Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P12527 (LOX5_RAT)

Entry version 162 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Polyunsaturated fatty acid 5-lipoxygenase

Gene

Alox5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the oxygenation of arachidonate to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation. Also catalyzes the oxygenation of arachidonate into 8-hydroperoxyicosatetraenoate (8-HPETE) and 12-hydroperoxyicosatetraenoate (12-HPETE). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene. Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (By similarity). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers. In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes. Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40. Also may play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK. Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe cationPROSITE-ProRule annotationBy similarityNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotationBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: leukotriene A4 biosynthesis

This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi17Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi18Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi19Calcium 2; structuralBy similarity1
Metal bindingi44Calcium 2; structuralBy similarity1
Metal bindingi45Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi47Calcium 2; structuralBy similarity1
Metal bindingi79Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi80Calcium 1; via carbonyl oxygen; structuralBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei103Essential for stabilizing binding to COTL1By similarity1
Metal bindingi367Iron; via tele nitrogen; catalyticBy similarity1
Metal bindingi372Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi550Iron; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi554Iron; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi673Iron; via carbonyl oxygen; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi673Iron; 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.13.11.34, 5301

Reactome - a knowledgebase of biological pathways and processes

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

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

More...UniPathwayi		UPA00877

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Polyunsaturated fatty acid 5-lipoxygenaseCurated (EC:1.13.11.-By similarity)
Alternative name(s):
Arachidonate 5-lipoxygenase (EC:1.13.11.34By similarity)
Short name:
5-LOBy similarity
Short name:
5-lipoxygenase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Alox5Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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

Organism-specific databases

Rat genome database

More...RGDi		2096, Alox5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL312

DrugCentral

More...DrugCentrali		P12527

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002206961 – 673Polyunsaturated fatty acid 5-lipoxygenaseAdd BLAST673

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei271PhosphoserineBy similarity1
Modified residuei523PhosphoserineBy similarity1

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

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect. Phosphorylation on Ser-271 prevents export from the nucleus. Phosphorylation at Ser-523 is stimulated by 8-bromo-3',5'-cyclic AMP or prostaglandin E2.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...PaxDbi		P12527

PRoteomics IDEntifications database

More...PRIDEi		P12527

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12527

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

More...PhosphoSitePlusi		P12527

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with ALOX5AP and LTC4S.

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

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

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

By similarity

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-48659N

Protein interaction database and analysis system

More...IntActi		P12527, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000017633

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P12527

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...SMRi		P12527

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 117PLATPROSITE-ProRule annotationAdd BLAST116
Domaini118 – 673LipoxygenasePROSITE-ProRule annotationAdd BLAST556

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQSP, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P12527

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12527

Family and domain databases

Conserved Domains Database

More...CDDi		cd01753, PLAT_LOX, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR042062, PLAT_LOX_verte

The PANTHER Classification System

More...PANTHERi		PTHR11771, PTHR11771, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00308, LH2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P12527-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG 
        60         70         80         90        100
RDSYDVTVDE ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY 
       110        120        130        140        150
RWITGEGEIV LRDGCAKLAR DDQIHILKQH RRKELETRQK QYRWMEWNPG 
       160        170        180        190        200
FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS 
       210        220        230        240        250
WHDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCTE 
       260        270        280        290        300
LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 
       310        320        330        340        350
THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA 
       360        370        380        390        400
KIWVRSSDFH IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV 
       410        420        430        440        450
RFTIAINTKA REQLNCEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF 
       460        470        480        490        500
PEAIKARGMD NTEDIPYYFY RDDGLLVWEA IQSFTTEVVS IYYEDDQVVE 
       510        520        530        540        550
EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH 
       560        570        580        590        600
AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH 
       610        620        630        640        650
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE 
       660        670 
RNKNKKLPYY YLSPDRIPNS VAI
Length:673
Mass (Da):78,087
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:i536B0BC27CB0A608
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LMM5F1LMM5_RAT
Polyunsaturated fatty acid 5-lipoxy...
Alox5
674Annotation score:

Annotation score:4 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>
A0A0G2JU29A0A0G2JU29_RAT
Polyunsaturated fatty acid 5-lipoxy...
Alox5
620Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA41538 differs from that shown. Reason: Frameshift.Curated

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
J03960 mRNA Translation: AAA41538.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...PIRi		A30882

NCBI Reference Sequences

More...RefSeqi		NP_036954.1, NM_012822.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25290

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25290

UCSC genome browser

More...UCSCi		RGD:2096, rat

<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
J03960 mRNA Translation: AAA41538.1 Frameshift.
PIRiA30882
RefSeqiNP_036954.1, NM_012822.1

3D structure databases

SMRiP12527
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-48659N
IntActiP12527, 1 interactor
STRINGi10116.ENSRNOP00000017633

Chemistry databases

BindingDBiP12527
ChEMBLiCHEMBL312
DrugCentraliP12527

PTM databases

iPTMnetiP12527
PhosphoSitePlusiP12527

Proteomic databases

PaxDbiP12527
PRIDEiP12527

Genome annotation databases

GeneIDi25290
KEGGirno:25290
UCSCiRGD:2096, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		240
RGDi2096, Alox5

Phylogenomic databases

eggNOGiENOG502QQSP, Eukaryota
InParanoidiP12527
PhylomeDBiP12527

Enzyme and pathway databases

UniPathwayiUPA00877
BRENDAi1.13.11.34, 5301
ReactomeiR-RNO-2142688, Synthesis of 5-eicosatetraenoic acids
R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-2142700, Synthesis of Lipoxins (LX)
R-RNO-6798695, Neutrophil degranulation
R-RNO-9018676, Biosynthesis of D-series resolvins
R-RNO-9018682, Biosynthesis of maresins
R-RNO-9018896, Biosynthesis of E-series 18(S)-resolvins
R-RNO-9020265, Biosynthesis of aspirin-triggered D-series resolvins
R-RNO-9023661, Biosynthesis of E-series 18(R)-resolvins
R-RNO-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins
R-RNO-9026290, Biosynthesis of DPAn-3-derived maresins
R-RNO-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins
R-RNO-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

Miscellaneous databases

Protein Ontology

More...PROi		PR:P12527

Family and domain databases

CDDicd01753, PLAT_LOX, 1 hit
InterProiView protein in InterPro
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR042062, PLAT_LOX_verte
PANTHERiPTHR11771, PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit
PRINTSiPR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOX5_RAT
<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: P12527
<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: April 7, 2021
This is version 162 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

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again