UniProtKB - O15296 (LX15B_HUMAN)
Polyunsaturated fatty acid lipoxygenase ALOX15B
ALOX15B
Functioni
Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids (PUFAs) generating a spectrum of bioactive lipid mediators (PubMed:9177185, PubMed:10625675, PubMed:12704195, PubMed:17493578, PubMed:18311922, PubMed:24282679, PubMed:10542053, PubMed:24497644, PubMed:32404334) (Probable).
It inserts peroxyl groups at C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing (15S)-hydroperoxyeicosatetraenoate/(15S)-HPETE (PubMed:17493578, PubMed:12704195, PubMed:24282679, PubMed:9177185, PubMed:11956198, PubMed:10625675, PubMed:24497644) (Probable).
Also peroxidizes linoleate ((9Z,12Z)-octadecadienoate) to 13-hydroperoxyoctadecadienoate/13-HPODE (Probable) (PubMed:10542053, PubMed:27435673).
Oxygenates arachidonyl derivatives such as 2-arachidonoylglycerol (2-AG) leading to the production and extracellular release of 15-hydroxyeicosatetraenoyl glycerol (15-HETE-G) that acts as a peroxisome proliferator-activated receptor alpha agonist (PubMed:18311922, PubMed:17493578, PubMed:11956198).
Has the ability to efficiently class-switch ALOX5 pro-inflammatory mediators into anti-inflammatory intermediates (PubMed:27145229).
Participates in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) resolvin D5 ((7S,17S)-diHPDHA), which can actively down-regulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334).
In addition to free PUFAs hydrolyzed from phospholipids, it directly oxidizes PUFAs esterified to membrane-bound phospholipids (PubMed:27435673).
Has no detectable 8S-lipoxygenase activity on arachidonate but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE (Probable). May regulate progression through the cell cycle and cell proliferation (PubMed:12704195, PubMed:11839751).
May also regulate cytokine secretion by macrophages and therefore play a role in the immune response (PubMed:18067895).
May also regulate macrophage differentiation into proatherogenic foam cells (PubMed:22912809).
4 Publications15 PublicationsDoes not convert arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE.
1 PublicationCatalytic activityi
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate3 Publications7 PublicationsEC:1.13.11.333 Publications7 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S)-hydroxy-(15S)-hydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 5-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.This reaction proceeds in the forward1 Publication direction.
- (5S,6R)-dihydroxy-(7E,9E,11Z,14Z)-eicosatetraenoate + O2 = (5S,6R)-dihydroxy-(15S)-hydroperoxy-(7E,9E,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 = (5S,15S)-dihydroperoxy-(6E,8Z,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[15(S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-glycerol1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 = (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-γ-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-γ-aminobutanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + O2 = 2-[12-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl]-glycerol1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- a 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol)1 PublicationThis reaction proceeds in the forward1 Publication direction.
- a 1-acyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = a 1-acyl-2-(15-hydroperoxy-8Z,11Z,13E-eicosatrienoyl)-sn-glycero-3-phospho-(1D-myo-inositol)1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + O2 = 1-octadecanoyl-2-(15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol)1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This 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.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 15-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
Cofactori
Kineticsi
- KM=1100 µM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
- KM=10 µM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
- KM=25 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
- KM=23 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (Sf9-expressed enzyme)1 Publication
- KM=15 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (E. Coli-expressed enzyme)1 Publication
- KM=9 µM for 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (Sf9-expressed enzyme)1 Publication
- KM=8 µM for 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (E. Coli-expressed enzyme)1 Publication
- KM=14 µM for anandamide (Sf9-expressed enzyme)1 Publication
- KM=11 µM for anandamide (E. Coli-expressed enzyme)1 Publication
- KM=8 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=11 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine1 Publication
- KM=6 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine1 Publication
- KM=8 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate1 Publication
- KM=1.2 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=4 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=3.3 µM for (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=19 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=1.74 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
- KM=3.46 µM for (8Z,11Z,14Z)-eicosatrienoate1 Publication
- Vmax=4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
- Vmax=2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
- Vmax=4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
- Vmax=0.82 nmol/sec/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoate (Sf9-expressed enzyme)1 Publication
- Vmax=4.3 nmol/sec/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoate (E. Coli-expressed enzyme)1 Publication
- Vmax=9 nmol/sec/mg enzyme with 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (Sf9-expressed enzyme)1 Publication
- Vmax=8 nmol/sec/mg enzyme with 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol (E. Coli-expressed enzyme)1 Publication
- Vmax=14 nmol/sec/mg enzyme with anandamide (Sf9-expressed enzyme)1 Publication
- Vmax=11 nmol/sec/mg enzyme with anandamide (E. Coli-expressed enzyme)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 | 15 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 17 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 39 | Calcium 21 Publication | 1 | |
Metal bindingi | 40 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 42 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 44 | Calcium 21 Publication | 1 | |
Metal bindingi | 85 | Calcium 11 Publication | 1 | |
Metal bindingi | 86 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 373 | Iron; catalyticPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 378 | Iron; catalyticPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 553 | Iron; catalyticPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 676 | Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- arachidonate 15-lipoxygenase activity Source: UniProtKB
- arachidonate 8(S)-lipoxygenase activity Source: Ensembl
- calcium ion binding Source: UniProtKB
- iron ion binding Source: UniProtKB
- linoleate 13S-lipoxygenase activity Source: UniProtKB
- linoleate 9S-lipoxygenase activity Source: Ensembl
- lipid binding Source: UniProtKB-KW
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: GO_Central
GO - Biological processi
- apoptotic process Source: UniProtKB
- arachidonic acid metabolic process Source: UniProtKB
- cannabinoid biosynthetic process Source: UniProtKB
- endocannabinoid signaling pathway Source: UniProtKB
- hepoxilin biosynthetic process Source: UniProtKB
- linoleic acid metabolic process Source: GO_Central
- lipid metabolic process Source: UniProtKB
- lipid oxidation Source: GO_Central
- lipoxin A4 biosynthetic process Source: UniProtKB
- lipoxygenase pathway Source: GO_Central
- negative regulation of cell cycle Source: UniProtKB
- negative regulation of cell migration Source: UniProtKB
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of growth Source: UniProtKB
- phospholipid metabolic process Source: UniProtKB
- positive regulation of chemokine production Source: UniProtKB
- positive regulation of keratinocyte differentiation Source: Ensembl
- positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
- positive regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
- prostate gland development Source: UniProtKB
- regulation of epithelial cell differentiation Source: UniProtKB
Keywordsi
Molecular function | Dioxygenase, Oxidoreductase |
Biological process | Lipid metabolism |
Ligand | Calcium, Iron, Lipid-binding, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.13.11.33, 2681 |
PathwayCommonsi | O15296 |
Reactomei | R-HSA-2142770, Synthesis of 15-eicosatetraenoic acid derivatives |
SABIO-RKi | O15296 |
SignaLinki | O15296 |
UniPathwayi | UPA00881 |
Chemistry databases
SwissLipidsi | SLP:000000651 SLP:000001469 [O15296-1] SLP:000001470 [O15296-4] |
Names & Taxonomyi
Protein namesi | Recommended name: Polyunsaturated fatty acid lipoxygenase ALOX15BCuratedAlternative name(s): 15-lipoxygenase 21 Publication Short name: 15-LOX-21 Publication Arachidonate 15-lipoxygenase type II Linoleate 13-lipoxygenase 15-LOb (EC:1.13.11.-1 Publication1 Publication) |
Gene namesi | Name:ALOX15BImported |
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:434, ALOX15B |
MIMi | 603697, gene |
neXtProti | NX_O15296 |
VEuPathDBi | HostDB:ENSG00000179593 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Note: Other isoforms are excluded from the nucleus.1 Publication
Plasma membrane
- Cell membrane 2 Publications
Cytoplasm and Cytosol
- cytosol 1 Publication
Cytoskeleton
- cytoskeleton 1 Publication
Other locations
- Membrane 2 Publications; Peripheral membrane protein 1 Publication
- adherens junction 1 Publication
- focal adhesion 1 Publication
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding.4 Publications
Cytoskeleton
- cytoskeleton Source: UniProtKB
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- adherens junction Source: UniProtKB
- extrinsic component of membrane Source: UniProtKB
- focal adhesion Source: UniProtKB
- membrane Source: UniProtKB
Keywords - Cellular componenti
Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 39 | D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication | 1 | |
Mutagenesisi | 44 | E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication | 1 | |
Mutagenesisi | 85 | D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication | 1 | |
Mutagenesisi | 602 | D → Y: No effect on the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with H-603. 1 Publication | 1 | |
Mutagenesisi | 603 | V → H: Changes the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with Y-602. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 247 |
OpenTargetsi | ENSG00000179593 |
PharmGKBi | PA24725 |
Miscellaneous databases
Pharosi | O15296, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2457 |
DrugCentrali | O15296 |
GuidetoPHARMACOLOGYi | 1389 |
Genetic variation databases
BioMutai | ALOX15B |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000220700 | 1 – 676 | Polyunsaturated fatty acid lipoxygenase ALOX15BAdd BLAST | 676 |
Proteomic databases
EPDi | O15296 |
jPOSTi | O15296 |
MassIVEi | O15296 |
PaxDbi | O15296 |
PeptideAtlasi | O15296 |
PRIDEi | O15296 |
ProteomicsDBi | 48566 [O15296-1] 48567 [O15296-2] 48568 [O15296-3] 48569 [O15296-4] |
PTM databases
iPTMneti | O15296 |
PhosphoSitePlusi | O15296 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000179593, Expressed in mammalian vulva and 130 other tissues |
ExpressionAtlasi | O15296, baseline and differential |
Genevisiblei | O15296, HS |
Organism-specific databases
HPAi | ENSG00000179593, Tissue enhanced (breast, prostate) |
Interactioni
Binary interactionsi
O15296
Protein-protein interaction databases
BioGRIDi | 106748, 21 interactors |
IntActi | O15296, 11 interactors |
STRINGi | 9606.ENSP00000369530 |
Chemistry databases
BindingDBi | O15296 |
Miscellaneous databases
RNActi | O15296, protein |
Structurei
Secondary structure
3D structure databases
SMRi | O15296 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 124 | PLATPROSITE-ProRule annotationAdd BLAST | 123 | |
Domaini | 125 – 676 | LipoxygenasePROSITE-ProRule annotationAdd BLAST | 552 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502QVKD, Eukaryota |
GeneTreei | ENSGT00940000161510 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | O15296 |
OMAi | DFNMHEL |
OrthoDBi | 385042at2759 |
PhylomeDBi | O15296 |
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 (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 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
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE
60 70 80 90 100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG
110 120 130 140 150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ
160 170 180 190 200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL
210 220 230 240 250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL
260 270 280 290 300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT
310 320 330 340 350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK
360 370 380 390 400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK
410 420 430 440 450
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN
460 470 480 490 500
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE
510 520 530 540 550
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS
560 570 580 590 600
AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT
610 620 630 640 650
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG
660 670
IQERNQGLVL PYTYLDPPLI ENSVSI
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketI3L1D5 | I3L1D5_HUMAN | Polyunsaturated fatty acid lipoxyge... | ALOX15B | 664 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 271 | V → L in AAB61706 (PubMed:9177185).Curated | 1 | |
Sequence conflicti | 271 | V → L in CAC34521 (PubMed:11350124).Curated | 1 | |
Sequence conflicti | 338 | G → C in AAD37786 (PubMed:15489334).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_083544 | 416 | A → D Loss of 15-lipoxygenase activity. 1 PublicationCorresponds to variant dbSNP:rs140152561Ensembl. | 1 | |
Natural variantiVAR_061334 | 486 | R → H Does not affect arachidonate 15-lipoxygenase activity; does not impact enzyme structure. 2 PublicationsCorresponds to variant dbSNP:rs9895916Ensembl. | 1 | |
Natural variantiVAR_024524 | 656 | Q → R Does not affect arachidonate 15-lipoxygenase activity; does not impact enzyme structure. 5 PublicationsCorresponds to variant dbSNP:rs4792147Ensembl. | 1 | |
Natural variantiVAR_024525 | 676 | I → V Does not affect arachidonate 15-lipoxygenase activity; destabilizes the enzyme structure. 1 PublicationCorresponds to variant dbSNP:rs7225107Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003142 | 401 – 429 | Missing in isoform B and isoform D. 1 PublicationAdd BLAST | 29 | |
Alternative sequenceiVSP_003143 | 483 – 527 | Missing in isoform B. 1 PublicationAdd BLAST | 45 | |
Alternative sequenceiVSP_003144 | 561 – 617 | FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. 1 PublicationAdd BLAST | 57 | |
Alternative sequenceiVSP_003145 | 618 – 676 | Missing in isoform C. 1 PublicationAdd BLAST | 59 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U78294 mRNA Translation: AAB61706.1 AJ305028 , AJ305029, AJ305030, AJ305031 Genomic DNA Translation: CAC34521.1 AF468051 mRNA Translation: AAL76274.1 AF468052 mRNA Translation: AAL76275.1 AF468053 mRNA Translation: AAL76276.1 AF468054 mRNA Translation: AAL76277.1 AC129492 Genomic DNA No translation available. CH471108 Genomic DNA Translation: EAW90098.1 CH471108 Genomic DNA Translation: EAW90100.1 BC035217 mRNA Translation: AAH35217.1 BC063647 mRNA Translation: AAH63647.1 AF149095 Genomic DNA Translation: AAD37786.1 Sequence problems. |
CCDSi | CCDS11128.1 [O15296-1] CCDS32558.1 [O15296-4] CCDS32559.1 [O15296-2] |
RefSeqi | NP_001034219.1, NM_001039130.1 [O15296-4] NP_001034220.1, NM_001039131.1 [O15296-2] NP_001132.2, NM_001141.2 [O15296-1] |
Genome annotation databases
Ensembli | ENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4] ENST00000380183; ENSP00000369530; ENSG00000179593 ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2] |
GeneIDi | 247 |
KEGGi | hsa:247 |
MANE-Selecti | ENST00000380183.9; ENSP00000369530.4; NM_001141.3; NP_001132.2 |
UCSCi | uc002gju.4, human [O15296-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U78294 mRNA Translation: AAB61706.1 AJ305028 , AJ305029, AJ305030, AJ305031 Genomic DNA Translation: CAC34521.1 AF468051 mRNA Translation: AAL76274.1 AF468052 mRNA Translation: AAL76275.1 AF468053 mRNA Translation: AAL76276.1 AF468054 mRNA Translation: AAL76277.1 AC129492 Genomic DNA No translation available. CH471108 Genomic DNA Translation: EAW90098.1 CH471108 Genomic DNA Translation: EAW90100.1 BC035217 mRNA Translation: AAH35217.1 BC063647 mRNA Translation: AAH63647.1 AF149095 Genomic DNA Translation: AAD37786.1 Sequence problems. |
CCDSi | CCDS11128.1 [O15296-1] CCDS32558.1 [O15296-4] CCDS32559.1 [O15296-2] |
RefSeqi | NP_001034219.1, NM_001039130.1 [O15296-4] NP_001034220.1, NM_001039131.1 [O15296-2] NP_001132.2, NM_001141.2 [O15296-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4NRE | X-ray | 2.63 | A | 1-676 | [»] | |
SMRi | O15296 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106748, 21 interactors |
IntActi | O15296, 11 interactors |
STRINGi | 9606.ENSP00000369530 |
Chemistry databases
BindingDBi | O15296 |
ChEMBLi | CHEMBL2457 |
DrugCentrali | O15296 |
GuidetoPHARMACOLOGYi | 1389 |
SwissLipidsi | SLP:000000651 SLP:000001469 [O15296-1] SLP:000001470 [O15296-4] |
PTM databases
iPTMneti | O15296 |
PhosphoSitePlusi | O15296 |
Genetic variation databases
BioMutai | ALOX15B |
Proteomic databases
EPDi | O15296 |
jPOSTi | O15296 |
MassIVEi | O15296 |
PaxDbi | O15296 |
PeptideAtlasi | O15296 |
PRIDEi | O15296 |
ProteomicsDBi | 48566 [O15296-1] 48567 [O15296-2] 48568 [O15296-3] 48569 [O15296-4] |
Protocols and materials databases
Antibodypediai | 12373, 295 antibodies from 31 providers |
DNASUi | 247 |
Genome annotation databases
Ensembli | ENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4] ENST00000380183; ENSP00000369530; ENSG00000179593 ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2] |
GeneIDi | 247 |
KEGGi | hsa:247 |
MANE-Selecti | ENST00000380183.9; ENSP00000369530.4; NM_001141.3; NP_001132.2 |
UCSCi | uc002gju.4, human [O15296-1] |
Organism-specific databases
CTDi | 247 |
DisGeNETi | 247 |
GeneCardsi | ALOX15B |
HGNCi | HGNC:434, ALOX15B |
HPAi | ENSG00000179593, Tissue enhanced (breast, prostate) |
MIMi | 603697, gene |
neXtProti | NX_O15296 |
OpenTargetsi | ENSG00000179593 |
PharmGKBi | PA24725 |
VEuPathDBi | HostDB:ENSG00000179593 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502QVKD, Eukaryota |
GeneTreei | ENSGT00940000161510 |
HOGENOMi | CLU_004282_3_3_1 |
InParanoidi | O15296 |
OMAi | DFNMHEL |
OrthoDBi | 385042at2759 |
PhylomeDBi | O15296 |
TreeFami | TF105320 |
Enzyme and pathway databases
UniPathwayi | UPA00881 |
BRENDAi | 1.13.11.33, 2681 |
PathwayCommonsi | O15296 |
Reactomei | R-HSA-2142770, Synthesis of 15-eicosatetraenoic acid derivatives |
SABIO-RKi | O15296 |
SignaLinki | O15296 |
Miscellaneous databases
BioGRID-ORCSi | 247, 5 hits in 1031 CRISPR screens |
ChiTaRSi | ALOX15B, human |
GeneWikii | ALOX15B |
GenomeRNAii | 247 |
Pharosi | O15296, Tchem |
PROi | PR:O15296 |
RNActi | O15296, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000179593, Expressed in mammalian vulva and 130 other tissues |
ExpressionAtlasi | O15296, baseline and differential |
Genevisiblei | O15296, 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | LX15B_HUMAN | |
Accessioni | O15296Primary (citable) accession number: O15296 Secondary accession number(s): D3DTR2 Q9UKM4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 11, 2001 |
Last sequence update: | January 11, 2011 | |
Last modified: | February 23, 2022 | |
This is version 195 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, 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