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UniProtKB - O35936 (ALOX8_MOUSE)

Protein

Arachidonate 8S-lipoxygenase

Gene

Alox8

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. Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively. From arachidonate mainly produces (8S)-HPETE and in addition, minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE. With arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity. However, it may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE. May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway.4 Publications

Caution

Despite its homology with human ALOX15B (AC O15296), it seems not to have any 15S-lipoxygenase activity on arachidonate. Based on its catalytic activity it is referred to as the mouse arachidonate 8S-lipoxygenase.Curated

<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 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

The highest catalytic efficiency is observed with arachidonate followed by (8S)-HPETE and(15S)-HPETE with similar efficiencies.
  1. KM=1.2 µM for arachidonate (at pH 7.4 and 25 degrees Celsius)1 Publication
  2. KM=2.1 µM for (8S)-HPETE (at pH 7.4 and 25 degrees Celsius)1 Publication
  3. KM=5.7 µM for (8S)-HETE (at pH 7.4 and 25 degrees Celsius)1 Publication
  4. KM=39 µM for (15S)-HPETE (at pH 7.4 and 25 degrees Celsius)1 Publication
  5. KM=15 µM for (15S)-HETE (at pH 7.4 and 25 degrees Celsius)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 bindingi15Calcium 1; via carbonyl oxygenBy similarity1
    Metal bindingi17Calcium 1; via carbonyl oxygenBy similarity1
    Metal bindingi39Calcium 2By similarity1
    Metal bindingi40Calcium 2; via carbonyl oxygenBy similarity1
    Metal bindingi42Calcium 2; via carbonyl oxygenBy similarity1
    Metal bindingi44Calcium 2By similarity1
    Metal bindingi86Calcium 1By similarity1
    Metal bindingi87Calcium 1; via carbonyl oxygenBy similarity1
    Metal bindingi374Iron; catalyticPROSITE-ProRule annotation1
    Metal bindingi379Iron; catalyticPROSITE-ProRule annotation1
    Metal bindingi554Iron; catalyticPROSITE-ProRule annotation1
    Metal bindingi677Iron; 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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

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

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

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

    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:000000650
    SLP:000000742

    <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 8S-lipoxygenase (EC:1.13.11.-)
    Short name:
    8-LOX
    Short name:
    8S-LOX
    Alternative name(s):
    15-lipoxygenase 2
    Short name:
    15-LOX-2
    Arachidonate 15-lipoxygenase B
    Short name:
    15-LOX-B
    <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:Alox8
    Synonyms:Alox15b
    <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>OrganismiMus musculus (Mouse)
    <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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
    <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
    • UP000000589 <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 11

    Organism-specific databases

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

    More...    MGIi    		MGI:1098228 Alox8

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, 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

    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>Mutagenesisi374H → L: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi558S → A, H or N: Retains catalytic activity indicating it is not required for iron ligand-binding. 1 Publication1
    Mutagenesisi603Y → D: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with V-604. 1 Publication1
    Mutagenesisi604H → V: Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with D-603. 1 Publication1

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002207011 – 677Arachidonate 8S-lipoxygenaseAdd BLAST677

    Proteomic databases

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

    More...    PaxDbi    		O35936

    PRoteomics IDEntifications database

    More...    PRIDEi    		O35936

    PTM databases

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

    More...    PhosphoSitePlusi    		O35936

    <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 epidermis and brain. No expression found in heart, spleen, liver, skeletal muscle, kidney or testis.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

    By phorbol ester.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSMUSG00000020891 Expressed in 41 organ(s), highest expression level in skin of back

    CleanEx database of gene expression profiles

    More...    CleanExi    		MM_ALOX8

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		O35936 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		O35936 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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		10090.ENSMUSP00000021262

    <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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		O35936

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

    More...    SMRi    		O35936

    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 – 125PLATPROSITE-ProRule annotationAdd BLAST124
    Domaini126 – 677LipoxygenasePROSITE-ProRule annotationAdd BLAST552

    <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    		ENOG410IF0U Eukaryota
    ENOG410YN4N LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000161510

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000234358

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG005150

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		O35936

    KEGG Orthology (KO)

    More...    KOi    		K08022

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		EFSIHEA

    Database of Orthologous Groups

    More...    OrthoDBi    		385042at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		O35936

    TreeFam database of animal gene trees

    More...    TreeFami    		TF105320

    Family and domain databases

    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

    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>Sequence (1+)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.

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

    O35936-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAKCRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE 
            60         70         80         90        100
    EDFEVTLPQD VGTVLMLRVH KAPPEVSLPL MSFRSDAWFC RWFELEWLPG 
           110        120        130        140        150
    AALHFPCYQW LEGAGELVLR EGAAKVSWQD HHPTLQDQRQ KELESRQKMY 
           160        170        180        190        200
    SWKTYIEGWP RCLDHETVKD LDLNIKYSAM KNAKLFFKAH SAYTELKVKG 
           210        220        230        240        250
    LLDRTGLWRS LREMRRLFNF RKTPAAEYVF AHWQEDAFFA SQFLNGINPV 
           260        270        280        290        300
    LIRRCHSLPN NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVH 
           310        320        330        340        350
    TNILNGKPQF SAAPMTLLHQ SSGSGPLLPI AIQLKQTPGP DNPIFLPSDD 
           360        370        380        390        400
    TWDWLLAKTW VRNSEFYIHE AVTHLLHAHL IPEVFALATL RQLPRCHPLF 
           410        420        430        440        450
    KLLIPHIRYT LHINTLAREL LVAPGKLIDK STGLGTGGFS DLIKRNMEQL 
           460        470        480        490        500
    NYSVLCLPED IRARGVEDIP GYYYRDDGMQ IWGAIKSFVS EIVSIYYPSD 
           510        520        530        540        550
    TSVQDDQELQ AWVREIFSEG FLGRESSGMP SLLDTREALV QYITMVIFTC 
           560        570        580        590        600
    SAKHAAVSSG QFDSCVWMPN LPPTMQLPPP TSKGQARPES FIATLPAVNS 
           610        620        630        640        650
    SSYHIIALWL LSAEPGDQRP LGHYPDEHFT EDAPRRSVAA FQRKLIQISK 
           660        670 
    GIRERNRGLA LPYTYLDPPL IENSVSI
    Length:677
    Mass (Da):76,230
    Last modified:January 1, 1998 - v1
    <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:i78DB1AC9C2F68399
    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
    B1ASX6B1ASX6_MOUSE
    Arachidonate 8S-lipoxygenase
    Alox8
    		648Annotation score:

    Annotation score:2 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>

    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 varianti32E → G in clone K12. 1
    Natural varianti38L → M in clone G2. 1
    Natural varianti58P → R in clone K12. 1
    Natural varianti76V → A in clones G2, G5, G11 and K1. 1
    Natural varianti413I → V in clone K7. 1
    Natural varianti536R → Q in clones G2, G5 and G11. 1

    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
    		U93277 mRNA Translation: AAC53356.1
    Y14696 mRNA Translation: CAA75003.1
    AK028724 mRNA Translation: BAC26085.1
    AL645527 Genomic DNA No translation available.
    BC015253 mRNA Translation: AAH15253.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS24886.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_033791.1, NM_009661.4

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Mm.289672

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENSMUST00000021262; ENSMUSP00000021262; ENSMUSG00000020891

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		11688

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mmu:11688

    UCSC genome browser

    More...    UCSCi    		uc007jpl.1 mouse

    Keywords - Coding sequence diversityi

    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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U93277 mRNA Translation: AAC53356.1
    Y14696 mRNA Translation: CAA75003.1
    AK028724 mRNA Translation: BAC26085.1
    AL645527 Genomic DNA No translation available.
    BC015253 mRNA Translation: AAH15253.1
    CCDSiCCDS24886.1
    RefSeqiNP_033791.1, NM_009661.4
    UniGeneiMm.289672

    3D structure databases

    ProteinModelPortaliO35936
    SMRiO35936
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000021262

    Chemistry databases

    SwissLipidsiSLP:000000650
    SLP:000000742

    PTM databases

    PhosphoSitePlusiO35936

    Proteomic databases

    PaxDbiO35936
    PRIDEiO35936

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000021262; ENSMUSP00000021262; ENSMUSG00000020891
    GeneIDi11688
    KEGGimmu:11688
    UCSCiuc007jpl.1 mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		11688
    MGIiMGI:1098228 Alox8

    Phylogenomic databases

    eggNOGiENOG410IF0U Eukaryota
    ENOG410YN4N LUCA
    GeneTreeiENSGT00940000161510
    HOGENOMiHOG000234358
    HOVERGENiHBG005150
    InParanoidiO35936
    KOiK08022
    OMAiEFSIHEA
    OrthoDBi385042at2759
    PhylomeDBiO35936
    TreeFamiTF105320

    Enzyme and pathway databases

    UniPathwayi
    UPA00881

    ReactomeiR-MMU-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

    Miscellaneous databases

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

    More...    ChiTaRSi    		Alox8 mouse

    Protein Ontology

    More...    PROi    		PR:O35936

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSMUSG00000020891 Expressed in 41 organ(s), highest expression level in skin of back
    CleanExiMM_ALOX8
    ExpressionAtlasiO35936 baseline and differential
    GenevisibleiO35936 MM

    Family and domain databases

    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
    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 nameiALOX8_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: O35936
    Secondary accession number(s): B1ASX5
    <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: January 11, 2001
    Last sequence update: January 1, 1998
    Last modified: January 16, 2019
    This is version 158 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

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

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