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Entry version 163 (07 Oct 2020)
Sequence version 3 (27 Jul 2011)
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Protein

Polyunsaturated fatty acid 5-lipoxygenase

Gene

Alox5

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

Catalyzes the oxygenation of arachidonic acid to 5-hydroperoxyicosatetraenoic acid (5-HPETE) followed by the dehydration of the hydroperoxide into an epoxide, 5,6- oxidoicosatetraenoic acid (LTA4), thereby participates in the first step in leukotriene biosynthesis and in the inflammatory processes (PubMed:7629107, PubMed:7809134, PubMed:7969451, PubMed:23246375, PubMed:31642348). Also catalyzes the oxygenation of arachidonic acid into 8-hydroperoxyicosatetraenoic acid (8-HPETE) and 12-hydroperoxyicosatetraenoic acid (12-HPETE) (PubMed:23246375). Although arachidonic acid is the preferred substrate, can also metabolize oxidized fatty acids derived from arachidonic acid such as (15S)-HETE, eicosapentaenoic acid (EPA) such as 18R- and 18S-HEPE or docosahexaenoic (DHA) acid which leads to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore plays a role in anti-inflammatory response (PubMed:31642348). Also displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (By similarity). Oxidation of docosahexaenoic acid directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma) (PubMed:21307302). Does not catalyzes the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxins isomers (PubMed:31642348). In addition to inflammatory processes, participates in dendritic cell migration, wound healing through an antioxidant mechanism based on HO1 regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (PubMed:24226420, PubMed:23720274, PubMed:17392829, PubMed:28965882). Moreover, establishes an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21224059). Also may play a role in glucose homeostasis, regulation of INS secretion and palmitic acid-induced insulin resistance via AMPK (PubMed:28694473, PubMed:18421434). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (PubMed:24906289).By similarity14 Publications

Miscellaneous

Can be converted from pro-inflammatory 5-lipoxygenase to anti-inflammatory 15-lipoxygenase by reducing the volume of the substrate-binding pocket.1 Publication

<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 '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

  1. KM=44.7 µM for arachidonic acid1 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: leukotriene A4 biosynthesis

    This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway leukotriene A4 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 bindingi17Calcium 1; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi18Calcium 2; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi19Calcium 2; structuralBy similarity1
    Metal bindingi44Calcium 2; structuralBy similarity1
    Metal bindingi45Calcium 2; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi47Calcium 2; structuralBy similarity1
    Metal bindingi79Calcium 1; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi80Calcium 1; via carbonyl oxygen; structuralBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei103Essential for stabilizing binding to COTL1By similarity1
    Metal bindingi368Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1
    Metal bindingi373Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1
    Metal bindingi551Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1
    Metal bindingi555Iron; catalyticPROSITE-ProRule annotationBy similarity1
    Metal bindingi674Iron; via carbonyl oxygen; catalyticPROSITE-ProRule annotationBy similarity1

    <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, Hydrolase, Oxidoreductase
    Biological processLeukotriene biosynthesis
    LigandCalcium, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.13.11.34, 3474

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-2142688, Synthesis of 5-eicosatetraenoic acids
    R-MMU-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
    R-MMU-2142700, Synthesis of Lipoxins (LX)
    R-MMU-6798695, Neutrophil degranulation
    R-MMU-9018676, Biosynthesis of D-series resolvins
    R-MMU-9018682, Biosynthesis of maresins
    R-MMU-9018896, Biosynthesis of E-series 18(S)-resolvins
    R-MMU-9020265, Biosynthesis of aspirin-triggered D-series resolvins
    R-MMU-9023661, Biosynthesis of E-series 18(R)-resolvins
    R-MMU-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins
    R-MMU-9026290, Biosynthesis of DPAn-3-derived maresins
    R-MMU-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins
    R-MMU-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

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

    More...
    UniPathwayi
    UPA00877

    <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 5-lipoxygenaseCurated (EC:1.13.11.-By similarity)
    Alternative name(s):
    Arachidonate 5-lipoxygenase (EC:1.13.11.341 Publication)
    Short name:
    5-LOBy similarity
    Short name:
    5-lipoxygenase1 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:Alox5Imported
    <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 6

    Organism-specific databases

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

    More...
    MGIi
    MGI:87999, Alox5

    <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

    Cytoplasm, Membrane, Nucleus

    <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

    Homozygous mice for ALOX5 are also present in the expected ratios. Mice are indistinguishable in growth and size from wild type littermates (PubMed:7809134). Homozygous mice for ALOX5 show no apparent abnormalities up to ten months of age under normal physiological conditions, except that the spleen is usually smaller for 8-week-old mice (PubMed:7969451).2 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>Mutagenesisi360F → W: Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE). Exhibits a (8S)-lipoxygenase activity; when associated with I-425. Exhibits a (15S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with G-411; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with G-411; I-425 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE;when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize proinflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426. 2 Publications1
    Mutagenesisi411A → G: Decreases (5S)-lipoxygenase activity. Forms 9-hydroperoxyicosatetraenoic acid (9-HPETE) as the major arachidonic acid oxygenation product. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; I-425 and M-426. 1 Publication1
    Mutagenesisi425A → I: Decreases arachidonate (5S)-lipoxygenase activity. Decreases arachidonate 5 lipoxygenase activity; when associated with A-604. Exhibits a (8S)-lipoxygenase activity; when associated with W-360. Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize proinflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426. 2 Publications1
    Mutagenesisi426N → M: Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE) and (12S)-hydroperoxyicosatetraenoic acid ((12S)-HPETE). Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and I-425. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and I-425. 2 Publications1
    Mutagenesisi604A → I: Decreases arachidonate (5S)-lipoxygenase activity. 1 Publication1
    Mutagenesisi672V → M: Loss of activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5211

    DrugCentral

    More...
    DrugCentrali
    P48999

    <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_00002206951 – 674Polyunsaturated fatty acid 5-lipoxygenaseAdd BLAST674

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei272PhosphoserineBy similarity1
    Modified residuei524PhosphoserineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-524 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus. Phosphorylation at Ser-524 is stimulated by 8-bromo-3',5'-cyclic AMP or prostaglandin E2.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P48999

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

    More...
    PaxDbi
    P48999

    PeptideAtlas

    More...
    PeptideAtlasi
    P48999

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P48999

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P48999

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

    More...
    PhosphoSitePlusi
    P48999

    <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

    Expressed in skin Langerhans cells and their emigrated counterparts in draining lymph nodes (PubMed:17392829). Highly expressed in circulating leukocytes (PubMed:21307302).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

    IncreaseD by both NF-kappa-B and SP1 in LPS-treated monocytes.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000025701, Expressed in granulocyte and 136 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P48999, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P48999, 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

    Homodimer.

    Interacts with ALOX5AP and LTC4S.

    Interacts with COTL1, the interaction is required for stability and efficient catalytic activity.

    Interacts with PIK3R1; this interaction bridges ALOX5 with CD40 after CD40 ligation in B cells and leads to the production of reactive oxygen species (ROS).

    Interacts (via PLAT domain) with DICER1 (via Dicer dsRNA-binding fold domain); this interaction enhances arachidonate 5-lipoxygenase activity and modifies the miRNA precursor processing activity of DICER1.

    By similarity

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    198076, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000026795

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P48999

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P48999, 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
    P48999

    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 – 118PLATPROSITE-ProRule annotationAdd BLAST117
    Domaini119 – 674LipoxygenasePROSITE-ProRule annotationAdd BLAST556

    <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
    ENSGT00940000156111

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P48999

    KEGG Orthology (KO)

    More...
    KOi
    K00461

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FPDMIKS

    Database of Orthologous Groups

    More...
    OrthoDBi
    385042at2759

    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%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>Sequence (1+)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.

    This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

    P48999-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA
    60 70 80 90 100
    VDSYDVTVDE ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC
    110 120 130 140 150
    YRWITGEGEI VLRDGRAKLA RDDQIHILKQ HRRKELEARQ KQYRWMEWNP
    160 170 180 190 200
    GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS
    210 220 230 240 250
    SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG CNPVLIKRCT
    260 270 280 290 300
    ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP
    310 320 330 340 350
    CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL
    360 370 380 390 400
    AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH
    410 420 430 440 450
    VRFTIAINTK AREQLICEYG LFDKANATGG GGHVQMVQRA VQDLTYSSLC
    460 470 480 490 500
    FPEAIKARGM DSTEDIPFYF YRDDGLLVWE AIQSFTMEVV SIYYENDQVV
    510 520 530 540 550
    EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL TVVIFTASAQ
    560 570 580 590 600
    HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW
    610 620 630 640 650
    HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA
    660 670
    ERNKNKKLPY YYLSPDRIPN SVAI
    Length:674
    Mass (Da):77,967
    Last modified:July 27, 2011 - 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:i130F27F9A77A3D88
    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 are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E9Q6H6E9Q6H6_MOUSE
    Polyunsaturated fatty acid 5-lipoxy...
    Alox5
    642Annotation 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>
    E9QA93E9QA93_MOUSE
    Polyunsaturated fatty acid 5-lipoxy...
    Alox5
    617Annotation 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>
    A0A0N4SW45A0A0N4SW45_MOUSE
    Polyunsaturated fatty acid 5-lipoxy...
    Alox5
    434Annotation 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 conflicti466I → M in AAC37673 (PubMed:7629107).Curated1
    Sequence conflicti646V → I in AAC37673 (PubMed:7629107).Curated1

    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
    L42198 mRNA Translation: AAC37673.1
    AK137481 mRNA Translation: BAE23373.1
    AK171413 mRNA Translation: BAE42439.1
    BC139102 mRNA Translation: AAI39103.1
    BC141213 mRNA Translation: AAI41214.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS20452.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I49479

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_033792.1, NM_009662.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    11689

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:11689

    UCSC genome browser

    More...
    UCSCi
    uc009dkd.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
    L42198 mRNA Translation: AAC37673.1
    AK137481 mRNA Translation: BAE23373.1
    AK171413 mRNA Translation: BAE42439.1
    BC139102 mRNA Translation: AAI39103.1
    BC141213 mRNA Translation: AAI41214.1
    CCDSiCCDS20452.1
    PIRiI49479
    RefSeqiNP_033792.1, NM_009662.2

    3D structure databases

    SMRiP48999
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi198076, 4 interactors
    STRINGi10090.ENSMUSP00000026795

    Chemistry databases

    BindingDBiP48999
    ChEMBLiCHEMBL5211
    DrugCentraliP48999

    PTM databases

    iPTMnetiP48999
    PhosphoSitePlusiP48999

    Proteomic databases

    MaxQBiP48999
    PaxDbiP48999
    PeptideAtlasiP48999
    PRIDEiP48999

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    3906, 749 antibodies

    Genome annotation databases

    EnsembliENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701
    GeneIDi11689
    KEGGimmu:11689
    UCSCiuc009dkd.1, mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    240
    MGIiMGI:87999, Alox5

    Phylogenomic databases

    eggNOGiENOG502QQSP, Eukaryota
    GeneTreeiENSGT00940000156111
    InParanoidiP48999
    KOiK00461
    OMAiFPDMIKS
    OrthoDBi385042at2759
    TreeFamiTF105320

    Enzyme and pathway databases

    UniPathwayiUPA00877
    BRENDAi1.13.11.34, 3474
    ReactomeiR-MMU-2142688, Synthesis of 5-eicosatetraenoic acids
    R-MMU-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
    R-MMU-2142700, Synthesis of Lipoxins (LX)
    R-MMU-6798695, Neutrophil degranulation
    R-MMU-9018676, Biosynthesis of D-series resolvins
    R-MMU-9018682, Biosynthesis of maresins
    R-MMU-9018896, Biosynthesis of E-series 18(S)-resolvins
    R-MMU-9020265, Biosynthesis of aspirin-triggered D-series resolvins
    R-MMU-9023661, Biosynthesis of E-series 18(R)-resolvins
    R-MMU-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins
    R-MMU-9026290, Biosynthesis of DPAn-3-derived maresins
    R-MMU-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins
    R-MMU-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    11689, 1 hit in 18 CRISPR screens

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

    More...
    ChiTaRSi
    Alox5, mouse

    Protein Ontology

    More...
    PROi
    PR:P48999
    RNActiP48999, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000025701, Expressed in granulocyte and 136 other tissues
    ExpressionAtlasiP48999, baseline and differential
    GenevisibleiP48999, 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

    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 nameiLOX5_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: P48999
    Secondary accession number(s): Q3TB75
    <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, 1996
    Last sequence update: July 27, 2011
    Last modified: October 7, 2020
    This is version 163 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

    <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
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