Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P16050 (LOX15_HUMAN)

Entry version 201 (10 Feb 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Polyunsaturated fatty acid lipoxygenase ALOX15

Gene

ALOX15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe cationPROSITE-ProRule annotationBy similarityNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotationBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 14.4 sec(-1) with (9Z,12Z)-octadecadienoate as substrate.1 Publication
  1. KM=3 µM for (9Z,12Z)-octadecadienoate1 Publication
  2. KM=12 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  3. KM=3.8 µM for (9Z,12Z)-octadecadienoate1 Publication
  1. Vmax=10.6 µmol/min/mg enzyme toward (9Z,12Z)-octadecadienoate1 Publication
  2. 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi360Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi365Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi540Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi544Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi662Iron; via carboxylate; catalyticPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandCalcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS08621-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.13.11.33, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P16050

Reactome - a knowledgebase of biological pathways and processes

More...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-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P16050

SIGNOR Signaling Network Open Resource

More...SIGNORi		P16050

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00881

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000667

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Polyunsaturated fatty acid lipoxygenase ALOX15Curated
Alternative name(s):
12/15-lipoxygenaseBy similarity
Arachidonate 12-lipoxygenase, leukocyte-typeBy similarity (EC:1.13.11.311 Publication)
Short name:
12-LOX
Arachidonate 15-lipoxygenase (EC:1.13.11.334 Publications)
Short name:
15-LOX
Short name:
15-LOX-1
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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ALOX15Imported
Synonyms:LOG15
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:433, ALOX15

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		152392, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P16050

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000161905.12

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi418M → V: Catalyzes 15- and 12-lipoxygenation. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		246

Open Targets

More...OpenTargetsi		ENSG00000161905

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA48

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P16050, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2903

Drug and drug target database

More...DrugBanki		DB08492, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID
DB09061, Cannabidiol
DB14009, Medical Cannabis
DB14011, Nabiximols
DB02709, Resveratrol

DrugCentral

More...DrugCentrali		P16050

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1388

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ALOX15

Domain mapping of disease mutations (DMDM)

More...DMDMi		126396

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002206972 – 662Polyunsaturated fatty acid lipoxygenase ALOX15Add BLAST661

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P16050

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P16050

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P16050

PeptideAtlas

More...PeptideAtlasi		P16050

PRoteomics IDEntifications database

More...PRIDEi		P16050

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53264 [P16050-1]
7049

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P16050

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P16050

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P16050

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells.2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by UV-irradiation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000161905, Expressed in nasal cavity epithelium and 107 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P16050, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000161905, Tissue enhanced (adipose tissue, blood, lung)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106747, 4 interactors

Database of interacting proteins

More...DIPi		DIP-60388N

Protein interaction database and analysis system

More...IntActi		P16050, 4 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000458832

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P16050

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P16050, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P16050

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 114PLATPROSITE-ProRule annotationAdd BLAST113
Domaini115 – 662LipoxygenasePROSITE-ProRule annotationAdd BLAST548

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQSP, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162807

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004282_3_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16050

Identification of Orthologs from Complete Genome Data

More...OMAi		LNILTCW

Database of Orthologous Groups

More...OrthoDBi		385042at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16050

TreeFam database of animal gene trees

More...TreeFami		TF105320

Family and domain databases

Conserved Domains Database

More...CDDi		cd01753, PLAT_LOX, 1 hit

Database of protein disorder

More...DisProti		DP02162

Integrated resource of protein families, domains and functional sites

More...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

The PANTHER Classification System

More...PANTHERi		PTHR11771, PTHR11771, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00308, LH2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P16050-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
Length:662
Mass (Da):74,804
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9ACF7FE7863A045C
GO
Isoform 2 (identifier: P16050-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-84: Missing.

Show »
Length:623
Mass (Da):70,108
Checksum:i71B99C6D8E707189
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti46E → V in AAC52118 (PubMed:9700053).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01874690D → H1 PublicationCorresponds to variant dbSNP:rs11568142EnsemblClinVar.1
Natural variantiVAR_035036102G → V. Corresponds to variant dbSNP:rs41439950EnsemblClinVar.1
Natural variantiVAR_018747103N → K1 PublicationCorresponds to variant dbSNP:rs11568099EnsemblClinVar.1
Natural variantiVAR_018748205R → 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_035037239V → M. Corresponds to variant dbSNP:rs3892408Ensembl.1
Natural variantiVAR_083449402R → W 36% of arachidonate 15-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083450422G → E Loss of arachidonate 15-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083451422G → R 46% of arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate. 1 Publication1
Natural variantiVAR_035038461A → P1 PublicationCorresponds to variant dbSNP:rs17852628Ensembl.1
Natural variantiVAR_035039560T → M Loss of catalytic activity; Loss of arachidonate 15-lipoxygenase activity.. 2 PublicationsCorresponds to variant dbSNP:rs34210653EnsemblClinVar.1
Natural variantiVAR_083452617P → S Does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05668146 – 84Missing in isoform 2. 1 PublicationAdd BLAST39

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11049.1 [P16050-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A31349

NCBI Reference Sequences

More...RefSeqi		NP_001131.3, NM_001140.3 [P16050-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000293761; ENSP00000293761; ENSG00000161905 [P16050-1]
ENST00000570836; ENSP00000458832; ENSG00000161905 [P16050-1]
ENST00000574640; ENSP00000460483; ENSG00000161905 [P16050-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		246

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:246

UCSC genome browser

More...UCSCi		uc002fyh.4, human [P16050-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS11049.1 [P16050-1]
PIRiA31349
RefSeqiNP_001131.3, NM_001140.3 [P16050-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
SMRiP16050
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106747, 4 interactors
DIPiDIP-60388N
IntActiP16050, 4 interactors
STRINGi9606.ENSP00000458832

Chemistry databases

BindingDBiP16050
ChEMBLiCHEMBL2903
DrugBankiDB08492, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID
DB09061, Cannabidiol
DB14009, Medical Cannabis
DB14011, Nabiximols
DB02709, Resveratrol
DrugCentraliP16050
GuidetoPHARMACOLOGYi1388
SwissLipidsiSLP:000000667

PTM databases

iPTMnetiP16050
MetOSiteiP16050
PhosphoSitePlusiP16050

Genetic variation databases

BioMutaiALOX15
DMDMi126396

Proteomic databases

jPOSTiP16050
MassIVEiP16050
PaxDbiP16050
PeptideAtlasiP16050
PRIDEiP16050
ProteomicsDBi53264 [P16050-1]
7049

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		2761, 326 antibodies

Genome annotation databases

EnsembliENST00000293761; ENSP00000293761; ENSG00000161905 [P16050-1]
ENST00000570836; ENSP00000458832; ENSG00000161905 [P16050-1]
ENST00000574640; ENSP00000460483; ENSG00000161905 [P16050-2]
GeneIDi246
KEGGihsa:246
UCSCiuc002fyh.4, human [P16050-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		246
DisGeNETi246

GeneCards: human genes, protein and diseases

More...GeneCardsi		ALOX15
HGNCiHGNC:433, ALOX15
HPAiENSG00000161905, Tissue enhanced (adipose tissue, blood, lung)
MIMi152392, gene
neXtProtiNX_P16050
OpenTargetsiENSG00000161905
PharmGKBiPA48
VEuPathDBiHostDB:ENSG00000161905.12

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QQSP, Eukaryota
GeneTreeiENSGT00940000162807
HOGENOMiCLU_004282_3_3_1
InParanoidiP16050
OMAiLNILTCW
OrthoDBi385042at2759
PhylomeDBiP16050
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayiUPA00881
BioCyciMetaCyc:HS08621-MONOMER
BRENDAi1.13.11.33, 2681
PathwayCommonsiP16050
ReactomeiR-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-RKiP16050
SIGNORiP16050

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		246, 3 hits in 878 CRISPR screens

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ALOX15

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		246
PharosiP16050, Tchem

Protein Ontology

More...PROi		PR:P16050
RNActiP16050, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000161905, Expressed in nasal cavity epithelium and 107 other tissues
GenevisibleiP16050, HS

Family and domain databases

CDDicd01753, PLAT_LOX, 1 hit
DisProtiDP02162
InterProiView 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
PANTHERiPTHR11771, PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit
PRINTSiPR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOX15_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16050
Secondary accession number(s): A8K2P4
, B7ZA11, Q8N6R7, Q99657
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again