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Reviewed, UniProtKB/Swiss-Prot P48999 (LOX5_MOUSE)

Last modified January 19, 2010. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Arachidonate 5-lipoxygenase
      Short name=5-lipoxygenase
      Short name=5-LO
    EC=1.13.11.34
Gene names
Name: Alox5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. Ref.1

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 By similarity.

Subcellular location

Cytoplasm. Nucleus matrix. Nucleus membrane; Peripheral membrane protein By similarity. Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association By similarity. Ref.1

Post-translational modification

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-524 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus By similarity.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 674673Arachidonate 5-lipoxygenase
PRO_0000220695

Regions

Domain2 – 118117PLAT
Domain119 – 674556Lipoxygenase

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 binding3681Iron; catalytic By similarity
Metal binding3731Iron; catalytic By similarity
Metal binding5511Iron; catalytic By similarity
Metal binding5551Iron; catalytic By similarity
Metal binding6741Iron; via carboxylate; catalytic By similarity

Amino acid modifications

Modified residue2721Phosphoserine By similarity
Modified residue5241Phosphoserine By similarity

Experimental info

Mutagenesis6721V → M: Loss of activity. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P48999-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4061CD107EE53B4F

FASTA67477,999
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC YRWITGEGEI VLRDGRAKLA 

       130        140        150        160        170        180 
RDDQIHILKQ HRRKELEARQ KQYRWMEWNP GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL 

       190        200        210        220        230        240 
NYSKAMENLF INRFMHMFQS SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG 

       250        260        270        280        290        300 
CNPVLIKRCT ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP 

       310        320        330        340        350        360 
CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL AKIWVRSSDF 

       370        380        390        400        410        420 
HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH VRFTIAINTK AREQLICEYG 

       430        440        450        460        470        480 
LFDKANATGG GGHVQMVQRA VQDLTYSSLC FPEAIKARGM DSTEDMPFYF YRDDGLLVWE 

       490        500        510        520        530        540 
AIQSFTMEVV SIYYENDQVV EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL 

       550        560        570        580        590        600 
TVVIFTASAQ HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 

       610        620        630        640        650        660 
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIISVIA ERNKNKKLPY 

       670 
YYLSPDRIPN SVAI

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References

[1]"cDNA cloning, expression, mutagenesis, intracellular localization, and gene chromosomal assignment of mouse 5-lipoxygenase."
Chen X.-S., Naumann T.A., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.
J. Biol. Chem. 270:17993-17999(1995) [PubMed: 7629107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-672.
Strain: C57BL/6 X 129/Sv.
Tissue: Peritoneal cavity.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42198 mRNA. Translation: AAC37673.1.
IPIIPI00115652.
PIRI49479.
UniGeneMm.41072

3D structure databases

SMRP48999. Positions 3-674.
ModBaseSearch...

Protein-protein interaction databases

STRINGP48999.

PTM databases

PhosphoSiteP48999.

Proteomic databases

PRIDEP48999.

Genome annotation databases

EnsemblENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:87999. Alox5.

Phylogenomic databases

eggNOGroNOG14414.
HOGENOMHBG443995.
HOVERGENP48999.
InParanoidP48999.

Enzyme and pathway databases

BRENDA1.13.11.34. 244.

Gene expression databases

ArrayExpressP48999.
BgeeP48999.
CleanExMM_ALOX5.
GenevestigatorP48999.
GermOnlineENSMUSG00000025701. Mus musculus.

Family and domain databases

InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHERPTHR11771. LipOase. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameLOX5_MOUSE
AccessionPrimary (citable) accession number: P48999
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents