Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 190 (08 May 2019)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Arachidonate 15-lipoxygenase

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. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

<p>This subsection of the ‘Function’ 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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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.
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 ‘Function’ 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

GO - Biological processi

<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

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_and_taxonomy_section">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:
Arachidonate 15-lipoxygenase (EC:1.13.11.332 Publications)
Short name:
15-LOX
Short name:
15-LOX-1
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.311 Publication)
Short name:
12-LOX
Arachidonate omega-6 lipoxygenase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ALOX15
Synonyms:LOG15
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

<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 variations 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_and_biotech_section">'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

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

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1388

Polymorphism and mutation 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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002206972 – 662Arachidonate 15-lipoxygenaseAdd BLAST661

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
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 human proteome resource

More...
ProteomicsDBi
53264

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
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 81 organ(s), highest expression level in nasal cavity epithelium

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P16050 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P16050 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004962
CAB004963
HPA013859

<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_section">'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_section">'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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
PEBP1P300863EBI-14035397,EBI-716384

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, 2 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000458832

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P16050

<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

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[»]

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

More...
SMRi
P16050

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_and_domains_section">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
ENOG410IKAN Eukaryota
ENOG410YN4N LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000162807

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16050

KEGG Orthology (KO)

More...
KOi
K00460

Identification of Orthologs from Complete Genome Data

More...
OMAi
TVATMRC

Database of Orthologous Groups

More...
OrthoDBi
696548at2759

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P16050-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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.

Note: No experimental confirmation available.
Show »
Length:623
Mass (Da):70,108
Checksum:i71B99C6D8E707189
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L175I3L175_HUMAN
Arachidonate 15-lipoxygenase
ALOX15
109Annotation score:

Annotation score:1 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 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:rs11568142Ensembl.1
Natural variantiVAR_035036102G → V. Corresponds to variant dbSNP:rs41439950Ensembl.1
Natural variantiVAR_018747103N → K1 PublicationCorresponds to variant dbSNP:rs11568099Ensembl.1
Natural variantiVAR_018748205R → Q1 PublicationCorresponds to variant dbSNP:rs11568101Ensembl.1
Natural variantiVAR_035037239V → M. Corresponds to variant dbSNP:rs3892408Ensembl.1
Natural variantiVAR_035038461A → P1 PublicationCorresponds to variant dbSNP:rs17852628Ensembl.1
Natural variantiVAR_035039560T → M Loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs34210653Ensembl.1

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, Polymorphism

<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_references_section">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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
SMRiP16050
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106747, 4 interactors
DIPiDIP-60388N
IntActiP16050, 2 interactors
STRINGi9606.ENSP00000458832

Chemistry databases

BindingDBiP16050
ChEMBLiCHEMBL2903
DrugBankiDB08492 (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID
GuidetoPHARMACOLOGYi1388
SwissLipidsiSLP:000000667

PTM databases

iPTMnetiP16050
PhosphoSitePlusiP16050

Polymorphism and mutation databases

BioMutaiALOX15
DMDMi126396

Proteomic databases

jPOSTiP16050
PaxDbiP16050
PeptideAtlasiP16050
PRIDEiP16050
ProteomicsDBi53264

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
HPAiCAB004962
CAB004963
HPA013859
MIMi152392 gene
neXtProtiNX_P16050
OpenTargetsiENSG00000161905
PharmGKBiPA48

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IKAN Eukaryota
ENOG410YN4N LUCA
GeneTreeiENSGT00940000162807
InParanoidiP16050
KOiK00460
OMAiTVATMRC
OrthoDBi696548at2759
PhylomeDBiP16050
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayi
UPA00881

BioCyciMetaCyc:HS08621-MONOMER
BRENDAi1.13.11.33 2681
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

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

Protein Ontology

More...
PROi
PR:P16050

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000161905 Expressed in 81 organ(s), highest expression level in nasal cavity epithelium
ExpressionAtlasiP16050 baseline and differential
GenevisibleiP16050 HS

Family and domain databases

CDDicd01753 PLAT_LOX, 1 hit
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...

<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_and_isoforms">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: May 8, 2019
This is version 190 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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