Reviewed,
UniProtKB/Swiss-Prot P12527 (LOX5_RAT)
Last modified
November 25, 2008.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Arachidonate 5-lipoxygenase Short name=5-lipoxygenase Short name=5-LO EC=1.13.11.34 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
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)
| Catalytic activity | Arachidonate + O(2) = leukotriene A(4) + H(2)O. |
| Cofactor | Binds 1 iron ion per subunit By similarity. Binds 2 calcium ions per subunit By similarity. |
| Pathway | |
| Subcellular location | Cytoplasm. Membrane; Peripheral membrane proteinBy similarity. Note= Calcium binding promotes binding to membranes By similarity. |
| Sequence similarities | Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain. |
| Sequence caution | The sequence AAA41538.1 differs from that shown. Reason: Frameshift at position 667. |
Ontologies
Keywords | |
|---|---|
| Biological process | Leukotriene biosynthesis |
| Cellular component | Cytoplasm Membrane |
| Ligand | Calcium Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arachidonate 5-lipoxygenase activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: InterPro 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 | ||||||
| Chain | 2 – 673 | 672 | Arachidonate 5-lipoxygenase | PRO_0000220696 | |||||
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 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 271 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 523 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Isolation and characterization of a cDNA clone encoding rat 5-lipoxygenase." Balcarek J.M., Theisen T.W., Cook M.N., Varrichio A., Hwang S.-M., Strohsacker M.W., Crooke S.T. J. Biol. Chem. 263:13937-13941(1988) [PubMed: 3417684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1." Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B. Biochemistry 32:6320-6323(1993) [PubMed: 8518276] [Abstract] Cited for: SEQUENCE REVISION TO 667-670. |
Cross-references
Sequence databases | |
|---|---|
| J03960 mRNA. Translation: AAA41538.1. Frameshift. | |
| PIR | A30882. |
| RefSeq | NP_036954.1. |
| UniGene | Rn.9662 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LOX based on UniProtKB P12530. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000012972. Rattus norvegicus. [Contig view] |
| GeneID | 25290. |
| KEGG | rno:25290. |
Organism-specific databases | |
| RGD | 2096. Alox5. |
Phylogenomic databases | |
| HOVERGEN | P12527. |
Gene expression databases | |
| ArrayExpress | P12527. |
| GermOnline | ENSRNOG00000012972. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000907. LipOase. IPR013819. LipOase_C. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view] |
| Gene3D | G3DSA:2.60.60.20. Lipase_LipOase. 1 hit. |
| PANTHER | PTHR11771. LipOase. 1 hit. |
| Pfam | PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view] |
| PRINTS | PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE. |
| SMART | SM00308. LH2. 1 hit. [Graphical view] |
| PROSITE | PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 606033. |
Entry information
| Entry name | LOX5_RAT | ||||||||
| Accession | Primary (citable) accession number: P12527 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


