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P12527 (LOX5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 5-lipoxygenase

Short name=5-LO
Short name=5-lipoxygenase
EC=1.13.11.34
Gene names
Name:Alox5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Lipid metabolism; leukotriene A4 biosynthesis.

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. Nucleus matrix. Nucleus membrane; Peripheral membrane protein. 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.

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.

Sequence caution

The sequence AAA41538.1 differs from that shown. Reason: Frameshift at position 667.

Ontologies

Keywords
   Biological processLeukotriene biosynthesis
   Cellular componentCytoplasm
Membrane
Nucleus
   LigandCalcium
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from mutant phenotype PubMed 20204486. Source: RGD

arachidonic acid metabolic process

Inferred from mutant phenotype PubMed 15107407. Source: RGD

leukotriene biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

lipoxygenase pathway

Inferred from mutant phenotype PubMed 15107407. Source: RGD

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 16331105. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 12490039. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 16956363. Source: RGD

sensory perception of pain

Inferred from mutant phenotype PubMed 19580807. Source: RGD

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 16606359. Source: RGD

nuclear envelope lumen

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from sequence or structural similarity. Source: UniProtKB

sarcolemma

Inferred from direct assay PubMed 15107407. Source: RGD

   Molecular_functionarachidonate 5-lipoxygenase activity

Inferred from mutant phenotype PubMed 15107407. Source: RGD

iron ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

lipoxygenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 673672Arachidonate 5-lipoxygenase
PRO_0000220696

Regions

Domain2 – 117116PLAT
Domain118 – 673556Lipoxygenase

Sites

Metal binding171Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding181Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding191Calcium 2; structural By similarity
Metal binding441Calcium 2; structural By similarity
Metal binding451Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding471Calcium 2; structural By similarity
Metal binding791Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding801Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding3671Iron; catalytic By similarity
Metal binding3721Iron; catalytic By similarity
Metal binding5501Iron; catalytic By similarity
Metal binding5541Iron; catalytic By similarity
Metal binding6731Iron; via carboxylate; catalytic By similarity
Site1031Essential for stabilizing binding to COTL1 By similarity

Amino acid modifications

Modified residue2711Phosphoserine By similarity
Modified residue5231Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P12527 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 536B0BC27CB0A608

FASTA67378,087
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG RDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY RWITGEGEIV LRDGCAKLAR 

       130        140        150        160        170        180 
DDQIHILKQH RRKELETRQK QYRWMEWNPG FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN 

       190        200        210        220        230        240 
YSKAMENLFI NRFMHMFQSS WHDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC 

       250        260        270        280        290        300 
NPVLIKRCTE LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 

       310        320        330        340        350        360 
THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA KIWVRSSDFH 

       370        380        390        400        410        420 
IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV RFTIAINTKA REQLNCEYGL 

       430        440        450        460        470        480 
FDKANATGGG GHVQMVQRAV QDLTYSSLCF PEAIKARGMD NTEDIPYYFY RDDGLLVWEA 

       490        500        510        520        530        540 
IQSFTTEVVS IYYEDDQVVE EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT 

       550        560        570        580        590        600 
VVIFTASAQH AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH 

       610        620        630        640        650        660 
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE RNKNKKLPYY 

       670 
YLSPDRIPNS VAI 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 667-670.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03960 mRNA. Translation: AAA41538.1. Frameshift.
IPIIPI00194785.
PIRA30882.
RefSeqNP_036954.1. NM_012822.1.
UniGeneRn.9662.

3D structure databases

ProteinModelPortalP12527.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48659N.
STRING10116.ENSRNOP00000017633.

PTM databases

PhosphoSiteP12527.

Proteomic databases

PRIDEP12527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25290.
KEGGrno:25290.
UCSCRGD:2096. rat.

Organism-specific databases

CTD240.
RGD2096. Alox5.

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidP12527.
KOK00461.
OrthoDBEOG46Q6S3.

Enzyme and pathway databases

UniPathwayUPA00877.

Gene expression databases

ArrayExpressP12527.
GenevestigatorP12527.
GermOnlineENSRNOG00000012972. Rattus norvegicus.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP12527.
ChEMBLCHEMBL312.
NextBio606033.

Entry information

Entry nameLOX5_RAT
AccessionPrimary (citable) accession number: P12527
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families