P51399 (LOX5_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arachidonate 5-lipoxygenase Short name=5-LO Short name=5-lipoxygenase EC=1.13.11.34 | ||
| Gene names |
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| Organism | Mesocricetus auratus (Golden hamster) | ||
| Taxonomic identifier | 10036 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus![]() |
Protein attributes
| Sequence length | 673 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. |
| Catalytic activity | Arachidonate + O2 = leukotriene A4 + H2O. |
| Cofactor | Binds 1 iron ion per subunit By similarity. Binds 2 calcium ions per subunit By similarity. |
| Pathway | |
| Subunit structure | Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity By similarity. |
| Subcellular location | Cytoplasm By similarity. Nucleus matrix By similarity. Nucleus membrane; Peripheral membrane protein By similarity. Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-271. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association By similarity. |
| Post-translational modification | 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 By similarity. |
| Sequence similarities | Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Leukotriene biosynthesis |
| Cellular component | Cytoplasm Membrane Nucleus |
| Ligand | Calcium Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological_process | leukotriene biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular_component | cytosol Inferred from sequence or structural similarity. Source: UniProtKB nuclear envelope lumenInferred from sequence or structural similarity. Source: UniProtKB nuclear matrixInferred from electronic annotation. Source: UniProtKB-SubCell nuclear membraneInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | arachidonate 5-lipoxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB iron ion bindingInferred from sequence or structural similarity. Source: UniProtKB lipoxygenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 673 | 672 | Arachidonate 5-lipoxygenase | PRO_0000220694 | |||||
Regions | |||||||||
| Domain | 2 – 117 | 116 | PLAT | ||||||
| Domain | 118 – 673 | 556 | Lipoxygenase | ||||||
Sites | |||||||||
| Metal binding | 17 | 1 | Calcium 1; via carbonyl oxygen; structural By similarity | ||||||
| Metal binding | 18 | 1 | Calcium 2; via carbonyl oxygen; structural By similarity | ||||||
| Metal binding | 19 | 1 | Calcium 2; structural By similarity | ||||||
| Metal binding | 44 | 1 | Calcium 2; structural By similarity | ||||||
| Metal binding | 45 | 1 | Calcium 2; via carbonyl oxygen; structural By similarity | ||||||
| Metal binding | 47 | 1 | Calcium 2; structural By similarity | ||||||
| Metal binding | 79 | 1 | Calcium 1; via carbonyl oxygen; structural By similarity | ||||||
| Metal binding | 80 | 1 | Calcium 1; via carbonyl oxygen; structural By similarity | ||||||
| Metal binding | 367 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 372 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 550 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 554 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 673 | 1 | Iron; via carboxylate; catalytic By similarity | ||||||
| Site | 103 | 1 | Essential for stabilizing binding to COTL1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 271 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 523 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Cloning, sequencing and expression of a 5-lipoxygenase from Syrian hamster embryo fibroblasts." Kitzler J.W., Eling T.E. Prostaglandins Leukot. Essent. Fatty Acids 55:269-277(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Syrian. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U43333 mRNA. Translation: AAA85257.1. |
3D structure databases | |
| ProteinModelPortal | P51399. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG005150. |
Enzyme and pathway databases | |
| UniPathway | UPA00877. |
Family and domain databases | |
| Gene3D | 2.60.60.20. 1 hit. |
| InterPro | IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view] |
| PANTHER | PTHR11771. PTHR11771. 1 hit. |
| Pfam | PF00305. Lipoxygenase. 2 hits. PF01477. PLAT. 1 hit. [Graphical view] |
| PRINTS | PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE. |
| SMART | SM00308. LH2. 1 hit. [Graphical view] |
| SUPFAM | SSF49723. Lipase_LipOase. 1 hit. SSF48484. Lipoxygenase. 1 hit. |
| PROSITE | PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LOX5_MESAU | ||||||||
| Accession | Primary (citable) accession number: P51399 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
