databases
BioMutai | ALOX15 |
DMDMi | 126396 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000220697 | 2 – 662 | Polyunsaturated fatty acid lipoxygenase ALOX15Add BLAST | 661 |
Proteomic databases
jPOSTi | P16050 |
MassIVEi | P16050 |
PaxDbi | P16050 |
PeptideAtlasi | P16050 |
PRIDEi | P16050 |
ProteomicsDBi | 53264 [P16050-1] 7049 |
PTM databases
iPTMneti | P16050 |
MetOSitei | P16050 |
PhosphoSitePlusi | P16050 |
Expressioni
Tissue specificityi
Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells.2 Publications
Inductioni
Up-regulated by UV-irradiation.1 Publication
Gene expression databases
Bgeei | ENSG00000161905, Expressed in nasal cavity epithelium and 107 other tissues |
Genevisiblei | P16050, HS |
Organism-specific databases
HPAi | ENSG00000161905, Tissue enhanced (adipose tissue, blood, lung) |
Interactioni
Subunit structurei
Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.
1 PublicationBinary interactionsi
P16050
With | #Exp. | IntAct |
---|---|---|
PEBP1 [P30086] | 3 | EBI-14035397,EBI-716384 |
Protein-protein interaction databases
BioGRIDi | 106747, 4 interactors |
DIPi | DIP-60388N |
IntActi | P16050, 4 interactors |
STRINGi | 9606.ENSP00000458832 |
Chemistry databases
BindingDBi | P16050 |
Miscellaneous databases
RNActi | P16050, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 114 | PLATPROSITE-ProRule annotationAdd BLAST | 113 | |
Domaini | 115 – 662 | LipoxygenasePROSITE-ProRule annotationAdd BLAST | 548 |
Domaini
The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity
Sequence similaritiesi
Belongs to the lipoxygenase family.Curated
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
GeneTreei | ENSGT00940000162807 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | P16050 |
OMAi | LNILTCW |
OrthoDBi | 385042at2759 |
PhylomeDBi | P16050 |
TreeFami | TF105320 |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
DisProti | DP02162 |
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 (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketIsoform 1 (identifier: P16050-1) [UniParc]FASTAAdd to basket
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
MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK
60 70 80 90 100
VEVPEYLGPL LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV
110 120 130 140 150
EGNGVLSLPE GTGRTVGEDP QGLFQKHREE ELEERRKLYR WGNWKDGLIL
160 170 180 190 200
NMAGAKLYDL PVDERFLEDK RVDFEVSLAK GLADLAIKDS LNVLTCWKDL
210 220 230 240 250
DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV LRRSAHLPAR
260 270 280 290 300
LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL
310 320 330 340 350
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS
360 370 380 390 400
DFQLHELQSH LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN
410 420 430 440 450
VRARTGLVSD MGIFDQIMST GGGGHVQLLK QAGAFLTYSS FCPPDDLADR
460 470 480 490 500
GLLGVKSSFY AQDALRLWEI IYRYVEGIVS LHYKTDVAVK DDPELQTWCR
510 520 530 540 550
EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH ASVHLGQLDW
560 570 580 590 600
YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ
610 620 630 640 650
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY
660
LRPSVVENSV AI
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 46 | E → V in AAC52118 (PubMed:9700053).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_018746 | 90 | D → H1 PublicationCorresponds to variant dbSNP:rs11568142EnsemblClinVar. | 1 | |
Natural variantiVAR_035036 | 102 | G → V. Corresponds to variant dbSNP:rs41439950EnsemblClinVar. | 1 | |
Natural variantiVAR_018747 | 103 | N → K1 PublicationCorresponds to variant dbSNP:rs11568099EnsemblClinVar. | 1 | |
Natural variantiVAR_018748 | 205 | R → Q Does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate.. 2 PublicationsCorresponds to variant dbSNP:rs11568101EnsemblClinVar. | 1 | |
Natural variantiVAR_035037 | 239 | V → M. Corresponds to variant dbSNP:rs3892408Ensembl. | 1 | |
Natural variantiVAR_083449 | 402 | R → W 36% of arachidonate 15-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083450 | 422 | G → E Loss of arachidonate 15-lipoxygenase activity. 1 Publication | 1 | |
Natural variantiVAR_083451 | 422 | G → R 46% of arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate. 1 Publication | 1 | |
Natural variantiVAR_035038 | 461 | A → P1 PublicationCorresponds to variant dbSNP:rs17852628Ensembl. | 1 | |
Natural variantiVAR_035039 | 560 | T → M Loss of catalytic activity; Loss of arachidonate 15-lipoxygenase activity.. 2 PublicationsCorresponds to variant dbSNP:rs34210653EnsemblClinVar. | 1 | |
Natural variantiVAR_083452 | 617 | P → S Does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate. 1 Publication | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056681 | 46 – 84 | Missing in isoform 2. 1 PublicationAdd BLAST | 39 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M23892 mRNA Translation: AAA36182.1 U88317 Genomic DNA Translation: AAB49305.1 AK290309 mRNA Translation: BAF82998.1 AK316126 mRNA Translation: BAH14497.1 AY505111 Genomic DNA Translation: AAR84235.1 AC118754 Genomic DNA No translation available. BC029032 mRNA Translation: AAH29032.1 U63384 Genomic DNA Translation: AAC52118.1 |
CCDSi | CCDS11049.1 [P16050-1] |
PIRi | A31349 |
RefSeqi | NP_001131.3, NM_001140.3 [P16050-1] |
Genome annotation databases
Ensembli | ENST00000293761; ENSP00000293761; ENSG00000161905 [P16050-1] ENST00000570836; ENSP00000458832; ENSG00000161905 [P16050-1] ENST00000574640; ENSP00000460483; ENSG00000161905 [P16050-2] |
GeneIDi | 246 |
KEGGi | hsa:246 |
UCSCi | uc002fyh.4, human [P16050-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
SeattleSNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M23892 mRNA Translation: AAA36182.1 U88317 Genomic DNA Translation: AAB49305.1 AK290309 mRNA Translation: BAF82998.1 AK316126 mRNA Translation: BAH14497.1 AY505111 Genomic DNA Translation: AAR84235.1 AC118754 Genomic DNA No translation available. BC029032 mRNA Translation: AAH29032.1 U63384 Genomic DNA Translation: AAC52118.1 |
CCDSi | CCDS11049.1 [P16050-1] |
PIRi | A31349 |
RefSeqi | NP_001131.3, NM_001140.3 [P16050-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ABT | model | - | A | 2-662 | [»] | |
SMRi | P16050 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106747, 4 interactors |
DIPi | DIP-60388N |
IntActi | P16050, 4 interactors |
STRINGi | 9606.ENSP00000458832 |
Chemistry databases
BindingDBi | P16050 |
ChEMBLi | CHEMBL2903 |
DrugBanki | DB08492, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID DB09061, Cannabidiol DB14009, Medical Cannabis DB14011, Nabiximols DB02709, Resveratrol |
DrugCentrali | P16050 |
GuidetoPHARMACOLOGYi | 1388 |
SwissLipidsi | SLP:000000667 |
PTM databases
iPTMneti | P16050 |
MetOSitei | P16050 |
PhosphoSitePlusi | P16050 |
Genetic variation databases
BioMutai | ALOX15 |
DMDMi | 126396 |
Proteomic databases
jPOSTi | P16050 |
MassIVEi | P16050 |
PaxDbi | P16050 |
PeptideAtlasi | P16050 |
PRIDEi | P16050 |
ProteomicsDBi | 53264 [P16050-1] 7049 |
Protocols and materials databases
Antibodypediai | 2761, 326 antibodies |
Genome annotation databases
Ensembli | ENST00000293761; ENSP00000293761; ENSG00000161905 [P16050-1] ENST00000570836; ENSP00000458832; ENSG00000161905 [P16050-1] ENST00000574640; ENSP00000460483; ENSG00000161905 [P16050-2] |
GeneIDi | 246 |
KEGGi | hsa:246 |
UCSCi | uc002fyh.4, human [P16050-1] |
Organism-specific databases
CTDi | 246 |
DisGeNETi | 246 |
GeneCardsi | ALOX15 |
HGNCi | HGNC:433, ALOX15 |
HPAi | ENSG00000161905, Tissue enhanced (adipose tissue, blood, lung) |
MIMi | 152392, gene |
neXtProti | NX_P16050 |
OpenTargetsi | ENSG00000161905 |
PharmGKBi | PA48 |
VEuPathDBi | HostDB:ENSG00000161905.12 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502QQSP, Eukaryota |
GeneTreei | ENSGT00940000162807 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | P16050 |
OMAi | LNILTCW |
OrthoDBi | 385042at2759 |
PhylomeDBi | P16050 |
TreeFami | TF105320 |
Enzyme and pathway databases
UniPathwayi | UPA00881 |
BioCyci | MetaCyc:HS08621-MONOMER |
BRENDAi | 1.13.11.33, 2681 |
PathwayCommonsi | P16050 |
Reactomei | R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-2142712, Synthesis of 12-eicosatetraenoic acid derivatives R-HSA-2142770, Synthesis of 15-eicosatetraenoic acid derivatives R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling R-HSA-9018677, Biosynthesis of DHA-derived SPMs R-HSA-9018681, Biosynthesis of protectins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins R-HSA-9025106, Biosynthesis of DPAn-6 SPMs R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins |
SABIO-RKi | P16050 |
SIGNORi | P16050 |
Miscellaneous databases
BioGRID-ORCSi | 246, 3 hits in 878 CRISPR screens |
GeneWikii | ALOX15 |
GenomeRNAii | 246 |
Pharosi | P16050, Tchem |
PROi | PR:P16050 |
RNActi | P16050, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000161905, Expressed in nasal cavity epithelium and 107 other tissues |
Genevisiblei | P16050, HS |
Family and domain databases
CDDi | cd01753, PLAT_LOX, 1 hit |
DisProti | DP02162 |
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 | LOX15_HUMAN | |
Accessioni | P16050Primary (citable) accession number: P16050 Secondary accession number(s): A8K2P4 Q99657 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 201 of the entry and version 3 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 chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - 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