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Entry version 168 (12 Aug 2020)
Sequence version 4 (11 Sep 2007)
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Protein

Polyunsaturated fatty acid lipoxygenase ALOX15

Gene

Alox15

Organism
Mus musculus (Mouse)
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:8188678). Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE (PubMed:8188678). Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid (PubMed:8188678). Converts epoxy fatty acids to hydroperoxy-epoxides derivatives followed by an intramolecular nucleophilic substitution between hydroperoxy and epoxy moieties leading to the formation of monocyclic endoperoxides (By similarity). May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3 (By similarity). Probably plays an important role in the immune and inflammatory responses (PubMed:11278875, PubMed:22503541, PubMed:10432118). 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 (PubMed:22503541). In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function (PubMed:11278875). May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway (PubMed:10432118). Finally, it is also involved in the cellular response to IL13/interleukin-13 (By similarity). 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 (PubMed:15708862). May also play a role in endoplasmic reticulum stress response and the regulation of bone mass (PubMed:14716014, PubMed:22215650).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 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 bindingi361Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi366Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi541Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi545Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi663Iron; 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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.13.11.31, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-MMU-2142712, Synthesis of 12-eicosatetraenoic acid derivatives
R-MMU-2142770, Synthesis of 15-eicosatetraenoic acid derivatives
R-MMU-9018677, Biosynthesis of DHA-derived SPMs
R-MMU-9018681, Biosynthesis of protectins
R-MMU-9018896, Biosynthesis of E-series 18(S)-resolvins
R-MMU-9023661, Biosynthesis of E-series 18(R)-resolvins
R-MMU-9025106, Biosynthesis of DPAn-6 SPMs
R-MMU-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins

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:000001638

<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-lipoxygenase1 Publication
Short name:
12/15-LO
Arachidonate 12-lipoxygenase, leukocyte-typeBy similarity (EC:1.13.11.311 Publication)
Short name:
12-LOX
Short name:
L-12LO1 Publication
Arachidonate 15-lipoxygenase (EC:1.13.11.331 Publication)
Short name:
15-LOX
Arachidonate omega-6 lipoxygenaseBy similarity
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:Alox12l
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:87997, Alox15

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are fertile and do not display overt phenotype. However, reduced endoplasmic reticulum stress response to high-fat diet is observed. Aged mice also display systemic autoimmunity, a significant and spontaneous production of several forms of autoantibodies being detected and glomerulonephritis and deposits of complement and immunoglobulins within their glomeruli being observed. They also display reduced bone mass.4 Publications

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>Mutagenesisi663Missing : Abolishes arachidonate 15-lipoxygenase activity. Abolishes arachidonate 12-lipoxygenase activity. Abolishes linoleate 13-lipoxygenase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3259476

<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 '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_00002206861 – 663Polyunsaturated fatty acid lipoxygenase ALOX15Add BLAST663

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P39654

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

More...
PaxDbi
P39654

PRoteomics IDEntifications database

More...
PRIDEi
P39654

PTM databases

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

More...
PhosphoSitePlusi
P39654

<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

Found in pituitary and pineal glands as well as leukocytes, kidney, aorta, small intestine and cornea (PubMed:15708862, PubMed:22503541, PubMed:8188678). Also expressed by resident peritoneal macrophages (at protein level) (PubMed:8798642).4 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 in response to endoplasmic reticulum stress (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000018924, Expressed in olfactory epithelium and 82 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P39654, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P39654, MM

<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.

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P39654, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000019068

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P39654

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P39654, 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

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SMRi
P39654

Database of comparative protein structure models

More...
ModBasei
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 – 115PLATPROSITE-ProRule annotationAdd BLAST114
Domaini116 – 663LipoxygenasePROSITE-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

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eggNOGi
ENOG502QQSP, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000162807

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_004282_3_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P39654

KEGG Orthology (KO)

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KOi
K00460

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
P39654

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

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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

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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>Sequencei

<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.

P39654-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGVYRIRVST GDSVYAGSNN EVYLWLIGQH GEASLGKLFR PCRNSEAEFK
60 70 80 90 100
VDVSEYLGPL LFVRVQKWHY LKEDAWFCNW ISVKGPGDQG SEYTFPCYRW
110 120 130 140 150
VQGTSILNLP EGTGCTVVED SQGLFRNHRE EELEERRSLY RWGNWKDGTI
160 170 180 190 200
LNVAATSISD LPVDQRFRED KRLEFEASQV LGTMDTVINF PKNTVTCWKS
210 220 230 240 250
LDDFNYVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM VLKRSTCLPA
260 270 280 290 300
RLVFPPGMEK LQAQLDEELK KGTLFEADFF LLDGIKANVI LCSQQYLAAP
310 320 330 340 350
LVMLKLQPDG QLLPIAIQLE LPKTGSTPPP IFTPLDPPMD WLLAKCWVRS
360 370 380 390 400
SDLQLHELQA HLLRGHLVAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI
410 420 430 440 450
NVRARSDLIS ERGFFDKVMS TGGGGHLDLL KQAGAFLTYS SLCPPDDLAE
460 470 480 490 500
RGLLDIDTCF YAKDALQLWQ VMNRYVVGMF DLYYKTDQAV QDDYELQSWC
510 520 530 540 550
QEITEIGLQG AQDRGFPTSL QSRAQACHFI TMCIFTCTAQ HSSIHLGQLD
560 570 580 590 600
WFYWVPNAPC TMRLPPPKTK DATMEKLMAT LPNPNQSTLQ INVVWLLGRR
610 620 630 640 650
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE
660
YLRPSLVENS VAI
Length:663
Mass (Da):75,445
Last modified:September 11, 2007 - v4
<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:i0D5412B4502B5799
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 conflicti37K → N in AAA64930 (PubMed:7811740).Curated1
Sequence conflicti119E → Q in AAA64930 (PubMed:7811740).Curated1
Sequence conflicti397T → N in AAA64930 (PubMed:7811740).Curated1
Sequence conflicti568K → T in CAJ18471 (Ref. 4) Curated1
Sequence conflicti568K → T in AAH56625 (PubMed:15489334).Curated1
Sequence conflicti568K → T in AAH81546 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U04331 mRNA Translation: AAA20658.1
L34570 mRNA Translation: AAA64930.1
AK142371 mRNA Translation: BAE25045.1
CT010263 mRNA Translation: CAJ18471.1
AL596096 Genomic DNA No translation available.
BC056625 mRNA Translation: AAH56625.1
BC081546 mRNA Translation: AAH81546.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS24944.1

Protein sequence database of the Protein Information Resource

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PIRi
B54075

NCBI Reference Sequences

More...
RefSeqi
NP_033790.3, NM_009660.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924

Database of genes from NCBI RefSeq genomes

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GeneIDi
11687

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11687

UCSC genome browser

More...
UCSCi
uc007juo.1, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04331 mRNA Translation: AAA20658.1
L34570 mRNA Translation: AAA64930.1
AK142371 mRNA Translation: BAE25045.1
CT010263 mRNA Translation: CAJ18471.1
AL596096 Genomic DNA No translation available.
BC056625 mRNA Translation: AAH56625.1
BC081546 mRNA Translation: AAH81546.1
CCDSiCCDS24944.1
PIRiB54075
RefSeqiNP_033790.3, NM_009660.3

3D structure databases

SMRiP39654
ModBaseiSearch...

Protein-protein interaction databases

IntActiP39654, 1 interactor
STRINGi10090.ENSMUSP00000019068

Chemistry databases

BindingDBiP39654
ChEMBLiCHEMBL3259476
SwissLipidsiSLP:000001638

PTM databases

PhosphoSitePlusiP39654

Proteomic databases

MaxQBiP39654
PaxDbiP39654
PRIDEiP39654

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
2761, 326 antibodies

Genome annotation databases

EnsembliENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924
GeneIDi11687
KEGGimmu:11687
UCSCiuc007juo.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
246
MGIiMGI:87997, Alox15

Phylogenomic databases

eggNOGiENOG502QQSP, Eukaryota
GeneTreeiENSGT00940000162807
HOGENOMiCLU_004282_3_3_1
InParanoidiP39654
KOiK00460
OMAiLNILTCW
OrthoDBi385042at2759
PhylomeDBiP39654
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayiUPA00881
BRENDAi1.13.11.31, 3474
ReactomeiR-MMU-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-MMU-2142712, Synthesis of 12-eicosatetraenoic acid derivatives
R-MMU-2142770, Synthesis of 15-eicosatetraenoic acid derivatives
R-MMU-9018677, Biosynthesis of DHA-derived SPMs
R-MMU-9018681, Biosynthesis of protectins
R-MMU-9018896, Biosynthesis of E-series 18(S)-resolvins
R-MMU-9023661, Biosynthesis of E-series 18(R)-resolvins
R-MMU-9025106, Biosynthesis of DPAn-6 SPMs
R-MMU-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
11687, 0 hits in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Alox15, mouse

Protein Ontology

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PROi
PR:P39654
RNActiP39654, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000018924, Expressed in olfactory epithelium and 82 other tissues
ExpressionAtlasiP39654, baseline and differential
GenevisibleiP39654, MM

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_MOUSE
<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: P39654
Secondary accession number(s): Q4FJY9, Q5F2E3, Q6PHB2
<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: February 1, 1995
Last sequence update: September 11, 2007
Last modified: August 12, 2020
This is version 168 of the entry and version 4 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

<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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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