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P12530 (LOX15_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 15-lipoxygenase
Short name=15-LOX
EC=1.13.11.33
Alternative name(s):
Erythroid cell-specific 15-lipoxygenase
Omega-6 lipoxygenase
Gene names
Name:ALOX15
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; leukotriene D4 biosynthesis.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLeukotriene biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processleukotriene biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarachidonate 15-lipoxygenase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: InterPro

lipoxygenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 663662Arachidonate 15-lipoxygenase
PRO_0000220699

Regions

Domain2 – 115114PLAT
Domain116 – 663548Lipoxygenase

Sites

Metal binding3611Iron; catalytic
Metal binding3661Iron; catalytic
Metal binding5411Iron; catalytic
Metal binding5451Iron; catalytic
Metal binding6631Iron; via carboxylate; catalytic

Experimental info

Sequence conflict1901N → D in AAB86978. Ref.2
Sequence conflict1941I → V in AAB86978. Ref.2

Secondary structure

1 .................................................................................................... 663
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12530 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C3391E1E6E7930BF

FASTA66375,310
        10         20         30         40         50         60 
MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK VNVSKYLGSL 

        70         80         90        100        110        120 
LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW VVGDGVQSLP VGTGCTTVGD 

       130        140        150        160        170        180 
PQGLFQKHRE QELEERRKLY QWGSWKEGLI LNVAGSKLTD LPVDERFLED KKIDFEASLA 

       190        200        210        220        230        240 
WGLAELALKN SLNILAPWKT LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM 

       250        260        270        280        290        300 
LLRRSVQLPA RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP 

       310        320        330        340        350        360 
LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS SDFQVHELNS 

       370        380        390        400        410        420 
HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI NVRARNGLVS DFGIFDQIMS 

       430        440        450        460        470        480 
TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD RGLLGVESSF YAQDALRLWE IISRYVQGIM 

       490        500        510        520        530        540 
GLYYKTDEAV RDDLELQSWC REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ 

       550        560        570        580        590        600 
HSSIHLGQLD WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD 

       610        620        630        640        650        660 
QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE YLRPSIVENS 


VAI

« Hide

References

[1]"The promoter structure and complete sequence of the gene encoding the rabbit erythroid cell-specific 15-lipoxygenase."
O'Prey J., Chester J., Thiele B.J., Janetzki S., Prehn S., Fleming J., Harrison P.R.
Gene 84:493-499(1989) [PubMed: 2612916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: comparison of the predicted amino acid sequence of the erythrocyte lipoxygenase with other lipoxygenases."
Fleming J., Thiele B.J., Chester J., O'Prey J., Janetzki S., Aitken A., Anton I.A., Rapoport S.M., Harrison P.R.
Gene 79:181-188(1989) [PubMed: 2777088] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31.
[3]"Cloning of a rabbit erythroid-cell-specific lipoxygenase mRNA."
Thiele B.J., Fleming J., Kasturi K., O'Prey J., Black E., Chester J., Rapoport S.M., Harrison P.R.
Gene 57:111-119(1987) [PubMed: 3123326] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
[4]"Structure of the mRNA and of the gene coding for the rabbit erythroid 15-lipoxygenase."
Thiele B.J., Fleming J., Chester J., O'Prey J., Prehn S., Janetzki S., Rapoport S.M., Harrison P.R.
Biomed. Biochim. Acta 49:S17-S24(1990) [PubMed: 2386503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, GENE STRUCTURE.
[5]"The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity."
Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F.
Nat. Struct. Biol. 4:1003-1009(1997) [PubMed: 9406550] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M33291 Genomic DNA. Translation: AAA75014.1.
M27214 mRNA. Translation: AAB86978.1.
M22617 mRNA. Translation: AAA31385.1.
PIRJQ0018.
RefSeqNP_001075751.1. NM_001082282.1.
UniGeneOcu.7470.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LOXX-ray2.40A2-663[»]
2P0MX-ray2.40A/B2-663[»]
ProteinModelPortalP12530.
SMRP12530. Positions 2-663.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009114.

Organism-specific databases

CTD246.

Phylogenomic databases

GeneTreeENSGT00550000074415.
HOVERGENHBG005150.

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. 2 hits.
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...

Entry information

Entry nameLOX15_RABIT
AccessionPrimary (citable) accession number: P12530
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 104 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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