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Entry version 150 (17 Jun 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Polyunsaturated fatty acid lipoxygenase ALOX15

Gene

ALOX15

Organism
Oryctolagus cuniculus (Rabbit)
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:18311922, PubMed:9414270, PubMed:9600854, PubMed:17493578, PubMed:15123652). Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE (PubMed:9414270, PubMed:9600854, PubMed:17493578, PubMed:15123652). Also converts linoleic acid into 13-hydroperoxyoctadecadienoic acid. 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 (PubMed:15123652). Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway (By similarity). 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. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass (By similarity).By similarity5 Publications

Caution

According to the authors the mRNA described in PubMed:9600854 may be encoded by a gene different from ALOX15.Curated

<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

kcat is 22.2 sec(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoate as substrate (PubMed:15123652). kcat is 1.34 sec(-1) with (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate as substrate (PubMed:15123652).1 Publication
  1. KM=20 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  2. KM=49 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine1 Publication
  3. KM=98 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine1 Publication
  4. KM=48 µM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate1 Publication
  5. KM=20.5 µM for (5Z,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  6. KM=91.5 µM for (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate1 Publication

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

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi361Iron; catalyticPROSITE-ProRule annotation1 Publication1
    Metal bindingi366Iron; catalyticPROSITE-ProRule annotation1 Publication1
    Metal bindingi541Iron; catalyticPROSITE-ProRule annotation1 Publication1
    Metal bindingi545Iron; catalyticPROSITE-ProRule annotation1 Publication1
    Metal bindingi663Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication1

    <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
    1.13.11.33 1749

    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:000001603

    <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 ALOX15By similarity
    Alternative name(s):
    12/15-lipoxygenaseBy similarity
    Arachidonate 12-lipoxygenase, leukocyte-typeBy similarity (EC:1.13.11.311 Publication)
    Short name:
    12-LOX
    Short name:
    L-12LO
    Arachidonate 15-lipoxygenase (EC:1.13.11.332 Publications)
    Short name:
    15-LOX
    Arachidonate omega-6 lipoxygenaseBy similarity
    Erythroid cell-specific 15-lipoxygenase1 Publication
    Hepoxilin A3 synthase Alox15By similarity (EC:1.13.11.-By similarity)
    Linoleate 13S-lipoxygenaseBy similarity (EC:1.13.11.12By similarity)
    <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:ALOX15By similarity
    <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>OrganismiOryctolagus cuniculus (Rabbit)
    <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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    <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
    • UP000001811 <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: Unplaced

    <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

    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>Mutagenesisi353F → L: Changes the stereoselectivity of the oxygenation reaction to produce (12S)-HPETE instead of (15S)-HPETE. 1 Publication1
    Mutagenesisi418I → A: Decreases 15 lipoxygenase activity. Exhibits hepoxilin A3 synthase activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4358

    DrugCentral

    More...
    DrugCentrali
    P12530

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00002206992 – 663Polyunsaturated fatty acid lipoxygenase ALOX15Add BLAST662

    PTM databases

    MetOSite database of methionine sulfoxide sites

    More...
    MetOSitei
    P12530

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

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

    Detected in reticulocytes (at protein level).1 Publication

    <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

    STRING: functional protein association networks

    More...
    STRINGi
    9986.ENSOCUP00000017072

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P12530

    <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

    Secondary structure

    1663
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P12530

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P12530

    <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

    More...
    eggNOGi
    ENOG410IKAN Eukaryota
    ENOG410YN4N LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P12530

    KEGG Orthology (KO)

    More...
    KOi
    K00460

    Database of Orthologous Groups

    More...
    OrthoDBi
    385042at2759

    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>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.

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

    P12530-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK
    60 70 80 90 100
    VNVSKYLGSL LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW
    110 120 130 140 150
    VVGDGVQSLP VGTGCTTVGD PQGLFQKHRE QELEERRKLY QWGSWKEGLI
    160 170 180 190 200
    LNVAGSKLTD LPVDERFLED KKIDFEASLA WGLAELALKN SLNILAPWKT
    210 220 230 240 250
    LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM LLRRSVQLPA
    260 270 280 290 300
    RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP
    310 320 330 340 350
    LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS
    360 370 380 390 400
    SDFQVHELNS HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI
    410 420 430 440 450
    NVRARNGLVS DFGIFDQIMS TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD
    460 470 480 490 500
    RGLLGVESSF YAQDALRLWE IISRYVQGIM GLYYKTDEAV RDDLELQSWC
    510 520 530 540 550
    REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ HSSIHLGQLD
    560 570 580 590 600
    WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD
    610 620 630 640 650
    QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE
    660
    YLRPSIVENS VAI
    Length:663
    Mass (Da):75,310
    Last modified:January 23, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC3391E1E6E7930BF
    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 conflicti42T → S in CAB10746 (PubMed:9600854).Curated1
    Sequence conflicti64R → K in CAB10746 (PubMed:9600854).Curated1
    Sequence conflicti190N → D in AAB86978 (PubMed:2777088).Curated1
    Sequence conflicti194I → V in AAB86978 (PubMed:2777088).Curated1
    Sequence conflicti353F → L in CAB10746 (PubMed:9600854).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
    M33291 Genomic DNA Translation: AAA75014.1
    Z97654 mRNA Translation: CAB10746.1
    M27214 mRNA Translation: AAB86978.1
    M22617 mRNA Translation: AAA31385.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JQ0018

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001075751.1, NM_001082282.1
    NP_001139620.1, NM_001146148.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    100009114
    100271999

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ocu:100009114
    ocu:100271999

    <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
    M33291 Genomic DNA Translation: AAA75014.1
    Z97654 mRNA Translation: CAB10746.1
    M27214 mRNA Translation: AAB86978.1
    M22617 mRNA Translation: AAA31385.1
    PIRiJQ0018
    RefSeqiNP_001075751.1, NM_001082282.1
    NP_001139620.1, NM_001146148.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1LOXX-ray2.40A2-663[»]
    2P0MX-ray2.40A/B2-663[»]
    SMRiP12530
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000017072

    Chemistry databases

    BindingDBiP12530
    ChEMBLiCHEMBL4358
    DrugCentraliP12530
    SwissLipidsiSLP:000001603

    PTM databases

    MetOSiteiP12530

    Genome annotation databases

    GeneIDi100009114
    100271999
    KEGGiocu:100009114
    ocu:100271999

    Organism-specific databases

    Comparative Toxicogenomics Database

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    CTDi
    239
    246

    Phylogenomic databases

    eggNOGiENOG410IKAN Eukaryota
    ENOG410YN4N LUCA
    InParanoidiP12530
    KOiK00460
    OrthoDBi385042at2759

    Enzyme and pathway databases

    UniPathwayiUPA00881
    BRENDAi1.13.11.33 1749

    Miscellaneous databases

    EvolutionaryTraceiP12530

    Protein Ontology

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    PROi
    PR:P12530

    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
    Search...

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

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOX15_RABIT
    <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: P12530
    Secondary accession number(s): O19043
    <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: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: June 17, 2020
    This is version 150 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

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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