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Entry version 155 (29 Sep 2021)
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:9600854, PubMed:9414270, PubMed:15123652, PubMed:17493578, PubMed:18311922).

It inserts peroxyl groups at C12 or C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing both 12-hydroperoxyeicosatetraenoate/12-HPETE and 15-hydroperoxyeicosatetraenoate/15-HPETE (PubMed:9600854, PubMed:9414270, PubMed:15123652, PubMed:17493578).

It may then act on 12-HPETE to produce hepoxilins, which may show proinflammatory properties (PubMed:15123652).

Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to 13-hydroperoxyoctadecadienoate. May participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs)like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively downregulate the immune response and have anti-aggregation properties with platelets. Can convert epoxy fatty acids to hydroperoxy-epoxides derivatives followed by an intramolecular nucleophilic substitution leading to the formation of monocyclic endoperoxides (By similarity).

Plays an important role during the maintenance of self-tolerance by peroxidizing membrane-bound phosphatidylethanolamine which can then signal the sorting process for clearance of apoptotic cells during inflammation and prevent an autoimmune response. In addition to its role in the immune and inflammatory responses, this enzyme may play a role in epithelial wound healing in the cornea through production of lipoxin A4 (LXA4) and docosahexaenoic acid-derived neuroprotectin D1 (NPD1; 10R,17S-HDHA), both lipid autacoids exhibit anti-inflammatory and neuroprotective properties. Furthermore, it may regulate actin polymerization which is crucial for several biological processes such as the phagocytosis of apoptotic cells. It is also implicated in the generation of endogenous ligands for peroxisome proliferator activated receptor (PPAR-gamma), hence modulating macrophage development and function. It may also exert a negative effect on skeletal development by regulating bone mass through this pathway. As well as participates in ER stress and downstream inflammation in adipocytes, pancreatic islets, and liver (By similarity).

Finally, it is also involved in the cellular response to IL13/interleukin-13 (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_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 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_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.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_section">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
1.13.11.31, 1749
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_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:
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_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:ALOX15By similarity
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<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
  • UP000001811 <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: 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

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_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>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_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator 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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.

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_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 – 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
ENOG502QQSP, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P12530

Identification of Orthologs from Complete Genome Data

More...
OMAi
WETISRY

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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

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

More...
CTDi
239
246

Phylogenomic databases

eggNOGiENOG502QQSP, Eukaryota
InParanoidiP12530
OMAiWETISRY
OrthoDBi385042at2759

Enzyme and pathway databases

UniPathwayiUPA00881
BRENDAi1.13.11.31, 1749
1.13.11.33, 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

MobiDB: a database of protein disorder and mobility annotations

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOX15_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_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: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 155 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
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